Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

Contents lists available at ScienceDirect

Biocatalysis and Agricultural Biotechnology

journal homepage: www.elsevier.com/locate/bab

Marine microbes as a valuable resource for brand new industrial biocatalysts MARK
a b,⁎
Azadeh Beygmoradi , Ahmad Homaei
a
Department of Marine Biology, Faculty of Sciences, University of Hormozgan, Bandar Abbas, Iran
b
Department of Biochemistry, Faculty of Sciences, University of Hormozgan, P.O. Box 3995, Bandar Abbas, Iran

A R T I C L E I N F O A B S T R A C T

Keywords: The marine environment is one of the most important sources of bioactive compounds in the world. Marine
Marine microbes, Valuable resource, Novel microbial communities from marine environments secrete variety enzymes based on their habitat and their
industrial biocatalysts ecological roles. They are considered important ecological components in marine environments due to their
Biochemical characteristics performance in biogeochemical processes. Marine microbial enzymes including protease, lipase, collagenase,
Biotechnological applications
agarase, cellulose and Tother enzymes are important in different industrial due to their properties and appli-
cations. The biochemical diversity of marine microbial makes them reasonable sources of a wide variety of
enzymes for use in different industrial including food, medicine and other biotechnological systems. Therefore,
marine microbial enzymes preparations due to a special applications and functions in the biotechnology projects,
also these can suggestion novel catalysts of biological and biochemical reactions with unique properties and
functions. In this review, we focus on microbial enzymes from marine derived and their biochemical significance
and their increasing importance in biotechnology.

1. Introduction special lighting conditions, microorganisms in the marine environment

The marine with more than 70% of Earth's area, not only has rich
biodiversity but also a source for the microorganisms with potential is
vast. Marine environment are including diverse communities of plants,
animals and microbes that marine microbial communities including
bacteria, fungi, viruses and etc. have several advantage in marine en-
vironments due to their performance in biotechnological processes
(Sowell et al., 2008). Marine environment contains huge potential of
microorganisms, fungi, plants and animals are a rich source of biodi-
versity, which have the capability to extract enzymes from marine
sources. A marine enzyme may be a unique protein molecule not found
in any terrestrial organism or it may be a known enzyme from a ter-
restrial source but with novel properties (Dadshahi et al.,
2016; Homaei, 2015b; Homaei et al., 2016a, 2016b). Microbial en-
zymes have more advantages than the enzymes are derived from plant
or animal because these enzymes have advantages such as broad bio-
chemical diversity, the ability to mass culture, ease of genetic manip-
ulation, a more catalytic activity, lower costs, equipment and sustain-
ability are relatively more abundant (Bull et al., 2000). With the
advancement of marine science, biotechnology and microbial fermen-
tation technology, demand and interest researchers to identify and
characterize microbial enzymes have been more sea (Sharifian et al.,
2017; Zeinali et al., 2015). Marine environment with extreme chemical
conditions, including high salinity, high pressure, low temperature and
compared to their unique living environments and habitats genetic
properties (Stach et al., 2003). Marine microbes of different habitats
and the habitats shelter a diverse range of microbes, including archaea,
cyanobacteria, eubacteria, Actinomycetes, yeasts, filamentous fungi,
microalgae, algae and protozoa. Almost all this potential source of
enzymes that are beneficial to their potential has not been fully un-
derstood. The main goal of modern enzyme technology and storage of
food components, effective use of raw materials, improve food quality,
food diet, raw food use in the preparation of animal feed and process
optimization is to reduce costs. The oceans, huge library of unique
compounds and natural products and bioactive substances enzymes
promising and surprising such as protease, amylase, lipase, chitinase,
cellulose, ligninase, pectinase, xylanase, nucleases (DNAase, RNAase,
restriction enzymes), and so are the potential application, which will
never be found in a dry environment (Mohebbi et al., 2014). For ex-
ample, marine actinomycetes not only in terms of ecological and tax-
onomical but also in terms of production and new biochemical bioac-
tive compounds such as antibiotics, anti-tumor, suppress the immune
system, enzymes, enzyme inhibitors (Dharmaraj, 2010), antimicrobial
compounds, including aminoglycosides, antracyclines, the glycopep-
tide, beta-lactams, macrolides, nucleosides, peptides, made of them,
polyester, polyketoides, actinomycin and tetracyclines are important
(Berdy, 2005). Marine actinomycetes are virtually unlimited sources of
novel compounds and streptomyces the most economical and the most

⁎
Corresponding author.
E-mail addresses: a.homaei@hormozgan.ac.ir, a.homaei@gmail.com (A. Homaei).

http://dx.doi.org/10.1016/j.bcab.2017.06.013
Received 22 May 2017; Received in revised form 26 June 2017; Accepted 26 June 2017
Available online 28 June 2017
1878-8181/ © 2017 Elsevier Ltd. All rights reserved.
A. Beygmoradi, A. Homaei Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

Table 1
Industrial and commercial applications of numerous marine microbial enzymes.

Enzymes Applications References

Lipase Food flavoring, organic synthesis, cosmetic production, detergents, paper production, (Chi et al., 2009; Ferreira-Dias et al., 2013)
biodiesel industry and textile industry
Protease Detergent industry, leather industry, pharmaceutical, commercial liquid and solid detergents (Chanalia et al., 2011; Ilona and Zdzislaw, 2007;
Sawant and Nagendran, 2014)
Chitinase and Increase immune function, improve digestive function, drug delivery, agriculture, wound care (Je and Kim, 2006; Kumar et al., 2014; Ngo et al.,
chitosanase application, metal capture from wastewater and prevent tumor cell growth 2008)
Agarases Additive in moisturizing cosmetic (Martin et al., 2014; Oren, 2004)
Carrageenase Aoagulant, adhesives, stabilizer, gelation and emulsifier (Zhao et al., 2012)
Amylase Added to flour at the mill or bread making and (Gupta et al., 2003)
oxidized gluten for improved dough properties
Cellulase Biotextile, cotton and linen products processing and biofertilizer (Sukharnikov et al., 2011; Zhao et al., 2012)
xylanase Useful in textiles, paper and pulp industry, decrease the usage of Cl2 and ClO2, reduce (Doi, 2008; Nishiyama et al., 2002)
pollution and cleavage some polysaccharides in juice or beer industry
Tannase Usage of antioxidants in fats and oils in the food industry, wines and beer, treated green tea, (Chávez-González et al., 2012; Du-Thumm et al.,
use of tannase as an ingredient of animal feed, treatment of fruit juices to reduce the bitterness 2005; Van de Lagemaat and Pyle, 2006)
and coffee flavored, discolor the tooth surface
Phytase Use in bakery and sweeteners (Jorquera et al., 2008; Lei and Porres, 2003)
Esterase Degradation of plastic, usage of food, textile industries and deinking (Sayali et al., 2013)

valuable biotechnology are prokaryotes. Studies have shown that
bioactive compounds derived from the genus streptomyces. In fact,
stereptomysis genus alone is capable of producing more than 80% of
natural products actinomycetes and analysis of complex biological
polymers, and in this regard remains unrivaled in the world of microbes
(Manivasagan et al., 2014).
According to recent problems such as high population most coun-
tries, the waste of resources and pollution, identify the marine sources
is important biological development. Marine microbial enzymes, par-
ticularly enzymes that have the ability to survive in extreme conditions
such as heat-resistant enzymes used in PCR thermal vents near the
ocean floor of the bacteria obtained the importance and more appli-
cation (Grace, 1997). This review wills briefly discus potential uses of
properties marine microbial enzymes with novel chemical biodiversity
for its various industrial and medical applications (Table 1).
2. Properties, importance and biotechnological applications of
marine microbial agarases
Agarases a colloid extracted from seaweed, which is used in the
decomposition of agar. Agar or agar-agar is a jelly-like substance, ob-
tained from algae is a mixture of agarose and agaropectin which is
extracted from red algae Gelidium robustum. Agarose, a polysaccharide
with a molecular weight of 120 kDa, which is a duplicate of D-galactose
and 3,6-anhydro-L-galactose β1 → 4 and α1 → 3 connected with the
gangs have been formed (Chi et al., 2012; Fernandes, 2014; Fu and Kim,
2010).
Agar pectin a heterogeneous mixture of small molecules with a
backbone, such as agarose, but shows the ionic nature of the acid
groups (such as sulphate, pyruvate) is covered is as natural compounds
(Delattre et al., 2011). Alpha and beta agarases has two classes that
according to research conducted by researchers in various marine or-
ganisms, most agarases been detected β-agarases category (Chi et al.,
2012; Han et al., 2013).
In 1902, Gran isolated agar-degrading Pseudomonas galatica from
seawater (Zhang and Kim, 2010). In 1987, Mervyn found the Strepto-
myces agarase gen (dagA) (Buttner et al., 1987). Marine bacteria Vibrio
sp. (JT0107) the ability to bond hydrolysis α-l, 3 glycosidic agar is by α
-Neoagaro-oligosaccharides (Sugano et al., 1993b). Rosert studied on
agaA gene of Pseudomonas and agarases gene sequencing (Belas, 1989).
In 1993 by Yasushi, agaA gene from Vibrio cloned and sequenced.
Suzuki et al. (2003) purified a new type beta-agarase agaropectin of
bacteria Bacillus sp. MK03, enzyme hydrolysis neoagarohexaose ability
to produce neoagarotetraose and its neoagarobiose.
Agarases have been isolated from several marine source, most
notably Vibrio sp., Pseudomonas stutzeri, Aeromonas sp, Cytophaga,
Bacillus, Alteromonas, Pseudoalteromonas, Streptomyces (Aoki et al.,
1990; Hosoda et al., 2003; Sugano et al., 1993b) and Alteromonas
agarlyticus GJ1B (P. Potin et al., 1993), Thalassomonas sp. JAMB-A33
(Ohta and Hatada, 2006), Alteromonas sp. E-l (Kirimura et al., 1999),
Microscilla (Naganuma et al., 1993), Streptomyces coelicolor A3 (Buttner
et al., 1987), Pseudoalteromonas sp. BL-3 (Lee et al., 2005), Vibrio sp.
AP-2 (Aoki et al., 1990), Pseudomonas atlantica (Belas, 1989), Bacillus
sp. MK03 (Suzuki et al., 2003), Catenovulum agarivorans (Cui et al.,
2014), Microbulbifermaritimus (Vijayaraghavan and Rajendran, 2012),
Alteromonas sp. C-1 (Leon et al., 1992), Vibrio sp. JT0107 (Sugano et al.,
1993a), Agarivorans sp. HZ105 (Hu et al., 2009), Bacillus cereus ASK202
(Kim et al., 1999), Alteromonas sp., Cytophaga sp., Agarivorans gilvus and
Pseudoalteromonas sp. (Chi et al., 2012; Fu and Kim, 2010). Halococcus
sp. is capable to production of β-agarases with molecular weight 55 kDa
and optimum pH 6 (Minegishi et al., 2013). Also gram-negative bacteria
Microbulbifer maritimus were detected in capable of producing extra-
cellular enzymes agarases with molecular weight 75.2 kDa and Km
3 mM (Vijayaraghavan and Rajendran, 2012).
Agarase is an enzyme with systematic name agarose 4-glycanohy-
drolase that found in agarolytic microorganisms (Parro and Mellado,
1994). An agarase marine bacterium are able to control many appli-
cations including red algae bloom, avoid biofouling on sea levels as a
food additive in food and cosmetics moisturizing additives, and has a
high level of activity for depolimerization the complex polysaccharides
such as agar and agarose. In addition emulsification capabilities, the
gelatinized and particles are stable, they also can be found in the food
industry in the manufacture of soft drinks, confectionary, jelly, bread
and produce some low-calorie foods used (Rasmussen and Morrissey,
2007; Yaphe and Morgan, 1959). Agarase in genetic science is im-
portant and necessary; also have applications in gene technology and
agarose gel electrophoresis to separate DNA fragments ( Table 2).
3. Extremozymes
The sea is extremely complex environment with a variety of dif-
ferent physicochemical conditions of extreme conditions such as large
fluctuations in temperature, strong alkaline, strong acid, high hydro-
static pressure and nutrient status is very poor. Microorganisms such as
fungi, bacteria, algae and other microorganisms that are able to grow in
extreme situations have been called extremophilic (Table 3). The ex-
tremophilic microorganisms in biotechnology research are a topic of
interest by many researchers (Danson and Hough, 1998).
Alteromonas, psychrotrophs and other microorganisms that are psy-
chrophilies due to resistant to low temperatures are very useful and has

132
 A. Beygmoradi, A. Homaei

Table 2
Important kinetic and biochemical properties of marine microbial agarases.

B Species Optimum pH Optimum Km Activators Inhibitors Other properties References

Temprature (°C)

Saccharophagus sp. 7.5 55 Ca2+, K+,Na+ and EDTA (each 2 mM) Ca2+, Mn2+, Zn2+ and EDTA (Lee et al., 2013)
(each 2 mM)
Catenovulum agarivorans 6.0 60 3.78 mg mL−1 Na+, K+, Ca2+ and SDS (each 1 mM) Cu2+, Fe3+, Mg2+, Mn2+, EDTA Molecular mass: 46.9 kDa, (Cui et al., 2014)
(each 1 mM) and Ni2+ (10 mM) Thermostable
Catenovulum sp. 7.4 52 Ca2+ and Mg2+ (each 2 and 10 mM), Mn2+ (2 mM and 10 mM), Fe3+ (Xie et al., 2013)
Na+ and K+ (each 10 mM) and β- (2 mM), EDTA (2 mM and
mercaptoethanol (10 mM) 10 mM), SDS (2 mM) and urea
(10 mM)
Zobellia galactanivorans 6.0 2 mM Molecular mass: 13.4 kDa, (Murielle et al., 2005)
(AgaAc) Kcat: 150 s−1
Zobellia galactanivorans 7.0 1 mM Molecular mass: 60 kDa, (Murielle et al., 2005)
(AgaB) Kcat: 100 s−1
Pseudoalteromonas sp. 6.0 40 8.36 mM Ca2+ and Ba2+ Hg2+, Cu2+, Mn2+ and EDTA Molecular mass: 50.4 kDa, (Ma et al., 2007)
CY24
−1
(AgaB) Kcat: 5.16 s

133
Acinetobacter junii PS12B
Pseudoalteromonas
hodoensis sp.a
Acinetobacter sp., AG
LSL−1
Alteromonas sp.b GNUM1
Microscilla
Alteromonas sp. E-l
Catenovulum agarivorans
YM01
7.0 35 Specific activity: 1.90+0.10 U/mg, (Roseline and
Enzyme activity: 0.37+0.12 U/mg Sachindra, 2016)
37 Molecular mass: 30 kDa (Ramos et al., 2016)
6.0 40 0.071 mg mL−1 Zn2+, Sn2+ and SDS Hg2+, Ag+ and Cu2+ Molecular mass: 100 kDa, (Lakshmikanth et al.,
Specific activity: 397 U/mg, 2009)
Vmax: 368 U/mg
7.0 40 (Seo et al., 2014)
6–8 24–37 10 mg/l to 500 mg/ Enzyme was stable in the presence of NaCl (Naganuma et al.,
l concentrations (0.5–0.7 M) 1993)
7.5 40 K+, Na+ and EDTA Mn2+, Cu2+, Fe2+, Zn2+ and Molecular masses: 82 (by SDS- (Kirimura et al., 1999)
Hg2+ polyacrylamide gel electrophoresis) and
180 kDa (by Superdex 200 kDa gel
filtration),
Specific activity: 34 U/mg
6.0 60 3.78 mg mL−1 Mg2+, urea, EDTA and SDS Cu2+, Mn2+, Fe3+ and Ni2+ Molecular mass: 46.9 kDa, (Cui et al., 2014)
Vmax: 1.14 × 104 U/mg

a
Expressed in Bacillus subtilis extracellular -agarase (AgaA7).
b
Expressed in Escherichia coli (AgaG1).
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
A. Beygmoradi, A. Homaei Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

Table 3
Diversity of microbes in extreme marine environmental conditions.

Living environment Properties species References

Psychrophilies Extracellular protease production by the marine Rhodotorula mucilaginosa L7 (Lario et al., 2016)
antarctic yeast,
Maximum proteolytic activity 23.98 U/mL at pH
4.0 and 10 ◦C
R. mucilaginosa L7, Rhodotorula glutinis (Kamada et al., 1972)
Exiguobacterium sp. (Kasana and Yadav, 2007)
SKPB5 (MTCC 7803)
Thermophilies Aeromonas sp. (Charoenpanich et al., 2011)
Hyperthermophilic archaebacteria Pyrococcus furiosus (Adams et al., 1995)
Thermotoga sp.
Bacillus stearothermophilus, Thermocrinis ruber, (Homaei et al., 2016)
Thermus Rt41A
Sulfolobus acidocaldariusis, Methanococcus (Tsuchiya et al., 1992)
jannaschii
Thermoactinomyces sp. HS682
Pyrococcus furiosus
Thermostable and halophilic Zunongwangia profunda (Vieille and Zeikus, 2001)
Thermo- and alkali-stable Bacillus licheniformis (Liu et al., 2014)
(Songsiriritthigul et al.,2010)
Bacillus sp. GX6638 (Durham et al., 1987)
Acidophilies Can be live at pH 5 and even below 1 Aspergillus awamori BTMFW032 (Beena et al., 2010)
Alkaliphilies Bacillus sp. (Fujiwara et al., 1993)
Halophilies Planococcus rifitoensis (Essghaier et al., 2010)
Haloalkaliphilic Bacillus pumilus (Menon et al., 2010)
Bacillus Clausii (Kumar et al., 2004)
Bacillus sp. (Ve2–20–91 [HM047794]) (Raval et al., 2014)
Alkaliphilie, halophilies, and Marinimicrobium sp. (Zhao et al., 2012)
thermostable

many advantages over a simple culture, reduce costs, save energy and
etc. The enzymes lipase and protease derived from them, especially has
great potential in terms of biochemical industry and has the highest
catalytic activity are most efficiently.
Thermophilies microorganisms in deep-sea volcanoes and hydro-
thermal vents are found that are capable of withstanding high tem-
peratures even higher than 100 °C. Thermophilies enzymes derived
from microorganisms for their good performance at high temperatures,
have great value in the biological sciences. For example, nucleic acid
enzymes such as DNA polymerase, ligase and restriction endonuclease
are high-value applications in the molecular biology and genetics sci-
ence. Lundberg team DNA polymerase enzyme purified from thermo-
philic archaeo Pyrococcus furiosus, which is due to polymerization,
reading errors and high activity at temperatures up to 100 °C, is widely
used in polymerase reaction chain (Cowan et al., 1987; Huber et al.,
1986).
Non-specific nucleases isolated from a thermophilic bacteriophage
GBSV1 ability to destroy various nucleic acids, including RNA, single-
stranded DNA and double-stranded DNA (Song and Zhang, 2008). Also
marine bacterium Alteromonas espejiana BAL 31 is capable of producing
the enzyme endonuclease and exonuclease activity for single-stranded
DNA, which is great value in genetic engineering. Lipase isolated from
pseudomonas from marine sediments which have the highest tempera-
ture range 30 °C to 80 °C and pH range is from 5.0 to 9.0. The maximum
activity for produced marine microbial lipase of 1980 U/mL, pH 7.5
and 35 °C is the temperature (Ramani et al., 2013).
Thermococcus genus of bacteria isolated from hydrothermal vents at
a concentration of 1–3% salt has been unable to work. Marine microbial
Bacillus sonorensis 4R, Thermococcus sibiricus, Pyrococcus furiosus,
Archaeoglobus fulgidus, Thermotoga sp., Pyrobaculus calidifontis,
Thermococcus celer and Sulfolobus sp. like S. solfataricus, S. acid-
ocaldarius, and S. shibatae except hyperthermophilic that are lipase
activity (Adams, 2004; Babu et al., 2008; Bhosale et al., 2016; Gantelet
and Duchiron, 1998; Renge et al., 2012). Species belonging to the genus
Salinivibrio capable of producing thermostable lipases and activities for
30 min at 80 °C and pH 7.5–8.0 and 0.1–3.0 M NaCl concentration is
tolerated (Dalmaso et al., 2015). Extracellular enzymes secreted from
the microorganisms or enzymes alkaliphilic acidophilus are generally
enzymes. In some areas of the ocean is conditions acidophilus or al-
kaliphilic, microorganisms can live there. For example acidophilies
microorganisms such as Acidianus, Desulfurolobus, Sulfolobus at pH 5
and even below 1 can operate or alkaliphilies microorganisms such as
Natronococcus, Bacillus in conditions pH above 9 can actively live.
3.5% average salinity of sea water in the ocean, but in some areas
can reach more. A large number of halophiles microorganisms can
tolerate high salinity in areas with high salinity. Halophilic enzymes of
these microorganisms can be high levels of salinity in good shape and
optimal activity (David and Michel, 1999; Niehaus et al., 1999).
A cold-active lipase isolated from bacterium Colwellia psychrery-
thraea exhibited optimum activity around 25 °C and pH 7.0 (Do et al.,
2013) and cold-active extracellular lipase isolated from psychotropic
Yersinia enterocolitica exhibited activity at temperature ranging from
0 °C to 60 °C with optimum activity at 37 °C (Ji et al., 2014).
4. Production of proteases by marine microbes and their
industrial applications
Proteases have been isolated from a large number of biological
sources including plants, animals and microbes that among them the
microbes of great importance in various industries. For example, nearly
two third of industrial and commercial proteases are produced by
marine microbial including fungi, yeasts and bacteria species (Wang
et al., 2013a, 2013b).
Among Bacillus genus, especially Bacillus subtilis is a super source for
protease production because of aptitude to secrete proteins into
medium and high growth rate (Joo and Choi, 2012).
For the first time in 1960, alkaline protease isolated from Bacillus
licheniformis. Then the enzyme from other marine microorganisms for
enzyme production in laboratory conditions was isolated. An alkaline
protease microbial obtained for the first time from Bacillus licheni-
formis in 1960 by Dane. Nobou Kato, 1972 isolated for the first time
alkaline protease from marine psychrobacter (Zhang and Kim, 2008).
Qiu et al. selected 30 kinds of marine bacteria from the sea water,
mud, fish and other samples; after UV mutagenesis they isolated the N1-

134
 Table 4
Unique biochemical and catalytic properties of microbial proteases from marine organisms.

Species Optimum pH Optimum Km Activators Inhibitors Other properties References

A. Beygmoradi, A. Homaei

Temperature (°C)

Aureobasidium 4.0 28.0 (Li et al., 2007)

Pullulans
Bacillus subtilis DR8806 8.0 45 Ca2+, K+, Mg2+, Fe2+ and DMSOa Hg2+, Ba2+, Cu2+, Zn2+, H2O2, CTABb Molecular mass: 37 kDa (Farhadian et al., 2015)
and SDS
Purpureocillium lilacinum 4.0 to 9.0 65 DMSO, methanol, isopropanol, Molecular mass: 37 kDa (Cavello et al., 2013)
LPS # 876 surfactants (Triton X−100, sodium
dodecylsulfate and Tween 85)
Bacillus sp. high pH (10) 60 0.57 mg/mL Molecular mass: 71 kDa, (Jain et al., 2012)
Vmax: 445.23 U/mL
Halophilic strain SD11 10 60 EDTA, PMSFc (5 mM) Molecular mass: 45 kDa, (Cui et al., 2015)
Ca2+, Mn2+, Zn2+, Cu2+, Na+ and K+ Alkaline serine Protease
Bacillus sp. MIG 11–12 50–55 Ag+, Alkaline serine Protease (Gouda, 2006)
Hg 2+ and
PMSF
Bacillus firmus CAS 7 11 70 Mn2+, Fe2+, Co2+, Mg2+, Ca2+ and PMSF, EDTA (1 and 10 mM), Molecular mass: 21 kDa, (Annamalai et al.,
Hg2+ (0.1 and 1 mM) phenanthrolein, mercaptoethanol, DTNBd Specific activity: 473.4 U/mg 2014a, 2014b)
and SBTIe (1 and 5 mM)
Rhodotorula mucilaginosa 5.0 50 Extracellular acid protease, Halostable in (Lario et al., 2015)
L7 the presence of high concentrations of
NaCl (0.5–3.5 M)
Bacillus alveayuensis CAS 9.0 50 Mn2+, Fe2+, Co2+, Mg2+, Ca2+, Hg2+ PMSF, Thermostable, halostable alkaline (Annamalai et al.,

135
5 and EDTA (0.1 and 1 mM) mercaptoethanol, DTNB and SBTI (1 and protease, Specific activity: 518.78 U/mg 2014a, 2014b)
5 mM)
Marinobacter MBRI 7 7.0 40 Extracellular protease, (Fulzele et al., 2011)
halotolerant and high thermostabe
Aspergillus ustus 9.0 20 PMSF Serine protease, (Damare et al., 2006)
Heat-sensitive,
relatively more active than mesophilic
enzymes at a low temperature
Bacillus sp. APCMST-RS3 9.0 60 0.6666 g/l NaCl (2.5 M), surfactants (Tween 20, 40 PMSF, DTT, iodoacetamide, Haloalkalophilic. Protease, Maximum (Maruthiaha et al.,
and SDS), CaCl2, CuSO4, MnCl2, BaCl2 mercaptoethanol, EDTA (5 mM) activity in the presence of NaCl (2.5 M), 2015)
and MgCl2 (5 ppm) Molecular mass: 40 kDa,
V max: 1111.11 U/mL
Specific activity: 28.62 and 1.68 U/mg
Pseudomonas SD11 10 40 Ca2+, Mn2+, Zn2+, Cu2+, Na+, and K+ SDS, PMFS (each 5 mM) and H2O2 (1% v/ Thermostable alkaline serine protease, (Cui et al., 2015)
(each 5 mM) v) Protease activity: 171.9 U/mL
Bacillus sp. 60 (Doddapaneni et al.,
2009)
Bacillus mojavensis A21 60 (Haddar et al., 2009b)
Bacillus firmus CAS 5 9 50 Mn2+, Fe2+, Co2+, Mg2+, Ca2+, Hg2+ PMSF, EDTA, mercaptoethanol, DTNB, Thermostable and halostable alkaline (Annamalai et al.,
and EDTA (0.1 and 1 mM) SBTI (1 and 5 mM) protease 2014a, 2014b)

a
Dimethylsulfoxide.
b
Cetyl trimethyl ammonium bromide.
c
Phenyl methyl sulfonyl fluoride.
d
Dithio-bis-nitrobenzoic acid.
e
Soybean trypsin.
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
A. Beygmoradi, A. Homaei
35 strain, this strain produced protease that had significant advantages
compared with the terrestrial ones (Graham et al., 1980).
Yeast Aureobasidium pullulans has a high efficiency alkaline protease
and the highest enzyme production with a value of 623.1 U/mg (7.2 U/
mL) protein (Chi et al., 2007). Haddar and colleagues in 2009, alkaline
protease from marine bacterium Bacillus mojavensis A21 isolated, they
have two stable detergents alkaline serine – protease (BM1 and BM2)
were purified from this strain. Both proteases for nonionic surfactant
showed high stability.
In fact, both of them excellent stability with a wide range of liquid
and solid showed great detergents (Haddar et al., 2009b). various
marine microorganisms, including bacteria, fungi, yeast, etc., that are
capable of producing a novel alkaline protease enzyme that in between
them yeasts including Aureobasidium pullulans (Chi et al., 2007), Can-
dida olea (Nelson and Young, 1987), Yarrowia lipolytica (Matoba et al.,
1988) and bacteria including Bacillus sp. (Beheshti Maal et al., 2009;
Nadeem et al., 2008; Sarethy et al., 2011), Bacillus mojavensis A21
(Haddar et al., 2009a), Bacillus mojavensis (Khalil Beg and Gupta, 2003),
B. stearothermophilus F1 (Rahman et al., 1994), Pseudomonas aeruginosa
MN1 (Bayoudh et al., 2000), Brevibacterium linens ATCC 9174 (Rattray
et al., 1994) and fungi, including Aspergillus, Mucor and Rhizopus
(Charles et al., 2008; Devi et al., 2008; Ghasemi et al., 2011; Kuberan
et al., 2010) the main manufacturers of these enzymes. The first time
protease-resistant to heat (thermophilic) and high pressure (barophilic)
were isolated from Methanococcus jannaschii (Michels and Clark, 1997).
Protease isolated and purified from archeo Pyrococcus abyssi is re-
sistant to high temperatures (Dib et al., 1998). New extracellular serine
proteinase of marine archeobacter Aeropyrum pernix identification has a
half-life of 85 min in temperature 100 °C and 12 min in temperature
110 °C (Chavez et al., 1999). According to research review paper
(Kumar and Takagi, 1999) optimum temperature (°C) of some proteases
in marine microbes including Penicillum griseofulvin is 28 °C (Dixit and
Verma, 1993), Bacillus sp. B21-2 is 30 °C (Fujiwara and Yamamoto,
1987), Aspergillus flavus is 32 °C (Malathi and Chakraborty, 1991), Ba-
cillus sp. Y is 35 °C (Shimogaki et al., 1991), Bacillus licheniformis is
36 °C (Mao et al., 1992), B. alcalophilus subsp. halodurans KP1239 is
37 °C (Takii et al., 1990), Bacillus licheniformis is 39.5 °C (Hübner et al.,
1993), Bacillus sp. strain B18′ is 40 °C (N. Fujiwara et al., 1993), Bacillus
thermoruber BT2T is 45 °C (Manachini et al., 1988), Thermo-
actinomycetes sp. HS682 is 52 °C (Tsuchiya et al., 1992), B. stear-
othermophilus AP-4 is 55 °C (Dhandapani and Vijayaragavan, 1994), B.
stearothermophilus F1 is 60 °C (Rahman et al., 1994), Aspergillus oryzae
MTCC 5341 is 55 °C (Vishwanatha et al., 2009). Extracellular proteases
from marine bacteria Sphingomonas paucimobilis isolated from stomach
south polar krill Euphausia superba is purification and identification
(Turkiewicz et al., 1999).
Vibrio spp. is capable to produce all kinds of extracellular proteases.
V. alginolyticus able to produce 6 types serine protease-resistant de-
tergents unusual and alkaline serine exoprotease. The marine bacteria
capable of producing the enzyme collagenase is widely used that this
very useful in cosmetic production and commercial industries (Alemán
and Martínez-Alvarez, 2008).
One of the most important enzymes is proteases that more than 60%
of the total industrial and commercial industrial enzymes in the world
are included. In modern society, proteases widely in various industries
including leather, industrial detergents, alcohol and beer, confectionery
and pharmaceuticals such as digestive, physiological activities in the
body, nutraceutical activity and anti-inflammatory drugs are the most
used (Alemán and Martínez-Alvarez, 2008; Kumar and Takagi, 1999).
Proteases are classified on the basis of their differences in optimal
conditions for specific activity, substrate, pH, temperature, stability,
active site and catalytic mechanisms have been (Charles et al., 2008).
Marine bacteria produce chemicals and enzymes are valuable source.
Proteases produced in some marine bacteria used in detergents and
cleaners. Vibrio alginolyticus produced protease 6 types that one of
which is resistant to detergents. Also this marine bacterium capable of
136
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
producing the collagenase is widely used in commercial industries
(Table 4).
5. Biochemical properties and biological functions of marine
microbial lipases
Lipase or acylglycerol acylhydrolases are ubiquitous enzymes that
ability to hydrolyze esters of long-chain aliphatic acids from their gly-
cerol (Jensen, 1983; Shahidi and JanakKamil, 2001). Lipase break-
downs triglycerides into fatty acids and glycerol. Among the variety of
lipase, including plant, animal, bacterial, microbial lipases because of
the ease culture and wide as a catalyst in many reactions and synthetic
hydrolytic most commercial applications (Saxena et al., 1999). Micro-
bial lipases are also non-toxic and adaption with environment
(Boonmahome and Mongkol Thanaruk, 2013). Lipase in various in-
dustries such as dairy, food, detergent, textile, pharmaceutical and
cosmetics used (Patnala et al., 2016).
The first microbial lipases in 1935 by Kirsh were found in fungi
Aspergillus flavus and Penicillium Oxalicum (David, 1935). Bacteria
Achromobacter sp., Alcaligenes sp., Arthrobacter sp., Chromobacterium sp.,
Staphylococcus sp. and Pseudomonas sp. are able to produce lipase.
Major producers of fungal lipases including Aspergillus niger,
Rhizopus delemar, Rhizopus japonicus, Rhizopus niveus and Rhizopus or-
yzae, Candida cylindracea, Humicola lanuginosa, Mucor miehei, M.pusillus
of thermophilic as a manufacturer of heat-resistant extracellular lipase
known. For extracting fungal lipases low cost, resistance to pH and
temperature, substrate selectivity and activity in organic solvents as
compared to bacterial lipases more. Most bacterial lipases non-selective
in choosing your substrate and few of them are also resistant to heat.
Physical parameters such as catalytic activity, pH, temperature etc.
affect the rate of lipase production (Table 5). Lipase production rate in
different species, different strains of the fungus is reported, for example,
Fusarium sp., the optimal pH and temperature are 2.5 and 30 °C re-
spectively, while in bacterial species such as Bacillus subtilis, the op-
timum temperature and optimum pH is 30 °C and 7.0, respectively
(Pallavi et al., 2014).
In 2009, Mo and colleague isolated and purified a new type extra-
cellular phospholipase C from 400 a marine streptomycete that was se-
lected from approximately 400 marine bacteria. This enzyme has an
optimal activity at pH 8 and temperature of 45 °C and cause the hy-
drolysis of phosphatidylcholine (Mo et al., 2009). It is reported that
lipase production of Burkholderia cenocepacia ST8 increased in presence
peptone as a nitrogen source (Ananthi et al., 2014). In 1935, the first
isolated lipase from Penicillium oxalicum and Aspergillus flavus (Zhang
and Kim, 2008). The production of lipase in the thermophilic bacterium
Bacillus sp. is higher when olive oil is used as carbon source. Other
studies have shown that the presence of simple sugar glucose in the
medium inhibited catabolic enzyme production is through suppression
(Sarethy et al., 2011). A small number of bacterial lipase is resistant to
high temperatures. Among the microbial species Achromobacter sp.,
Alcaligenes sp., Arthrobacter sp., Pseudomonas sp., Staphylococcus sp., and
Chromobacterium sp. are able to produce lipase (Jaeger and Eggert,
2002). This means that marine resources are bacteria extremophiles
tolerate contain data extreme conditions of temperature, pH, salinity,
acidic or alkaline, etc. According to studies, bacteria belonging to the
genus pseudomonas are able to produce lipase resistant to high tem-
peratures, high enantiomer sensitivity and maintain its activities in a
wide range of kinetic parameters such as temperature and pH (Patnala
et al., 2016). Bacterial lipase from Pseudomonas otitidis of marine se-
diments activity in the temperature range 30 °C to 80 °C and pH range is
from 5 to 9 and maximum lipase production in pH and temperature
have been reported at 7.5 and 35 °C respectively. It is reported that
Thermococcus genus of bacteria that have been isolated from hydro-
thermal lake's ability to produce lipase. In addition, the bacterium
Thermococcus sibiricus obtained from the oil reservoir Samotlor (West
Siberia) is containing 15 genes to produce lipase / esterase. Other
A. Beygmoradi, A. Homaei Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

bacteria that have been are reported include lipase activity Archae-

(Balakrishna et al., 2017)

oglobus fulgidus, Pyrobaculus calidifontis and Sulfolobus sp. S. solfataricus,

(Basheer et al., 2011)

(Bhosale et al., 2016)

(Ramakrishnan et al.,
(Sathishkumar et al.,

(Hardeman and Sara

(Vyas and Chhabra,
S. acidocaldarius and S. shibatae (Renge et al., 2012). Cold-active lipase

(Diaz et al., 2006)

(Cho et al., 2007)
(Lan et al., 2016)
from Colwellia psychrerythraea isolated from marine environment was

Sjoling, 2007)
References

observed at pH and temperature 7.0 and 25 °C, respectively (Do et al.,

2013). Cold-active extracellular lipase isolated from marine bacteria
2015)

2016)

2017)
Yersinia psychotropic showed an operating temperatures ranging from
0 °C to 60 °C, that maximum lipase production was observed at tem-

Lipase activity: 185 and 220 U/mL at 24 and

perature is 37 °C (Ji et al., 2014). One of the key factors in increasing
Optimal medium constituents: tuna powder
Maximum lipase activity: 1355.81 U/mL,

the production of lipase is metal ions. The most desirable metal ions
(14.58 g/l), olive oil (5.05 mL/l), NaCl

Ca2+ and Mg2+ are used to produce lipase. The lipase activity by these
Hyperthermostable alkaline lipase,

ions increases and partly by Cu2+, Al3+, Zn2+, Ba2+, Pb2+, Fe2+ and
Medium stability alkaline lipase,

Low-temperature-active lipase,
Mn2+ inhibited the activity of the bacterial lipase cold Pseudoalter-
Molecular mass: 21.87 kDa

omonas sp. NJ 70 isolated from Antarctic ice has been demonstrated

Molecular mass: 35.4 kDa

Molecular mass: 44 kDa

Molecular mass: 19 kDa

(Huang et al., 2004). Extracellular phospholipase C, isolated from the
Thermostable lipase,

Curcin and trypsin

marine Streptomycete is able to decompose phosphatidylcholine with
Other properties

the highest enzyme activity at a temperature of 40 °C and pH 8 (Zhang

(72.42 g/l),

and Kim, 2010). Bacteria that grow on the whales are a rich source of
lipase and esterase enzymes that are used in industry huge (Wells,
22 °C

1999). Aeromonas sp. EBB-1-a from sea mud is able to produce extra-
cellular lipase in medium heat with maximum lipase activity after 15 h
PMSF, orlistat, oleic acid, iodine, EDTA,

at temperature 25 °C and pH 8.0 in the presence of olive oil 0.5% (v / v)

CoCl2, CdCl2, HgCl2, CuCl2, Pb(NO3)2,

as the carbon source (Charoenpanich et al., 2011). Nearly to 2000

PMSF, EDTA (each 1, 5 mM) and

species fungi identified that about 600 species are found in the seas.
Since marine fungi resistance is more than physical and biological
DEPC, PMSF, EDAC and NBS
mercaptoethanol (1, 5 mM)

conditions, thus making them a good choice for the production of

secondary metabolites in front of their terrestrial counterparts. In
general they are more tolerant to physicochemical parameters such as
temperature, pH, salinity, and other conditions are associated with
ground fungi. Until now, researchers have found a wide range of mi-
Inhibitors

and urea

croorganisms that can produce lipase, including fungi such as Peni-

cillium, Aspergillus, Rhizopus, Scopulariopsis, Trichoderma, Mucor and
bacteria such as Pseudomonas, Bacillus, Staphylococcus, Aeromonas
(each 0.1, 1 mM), Tween 80, Triton X 100, SDS and

Ethanol and xylene, acetone, propanol and hexane

(Ananthi et al., 2014; Arora, 2013; Charoenpanich et al., 2011; Cho

MgSO4 (0.1 mM), CaCl2, MnSO4, CoCl2, HgCl2

et al., 2007; Ramani et al., 2013).

Lipases are important biocatalysts that break down fat and oil major
release of free fatty acids, and glycerol are the catalyst role. On the
Sodium deoxycholate (each 1,10 mM)

other hand the lipase in a variety of reactions such as esterification,

transesterification and aminolysis play an important role in industrials
Characterization and enzymatic properties of lipases as practical biocatalysts from marine microbes.

(Babu et al., 2008). Biocatalyst potential microbial lipase in aqueous

and non-aqueous as well as good resistance in alkaline environments
and high temperatures Lead to wider use in the broad fields of bio-
MgSO4 and CaSO4

technology, especially dairy, detergents, drugs, chemicals, agricultural

chemicals, oil is the synthesis of fatty substances (Mustranta et al.,
Activators

1995). Microbial lipases are widely used in commercial products and

the majority in diverse industries including food, pharmaceutical, cos-
metic and agricultural has many applications (Chi et al., 2009;
Kobayashi et al., 2008). Lipase biological catalysts are valuable because
they have done little in terms of moderation and stability is high in
Temperature (°C)

organic solvents (Davidson, 2006). According to Koop and Griffiths

these creatures can live for about 70% of organic matter and minerals.
Optimum

A lot of organic matter in marine ecosystems of compounds with high

molecular weight polymeric structure, mainly protein, starch, fat,
45

80

22

40

28

37
35

20
40
40

pectin, cellulase, chitin, nucleic acids, or lignin is formed (Arnos et al.,

Optimum pH

1998; PO Remba, 1995; Unanue et al., 1999). They must extracellular

enzymes break down into simpler compounds (Unanue et al., 1999).
Hence, the measurement and characterization of enzymes is a useful
10.8
9.0

6.0

6.0

8.0
8.0

6.0
7.0
7.5

tool to check the destruction of organic matter and nutrient cycling in

9

aquatic ecosystems provide (Boetius, 1995; Jackso et al., 1995). Lipases

Halobacillus trueperi RSK

Penicillium chrysogenum
Streptomyces sp. MAS1

Rhizopus homothallicus

are widely used in commercial products, biotechnology, organic

Bacillus sonorensis 4 R

Enterococcus faecium

Candida parapsilosis

Aspergillus awamori
uncultured bacteria

synthesis and some other industrial applications (Kempka et al., 2008).

oligophagum
MTCC5695

Due to the ease of recovery of the enzyme from the culture medium of
Cystobasidium

h1Lip1

microorganisms such as bacteria, fungi, yeasts, and actinomycetes are

CAS9
Species

known as extracellular lipase resources. Species of Bacillus, Acromo-

Table 5

bacter, Acinetobacter, Candida, Pseudomonas, Rhizopus, and Geotrichum

are known as the main commercial species (Ertugrul et al., 2007). Some

137
A. Beygmoradi, A. Homaei
40 species are isolated of Aspergillus and Penicillium to produce lipase
broth agar medium containing olive oil as a substrate (Yadav et al.,
1998). Also, many microbial lipases are very useful for heart disease
prevention role (Kinsella, 1986; Strom and Raa, 1993). The beneficial
effect is produced of polyunsaturated fatty acids (PUFA), acid eicosa-
pentaenoic (EPA), acid docosapentaenoic (DPA) and acid docosahex-
aenoic (DHA). Lipases used for commercial and industrial applications
mainly from bacterial sources. They belong to the family of serine hy-
drolases include α / β hydrolase are in their original structure. Enzy-
matic activity of bacteria isolated from marine sediments off the
southern coast of the Baltic, looked at Sopot beach (Mudryk and
Podgórska, 2006). Finally, it should be noted that bacteria play a key
role in the processes of decomposition of organic matter accumulated in
the marine coast (Jedrzejczak, 1999).
6. Research and application of marine microbial cellulase
Cellulose is a polysaccharide with the formula (C6H10O5) n the first
biopolymer abundant in nature. Cellulase about 50% of all plant ma-
terial and hemicelluloses is a polysaccharide related to cellulose make
up about 20–30% (Klemm et al., 2005; Nishiyama et al., 2002). Cel-
lulase enzymes that break down cellulose and polysaccharides it turn
cellodextrin younger. The polysaccharide is consisting of a linear chain
with several unit D-glucose β (1 → 4). Hemicelluloses is a poly-
saccharide related to cellulose with shorter chains of sugar is about 200
units, and unlike cellulose, it can be a few simple sugars such as xylose,
mannose, galactose and rhamnose, etc., derived (Nishiyama et al.,
2002). Since the connection is tightly between cellulose molecules
thereby breaking the cellulose is relatively hard compared to other
polysaccharides (Brás et al., 2008).
Until now, researchers have found a wide range of marine microbes
belonging to Cytophaga (C. diffluens، C. hutchinsonii), Marinobacter sp.
MS1032, Cellulomonas, Vibrio, Paenibacillus sp. BME-14, Clostridium,
Nocardia, Streptomyces, Trichoderma, Aspergillus, Fusarium, Chaetomium,
Phoma, Sporotrichum, Penicillium, etc., which can generate cellulase
(Dong et al., 2010; Fu et al., 2010; Vaidya et al., 2001; Zhang and Kim,
2008).
Marine bacteria coexist in the gland of Deshayes cream naval ships
and Aspergillus terreus are capable of producing cellulase. The thermo-
philic bacterium Thermotoga sp. is producing exo-1, 4- β-cellobiohy-
drolase at temperature 105 °C. According to studies reported that
Bacillus sp. associated with the marine sponge Axinella sp. is capable of
producing carboxy methyl cellulose (Mohapatra, 1997).
Marinimicrobium sp. LS-A18 is capable of producing carbox-
ymethylcellulose with maximum activity in the temperature and pH
55 °C and 7.0, respectively (Zhao et al., 2012).
Cellulase can be used in various industries including the construc-
tion of alcohol, flavors food, paper, corn gluten, detergents, sewage
treatment, bio-textile auxiliaries, cotton, flax and bio-fertilizers pro-
cessing (Shanmughapriya et al., 2010). Since the use of seaweed in the
industry can create very serious problems of environmental pollution
from the use of cellulase is useful to reduce waste and can easily be
absorbed by the plants as bio-fertilizer.
7. Investigation and applications of marine microbial alginate
lyases
Brown algae are one of the biggest sources of marine biomass that
alginate has been made and it has many applications in various in-
dustries including food, pharmaceutical and so on. In recent years, huge
sea-microbial alginate lyases have been developed.
Alginate lyase is linear polymer (1, 4) glycuronans that has been
established of residues β-D-mannosyluronic acid (M) or Apymran α-L
gulosyluronic acid (G). Alginate lyase in C5 is a β-D-mannuronate
138
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
epimer.
These residues are like the building blocks of homopolymer poly-M
(ManA) or poly G (GulA) extend sequences were created by mixing the
Heteropolymeric MG (Yamasaki et al., 2004). Based on the primary
structure of the enzyme alginate lyase divided in three families with
names PL-5, 7, 14 (Hisano et al., 1993).
The family, in particular PL5 and PL-7 made of poly-M but PL- 14
contains poly G or M (Yamasaki et al., 2004). Commercial alginate,
often with the M: G defined. Pseudomonas aeruginosa is a pathogen
opportunistic in immunocompromised hosts caused disorders including
sepsis, urinary tract and respiratory tract. P. aeruginosa bacteria secrete
excessive amounts of exopolysaccharide alginate, mucoid colonies
(Albrecht and Schiller, 2005).
Alginate as a member of the cell wall, the brown seaweeds and some
bacteria belonging to the genus as exopolysaccharide by Azotobacter
and Pseudomonas are made. Alginate polymer is one of the most im-
portant members of biofilm of P. aeruginosa strains of the mucoid co-
lonies to be considered.
Unlike alginate which is made by algae, the bacteria produce a
polysaccharide that most of the acetyl group in position D-mannuronate
is two or three units. Additionally, some of the references that are made
of alginate by Pseudomonas G have no production (Yamasaki et al.,
2004). Type of monomer comprising alginate and alginate acetylation
determines sensitivity to it is destroyed (Yamasaki et al., 2004).
Alginate lyase enzyme linked alginate glycosides by reacting beta
unsaturated acid oligouronic breaks and at the end of the non-renewal
of the production (Yamasaki et al., 2004). Related illnesses due to in-
fection of pseudomonas biofilm, the bacteria can be Fibrous cystic
chronic lung infections and urinary tract infections associated with
catheters pointed (Dunne and Buckmire, 1985; Henrissat et al., 2005; Li
et al., 2011).
Especially poly-M alginate acetylated form of the enzyme that de-
stroys is more significant (Yamasaki et al., 2004). Since few of alginate
lyase enzymes have this property (Hoshino and Kageyama, 1980;
Yamasaki et al., 2004). Thus, one of the striking points for researchers
to find alginate lyase with this feature is to end the destruction of
bacterial biofilm is used.
Alginate-lyase from the marine bacterium Bacillus sp.,
Photobacterium and Alteromonas sp. symbiotic with Laminaria known
isolated and recognition (Sawabe et al., 1997).
Alginate is a polysaccharide found in wide algae and marine and
terrestrial microorganisms. This combination of useful properties such
as having high biocompatibility, biodegradability and, low toxicity and
properties of gel formation, etc., that widely used in various industrial
and medical biomaterials (Gomez d′Ayala et al., 2008; Wong et al.,
2000; Yang et al., 2011). These enzymes have many biotechnology
applications in various industrial such as food, cosmetics, agricultural
and medical fields and are useful in the conversion of biomass brown
algae to methane (Gacesa, 1992; Rasmussen and Morrissey, 2007;
Wong et al., 2000). Alginate lyase activity as a therapeutic aid in the
treatment of infections caused by P. aeruginosa mucoid colonies and the
destruction of the biofilm can be used (Bugli et al., 2013; Laemmeli,
1970). Moreover, alginate lyases removed alginate from the cell surface
mucoid colonies of Pseudomonas and inhibit the attachment of P. aer-
uginosa strains are mucoid colonies (Yamasaki et al., 2004). Alginate in
combination with specialized additives such as chitosan, fibrin, col-
lagen and etc, to get the right combination to produce ideal for a variety
of wounds, including chronic wounds dressing used (Willi and Sharma,
2004).
8. Importance and properties of chitinolytic enzymes isolated
from marine microbes
Chitin is a biopolymer with non-toxic that after cellulose is one of
A. Beygmoradi, A. Homaei Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

the most common polysaccharides found in nature. Most of the com-

(Fu et al., 2016)

ponents of fungal cell wall structure and also one of the most abundant

(Fenice et al.,
(Gaber et al.,

(Wang et al.,
(Farag et al.,

(Yang et al.,
References
in the outer shell of insects and crustaceans such as crab, shrimp, lob-
ster and squid (Table 6).
2016)

2016)

2016)

2014)

1998)
Chitin with chemical formula (C8H13O5N) n and linear chain of
was analysed by incubating 1 mM of substrate with 1 μM of enzyme in acethylglucosamine groups and chitosan with chemical formula

The kinetic parameters, Km and Vmax values of PbChi70 for colloidal

Km and Vmax values of PbChi67 for colloidal chitin and glycol chitin
Purified by 65% ammonium sulphate precipitation, followed by gel

chitin and regenerated chitin were determined to be 7.91 mg mL−1

were 3.35 mg mL−1 and 17.1 mol/min/mg, and 2.66 mg mL−1 and
(C6H11O4N) obtained from residues removal of acetyl glucosamine.
Activity on soluble fully acetylated chitooligosaccharides (A2– A6)

filtration on Sephadex G−100 and DEAE-Sephadex A−50 ion Chitin with the scientific name β- (1 → 4) - 2-acetamido - 2 doxy - D-
glucopyranose and chitosan with the scientific name β- (1 → 4) - 2-
amino - doxy 2 - D- glucopyranose.
Chitin and chitosan history dates back to the 19th century for the
and 28.4 lmol min−1 mg−1, and 14.2 mg mL−1 and
first time in 1811 a French scientist named Braconnot chitin extracted
Product formation was analysed using HPLC.

from fungi. Then Rouget in 1859, chitosan deacetylation of the chitin in

the presence of potassium hydroxide won the game and finally in 1950
was to fully explore its structure (Khor, 2001).
21.8 lmol min−1 mg−1, respectively

High catalytic activity, even at 4 ◦C

Postoperative hydrolase, chitin and chitosan can be high perfor-

Marine psychrophilic bacterium.

15.0 mol/min/mg, respectively

mance, safety, and remove toxins from the body's digestive function
improved, even inhibiting tumor growth and other physiological
exchange chromatography

functions important to make (Ngo et al., 2008). Therefore, chitin and

chitosan hydrolyzate recently has become a hot topic and importance.
Other properties

Until now, it was found that marine microbes can produce chitinase
10 mM BisTris

and chitosanase, including Vibrio fluvialis, Vibrio parahaemolyticus,

Vibrio mimicus, Vibrio alginolyticus, Listonella anguillarum and Aeromonas
hydrophila, Aspergillus, Alteromonas, Penicillium, Rhizopus, Trichoderma,
Myxobacter, Sporocytophaga, Bacillus, Enterobacter, Klebsiella,
Pseudomonas, Serratia, Chromobacterium, Clostridium, Flavobacterium,
Co2+, Fe3+, and Mn2+
ethanol, methanol and

Arthrobacter and Streptomyces (Fukamizo, 2000; Osama and Koga, 1995;

Fe2+, Cu2+,Zn2+,

Tsujibo et al., 1992; Xia et al., 2008).

Hg+, pb, EDTA,

Chitinase genes have been cloned variety of marine fungi and bac-
Inhibitors

teria. Suolow and Jone chitinase genes including ChiB and ChiA in-
acetone

jected into E. coli and these genes transferred into Pseudomonas; finally
obtained 4 chitinase strains with high efficiency (Suolow and Jones,
1988). Meanwhile, Roberts and Cabib, chitinase genes into plant cells
Na+, Mg2+, K+, and

tobacco and are able to develop a new tobacco plant with strong disease
Metal ions such as
Ca2+, Mn2+ and

tolerance to the pathogen Alternaria Longipes (Roberts and Cabib,

1982).
Activators

Chitin and chitosan could be hypoallergenic and antibacterial

Na2+

Ca2+

properties promote digestive function and eliminate toxins from the

body, even inhibit tumor cell growth and great importance in medicine
functions and food industry (Fukamizo, 2000; Ngo et al., 2008).
Molecular mass (kDa)

67.0 kDa by SDS-PAGE

In addition, bio biological properties such as adhesion, anti-cancer,

and 67.9 kDa by gel
Novel features of chitinases from various marine microbes and their biochemical parameters.

anti-microbial, reduce inflammation and pain, antioxidants, choles-

terol-lowering and blood coagulant, have distinguished them from
other biopolymers (Kumar et al., 2004; Kurita, 2006).
filtration

Moreover, fibers made from chitin and chitosan absorbable sutures

113.5
60

70

for preparing and supplying fabrics that are highly effective for wound
healing (Jenkins and Hudson, 2001), chitin and chitosan can be used
for wastewater treatment, heavy metal ions, tissue engineering, anti-
Temperature (°C)

oxidant, anticancer, burn and wound healing, drug delivery and re-
ducer cholestrol (Kumar et al., 2004; Madhumathi et al., 2010; Seol
Optimum

et al., 2004).
Cloned and functionally expressed in Escherichia coli.
(4–30)

28.0

For example, Weltroswki and colleagues were able to use chitosan

45

50

55

20

60

derivatives in an acidic solution to remove metal ions from waste water

Optimum pH

(Weltrowski et al., 1996). A mixture of chitin and chitosan is used to

absorb arsenic in drinking waters (Elson et al., 1980). Chitosan because
of very similar structure of cellulose can be easily factories, paper use
6.0

5.6

5.5

8.0

3.5

4.0

and paper production from chitosan has a smooth surface and high
resistance to moisture much for printing and painting are suitable.
Pseudoalteromonas sp. DL−6
Paenicibacillus barengoltziia

Unlike most chitosan hydrogel properties that are anionic, cationic

Paenicibacillus barengoltzii

property that causes the same features as a preservative in cosmetics

Aspergillus terreus (EC

applied to the skin and hair. Chitosan with many compounds used in
Thermobifida fusca

janthinellum P9

cosmetics, adapted to absorb ultraviolet rays and many or reduce their

(PbChi70)
3.2.1.14)

CAU904

impact (Dutta et al., 2004). Chitosan and hair are complementary in

Penicillium
Species

terms of electric charge, as positively charged chitosan and negatively

(ChiA)
Table 6

charged hair, and a transparent solution of chitosan in the form of a

a

flexible cover is placed on the skin and hair and enhances the softness

139
A. Beygmoradi, A. Homaei Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

and freshness it. Chitin and chitosan both in shampoos, hair dyes,

(Marokhazi et al., 2004)

(Rochima et al., 2016)

(Petrova et al., 2006)

emulsifiers, hair spray and amplifiers are used (Dutta et al., 2004).

(Lima et al., 2009)

Chitosan is used as a dental filling material that can kill fungi on the
surface of the teeth (Sapelli et al., 1986).
References

Chitosan has all the characteristics that should ideally be a lens such
as mechanical stability, cabn high permeability to air, especially
oxygen, moist, antimicrobial and biocompatible is being so widely In
ophthalmology for the preparation of contact lenses (Jing et al., 1996).
The substrate collagen derived of Tilapia fish skin

Chitosan is abundant in the crustaceans and crust of insects that widely

used in bone tissue engineering (Seol et al., 2004). Report on the use of
chitosan composite scaffold of calcium phosphate to be published -More
strength (Lian et al., 2009). Also, chitosan recover and rebuild cartilage
Collagenase activity: 1298 Unit mL–1

(Yamane et al., 2005), neurons (Freier et al., 2005), and liver plays an
important role (Wang et al., 2003). Also chitosan has anti-acid activity
that prevents reducing the effects of drugs in stomach (Miyazaki et al.,
1981). Chitosan-based polymer systems that have been built in the
transfer and release of proteins/peptides (Grenha et al., 2005), growth
Other properties

factors (Elcin et al., 1996), inflammatory pain medications (Aggarwal

et al., 2001), anticancer drugs (Wei et al., 2010), antibiotics (Kavaz
et al., 2010) and also are used in the treatment of genetic incompetence
waste,

(Mansouri et al., 2004).

9. Characteristics and applications of marine microbial

carrageenases
Cu2+, Zn2+, Hg2+ and

Carrageenan is family of linear sulfated polysaccharides that ex-

Mn2+ and Ca2+

tracted from marine red alga Delesseria sanguinea. In early 1943 by

Inhibitors

Mori, carrageenases extracted from marine mollusk. Sarwar et al. from

the culture medium cytophaga lk-C783, κ-carrageenase molecular
Fe2+

weight of 10 kDa extracellular won (Sarwar et al., 1987a, 1987b). In

2004, Mou et al. first isolated a new type of extracellular κ-carrageenase
Mg2+, Ca2+ and Ba2+

from Cytophaga MCA-2 from marine environment that molecular

weight determined 30 kDa (Renner and Breznak, 1998). In 2006, Yu-
Zn2+ and Co2+

kari and Yuji; λ-Carrageenan purified from bacteria Pseudoalteromonas

Activators

CL19 isolated from sediments deep-sea that molecular weight of ap-

Some properties of biophysicochemical, activators and inhibitors of collagenases from different marine microbes.

proximately 100 kDa (Ohta and Hatada, 2006). Bacterial species Pseu-
domonas, Pseudomonas elongata, Cytophaga, Alteromonas atlantica, Al-
teromonas carrageenovora are able to produce carrageenases
Molecular mass (kDa)

(Khambhaty et al., 2007; Potin et al., 1991; Roberts et al., 2007; Sarwar
et al., 1987a, 1987b).
Carrageenanases in industrial processing have many advantages.
The potential applications of carrageenanases enzymes have been re-
116. 97

ported by several authors. This enzyme can be used in food industry,

pharmaceuticals and cosmetics. For example, their potential applica-
74

tions for seafood processing are coagulant, adhesives, stabilizers and

Optimum Temperature (°C)

emulsifiers and their potential applications for medical processing are

anti-viral, anti-bacterial, anti-tumor, anti-coagulation, etc. (Roberts
et al., 2007; Sarwar et al., 1987a, 1987b).

10. Properties and applications of marine microbial xylanases

Xylanases is an enzyme that catalyzes the breakdown xylan.

50

45
37

Xylanases can produce by several microorganisms, including fungi,

–

bacteria, yeast and seaweed that the main commercial source of the
Optimum pH

enzyme is filamentous. Indian researchers showed alkaline xylanase

5 to 10

activity in several marine fungi. Aspergillus niger is able to produce

xylanase with high biological activity (Raghukumar et al., 2004).
8.2
7.5

7.0

Streptomyces viridochromogenes, Streptomyces M11, Trichoderma long-

Candida albicans URM3622
Bacillus subtilis ATCC 6633

ibrachiatum, Thermotoga maritima, Aureobasidium pullulans, Glaciecola

Photorhabdus luminescens

mesophila are able to produce xylanase (Guo et al., 2013; Jiang et al.,
Streptomyces strain 3B

2008; Jiang et al., 2004; Liu et al., 2014). Yin et al., 2010, Bacillus sp.
producing xylanase was isolated from seawater., and they purified this
enzyme in the optimum temperature and pH at 50 °C and 5, respec-
Species

tively (Yin et al., 2010). Xylanase is widely used in production of nat-

Table 7

ural sweeteners, dough-softening ability and paper and pulp industry

(Guo et al., 2009; Subramani and Aalbersberg, 2012).

140
A. Beygmoradi, A. Homaei
11. Marine microbes as a potential source of collagenase enzymes
Collagen is a major protein of skin, ligaments, tendon, bones and
elastic tissues in the more organisms that composed of glysin, proline
and hydroxyl proline.
Collagenolytic enzymes including cathepsin and elastase are cap-
able of degrading collagen (Table 7).
Collagenase enzymes isolated and described from organisms in-
cluding microbes and animals (Daboor et al., 2010). Microbial col-
lagenases have been obtained from microorganisms including Asper-
gillus oryzae, Clostridium histolyticum, Streptomyces parvulus, Streptomyces
sp., actinomycete and etc. (Endo et al., 1987; Goldberg et al., 1986;
Goshev et al., 2005; Nordwig and Jahin, 1968).
Isolated collagenases from bacteria are capable of hydrolyzing both
water-insoluble native collagens and water-soluble (Mookhtiar et al.,
1985).
Harper et al. (1965) reported that collagenases isolated from Clos-
tridium histolyticum had molecular weights ranging from 57 to 105 kDa
(Harper et al., 1965).
In 1984 by Bond and Van Wart; six different collagenases isolated
from the same species with molecular weights ranging from 68 to
128 kDa (Bond and Van Wart, 1984). Afterward, collagenases isolated
from Clostridium perfringens with molecular weights ranging from 80 to
120 kDa (Matsushita et al., 1994).
According to studies collagenases obtained from bacterial have
molecular weight > 55 kDa while molecular weights of collagenases
obtained from animal tissues tend to be lower (Daboor et al., 2010).
For the first time, collagenase was discovered from Clostridium
histolyticum. Collagenase enzymes have a several industrial applications
in foods, medicinal products and cosmetics (Chung et al., 2004; Shahidi
and JanakKamil, 2001; Spök, 2006). Most common uses of these en-
zymes seem to be in medicine. Collagenase plays an important role in
the successful transplantation of specific organs (Kin et al., 2007; Klock
et al., 1996).
12. Marine microbial xylanases with special characteristics for
biotechnological applications
Xylanases is a hydrolytic enzyme that degrades xylan that can
produce economic and industrial high-value products such as xylitol.
Xylanases can be used in the paper industry to improve the dissolution
rate of lignin and reduce the use of Cl2 and ClO2 payments thus redu-
cing pollution and improving the properties of the pulp. Also xylanase
can damage some juice drinks and beer polysaccharides in thus helps to
produce better, more transparent and drinks (Doi, 2008; Klemm et al.,
2005; Nishiyama et al., 2002; Tong et al., 1980). It was found in the
some marine microbes including Aureobasidium pullulans, Trichoderma
longibrachiatum, T. neapolitana, Thermotoga maritime, Glaciecola meso-
phila KMM 241, Nocardioides sp. KP7 and Cycloclasticus sp. A5 (Guo
et al., 2009; Jiang et al., 2008; Jiang et al., 2004).
13. Oxidoreductase isolated from marine microbes
Chloroperoxidase isolated from a marine fungus Caldariomyces fu-
mago the peroxide is unique because it contains cysteinic thiolate as the
fifth ligand accommodate axial ligand is imidazole. This is not only
versatile enzyme peroxidase reactions but mono oxygenasis and cata-
lysis in the presence of halogen ions and H2O2 does (Colonna et al.,
1999).
Flavodon flavus fungus isolated from seaweed degraded coral lagoon
on the coast of the West Indies three vessels, extracellular enzyme is
produced which contains manganese dependent some enzymes such as
peroxidase, lignin peroxidase and laccase (Raghukumar et al., 1999).
A manganese-dependent peroxidase activity was reported of
Debaryomyces polymorphus, Candida tropicalis and Umbelopsis isabellina
(Yang et al., 2003).
141
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
Three structure-activity of superoxide dismutase (iron, copper/zinc
and an anonymous form) showed in marine Cyanobacterium synecho-
coccus sp. (Chadd et al., 1996). Superoxide dismutase was isolated from
marine yeast Debaryomyces hansenii (Hernandez-Saavedra and Ochoa,
1999).
Novel glucose dehydrogenases were isolated of Cytophaga marino-
flava (Tsugawa et al., 1996). Glucose dehydrogenase reacts under high
salinity. New type glucose dehydrogenase was purified of marine Gram-
negative bacterium Deleya sp. (Tsugawa et al., 1998).
Nitrite reductase purified by electrophoretic homogeneity of nitrite-
free extract of a marine bacterium Pseudomonas nautical (Besson et al.,
1995).
Pseudomonas doudoroffii strains are able to produce dimethylsulfo-
niopropionate lyase (De Souza and Yoch, 1995).
Carpenter et al. showed that marine cyanobacteria cells
Trichodesmium thiebautii are able to produce Glutamine synthetase
(Carpenter et al., 1992). Cyanobacteria Prochlorococcus sp. are able to
produce glutamine synthetase. Unusual responses were analysed and
adapted to the darkness and famine mechanism of nitrogen from Pro-
chlorococcus sp. for coping with the environment reflect light and nu-
trient limited (El Alaoui et al., 2001).
14. Characteristics and biotechnological importance of marine
microbial amylase
Amylases were found in bread and can break down starch into
simple sugars like compound, such as glucose, maltose and dextrin.
They can classified be β -amylase, α-amylase and γ-amylase. Unlike
other forms of amylase, γ-amylase is most effective in acidic environ-
ments. So far, the production of amylase was reported in some microbes
including Mucor sp., Thermotoga celer, Thermotoga maritime, Arxula
adeninivorans, Pyrococcus furiosus, Lipomyces, Altermonas haloplanctis,
Saccharomycopsis, Schwanniomyces, Vibrio sp., Streptomyces sp., Candida
japonica and Filobasidium capsuligenum (Gupta et al., 2003; Liu et al.,
2012; Manivasagan et al., 2015; Mohapatra et al., 1998). Marine Sci-
ence and Technology developed by researchers at the more micro-or-
ganisms of marine habitats that are capable of producing amylase have
been reported. Marine yeast Aureobasidium pullulans is capable of pro-
ducing exocellular amylase were isolated of depths of the Pacific Ocean
sediments (Li et al., 2007). A novel α-amylase was isolated from marine
Streptomyces sp. and using the medium containing 2% sucrose, 0.35%
and 0.15% peptone malt extract (Chakraborty et al., 2009).
A novel amylase was isolated from Mucor sp. associated with marine
sponge Spirastrella sp. and showed maximum enzyme activity till 60 °C
and pH 5.0 (Mohapatra et al., 1998).
Marine amylase is a subject of interest from the perspective of
biotechnology (Table 8). Production of α-amylase identified and iso-
lated by marine bacteria Pseudoalteromonas undina NKMB 0074
(Matsumoto et al., 2003). Recently reported that the enzyme α-amylase
of marine Streptomyces sp. D1 able to hydrolysis of both α-1–4 and α-
1–6 (Chakraborty et al., 2009).
Amylase in phosphate buffer systems with pH 7–8 buffers are well
within the range pH 9–11 glycine-NaOH was stable when incubated for
6–48 h. The production of amylase was first reported in Streptomyces
with a wide range of pH. This strain is optimum growth temperature
range of 37–55 °C and 45 °C maximum production of amylase is ob-
served. This enzyme is almost 50% of its activity at 85 °C is maintained.
This clearly shows the nature of thermostable enzymes.
To date, the bacteria belonging to the genus Bacillus are used for
commercial production of heat-stable amylase, but such reports of
isolated heat-stable amylase from marine Streptomyces were not re-
ported.
Both terrestrial and marine microorganisms may be adapted to the
optimum growth temperature at 80–108 °C.
Most marine microorganisms belonging to Thermotoga sp. it has
been interesting glycoside hydrolase that can be used in
A. Beygmoradi, A. Homaei Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

transglycosylation reactions (Goyal et al., 2001a; Tramice et al., 2007).

(Santorelli et al., 2016)

(Vijayaraghavan et al.,
Pullulanase, α-amylase and α-glucosidase belonging to archaea

(Mesbah and Weigel,

(Song et al., 2016)

(Sen et al., 2016)

have been active in the high-temperature. These enzymes used for
commercial and industrial applications and used in the starch industry.
References

Pullulanases type I very rare in thermophilic microorganisms that

temperature of at 90 °C is optimal activity. This enzyme capable of

2014)

2015)
hydrolyzing α-1,6 and α-1,4, but cannot break. This enzyme has been
reported only in Fervidobacterium pullulanolyticum. This enzyme is pre-
Halophilic and alkalithermostable glucoamylopullulanase sent in the anaerobic bacteria and archaea also heat-loving bacteria

Maximal amylase production of 464 units/mL of enzyme

was observed in the presence of 100% moisture, 0.1%
have a wide distribution. Marine thermophilic bacteria, Thermococcus
litoralis (optimal temperature of 90 °C) and Pyrococcus furiosus (optimal
temperature of 98 °C) are produced Pullulanases type II. Other bacteria
from which the Pullulanases activity is reported are Pyrococcus woesei,
Molecular mass determined by SDS-PAGE.

Molecular mass estimated by SDS- PAGE,

fructose and 0.01% ammonium sulphate.
Medium stability high-active alkalophilic
Alkali-tolerant and high-active amylase,

Thermococcus celer, Fervidobacterium pennavorans and Desulfurococcus

Extracellular gluco-amylo-pullulanase,

mucosus. Cyclomaltodextrin-glucanotransferase has potential applica-

tion in the production of cyclodextrin and alkaliphilic bacteria Bacillus
Vmax: 250 mmol/min/mL
subtilis from deep-sea mud is separated. β-Glucosidases (3.2.1.21) re-
sponsible for the breakdown terminals, without reducing residues β-D-
Thermostable amylases,
Extreme haloarchaeon.

glucosyl of alkyl and aryl β-glycosides in disaccharides and short chain

Other properties

oligosaccharides, with the release of β-D-glucose are residues (Bhatia

Km: 5.88 mg/mL,
alpha-amylase

et al., 2002). This enzymatic conversion of starch to sugar combined

with glucomylase effective are the glucose and hence a high efficiency.
Wu and Chen, Pullulanases from yeast Aureobasidium pullulans in
flower shape isolated sea (Wu and Chen, 2014). Optimal conditions for
decomposition Pullulan is 47.9◦C and pH 4.92 and incubation period
Mn2+ (each 10 mM), Fe3+ (each 10 mM),
Na+ (each 10 mM), K+ (each 100 mM),

9.40 h.
Al3+ (each 10 mM), Zn2+, Mg2+, Ca2+

Amylopullulunase isolated from high thermophilic archaea

Thermococcus hydrothermalis from deep-sea hydrothermal vents and
showed high activity around pH range 4.0–8.0 with the optimum pH
5.5 (Gantelet and Duchiron, 1998). Similarly, another Pullulanases
Cu2+, Co2+ and Zn2+

isolated from archaea Thermococcus sp. HJ21 (Xu et al., 2009). Ac-
cording efforts produce a variety of high thermophilic Pullulanases
strains or similar high thermal stability, while the optimum tempera-
ture depends on the activity profile.
Inhibitor

and SDS

Archeo Thermococcus able to produce Pullulanase, glucosidase and

EDTA
Marine microbial amylases with desirable properties to be suggested for utilizing different industrial applications.

amylase is Legin et al. (1997). Brown and Kelly (1993) purified extra-
cellular pullulanase from marine Thermococcus litoralis and Pyrococcus
PMSF, DTT, H2O2, Triton-

furiosus (Brown and Kelly, 1993). These two species have high activity
X−100, Tween 20 and

Ca2+, Mg2+ and Na+

amylopullulanases in extreme heat. Pullulanase extracellular enzyme

Na+, K+, and Mn2+

was purified from marine archeo thermostable Thermococcus hydro-

Tween 80. Ca2+

thermalis from hydrothermal vents in the east Pacific (Gantelet and

(each 1 mM)

and EDTA
Activator

Duchiron, 1998).
β-Glucosidases divided to two glycoside hydrolyze family GH1 and
Ca2+

GH3 that most enzymes β-galactosidase and β-glucosidase activity in-

dicator GH1, whereas recent activity shows GH3 enzymes (Henrissat,
Molecular mass

1991). The β-Glucosidases from marine microbes can be used in a

variety of industrial sectors including juices, wine and beer, fragrances
54.0 (SEC)
66.0 (SDS-

and flavors compounds (Kang et al., 2010; Trincone, 2013; Wang et al.,
PAGE)
(kDa)

2013). β-Glucosidases can also be linked to cellulose borers feed ad-

49

50

54

ditives for monogastric animals such as poultry or pig feed is used

Temperature (°C)

which causes gastrointestinal (Zhang et al., 1996).

Applications in Biotechnology hydrolase enzymes have high ac-
tivity, glucose tolerance, resistance to acid and heat and finally have
Optimum

transglycosylation activity (Bohlin et al., 2013). Thermotoga maritima on

marine resources has been identified as producing the enzyme β-Glu-
50

54

55

50

45

cosidases (Goyal et al., 2001b). In T. neopolitana was showed that

Optimum

produces β-glucosidase, GH3 (Turner et al., 2007).

Applications in Biotechnology hydrolase enzymes have high ac-
9.0

8.0

8.5

8.0

8.5
pH

tivity, glucose tolerance, resistance to acid and heat and finally have
transglycosylation activity (Bohlin et al., 2013). Thermotoga maritima
Amphibacillus sp. NM-

Exiguobacterium sp.

on marine resources has been identified as producing the enzyme β-

Luteimonas abyssi

Glucosidases (Goyal et al., 2001b). Marine Actinobacteria Streptomyces

turkmenica
Haloterrigena
XH031

sp. MBRC-82 for the production of secondary metabolites with biolo-

Ra2
species

gical activity such as immunosuppression and antibiotics has attracted

Table 8

considerable attention in Bio-Nano Technology (Manivasagan et al.,

2014). This species is capable of producing α-amylase is an

142
A. Beygmoradi, A. Homaei
environmentally friendly tool.
Most studies show that about 77% of marine bacteria resistant to the
cold poles and 23% are accustomed to the cold. In Feller et al. (1994),
showed that α-amylase obtained from polar marine bacteria Alter-
omonas haloplanktis can grow well at 4 °C and activity of α-amylase is
seven times higher than the α-amylase warm-blooded animals.
α-Galactosidase in the sugar industry to increase efficiency by hy-
drolysis of sucrose, raffinose, α-galactoside is used. α-Galactosidase
obtained from marine Alteromonas spp. α-Galactosidase isolated from
sponges and algae Polysiphonia sp. and bacteria associated with muscle
Crenomytilus grayanus and scallops Patinopecten jessoensis.
Glucoamylases produced has been reported by marine microorganisms.
Marine yeast Aureobasidiumpullulans N13d capable of producing glu-
coamylase with catalytic activity temperature is more than 60 °C (Li
et al., 2007). Also marine fungi endophytic Aspergillus sp. JAN-25
capable of producing glucoamylase has the maximum activity is be-
tween 50 and 60 °C (Matsumoto et al., 2003).
α-amylase has been used extensively in the construction industry,
especially alcoholic beverages such as beer, alcohol, animal feed, de-
tergents for clothes, starch industry, confection and textile industry
(Debashish et al., 2005; Lee et al., 2010; Trincone, 2011; Venugopal,
2016). α-amylase obtained from thermophilic arceo include the Pyr-
ococcus woesei, Pyrococcus furiosus, Thermococcus celer, Fervidobacterium
pennavorans, Desulfurococcus mucosus and Thermotoga maritime; psico-
trophic vibrio isolated from the muds of the sea floor, Vibrio gazogenes,
Alteromonas rubra and Mucor sp. α-Glucosidase use in industry, such as
α-amylase is starch. α-Glucosidase tolerant to heat were isolated from a
marine thermophilic arceobacter (hyperthermophilic) include the Pyr-
ococcus furiosus and Pyrococcus wesei.
15. Transglutaminase from marine microbes (TGases)
Transglutaminase enzyme is known with name EC 2.3.3.13, there
are widespread in nature. The enzyme transglutaminase is a protein
with a molecular weight of 37368 Da that contain 331 amino acids.
This enzyme can be between amino acids glutamine and lysine of a
protein from binding to other proteins. It is remarkable that this en-
zyme does not adversely affect the bioavailability of lysine (Trachoo
and Mistry, 1998). Until the 1989 transglutaminase enzyme was ex-
tracted from the swine liver but research led to the identification of a
bacterial enzyme was produced. The enzyme was extracted and purified
of a bacterial species called Streptoverticillium. Transglutaminase de-
rived from the bacterium has a molecular weight of 40,000 Da by SAS-
PAGE (Sodium Dodecyl Sulphate Poly Acrylamide Gel Electro Phoresis)
and isoelectric pH is about 9.8. The optimal pH of the enzyme activity
between 5 and 9 and between 37° and 50° is the best temperature for its
operation. Generally, transglutaminase enzyme is stable in a wide
temperature range. This enzyme at 50 °C for 10 min retains its activity.
Transglutaminase derived from microorganisms (MTGase) against
transglutaminase derived from pig liver that is calcium-dependent en-
zyme, is independent of calcium ions (Kuraishi et al., 2001). It is re-
ported that marine yeasts, marine fungi and marine bacteria produce
extracellular L-glutaminase (Kashyap et al., 2002; Kumar and
Chandrasekaran, 2003; Sabu et al., 2000).
TGases in regulating cell growth, differentiation, blood coagulation,
keratin of the epidermis and tighten the red blood cell membrane plays
a role. TGases acyl transfer reaction of the γ-carboxamide groups of
glutamine residues peptide bond with the ε-amino residues of lysine
and other amino groups of the protein catalyzes (Venugopal, 2016). L-
glutaminase (L-glutamine amidohydrolase, EC 3.5.1.2) is parser L-glu-
tamine. L-glutaminase has industrial applications and treatment. This
enzyme as anti-cancer, sour taste of food by increasing glutamic acid is
used (Kashyap et al., 2002; Kumar and Chandrasekaran, 2003; Sabu
et al., 2000).
Also the enzyme can be used as biosensors for monitoring and
glutamine levels in mammalian cell cultures hybridoma to be used
143
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
(Katikala et al., 2009). Glutaminase from marine microbes to salinity
and temperature is stable because of an enzyme mode is interest in
many industries like food, pharmaceutical, etc.
16. Microbial phytase in marine environment
Phytase enzyme is belonging to the family phosphatases. This en-
zyme breaks down the phytic acid to smaller parts. The enzyme to
neutralize the negative effect of phytate on protein and nutrients in
monogastric animal diets and increase uptake (Vats et al., 2009; Xiong
et al., 2004).
Phytase is widely used in many industries. Are used in food, dairy,
nutrition industries and has potential applications in other fields.
Several species of marine microorganisms including bacteria, yeast and
fungi are capable of producing phytase (Jorquera et al., 2008;
Noureddini and Dang, 2009).
Recent studies have shown that microbial phytase produced eco-
nomically very significant and used in industry and stake (Lei and
Porres, 2003).
Now, the mushrooms are having efficient enzyme system, the bio-
degradation of undesirable substances such as industrial and agri-
cultural waste, etc., and convert them into usable products and harm-
less, are very important. Some fungi such as Aspergillus, Penicillium,
Mucor and Rhizopus species are commonly used for the commercial
production of extracellular phytase (Pandey et al., 2001).
In 2015 by Sadati and Barghi, 6 species of fungus produces extra-
cellular phytase from coastal waters of the Caspian Sea in Iran was
isolated and identified (Sadati and Barghi, 2014). These include As-
pergillus flavus, Aspergillus ochraceus, Penicillium olsonii, Penicillium digi-
tatum, Discostroma tricellulare and Cladosporium gossypiicola (Chi et al.,
2009; Jorquera et al., 2008; Noureddini and Dang, 2009; Pandey et al.,
2001; Vats et al., 2009; Xiong et al., 2004). These three species Asper-
gillus flavus, Aspergillus ochraceus and Penicillium olsonii showed the
highest phytase activity (Table 9).
17. Biochemical properties and biotechnological aspects of
marine microbial inulinases
Inulinases enzyme responsible for the breakdown of inulin, fructose
or fructo oligosacharide produces the ultimate respectively. Inulinases a
polyfructan in some plants such as Jerusalem artichoke and chicory are
connected by connections β 2,1. The enzymes or probiotics as a
sweetener, has been used extensively in the food industry (Li et al.,
2007; Lima et al., 2011). Inulinase for endo-inulinases (EC 3.2.1.7) or
exoinulinases (EC 3.2.1.80) ranks collapsed and have the ability to
break the chain inulin-type oligosaccharides are smaller (Basso et al.,
2010).
The cleavage reaction can be performed in a temperature range of
40–75 but most analysis is done in 45–55 °C (Kerkhoffs and, 1981;
Ricca et al., 2007). Marinimicrobium sp. LS-A18 able to produce extra-
cellular inulinase is bearing alkaline conditions pH 9. In addition, in-
ulinase able to tolerate salt that has seen the most activity by 0.5% (w/
V) NaCl and 20% NaCl is about 60% active. Inulin can be decomposed
by inulinase under alkaline conditions, temperature and pH 65◦C be at
least 10 (Li et al., 2012). In Nocardiopsis sp. DN-K15 (Lu et al., 2014)
and Bacillus cereus MU-31 (Meenakshi et al., 2013) have been identified
that are capable of producing extracellular exo-inulinase.
18. Marine microbial tannases
Tannases (EC 3.1.1.20) breaks down glucose and tannic acid and
gallic acid is produced in the end. Gallic acid, gallate as antioxidants,
the production of flavors of coffee and brew the tea plays an important
role (Aguilar et al., 2001). Aspergillusawamori BTMFW032 is acid-
ophilus enzyme with optimal pH 2 (Beena et al., 2010). The first time in
2012, it was reported that marine Cyanobacteria Phormidium
A. Beygmoradi, A. Homaei Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

valderianum BDU140441 is able to produce the enzyme Tannases

(Zhang and Kim, 2010)

(Mullaney et al., 2002)

(Palanisami et al., 2011) (Table 10).

(Balakrishna et al.,
(Casey and Walsh,

(Vats et al., 2009)

19. 1Fucoidanase isolated from marine microbes
References

Fucoidan is a sulfated polysaccharide composed of some simple

2003)

2017)
sugars. Fucoidan oligosaccharides with a molecular weight < 1000 Da
and can be used as an activator of human epidermal keratinocytes.
Enzyme activity was not significantly affected by metal ions such as Ca2+, Mg2+,

Fucoidanase obtained from marine Vibrio (Furukawa et al., 1992),

Pseudomonas atlantica and Pseudoalteromonas carrageenovora (Yaphe
and Morgan, 1959).
Marine fungi Marinimicrobium sp. LS-A18 isolated from sea sand
(Baltic Sea, Germany) is capable of producing fucoidanase with max-
Mn2+, Zn2+, but was slightly stimulated in the presence of EDTA

imum activity in the temperature and pH 50 °C and 6.0, respectively

Molecular mass determined by gel filtration and SDS–PAGE,

(Wu et al., 2011).

20. Marine microbial Glucanases

Japanese researchers focused on the extraction glucanase bacteria

Bacillus circulans. They isolated the bacteria from muds Tokyo Bay, but
when put in proper watery environment that could grow and produce
new glucanase.glucanase could α-1,3 bond and the bond α-1,6 glucan
activity in and breaks it up. Researchers isolated a new glucanase from
marine bacterium Bacillus at a temperature of 37 °C best practices
showed that it is medically appropriate for dental and other health care
(Yahata et al., 1990). So far, the production of glucanase was reported
Curcin and trypsin
Other properties

in some microbes including marine streptomycete S. xinghaiensis,

Streptomyces sp. SPB74, Micromonospora sp. ATCC 39149, Streptomyces
albogriseolus, Marinimicrobium sp. LS-A18, Saccharomyces cerevisiae and
marine fungus Chaetomium indicum (Burtseva et al., 2003; Mollers et al.,
2014; Zhao et al., 2012).
Glucanase can be used in various industries, including detergent,
textile, brewing, paper manufacturing (Sukharnikov et al., 2011)
Molecular mass

21. Other marine microbial enzymes

(kDa)

65.5

353

According to recent reports from other enzymes in the sea water and
85

84

sediment microbial enzymes lycopene k-cyclase (Stickforth et al.,

55.9 mg mL−1

2003), L-serine dehydratase (Laroche and Ulber, 2002), poly-

hydroxybutyrate depolymerase (Kita et al., 1995), polyhydroxybutyrate
Vmax

depolymerase (Kita et al., 1995), quinol oxidase (Simpson et al., 1997)

and arylsulphatase (Barbeyron et al., 1995) have been obtained.
Biological resources, including animals, plants and microbes has a
0.295 mM

huge potential for biotechnological applications and valuable products

Km

such as drug, bioactive additives and cosmetics (Lima and Porto, 2016).
Actinomycetales is a very useful bacterium in producing many
bioactive compounds, including antibiotics, probiotics, melanin, anti-
Optimum Temperature

cancer compounds and enzyme inhibitors. Therefore, research on

Actinobacteria is important in the discovery of new bioactive com-
pounds (Manivasagan et al., 2013).
Species of the genus Streptomyces is capable of producing metabo-
lites such as antibiotics, anti-cancer compounds, enzyme inhibitors,
52–55
(°C)
Marine microbes as a resource for novel phytases.

pigments, peptides, trioxacarcins, methylpyridine, macrolides, ter-

67

58

65

37

penes, polyketides, flavonoids and other ingredients (Dharmaraj,

Optimum pH

2010).
25.50–55

Halophillic actinomycetes halotolerant salts as a source of bioactive

metabolites have been less studied. The Actinomycetes capable of de-
1.3

5.0

2.5

5.0

grading organic compounds in contaminated water, soil aliphatic,

aromatic, enzyme inhibitors and metabolites such as antibiotics and
enzymes (Hamedi et al., 2013). B. subtilis SK11.004 is capable of pro-
Aspergillus niger NRRL

Aspergillus niger ATCC

Aspergillus niger van

Candida parapsilosis

ducing γ-glutamyl transpeptidase (GGT) with theanine-forming ability.

Aspergillus ficuum

This enzyme synthesis of theanine using from GGT a potential appli-

NTG−23

Teighem

cation in the production of theanine and other ingredients is γ-glutamyl

3135

9142
Species

(Shuai et al., 2010).

Table 9

Bacillus spp. coastal sediment samples can be isolated from 48 h and

pH 2.5, 35 °C, gelatinase produce. Gelatinase can cause tissue analysis

144
A. Beygmoradi, A. Homaei Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152

Table 10
Biochemical features of tannases extracted from different marine microbes.

Species Optimum pH Optimum Inhibitor Other properties References

Temperature (°C)

Aspergillus tubingensis 6 and 7 50 Km: 0.45 and 0.29 mM, (Wu et al., 2016)
Vmax: 0.26 µM min−1
Aspergillus niger ATTC 5.5 30 (Sabu et al., 2005)
16620
Aspergillus ruber 6.0 30 (Kumar et al., 2007)
Aspergillus fumigatus MA 5.0 25 (Manjit et al., 2008)
Penicillium variable 5.0 50 PMSF and N- ethylmaleimide Molecular mass: 158 kDa (Sharma et al., 2008)
retaining
Bacillus cereus KBR9 4.5 40 Halostable in the presence of high concentrations (Mondal et al., 2001)
of NaCl (2 M)

Table 11
Purification procedures of some microbial enzymes from marine environment.

Species Enzymes Total protein Specific activity Total activity Yield (%) Purification fold References
(mg) (U/mg) (U)

Microscilla Agarase 0.28 10.9 3.1 14 2.5 (Naganuma et al., 1993)

Alteromonas sp. E-l Agarase 0.026 34.0 0.87 1.49 40.9 (Kirimura et al., 1999)
Bacillus sonorensis 4 R Lipase 0.355 2152.08 3055.96 1.98 12.15 (Bhosale et al., 2016)
Halobacillus trueperi RSK Lipase 3.42 1193.59 4082.10 14.31 8.46 (Sathishkumar et al.,
CAS9 2015)
Aspergillus terreus Chitinase 8.79 182.08 1607.15 12 5.16 (Farag et al., 2016)
Paenicibacillus barengoltziia Chitinase 11.0 30.3 333.8 51.9 51.9 (Yang et al., 2016)
Paenicibacillus barengoltzii Chitinase 8.0 10.2 (Fu et al., 2016)
CAU904
Pseudomonas elongata κ-Carrageenase 60.7 (Khambhaty et al., 2007)
Cytophaga Carrageenase 1.69 9633 16,280 32 37 (Potin et al., 1991)
Luteimonas abyssi XH031 α-Amylase 8881 (Song et al., 2016)
Haloterrigena turkmenica α-Amylase 298 79.8 23,794 (mU) 18.9 33.1 (Santorelli et al., 2016)
Anoxybacillus beppuensis Amylase 12 10,000 120,000 20 44 (Kikani and Singh, 2012)
TSSC−1
Bacillus cereus Amylase 8.1 44 180 16 (Annamalai et al., 2011)
Streptomyces A3 Amylase 4.1 1755 7139 58 20 (Chakraborty et al., 2012)
Amphibacillus sp. NM-Ra2 Amylase 2.4 250 600 15.4 4.5 (Mesbah and Weigel,
2014)
Saccharoplyspora A9 Amylase 5.7 1641 9369 25 39 (Chakraborty et al., 2011)
Wangia sp. C52 Amylase 2.6 146 379 56 24 (Liu et al., 2011a)
Nocardiopsis sp. B2 Amylase – 1755 – 20 44 (Chakraborty et al., 2014)
Bacillus cereus IND4 Amylase 54.6 3.9 (Vijayaraghavan et al.,
2015)
Pseudomonas sp. K6–28–040 Amylase 6.5 135 875 44 5 (Liu et al., 2011b)
Zunongwangia profunda Amylase 0.7 1663 1164 20 333 (Wu et al., 2014a)
(AmyZ2)
Exiguobacterium sp. Amylase 50.5 1083 U/mL 54,668 (Sen et al., 2016)
Vibrio sp. Amylase 1.4 327 461 78 163 (Najafi and Kembhavi,
2005)
Candida parapsilosis Phytase 637.66 U/g (Balakrishna et al., 2017)
Aspergillus ficuum NTG−23 Phytase 150.1 615 4.1 mg 71.5 (Zhang et al., 2010)
Rhodotorula mucilaginosa L7 Acid protease 0.58 5218 3026 40.42 41.77 (Lario et al., 2015)
Aspergillus oryzae MTCC Acid protease 8 43,658 3,49,264 29 16.6 (Vishwanatha et al., 2009)
5341
Bacillus sp. APCMST-RS3 Protease 8.60 28.62 246.15 U/mL 22.66 8.49 (Maruthiaha et al., 2015)
Purpureocillium lilacinum LPS Serine protease 0.32 1432.7 458.5 1.3 (Cavello et al., 2013)
# 876
Bacillus subtilis DR8806 Serine protease 53 79.3 37.5 3.4 (Farhadian et al., 2015)
Bacillus alveayuensis CAS 5 Alkaline protease 7.83 518.78 4062.1 12.86 7.77 (Annamalai et al., 2014b)
Bacillus sp. Alkaline protease 1.4 657.14 920 64.11 (Jain et al., 2012)
Bacillus firmus CAS 7 Alkaline protease 7.3 473.4 3456.2 12.3 2.6 (Annamalai et al., 2014b)
Halophilic strain SD11 Alkaline protease 3.10 432.32 1340.18 68 2.38 (Cui et al., 2015)
Rhodococcus sp. YM12 Phosphinothricin N- 1.08 23.40 25.27 19.60 334.3 (Wu et al., 2014b)
acetyltransferase

a
Cloned and expressed in Escherichia coli (PbChi70).

during tumor metastasis and swollen joints (Balan et al., 2012). Araki macrura ability to synthesize extracellular β-galactosidase is adapted to
et al., 117 marine bacteria belonging to Pseudomonas, Alcaligenes, cold conditions (Turkiewicz et al., 2003).
Klebsiella, Enterobacter, Vibrio, Aeromonas, Moraxella, Bacillus, etc., each
of which can be detected and isolated β-mannanase were produced
22. Conclusions
(Amki, 1981).
Pseudoalteromonas sp. isolated from the Antarctic krill Thyssanoessa
Our growing knowledge and technique improvement regarding

145
A. Beygmoradi, A. Homaei
protein extraction and purifi cation has led to the production of many
enzymes at analytical-grade purity for research and biotechnological
applications (A. Homaei, 2015a; Homaei et al., 2014; Homaei and
Etemadipour, 2015; Sharifian et al., 2017; Zeinali et al., 2015). Recent
advances in biotechnology, particularly in protein engineering, have
provided the basis for the efficient development of enzymes with im-
proved properties. This has led to establishment of novel, tailor-made
enzymes for completely new applications (Dadshahi et al.,
2016; Homaei, 2015b; Homaei and Saberi, 2015; Homaei and Samari,
2017; Homaei et al., 2017; Homaei et al., 2013a; Homaei et al.,
2010; Homaei et al., 2013b; Rouzbahan et al., 2016; Rouzbehan et al.,
2017). Studies related to the prospecting of microbial enzymes from
marine environments that are different from their terrestrial counter-
parts and also increase our understanding about the function, applica-
tion, diversity and ecology of this microbial group.
Microbes and microorganisms from marine environments secret
different enzymes based on their function and their habitat. In the
present review, several marine microbial enzymes were isolated from
seawater and marine sediments, purified and characterized for this
properties and applications (Table 11). Marine microbial enzymes,
especially extremophiles, have become more and more important in
applications. Clinical and industrial application of marine microbial
enzymes has been developing also. Collectively, this article has pro-
vided many examples of marine microbial from marine sources which
are being used as successful biocatalysts. Their use highlights a pros-
pering and exciting area of industrial biotechnology.
Acknowledgements
The authors express their gratitude to the research council of the
University of Hormozgan for financial support during the course of this
project.
References
Adams, D.J., 2004. Fungal cell wall chitinases and glucanases. Microbiology 150 (Pt 7),
2029–2035.
Adams, M.W., Perler, F.B., Kelly, R.M., 1995. Extremozymes: expanding the limits of
biocatalysis. Biotechnology (N.Y.) 13 (7), 662–668.
Aggarwal, A., Kaur, S., Tiwary, A.K., Gupta, S., 2001. Chitosan microspheres prepared by
an aqueous process: release of indomethacin. J. Microencapsul. 18 (6), 819–823.
Aguilar, C.N., Augur, C., Favela-Torres, E., Viniegra-Gonzalez, G., 2001. Production of
tannase by Aspergillus niger Aa-20 in submerged and solid-state fermentation: in-
fluence of glucose and tannic acid. J. Ind. Microbiol. Biotechnol. 26 (5), 296–302.
Albrecht, M.T., Schiller, N.L., 2005. Alginate Lyase (AlgL) activity is required for alginate
biosynthesis in Pseudomonas aeruginosa. J. Bacteriol. 187, 3869–3872.
Alemán, A., & Martínez-Alvarez, O. (2008). Marine collagen as a source of bioactive
molecules.
Amki, T., 1981. β-mannanse of bacteria isolated from natural habitats. Bull. Jpn. Soc. Sci.
Fish. 47, 753–760.
Ananthi, S., Ramasubburayan, R., Palavesam, A., Immanuel, G., 2014. Optimisation and
purification of lipase through solid state fermentation by Bacillus cereus MSU as
isolated from the gut of a marine fish Sardinella longiceps. Int. J. Pharm. Pharm. Sci. 6
(5), 291–298.
Annamalai, N., Rajeshwari, M.V., Sahu, S.K., Balasubramanian, T., 2014a. Purification
and characterization of solvent stable, alkaline protease from Bacillus firmus CAS7 by
microbial conversion of marine wastes and molecular mechanism underlying solvent
stability. Process Biochem. 49, 1012–1019.
Annamalai, N., Rajeswari, M.V., Balasubramanian, T., 2014b. Extraction, purification and
application of thermostable and halostable alkaline protease from Bacillus al-
veayuensis CAS 5 using marine wastes. Food Bioprod. Process. 92, 335–342.
Annamalai, N., Thavasi, R., Vijayalakshmi, S., Balasubramanian, T., 2011. Extraction,
purification and characterization of thermostable, alkaline tolerant α-amylase from
Bacillus cereus. Indian J. Microbiol. 51 (4), 424–429.
Aoki, T., Araki, T., Kitamikado, M., 1990. Purification and characterization of a novel
beta-agarase from Vibrio sp. AP-2. Eur. J. Biochem. 187 (2), 461–465.
Arnos, T.C., Jorgensen, B.B., Sagemann, J., Tramdrup, T., 1998. Temperature dependence
of microbial degradation of organic matter in marine sediment: polysaccharide hy-
drolysis, oxygen consumption, and sulphate reduction. Mar. Ecol. Prog. Ser. 165, 59.
Arora, P.K., 2013. Staphylococcus lipolyticus sp. nov., a new cold-adapted lipase producing
marine species. Ann. Microbiol. 63 (3), 913–922.
Babu, J., Pramod, W.R., George, T., 2008. Cold active microbial lipases: some hot issues
and recent developments. Biotechnol. Adv. 26, 457–470.
Balakrishna, K., Swaruparani, G., Hanumalal, N., Bindu, S., Bhima, B., 2017. Plausible
exploitation of Jatropha de-oiled seed cake for lipase and phytase production and
146
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
simultaneous detoxification by Candida parapsilosis isolated from poultry garbage.
Bioresour. Technol. 225, 215–224.
Balan, S.S., Nethaji, R., Sankar, S., Jayalakshmi, S., 2012. Production of gelatinase en-
zyme from Bacillus spp. isolated from the sediment sample of Porto Novo coastal
sites. Asian Pac. J. Trop. Biomed. 2 (3).
Barbeyron, T., Potin, P., Richard, C., Collin, O., Kloareg, B., 1995. Arylsulphatase from
Alteromonas carrageenovora. Microbiology 141 (11), 2897–2904.
Basheer, S.M., Chellappan, S., Beena, P.S., Sukumaran, R.K., Elyas, K.K., Chandrasekaran,
M., 2011. Lipase from marine Aspergillus awamori BTMFW032: production, partial
purification and application in oil effluent treatment. New Biotechnol. 28 (6),
627–638.
Basso, A., Spizzo, P., Ferrario, V., Knapic, L., Savko, N., Braiuca, P., Ebert, C., Ricca, E.,
Calabro, V., Gardossi, L., 2010. Endo- and exo-inulinases: enzyme-substrate interac-
tion and rational immobilization. Biotechnol. Prog. 26 (2), 397–405.
Bayoudh, A., Gharsallah, N., Chamkha, M., Dhouib, A., Ammar, S., Nasri, M., 2000.
Purification and characterization of an alkaline protease from Pseudomonas aerugi-
nosa MN1. J. Ind. Microbiol. Biotechnol. 24, 291–295.
Beena, P.S., Soorej, M.B., Elyas, K.K., Sarita, G.B., Chandrasekaran, M., 2010. Acidophilic
tannase from marine Aspergillus awamori BTMFW032. J. Microbiol. Biotechnol. 20
(10), 1403–1414.
Beheshti Maal, K., Emtiazi, G., Nahvi, I., 2009. Production of alkaline protease by Bacillus
cereus and Bacillus polymixa in new industrial culture mediums and its immobiliza-
tion. Afr. J. Biotech. 3 (9), 491–497.
Belas, R., 1989. Sequence analysis of the agrA gene encoding beta-agarase from
Pseudomonas atlantica. J. Bacteriol. 171 (1), 602–605.
Berdy, J., 2005. Bioactive microbial metabolites. J. Antibiot. (Tokyo) 58 (1), 1–26.
Besson, S., Carneiro, C., Moura, J.J., Moura, I., Fauque, G., 1995. A cytochrome cd1-type
nitrite reductase isolated from the marine denitrifier Pseudomonas nautica 617: pur-
ification and characterization. Anaerobe 1 (4), 219–226.
Bhatia, Y., Mishra, S., Bisaria, V.S., 2002. Microbial beta-glucosidases: cloning, proper-
ties,and applications. Crit. Rev. Biotechnol. 22, 375–407.
Bhosale, H., Shaheen, U., Kadam, T., 2016. Characterization of a Hyperthermostable al-
kaline lipase from Bacillus sonorensis 4R. Enzym. Res. 2016, 11.
Boetius, A., 1995. Microbial hydrolytic enzyme activities in deep-sea sediments. Hel.
Meer 49, 177.
Bohlin, C., Praestgaard, E., Baumann, M.J., Borch, K., Praestgaard, J., Monrad, R.N.,
Westh, P., 2013. A comparative study of hydrolysis and transglycosylation activities
of fungal β-glucosidases. Appl. Microbiol. Biotechnol. 97 (1), 159–169.
Bond, M.D., Van Wart, H.E., 1984. Characterization of the individual collagenases from
Clostridium histolyticum. Biochemistry 23 (13), 3085–3091.
Boonmahome, P., Mongkol thanaruk, W., 2013. Lipase-producing bacterium and its en-
zyme characterization. J. Life Sci. Technol. 1 (4), 196–200.
Brás, N.F., Cerqueira, N.M.F.S.A., Fernandes, P.A., Ramos, M.J., 2008. Carbohydrate
binding modules from family 11: understanding the binding mode of polysaccharides.
Int. J. Quantum Chem. 108, 2030–2040.
Brown, S.H., Kelly, R.M., 1993. Characterization of amylolytic enzymes, having both
alpha- 1, 4 and alph- 1, 6 hydrolytic activity, from the thermophilic archaea pyr-
ococcus furiosus and thermococcus litorlis. Appl. Environ. Microbiol. 59, 2614–2621.
Bugli, F., Posteraro, B., Papi, M., Torelli, R., Maiorana, A., Sterbini, F., Posteraro, P.,
Sanguinetti, M., De Spirito, M., 2013. In vitro interaction between Alginate lyase
fumigatus and Amphotericin B against Aspergillus biofilm determined by different
methods. Antimicrob. Agents Chemother. 57, 1275–1282.
Bull, A.T., Ward, A.C., Goodfellow, M., 2000. Search and discovery strategies for bio-
technology: the paradigm shift. Microbiol. Mol. Biol. Rev. 64 (3), 573–606.
Burtseva, Y.V., Verigina, N.S., Sova, V.V., Pivkin, M.V., Zvyagintseva, T.N., 2003. O-
Glycosylhydrolases of marine filamentous fungi: β-1,3-glucanases of Trichoderma
aureviride. Appl. Biochem. Microbiol. 39 (5), 475–481.
Buttner, M.J., Fearnley, I.M., Bibb, M.J., 1987. The agarase gene (dagA) of Streptomyces
coelicolor A3(2): nucleotide sequence and transcriptional analysis. Mol. Gen. Genet.
209 (1), 101–109.
Carpenter, E.J., Bergman, B., Dawson, R., Siddiqui, P.J., Söderbäck, E., Capone, D.G.,
1992. Glutamine synthetase and nitrogen cycling in colonies of the marine diazo-
trophic cyanobacteria Trichodesmium spp. Appl. Environ. Microbiol. 58 (9),
3122–3129.
Casey, A., Walsh, G., 2003. Purification and characterization of extracellular phytase from
Aspergillus niger ATCC 9142. Bioresour. Technol. 86 (2), 183–188.
Cavello, I.A., Hours, R.A., Rojas, N.L., Cavalitto, S.F., 2013. Purification and character-
ization of a keratinolytic serine protease from Purpureocillium lilacinum LPS# 876.
Process Biochem. 48 (5), 972–978.
Chadd, H.E., Newman, J., Mann, N.H., Carr, N.G., 1996. Identification of iron superoxide
dismutase and a copper/zinc Superoxide dismutase enzyme activity within the
marine cyanobacterium Synechococcus sp. WH 7803. FEMS Microbiol. Lett. 138
(2–3), 161–165.
Chakraborty, S., Jana, S., Gandhi, A., Sen, K.K., Zhiang, W., Kokare, C., 2014. Gellan gum
microspheres containing a novel α-amylase from marine Nocardiopsis sp. strain B2 for
immobilization. Int. J. Biol. Macromol. 70, 292–299.
Chakraborty, S., Khopade, A., Biao, R., Jian, W., Liu, X.Y., Mahadik, K., Chopade, B.,
Zhang, L., Kokare, C., 2011. Characterization and stability studies on surfactant,
detergent and oxidant stable -amylase from marine haloalkaliphilic Saccharopolyspora
sp. A9. J. Mol. Catal. B: Enzym. 68, 52–58.
Chakraborty, S., Khopade, A., Kokare, C., Mahadika, K., Chopade, B., 2009. Isolation and
characterization of novel α-amylase from marine Streptomyces sp. D1. J. Mol. Catal. B
Enzym 58, 17–23.
Chakraborty, S., Raut, G., Khopade, A., Mahadik, K., Kokare, C., 2012. Study on calcium
ion independent α-amylase from haloalkaliphilic marine. Streptomyces Strain A3.
Chanalia, P., Gandhi, D., Jodha, D., Singh, J., 2011. Applications of microbial proteases in
A. Beygmoradi, A. Homaei
pharmaceutical industry: an over view. Rev. Med. Microb. 22 (4), 96–101.
Charles, P., Devanathan, V., Anbu, P., Ponnuswamy, M.N., Kalaichelvan, P.T., Hur, B.K.,
2008. Purification, characterization and crystallization of an extracellular alkaline
protease from Aspergillus nidulans HA-10. J. Basic Microbiol. 48 (5), 347–352.
Charoenpanich, J., Suktanarag, S., Toobbucha, N., 2011. Production of a thermostable
lipase by Aeromonas sp. EBB-1 isolated from marine sludge in Angsila, Thailand. Sci.
Asia 37, 105–114.
Chávez-González, M., Rodríguez-Durán, L.V., Balagurusamy, N., Prado-Barragán, A.,
Rodríguez, R., Contreras, J.C., Aguilar, C.N., 2012. Biotechnological advances and
challenges of tannase. Food Bioprocess Technol. 5 (2), 445–459.
Chavez Croocker, P., Sako, Y., A., U, 1999. Purification and characterization of an in-
tracellular heat-stable proteinase (pernilase) from the marine hyperthermophilic ar-
chaeon Aeropyrum pernix K1. Extremophiles 3, 3–9.
Chi, W.J., Chang, Y.K., Hong, S.K., 2012. Agar degradation by microorganisms and agar-
degrading enzymes. Appl. Microbiol. Biotechnol. 94, 917–930.
Chi, Z., Chi, Z., Zhang, T., Liu, G., Li, J., Wang, X., 2009. Production, characterization and
gene cloning of the extracellular enzymes from the marine-derived yeasts and their
potential applications. Biotechnol. Adv. 27 (3), 236–255.
Chi, Z., Ma, C., Wang, P., Li, H.F., 2007. Optimization of medium and cultivation con-
ditions for alkaline protease production by the marine yeast Aureobasidium pull-
ulans. Bioresour. Technol. 98 (3), 534–538.
Cho, H.Y., Bancerz, R., Ginalska, G., Leonowicz, A., Cho, N.S., Ohga, S., 2007. Culture
conditions of psychrotrophic fungus, Penicillium chrysogenum and its lipase char-
acteristics. J. Fac. Agric. 52 (2), 281–286.
Chung, L., Dinakarpandian, D., Yoshida, N., Lauer Fields, J.L., Fields, G.B., al., e, 2004.
Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis. Eur.
Mol. Biol. Organ. J. 23, 3020–3030.
Colonna, S., Gaggero, N., Richelmi, C., Pasta, P., 1999. Recent biotechnological devel-
opments in the use of peroxidases. Trends Biotechnol. 17, 163–168.
Cowan, D.A., Smolenski, K.A., Daniel, R.M., Morgan, H.W., 1987. An extremely ther-
mostable extracellular proteinase from a strain of the archaebacterium
Desulfurococcus growing at 88 °C. Biochem. J. 247, 121–133.
Cui, F., Dong, S., Shi, X., Zhao, X., Zhang, X.H., 2014. Overexpression and character-
ization of a novel thermostable β-agarase YM01–3, from marine bacterium
Catenovulum agarivorans YM01T. Mar. Drugs 12 (5), 2731–2747.
Cui, H., Wang, L., Yu, Y., 2015. Production and characterization of alkaline protease from
a high yielding and moderately halophilic strain of SD11 marine bacteria. J. Chem.
2015, 8.
Daboor, S.M., Budge, S.M., Ghaly, A.E., Brooks, S.L., Dave, D., 2010. Extraction and
purification of collagenase enzymes: aa critical review. Am. J. Biochem. Biotechnol. 6
(4), 239–263.
Dadshahi, Z., Homaei, A., Zeinali, F., Sajedi, R.H., Khajeh, K., 2016. Extraction and
purification of a highly thermostable alkaline caseinolytic protease from wastes
Penaeus vannamei suitable for food and detergent industries. Food Chem. 202,
110–115.
Dalmaso, G.Z., Ferreira, D., Vermelho, A.B., 2015. Marine extremophiles: a source of
hydrolases for biotechnological applications. Mar. Drugs 13 (4), 1925–1965.
Damare, S., Raghukumar, C., Raghukumar, S., 2006. Fungi in deep-sea sediments of the
Central Indian Basin. Deep Sea Res. 53 (1), 14–27.
Danson, M.J., Hough, D.W., 1998. Structure, function and stability of enzymes from the
Archaea. Trends Microbiol. 6 (8), 307–314.
David, K., 1935. Lipase production by Penicillium oxalicum and Aspergillus flavus. Int. J.
Plant Sci. 97, 2.
David, W., Michel, J., 1999. Extremozymes. Curr. Opin. Chem. Biol. 3, 39–46.
Davidson, M.H., 2006. Mechanisms for the hypotriglyceridemic effect of marine omega-3
fatty acids. Am. J. Cardiol. 98 (4A), 27i–33i.
De Souza, M.P., Yoch, D.C., 1995. Comparative physiology of dimethyl sulfide production
by dimethylsulfoniopropionate lyase in Pseudomonas doudoroffii and Alcaligenes sp.
strain M3A. Appl. Environ. Microbiol. 61 (11), 3986–3991.
Debashish, G., Malay, S., Barindra, S., Joydeep, M., 2005. Marine enzymes. Adv.
Biochem. Eng. Biotechnol. 96, 189–218.
Delattre, C., Fenoradosoa, T.A., Michaud, P., 2011. Galactans: an overview of their most
important sourcing and applications as natural polysaccharides. Braz. Arch. Biol.
Technol. 54, 1075–1092.
Devi, M.K., Banu, A.R., Gnanaprabhal, G.R., Pradeep, B.V., Palaniswamy, M., 2008.
Purification characterization of alkaline protease enzyme from native isolate
Aspergillus niger and compatibility with commercial detergent. Indian J. Sci. Technol.
1 (7), 250–259.
Dhandapani, R., Vijayaragavan, R., 1994. Production of a thermophilic, extracellular
alkaline protease by Bacillus stearothermophilus AP-4. World J. Microbiol.
Biotechnol. 10 (1), 33–35.
Dharmaraj, S., 2010. Marine Streptomyces as a novel source of bioactive substances.
World J. Microbiol. Biotechnol. 26 (12), 2123–2139.
Diaz, J.M., Rodríguez, J.A., Roussos, S., Cordova, J., Abousalham, A., Carriere, F., Baratti,
J., 2006. Lipase from the thermotolerant fungus Rhizopus homothallicus is more
thermostable when produced using solid state fermentation than liquid fermentation
procedures. Enzym. Microb. Technol. 39 (5), 1042–1050.
Dib, R., Chobert, J.M., Dalgalarrondo, M., Barbier, G., Haertle, T., 1998. Purification,
molecular properties and specificity of a thermoactive and thermostable proteinase
from Pyrococcus abyssi, strain st 549, hyperthermophilic archaea from deep-sea hy-
drothermal ecosystem. FEBS Lett. 431, 279–284.
Dixit, G., Verma, S.C., 1993. Production of alkaline proteases by Penicillium griseofulvin.
Indian J. Microbiol. 33, 257–260.
Do, H., Lee, J.H., Kwon, M.H., Song, H.E., An, J.Y., Eom, S.H., Kim, H.J., 2013.
Purification, characterization and preliminary X-ray diffraction analysis of a cold-
active lipase (CpsLip) from the psychrophilic bacterium Colwellia psychrerythraea
147
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
34H. Struct. Biol. Cryst. Commun. 69 (8), 920–924.
Doddapaneni, K.K., Tatineni, R., Vellanki, R.N., Rachcha, S., Anabrolu, N., Narakuti, V.,
Mangamoori, L.N., 2009. Purification and characterization of a solvent and de-
tergent-stable novel protease from Bacillus cereus. Microbiol. Res. 164 (4), 383–390.
Doi, R.H., 2008. Cellulases of mesophilic microorganisms: cellulosome and noncellulo-
some producers. Ann. N.Y Acad. Sci. 1125, 267–279.
Dong, J., Hong, Y., Shao, Z., Liu, Z., 2010. Molecular cloning, purification, and char-
acterization of a novel, acidic, pH-stable endoglucanase from Martelella medi-
terranea. J. Microbiol. 48 (3), 393–398.
Du-Thumm., L., Szeles, L. H., Sullivan, R. J., Masters, J. G., & Robinson, R. S. (2005).
Chewable antiplaque confectionery dental composition. US20050008582.
Dunne, W.M., Buckmire, F., 1985. Partial purification and characterization of a poly-
mannuronic acid depolymerase produced by a mucoid strain of Pseudomonas aeru-
ginosa isolated from a patient with cystic fibrosis. Appl. Environ. Microbiol. 50,
562–567.
Durham, D.R., Stewart, D.B., Stellwag, E.J., 1987. Novel alkaline- and heat-stable serine
proteases from alkalophilic Bacillus sp. strain GX6638. J. Bacteriol. 169 (6),
2762–2768.
Dutta, P.K., Dutta, J., Tripathi, V.S., 2004. Chitin and chitosan: Chemistry, properties and
applications. J. Sci. Ind. Res. 63 (1), 20–31.
El Alaoui, S.E., Diez, J., Humanes, L., Toribio, F., Partensky, F., García-Fernández, J.M.,
2001. In vivo regulation of glutamine synthetase activity in the marine chlorophyll b-
containing cyanobacterium Prochlorococcus sp. strain PCC 9511 (Oxyphotobacteria).
Appl. Environ. Microbiol. 67, 2202–2207.
Elcin, Y.M., Dixit, V., Gitnick, G., 1996. Controlled release of endothelial cell growth
factor from chitosan-albumin microspheres for localized angiogenesis: in vitro and in
vivo studies. Artif. Cells Blood Substit. Immobil. Biotechnol. 24 (3), 257–271.
Elson, C.M., Davies, D.H., Hayes, E.R., 1980. Removal of arsenic from contaminated
drinking water by a chitosan/chitin mixture. Water Res. 14 (9), 1307–1311.
Endo, A., Murakawa, S., Shimizu, H., Shiraishi, Y., 1987. Purification and properties of
collagenase from a Streptomyces Species. J. Biochem. 102, 163–170.
Ertugrul, S., Donmez, G., Takac, S., 2007. Isolation of lipase producing Bacillus sp. from
olive mill wastewater and improving its enzyme activity. J. Hazard Mater. 149 (3),
720–724.
Essghaier, B., Rouaissi, M., Boudabous, A., Jijakli, H., Sadfi-Zouaoui, N., 2010. Production
and partial characterization of chitinase from a halotolerant Planococcus rifitoensis
strain M2-26. World J. Microbiol. Biotechnol. 26 (6), 977–984.
Farag, A.M., Abd-Elnabey, H.M., Ibrahim, H.A.H., El-Shenawy, M., 2016. Purification,
characterization and antimicrobial activity of chitinase from marine-derived
Aspergillus terreus. Egypt. J. Aquat. Res. 42, 185–192.
Farhadian, S., Asoodeh, A., Lagzian, M., 2015. Purification, biochemical characterization
and structural modeling of a potential htrA-like serine protease from Bacillus subtilis
DR8806. J. Mol. Catal. B: Enzym. 115, 51–58.
Feller, G., Narinx, E., L., A.J., Zekhnini, Z., Swing, J., Gerday, C., 1994. Temperature
dependence of growth, enzyme secretion and activity of psychrophilic Antarctic
bacteria. Appl. Microbiol. Biotechnol. 41 (40), 477–479.
Fenice, M., Leuba, J., Federici, F., 1998. Chitinolytic enzyme activity of Penicillium jan-
thinellum P9 in bench-top bioreactor. J. Ferment. Bioeng. 86, 620–623.
Fernandes, P., 2014. Marine enzymes and food industry: insight on existing and potential
interactions. Front. Mar. Sci. 1.
Ferreira-Dias, S., Sandoval, G., Plou, F., Valero, F., 2013. The potential use of lipases in
the production of fatty acid derivatives for the food and nutraceutical industries.
Electron. J. Biotechnol. 16 (3), 12.
Freier, T., Montenegro, R., Shan Koh, H., Shoichet, M.S., 2005. Chitin-based tubes for
tissue engineering in the nervous system. Biomaterials 26 (22), 4624–4632.
Fu, X., Liu, P., Lin, L., Hong, Y., Huang, X., Meng, X., Liu, Z., 2010. A novel endoglucanase
(Cel9P) from a marine bacterium Paenibacillus sp. BME-14. Appl. Biochem.
Biotechnol. 160 (6), 1627–1636.
Fu, X., Yan, Q., Wang, J., Yang, S., Jiang, Z., 2016. Purification and biochemical char-
acterization of novel acidic chitinase from Paenicibacillus barengoltzii. Int. J. Biol.
Macromol. 91, 973–979.
Fu, X.T., Kim, S.M., 2010. Agarase: review of major sources, categories, purification
method, enzyme characteristics and applications. Mar. Drugs 26, 200–218.
Fujiwara, N., Masui, A., Imanaka, T., 1993. Purification and properties of the highly
thermostable alkaline protease from an alkaliphilic and thermophilic Bacillus sp. J.
Biotechnol. 30 (2), 245–256.
Fujiwara, N., Yamamoto, K., 1987. Production of alkaline protease in a low-cost medium
by alkalophilic Bacillus sp. and properties of the enzyme. J. Ferment. Technol. 65,
345–348.
Fukamizo, T., 2000. Chitinolytic enzymes: catalysis, substrate binding, and their appli-
cation. Curr. Protein Pept. Sci. 1 (1), 105–124.
Fulzele, R., DeSa, E., Yadav, A., Shouche, V., Bhadekar, R., 2011. Characterization of
novel extracellular protease produced by marine bacterial isolate from the Indian
ocean. Braz. J. Microbiol. 42, 1364–1373.
Furukawa, S.I., Fujikawa, T., Koga, D., Ide, A., 1992. Purification and some properties of
exo-type fucoidanases from Vibrio sp. N-5. Biosci. Biotech. Biochem. 56 (11),
1829–1834.
Gaber, Y., Mekasha, S., Vaaje-Kolstad, G., Eijsink, V.G., Fraaije, M.W., 2016.
Characterization of a chitinase from the cellulolytic actinomycete Thermobifida fusca.
Biochim. Et. Biophys. Acta (BBA)-Proteins Proteom. 1864 (9), 1253–1259.
Gacesa, P., 1992. Enzymic degradation of alginates. Int. J. Biochem. 24 (4), 545–552.
Gantelet, H., Duchiron, F., 1998. Purification and properties of a thermoactive and
thermostable pullulanase from Thermococcus hydrothermalis, a hyperthermophilic
archaeon isolated from a deep-sea hydrothermal vent. Appl. Microbiol. Biotechnol.
49 (6), 770–777.
Ghasemi, Y., Rasoul-Amini, S., Ebrahiminezhad, A., Kazemi, A., Shahbazi, M., Talebnia,
A. Beygmoradi, A. Homaei
N., 2011. Screening and isolation of extracellular protease producing bacteria from
the Maharloo salt lake. Iran. J. Pharm. Sci. 7, 175–180.
Goldberg, G.I., Wilhelm, S.M., Kronberger, A., Bauer, E.A., Grant, G.A., Eisen, A.Z., 1986.
Human fibroblast collagenase. Complete primary structure and homology to an on-
cogene transformation-induced rat protein. J. Biol. Chem. 261 (14), 6600–6605.
Gomez d′Ayala, G., Malinconico, M., Laurienzo, P., 2008. Marine derived polysaccharides
for biomedical applications: chemical modification approaches. Molecules 13,
2069–2106.
Goshev, I., Gousterova, A., Vasileva-Tonkova, E., Nedkov, P., 2005. Characterization of
the enzyme complexes produced by two newly isolated thermophylic actinomycete
strains during growth on collagen-rich materials. Proc. Biochem. 40, 1627–1631.
Gouda, M.K., 2006. Optimization and purification of alkaline proteases produced by
marine Bacillus sp. MIG newly isolated from eastern harbour of Alexandria. Pol. J.
Microbiol. 55, 19–126.
Goyal, K., Selvakumar, P., Hayashi, K., 2001a. Characterization of a thermostable β-
glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity. J.
Mol. Catal. B Enzym. 15, 45–53.
Goyal, K., Selvakumar, P., Hayashi, K., 2001b. Characterization of a thermostable β-
glucosidase (BglB) from Thermotoga maritima showing transglycosylation activity. J.
Mol. Catal. B Enzym. 15, 45–53.
Grace, E.S., 1997. Biotechnology in Seas and Trees. Biotechnology Unzipped: Promises
and Realities. National Academies Press, Washington, pp. 170.
Graham, C.R., David, R.W., Frank, T.R., 1980. Peptone induction and Rifampin-in-
sensitive collagenase production by Vibrio alginolyticus. J. Bacteriol. 142, 447–454.
Grenha, A., Seijo, B., Remunan-Lopez, C., 2005. Microencapsulated chitosan nano-
particles for lung protein delivery. Eur. J. Pharm. Sci. 25 (4–5), 427–437.
Guo, B., Chen, X.L., Sun, C.Y., Zhou, B.C., Zhang, Y.Z., 2009. Gene cloning, expression
and characterization of a new cold-active and salt-tolerant endobeta-1,4-xylanase
from marine Glaciecola mesophila KMM 241. Appl. Microbiol. Biotechnol. 84,
1107–1115.
Guo, B., Li, P.Y., Yue, Y.S., Zhao, H.L., Dong, S., Song, X.Y., al., e, 2013. Gene cloning,
expression and characterization of a novel xylanase from the marine bacterium,
Glaciecola mesophila KMM241. Mar. Drugs 11, 1173–1187.
Gupta, R., Gigras, P., Mohapatra, H., Goswami, V.K., Chauhan, B., 2003. Microbial α-
amylases: a biotechnological perspective. Process Biochem. 38, 1599–1616.
Haddar, A., Agrebi, R., Bougatef, A., Hmidet, N., Sellami-Kamoun, A., Nasri, M., 2009a.
Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: pur-
ification, characterization and potential application as a laundry detergent additive.
Bioresour. Technol. 100 (13), 3366–3373.
Haddar, A., Agrebi, R., Bougatef, A., Hmidet, N., Sellami-Kamoun, A., Nasri, M., 2009b.
Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: pur-
ification, characterization and potential application as a laundry detergent additive.
Bioresour. Technol. 100, 3366–3373.
Hamedi, J., Mohammadipanah, F., Ventosa, A., 2013. Systematic and biotechnological
aspects of halophilic and halotolerant actinomycetes. Extremophiles 17 (1), 1–13.
Han, W.J., Gu, J.Y., Liu, H.H., Li, F.C., Wu, Z.H., Li, Y.Z., 2013. An extra peptide within
the catalytic module of a β-agarase affects the agarose degradation pattern. J. Biol.
Chem. 288, 9519–9531.
Hardeman, F., Sara Sjoling, S., 2007. Metagenomic approach for the isolation ofa novel
low-temperature-active lipase from uncultured bacteria of marine sediment. FEMS
Microbiol. Ecol. 59, 524–534.
Harper, E., Seifter, S., Hospelhorn, V.D., 1965. Evidence for subunits in bacterial col-
lagenase. Biochem. Biophys. Res Commun. 18, 627–632.
Henrissat, B., 1991. A classification of glycosyl hydrolases based on amino acid sequence
similarities. Biochem. J. 280, 309–316.
Henrissat, B., Coutinho, P., Deleury, E., 2005. CAZy-Carbohydrate- Active Enzymes:
Polysaccharide Lyase Families. fr/_cazy/CAZY/index. Html.
Hernandez-Saavedra, N., Ochoa, J.L., 1999. Copper-zinc superoxide dismutase from the
marine yeast Debaryomyces hansenii. Yeast 15 (8), 657–668.
Hisano, T., Nishimura, M., Yonemoto, Y., Abe, S., Yamashita, T., Sakaguchi, K., Kimura,
A., Murata, K., 1993. Bacterial Alginate lyase highly active on acetylated alginates. J.
Ferment. Bioeng. 75, 332–335.
Homaei, A., 2015a. Enhanced activity and stability of papain immobilized on CNBr-ac-
tivated sepharose. Int. J. Biol. Macromol. 75, 373–377.
Homaei, A., 2015b. Purification and biochemical properties of highly efficient alkaline
phosphatase from Fenneropenaeus merguiensis brain. J. Mol. Catal. B: Enzym. 118,
16–22.
Homaei, A., Barkheh, H., Sariri, R., Stevanato, R., 2014. Immobilized papain on gold
nanorods as heterogeneous biocatalysts. Amino Acids 46 (7), 1649–1657.
Homaei, A., Etemadipour, R., 2015. Improving the activity and stability of actinidin by
immobilization on gold nanorods. Int. J. Biol. Macromol. 72, 1176–1181.
Homaei, A., Ghanbarzadeh, M., Monsef, F., 2016a. Biochemical features and kinetic
properties of α-amylases from marine organisms. Int. J. Biol. Macromol. 83, 306–314.
Homaei, A., Lavajoo, F., Sariri, R., 2016b. Development of marine biotechnology as a
resource for novel proteases and their role in modern biotechnology. Int. J. Biol.
Macromol. 88, 542–552.
Homaei, A., Saberi, D., 2015. Immobilization of α-amylase on gold nanorods: an ideal
system for starch processing. Process Biochem. 50 (9), 1394–1399.
Homaei, A., Samari, F., 2017. Investigation of activity and stability of papain by ad-
sorption on multi-wall carbon nanotubes. Int. J. Biol. Macromol.
Homaei, A., Stevanato, R., Etemadipour, R., Hemmati, R., 2017. Purification, catalytic,
kinetic and thermodynamic characteristics of a novel ficin from Ficus johannis.
Biocatal. Agric. Biotechnol. 10, 360–366.
Homaei, A.A., Mymandi, A.B., Sariri, R., Kamrani, E., Stevanato, R., Etezad, S.-M., Khajeh,
K., 2013a. Purification and characterization of a novel thermostable luciferase from
Benthosema pterotum. J. Photochem. Photobiol. B: Biol. 125, 131–136.
148
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
Homaei, A.A., Sajedi, R.H., Sariri, R., Seyfzadeh, S., Stevanato, R., 2010. Cysteine en-
hances activity and stability of immobilized papain. Amino Acids 38 (3), 937–942.
Homaei, A.A., Sariri, R., Vianello, F., Stevanato, R., 2013b. Enzyme immobilization: an
update. J. Chem. Biol. 6 (4), 185–205.
Hosoda, A., Sakai, M., Kanazawa, S., 2003. Isolation and characterization of agar-de-
grading Paenibacillus spp. associated with the rhizosphere of spinach. Biosci.
Biotechnol. Biochem. 67 (5), 1048–1055.
Hoshino, T., Kageyama, M., 1980. Purification and properties of a binding protein for
branched-chain amino acids in Pseudomonas aeruginosa. J. Bacteriol. 141 (3),
1055–1063.
Hu, Z., Lin, B.K., Xu, Y., Zhong, M.Q., Liu, G.M., 2009. Production and purification of
agarase from a marine agarolytic bacterium Agarivorans sp. HZ105. J. Appl.
Microbiol. 106, 181–190.
Huang, Y., Locy, R., Weete, J.D., 2004. Purification and characterization of an extra-
cellular lipase from Geotrichum marinum. Lipids 39 (3), 251–257.
Huber, R., Langworthy, T.A., Konig, H., Thomm, M., Woese, C.R., Sleytr, U.B., Stetter,
K.O., 1986. Thermotoga maritima sp. nov. represents a new genus of unique ex-
tremely thermophilic eubacteria growing up to 90 °C. Arch. Microbiol. 144, 324–333.
Hübner, U., Bock, U., Schügerl, K., 1993. Production of alkaline serine protease subtilisin
Carlsberg by Bacillus licheniformis on complex medium in a stirred tank reactor.
Appl. Microbiol. Biotechnol. 40, 182–188.
Ilona, K., Zdzislaw, E.S., 2007. Neutral and alkaline muscle proteases of marine fish and
invertebrates. Artic. J. Food Biochem. 20 (3), 349–364.
Jackso, N.C.R., Foreman, C.M., Sinsabaugh, R.L., 1995. Microbial enzyme activities as
indicator of organic matter processing rates in a lake Erie coastal wetland. Fresh Biol.
34, 329.
Jaeger, K.E., Eggert, T., 2002. Lipases for biotechnology. Curr. Opin. Biotechnol. 13 (4),
390–397.
Jain, D., Pancha, I., Mishra, S.K., Shrivastav, A., Mishra, S., 2012. Purification and
characterization of haloalkaline thermoactive, solvent stable and SDS-induced pro-
tease from Bacillus sp.: a potential additive for laundry detergents. Bioresour.
Technol. 115, 228–236.
Je, J.Y., Kim, S.K., 2006. Antimicrobial action of novel chitin derivative. Biochim.
Biophys. Acta 1760 (1), 104–109.
Jedrzejczak, M.F., 1999. The degradation of stranded carrion on a Baltic Sea sandy beach.
Oceanol. Stud. 3, 109.
Jenkins, D.W., Hudson, S.M., 2001. Review of vinyl graft copolymerization featuring
recent advances toward controlled radical-based reactions and illustrated with
chitin/chitosan trunk polymers. Chem. Rev. 101 (11), 3245–3273.
Jensen, R.G., 1983. Detection and determination of lipase (acylglycerol hydrolase) ac-
tivity from various sources. Lipids 18 (9), 650–657.
Ji, C., Cao, X., Yao, C., Xue, S., Xiu, Z., 2014. Protein-protein interaction network of the
marine microalga Tetraselmis subcordiformis: prediction and application for starch
metabolism analysis. J. Ind. Microbiol. Biotechnol. 41 (8), 1287–1296.
Jiang, Z., Le Bail, A., Wu, A., 2008. Effect of the thermostable xylanase B (XynB) from
Thermotoga maritima on the quality of frozen partially baked bread. J. Cereal Sci. 47,
172–179.
Jiang, Z.Q., Deng, W., Zhu, Y.P., Li, L.T., Sheng, Y.J., Hayashi, K., 2004. The recombinant
xylanase B of Thermotoga maritima is highly xylan specific and produces exclusively
xylobiose from xylans, a unique character for industrial applications. J. Mol. Catal. B
Enzym. 27, 207–213.
Jing, H., Su, W., Caracci, S., Bunning, T.G., Cooper, T., Adams, W., 1996. Optical wa-
veguiding and morphology of chitosan thin film. J. Appl. Polym. Sci. 61 (7),
1163–1171.
Joo, H.S., Choi, J.W., 2012. Purification and characterization of a novel alkaline protease
from Bacillus horikoshii. J. Microbiol. Biotechnol. 22 (1), 58–68.
Jorquera, M., Martinez, O., Maruyama, F., Marschner, P., de la Luz Mora, M., 2008.
Current and future biotechnological applications of bacterial phytases and phytase-
producing bacteria. Microb. Environ. 23 (3), 182–191.
Kamada, M., Oda, K., Murao, S., 1972. The purification of the extracellular acid protease
of Rhodotorula glutinis K-24 and its general properties. Agric. Biol. Chem. 36 (7),
1095–1101.
Kang, W., Xu, Y., Qin, L., Wang, Y., 2010. Effects of Different β-D-glycosidases on bound
aroma compounds in muscat grape determined by HS- SPME and GC-MS. J. Inst.
Brew. 116, 70–77.
Kasana, R.C., Yadav, S.K., 2007. Isolation of a psychrotrophic Exiguobacterium sp. SKPB5
(MTCC 7803) and characterization of its alkaline protease. Curr. Microbiol. 54 (3),
224–229.
Kashyap, P., Sabu, A., Pandey, A., Szakacs, G., Soccol, C.R., 2002. Extra-cellular L-glu-
taminase production by Zygosaccharomyces rouxii under solid-state fermentation.
Process Biochem. 38 (3), 307–312.
Katikala, P.K., Bobbarala, V., Tadimalla, P., Guntuku, G.S., 2009. Screening of L-gluta-
minase producing marine bacterial cultures for extracellular production of L-gluta-
minase. Int. J. ChemTech Res. 1, 1232–1235.
Kavaz, D., Odabas, S., Güven, E., Demirbilek, M., Denkbas, E., 2010. Bleomycin loaded
magnetic chitosan nanoparticles as multifunctional nanocarriers. J. Bioact. Compat.
Polym. 25 (3), 305–318.
Kempka, A.P., Lipke, N.L., da Luz Fontoura Pinheiro, T., Menoncin, S., Treichel, H.,
Freire, D.M., Di Luccio, M., de Oliveira, D., 2008. Response surface method to opti-
mize the production and characterization of lipase from Penicillium verrucosum in
solid-state fermentation. Bioprocess Biosyst. Eng. 31 (2), 119–125.
Kerkhoffs, P.L., 1981. & . Preparation of fructose. In 4277563 (Ed.), (US Patent).
Khalil Beg, Q., Gupta, R., 2003. Purification and characterization of an oxidation-stable,
thiol-dependent serine alkaline protease from Bacillus mojavensis. Enzym. Microb.
Technol. 32, 294–304.
Khambhaty, Y., Mody, K., Jha, B., 2007. Purification and characterization of k-
A. Beygmoradi, A. Homaei
carrageenase from a novel g-Proteobacterium, Pseudomonas elongata (MTCC 5261)
syn Microbulbifer elongates comb. nov. Biotechnol. Bioprocess Eng. 12, 668–675.
Khor, E., 2001. Chitin: fulfilling a biomaterials promise.
Kikani, B.A., Singh, S.P., 2012. The stability and thermodynamic parameters of a very
thermostable and calcium-independent -amylase from a newly isolated bacterium.
Anoxybacillus beppuensis TSSC-1. Process Biochem. 47, 1791–1798.
Kim, B.J., Kim, H.J., Ha, S.D., Hwang, S.H., Byun, D.S., Lee, T.H., Kong, J.Y., 1999.
Purification and characterization of -agarase from marine bacterium Bacillus cereus
ASK202. Biotechnol. Lett. 21, 1011–1015.
Kin, T., Johnson, P.R., Shapiro, A.M., Lakey, J.R., 2007. Factors influencing the col-
lagenase digestion phase of human islet isolation. Transplantation 83 (1), 7–12.
Kinsella, L.E., 1986. Food components with potential therapeutic benefits: the n-3 poly-
unsaturated fatty acids with fish oils. Food Technol. 40 (2), 89–97.
Kirimura, K., Masuda, N., Iwasaki, Y., Nakagawa, H., Kobayashi, R., Usami, S., 1999b.
Purification and characterization of a novel β-agarase from an alkalophilic bac-
terium, Alteromonas sp. E-1. J. Biosci. Bioeng. 87 (4), 436–441.
Kita, K., Ishimaru, K., Teraoka, M., Yanase, H., Kato, N., 1995. Properties of poly (3-
hydroxybutyrate) depolymerase from a marine bacterium. Alcaligenes faecalis AE122.
Appl. Environ. Microbiol. 61 (5), 1727–1730.
Klemm, D., Heublein, B., Fink, H.P., Bohn, A., 2005. Cellulose: fascinating biopolymer
and sustainable raw material. Angew. Chem. Int Ed. Engl. 44 (22), 3358–3393.
Klock, G., Kowalski, M.B., Hering, B.J., Eiden, M.E., Weidemann, A., Langer, S.,
Zimmermann, U., Federlin, K., Bretzel, R.G., 1996. Fractions from commercial col-
lagenase preparations: use in enzymic isolation of the islets of Langerhans from
porcine pancreas. Cell Transplant. 5 (5), 543–551.
Kobayashi, T., Koide, O., Mori, K., Shimamura, S., Matsuura, T., Miura, T., Takaki, Y.,
Morono, Y., Nunoura, T., Imachi, H., Inagaki, F., Takai, K., Horikoshi, K., 2008.
Phylogenetic and enzymatic diversity of deep subseafloor aerobic microorganisms in
organics- and methane-rich sediments off Shimokita Peninsula. Extremophiles 12 (4),
519–527.
Kuberan, T., Sangaralingam, S., Thirumalaiarasu, V., 2010. Isolation and optimization of
protease producing bacteria from halophilic soil. J. Biol. Sci. Res. 1, 163–174.
Kumar, C., Joo, H.S., Koo, Y.M., Paik, S., Chang, C.S., 2004. Thermostable alkaline pro-
tease from a novel marine haloalkalophilic Bacillus Clausii isolate. World J. Microbiol.
Biotechnol. 20, 351–357.
Kumar, C.G., Takagi, H., 1999. Microbial alkaline proteases: from a bioindustrial view-
point. Biotechnol. Adv. 17 (7), 561–594.
Kumar, M.N.V.R., Muzarelli, R.A.A., Muzarelli, C., Sashiwa, H., Domb, A.J., 2004.
Chitosan chemistry and pharmaceutical perspectives. Chem. Rev. 104 (12),
6017–6084.
Kumar, R., Sharma, J., Singh, R., 2007. Production of tannase from Aspergillus ruber under
solid-state fermentation using jamun (Syzygium cumini) leaves. Microbiol. Res. 162,
384–390.
Kumar, S.R., Chandrasekaran, M., 2003. Continuous production of L-glutaminase by an
immobilized marine Pseudomonas sp. BTMS-51 in a packed bed reactor. Process
Biochem. 38 (10), 1431–1436.
Kuraishi, C., Yamazaki, K., Susa, Y., 2001. Transglutaminase: its utilization in the food
industry. Food Rev. Int 17, 221–246.
Kurita, K., 2006. Chitin and chitosan: functional biopolymers from marine crustaceans.
Mar. Biotechnol. (NY) 8 (3), 203–226.
Laemmeli, U., 1970. Cleavage of structural proteins during the assemble of the head of
bacteriophage T4. Nature 227, 680–685.
Lakshmikanth, M., Manohar, S., Lalitha, J., 2009. Purification and characterization of β-
agarase from agar-liquefying soil bacterium Acinetobacter sp., AG LSL-1. Process
Biochem. 44 (9), 999–1003.
Lan, D., Qu, M., Yang, B., Wang, Y., 2016. Enhancing production of lipase MAS1 from
marine Streptomyces sp. strain in Pichia pastoris by chaperones co-expression.
Electron. J. Biotechnol. 22, 62–67.
Lario, L.D., Chaud, L., das Graças Almeida, M., Converti, A., Sette, L.D., Pessoa, A., 2015.
Production, purification, and characterization of an extracellular acid protease from
the marine Antarctic yeast Rhodotorula mucilaginosa L7. Fungal Biol. 119 (11),
1129–1136.
Lario, L.D., Malpiedi, L.P., Pereira, J.F.B., Sette, L.D., Pessoa-Junior, A., 2016. Liquid-
liquid extraction of protease from cold-adapted yeast Rhodotorula mucilaginosa L7
using biocompatible and biodegradable aqueous two-phase systems. Sep. Sci.
Technol. 51 (1), 57–67.
Laroche, M., Ulber, R., 2002. Natural Products from Marine Microorganisms.
(International Symposiumon Natural Products from Marine Microorganisms).
Greifswald, Germany.
Lee, H.S., Kwon, K.K., Kang, S.G., Cha, S.S., Kim, S.J., Lee, J.H., 2010. Approaches for
novel enzyme discovery from marine environments. Curr. Opin. Biotechnol. 21 (3),
353–357.
Lee, Y., Oh, C., De Zoysa, M., Kim, H., Wickramaarachchi, W.D., Whang, I., Lee, J., 2013.
Molecular cloning, overexpression and enzymatic characterization of glycosyl hy-
drolase family 16 β-agarase from marine bacterium Saccharophagus sp. AG21 in
Escherichia coli. J. Microbiol. Biotechnol. 23 (7), 913–922.
Lee, Y.H., Jun, S.E., Shin, H.D., 2005. Low molecular weight agarose-specific alpha-
agarase from agarolytic marine microorganism Pseudoalteromonas sp. BL-3 which
hydrolyzes alpha-1,3-glycoside bond of agar or agarose to produce agarobiose and
agarotetraose. In,vol.KR2005079035–A).
Legin, E., Ladrat, C., Godfroy, A., Barbier, G., Duchiron, F., 1997. Thermostable amylo-
lytic enzymes of thermophilic microorganisms from deep-sea hydrothermal vents.
Comptes rendus de l'Academiel′Academie des sciences Ser. 3, Sci. De. la vie 320 (11),
893–898.
Lei, X.G., Porres, J.M., 2003. Phytase enzymology, applications, and biotechnology.
Biotechnol. Lett. 25 (21), 1787–1794.
149
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
Leon, O., Quintana, L., Peruzzo, G., Slebe, J.C., 1992. Purification and properties of an
extracellular agarase from Alteromonas sp. strain C-1. Appl. Environ. Microbiol 58
(12), 4060–4063.
Li, H., Chi, Z., Duan, X., Wang, L., Sheng, J., Wu, L., 2007. Glucoamylase production by
the marine yeast Aureobasidium pullulans N13d and hydrolysis of potato starch
granules by the enzyme. Process Biochem. 42, 462–465.
Li, H.F., Chi, Z.M., Wang, X.H., Ma, C.L., 2007. Amylase production by the marine yeast
Aureobasidium pullulans N13d. J. Ocean Univ. Chin. 6, 61–66.
Li, J., Yang, J., Zhu, W.Y., He, J., Tian, X.P., Xie, Q., al., e, 2012. Nocardiopsis coralliicola
sp. nov., isolated from the gorgonian coral, Menella praelonga. Int. J. Syst. Evol.
Microbiol. 62, 1653–1658.
Li, J.W., Dong, S., Song, J., Li, C.B., Chen, X.L., Xie, B.B., Zhang, Y.Z., 2011. Purification
and characterization of a bifunctional alginate lyase from Pseudoalteromonas sp.
SM0524. Mar. Drugs 9 (1), 109–123.
Lian, Q., Li, D., Jin, Z., Wang, J., Li, A., Wang, Z., Jin, Z., 2009. Fabrication and in vitro
evaluation of calcium phosphate combined with chitosan fibers for scaffold struc-
tures. J. Bioact. Compat. Polym. 24 (1), 113–124.
Lima, C.A., Rodrigues, P.M.B., Porto, T.S., Viana, D.A., Lima Filho, J.L., Porto, A.L.F.,
Cunha, M.G.C., 2009. Production of a collagenase from Candida albicans URM362.
Biochem. Eng. J. 43, 315–320.
Lima, D.M., Fernandes, P., Nascimento, D.S., Ribeiro, R.C.L.F., de Assis, S.A.A., 2011.
Fructose syrup: a biotechnology asset. Food Technol. Biotechnol. 49, 424–434.
Lima, R.N., Porto, A.L.M., 2016. Chapter eight-recent advances in marine enzymes for
biotechnological processes. Adv. Food Nutr. Res. 78, 153–192.
Liu, J., Zhang, Z., Dang, H., Jianren Lu, J., Cui, Z., 2011a. Isolation and characterization
of a cold-active amylase from marine Wangia sp. C52. Afr. J. Microbiol. Res. 5 (10),
1156–1162.
Liu, J., Zhang, Z., Zhu, H., Dang, H., Lu, J., Cui, Z., 2011b. Isolation and characterization
of α-amylase from marine Pseudomonas sp. K6-28-040. Afr. J. Biotechnol. 10 (14),
2733–2740.
Liu, X., Huang, Z., Zhang, X., Shao, Z., Liu, Z., 2014. Cloning, expression and char-
acterization of a novel cold-active and halophilic xylanase from Zunongwangia
profunda. Extremophiles 18 (2), 441–450.
Liu, Y., Lei, Y., Zhang, Z., Gao, Y., Xiao, Y., Peng, H., 2012. Identification and phyloge-
netic characterization of a new subfamily of α-amylase enzymes from marine mi-
croorganisms. Mar. Biotechnol. 14 (3), 253–260.
Lu, W.D., Li, A.X., Guo, Q.L., 2014. Production of novel alkalitolerant and thermostable
inulinase from marine actinomycete Nocardiopsis sp. DN-K15 and inulin hydrolysis
by the enzyme. Ann. Microbiol. 64, 441–449.
Ma, C., Lu, X., Shi, C., Li, J., Gu, Y., Ma, Y., Yu, W., 2007. Molecular cloning and char-
acterization of a novel β-agarase, AgaB, from marine Pseudoalteromonas sp. CY24. J.
Biol. Chem. 282 (6), 3747–3754.
Madhumathi, K., Sudheesh Kumar, P.T., Abilash, S., Sreeja, V., Tamura, H., Manzoor, K.,
al., e, 2010. Development of novel chitin/nanosilver composite scaffolds for wound
dressing applications. J. Mater. Sci.: Mater. Med. 21 (2), 807–813.
Malathi, S., Chakraborty, R., 1991. Production of alkaline protease by a new Aspergillus
flavus isolate under solidsubstrate fermentation conditions for use as a depilation
agent. Appl. Environ. Microbiol. 57, 712–716.
Manachini, P., Fortina, M., Parini, C., 1988. Thermostable alkaline protease produced by
Bacillus thermoruber a new species of Bacillus. Appl. Microbiol. Biotechnol. 28,
409–413.
Manivasagan, P., Venkatesan, J., Kang, K.H., Sivakumar, K., Park, S.J., Kim, S.K., 2015.
Production of α-amylase for the biosynthesis of gold nanoparticles using
Streptomyces sp. MBRC-82. Int. J. Biol. Macromol. 72, 71–78.
Manivasagan, P., Venkatesan, J., Sivakumar, K., Kim, S.K., 2013. Marine actinobacterial
metabolites: current status and future perspectives. Microbiol. Res. 168 (6), 311–332.
Manivasagan, P., Venkatesan, J., Sivakumar, K., Kim, S.K., 2014. Pharmaceutically active
secondary metabolites of marine actinobacteria. Microbiol. Res. 169 (4), 262–278.
Manjit, A.Y., Aggarwal, N.K., Kumar, K., Kumar, A., 2008. Tannase production by
Aspergillus fumigatus MA under solid-state fermentation. World J. Microbiol.
Biotechnol. 24 (12), 3023–3030.
Mansouri, S., Lavigne, P., Corsi, K., Benderdour, M., Beaumont, E., Fernandes, J.C., 2004.
Chitosan-DNA nanoparticles as non-viral vectors in gene therapy: strategies to im-
prove transfection efficacy. Eur. J. Pharm. Biopharm. 57 (1), 1–8.
Mao, W., Pan, R., Freedman, D., 1992. High production of alkaline protease by Bacillus
licheniformis in a fed-batch fermentation using a synthetic medium. J. Ind. Microbiol.
11, 1–6.
Marokhazi, J., Koczan, G., Hudecz, F., Graf, L., Fodor, A., Venekei, I., 2004. Enzymic
characterization with progress curve analysis of a collagen peptidase from an en-
thomopathogenic bacterium, Photorhabdus luminescens. Biochem. J. 379 (3),
633–640.
Martin, M., Portetelle, D., Michel, G., Vandenbol, M., 2014. Microorganisms living on
macroalgae: diversity, interactions, and biotechnological applications. Appl.
Microbiol. Biotechnol. 98 (7), 2917–2935.
Maruthiaha, T., Somanathb, B., Immanuela, G., Palavesam, A., 2015. Deproteinization
potential and antioxidant property of haloalkalophilic organic solvent tolerant pro-
tease from marine Bacillus sp. APCMST-RS3 using marine shell wastes. Biotechnol.
Rep. 8, 124–132.
Matoba, S., Fukayama, J., Wing, R.A., Ogrydziak, D.M., 1988. Intracellular precursors and
secretion of alkaline extracellular protease of Yarrowia lipolytica. Mol. Cell Biol. 8
(11), 4904–4916.
Matsumoto, M., Yokouchi, H., Suzuki, N., Ohata, H., Matsunaga, T., 2003.
Saccharification of marine microalgae using marine bacteria for ethanol production.
Appl. Biochem. Biotechnol. 105–108, 247–254.
Matsushita, O., Yoshihara, K., Katayama, S., Minami, J., Okabe, A., 1994. . Purification
and characterization of Clostridium perfringens 120-kilodalton collagenase and
A. Beygmoradi, A. Homaei
nucleotide sequence of the corresponding gene. J. Bacteriol. 176 (1), 149–156.
Meenakshi, S., Umayaparvathi, S., Manivasagan, P., Arumugam, M., Balasubramanian, T.,
2013. Purification and characterization of inulinase from marine bacterium Bacillus
cereuscereus MU. Indian J. Geo-Mar. Sci. 31.
Menon, G., Mody, K., Keshri, J., Jha, B., 2010. Isolation, purification, and characteriza-
tion of haloalkaline xylanase from a marine Bacillus pumilus strain, GESF-1.
Biotechnol. Bioprocess Eng. 15 (6), 998–1005.
Mesbah, N.M., Weigel, J., 2014. Purification and biochemical characterization of halo-
philic, alkalithermophilic protease AbCP from Alkalibacillus sp. NM-Fa4. J. Mol.
Catal. B: Enzym. 105, 74–81.
Michels, P.C., Clark, D.S., 1997. Pressure enhanced activity and stability of a hy-
perthermophilic protease from a deep sea methanogen. Appl. Environ. Microbiol. 63,
3985–3991.
Minegishi, H., Shimane, Y., Echigo, A., Ohta, Y., Hatada, Y., Kamekura, M., al., e, 2013.
Thermophilic and halophilic β-agarase from a halophilic archaeon Halococcus sp.
197A. Extremophiles 17, 931–939.
Miyazaki, S., Ishii, K., Nadai, T., 1981. The use of chitin and chitosan as drug carriers.
Chem. Pharm. Bull. (Tokyo) 29 (10), 3067–3069.
Mo, S., Kim, J.H., Cho, K.W., 2009. Enzymatic properties of an extracellular phospholi-
pase C purified from a marine streptomycete. Biosci. Biotechnol. Biochem. 73 (9),
2136–2137.
Mohapatra, B.R., 1997. Properties of carboxymethylcellulase (endo-1,4-β-glucanase)
from Bacillus sp. isolated from the marine sponge (Axinella sp.). Indian J. Mar. Sci. 26,
292–296.
Mohapatra, B.R., Banerjee, U.C., Bapuji, M., 1998. Characterization of a fungal amylase
from Mucor sp. associated with the marine sponge Spirastrella sp. J. Biotechnol. 60,
113–117.
Mohebbi, G.H., Nabipour, I., Vazirizadeh, A., 2014. The sea, the future pharmacy. Iran.
South Med. J. 17 (4), 748–788.
Mollers, K.B., Cannella, D., Jorgensen, H., Frigaard, N.U., 2014. Cyanobacterial biomass
as carbohydrate and nutrient feedstock for bioethanol production by yeast fermen-
tation. Biotechnol. Biofuels 7, 64.
Mondal, K.C., Banerjee, D., Banerjee, R., Pati, B.R., 2001. Production and characterization
of tannase from Bacillus cereus KBR9. J. General. Appl. Microbiol. 47 (5), 263–267.
Mookhtiar, K.A., Steinbrink, D.R., Van Wart, H.E., 1985. Mode of hydrolysis of collagen-
like peptides by class I and class II Clostridium histolyticum collagenases: evidence
for both endopeptidase and tripeptidylcarboxypeptidase activities. Biochemistry 24
(23), 6527–6533.
Mudryk, Z.J., Podgórska, B., 2006. Enzymatic activity of bacterial strains isolated from
marine beach sediments. Pol. J. Environ. Stud. 15 (3), 441–448.
Mullaney, E.J., Daly, C.B., Kim, T., Porres, J.M., Lei, X.G., Sethumadhavan, K., Ullah,
A.H., 2002. Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at re-
sidue 300 to enhance catalysis at pH 4.0. Biochem. Biophys. Res. Commun. 297 (4),
1016–1020.
Murielle, J.A.M., Flament, D., Allouch, J., Potin, P., Thion, L., Kloareg, B., Barbeyron, T.,
2005. The endo-β-agarases AgaA and AgaB from the marine bacterium Zobellia ga-
lactanivorans: two paralogue enzymes with different molecular organizations and
catalytic behaviours. Biochem. J. 385 (3), 703–713.
Mustranta, A., Forssell, P., Poutanen, K., 1995. Comparison of lipases and phospholipases
in the hydrolysis of phospholipids. Process Biochem. 30, 393–401.
Nadeem, M., Qazi, J.I., Baij, S., Syed, Q.A., 2008. Effect of medium composition on
commercially important alkaline protease production by Bacillus licheniformis N-2.
Food Technol. Biotech. 46 (4), 388–394.
Naganuma, T., Coury, D.A.M.P.A.G., Horikoshi, K., 1993. Characterization of agarolytic
microscilla isolates and their extracellular agarases. Syst. Appl. Microbiol. 16,
183–190.
Najafi, M.F., Kembhavi, A., 2005. One step purification and characterization of an ex-
tracellular α-amylase from marine Vibrio sp. Enzym. Microb. Technol. 36 (4),
535–539.
Nelson, G., Young, W.T., 1987. Extracellular acid and alkaline protease from Candida olea.
J. General. Microbiol. 133, 1461–1469.
Ngo, D.N., Kim, M.M., Kim, S.K., 2008. Chitin oligosaccharides inhibit oxidative stress in
live cells. Carbohydr. Polym. 74, 228–234.
Niehaus, F., Bertoldo, C., Kähler, M., Antranikian, G., 1999. Extremophiles as a source of
novel enzymes for industrial application. Appl. Microbiol. Biotechnol. 51, 711–729.
Nishiyama, Y., Langan, P., Chanzy, H., 2002. Crystal structure and hydrogen-bonding
system in cellulose Ibeta from synchrotron X-ray and neutron fiber diffraction. J. Am.
Chem. Soc. 124 (31), 9074–9082.
Nordwig, A., Jahin, W.F., 1968. A collagenolytic enzyme from aspergillus oryzae pur-
ification and properties. Eur. J. Biochem. 3, 519–529.
Noureddini, H., Dang, J., 2009. Degradation of phytates in distillers' grains and corn
gluten feed by Aspergillus niger phytase. Appl. Biochem. Biotechnol. 159 (1), 11–23.
Ohta, Y., Hatada, Y., 2006. A novel enzyme, lambda-carrageenase, isolated from a deep-
sea bacterium. J. Biochem. 140 (4), 475–481.
Oren, A., 2004. Prokaryote diversity and taxonomy: current status and future challenges.
Philos. Trans. R. Soc. Lond. B Biol. Sci. 359 (1444), 623–638.
Osama, R., Koga, T., 1995. An investigation of aquatic bacteria capable of utilizing chitin
as the sole source of nutrients. Lett. Appl. Microbiol. 21, 288–291.
Palanisami, S., Kannan, K., Lakshmanan, U., 2011. Tannase activity from the marine
bacterium Phormidium valderium BDU 140441. J. Appl. Phycol.
Pallavi, P., Chandra, S.J., Reddy, V.K., Reddy, S.R., 2014. Optimization of cultural
parameters for lipase production by Bacillus subtilis Y-IVI. Int. J. Curr. Microbiol.
Appl. Sci. 3 (12), 194–200.
Pandey, A., Szakacs, G., Soccol, C.R., Rodriguez-Leon, J.A., Soccol, V.T., 2001.
Production, purification and properties of microbial phytases. Bioresour. Technol. 77
(3), 203–214.
150
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
Parro, V., Mellado, R.P., 1994. Effect of glucose on agarase overproduction by
Streptomyces. Gene 145 (1), 49–55.
Patnala, H.S., Kabilan, U., Gopalakrishnan, L., Rao, R.M., Kumar, D.S., 2016. Marine
fungal and bacterial isolates for lipase production: a comparative study. Adv. Food
Nutr. Res 78, 71–94.
Petrova, D., Derekova, A., Vlahov, S., 2006. Purification and properties of individual
collagenases from Streptomyces sp. strain 3B. Folia Microbiol. (Praha) 51 (2), 93–98.
PO, Remba, K., 1995. Hydrolytic enzymatic activity in deep-sea sediments. FEMS Microb.
Ecol. 16, 213.
Potin, P., Richard, C., Rochas, C., Kloareg, B., 1993. Purification and characterization of
the α-agarase from Alteromonas agarlyticus (Cataldi) comb. nov., strain GJ1B. Eur. J.
Biochem. 214, 599–607.
Potin, P., Sanseau, A., Le Gall, Y., Rochas, C., Kloareg, B., 1991. Purification and char-
acterization of a new kappacarrageenase from a marine Cytophaga-like bacterium.
Eur. J. Biochem. 201, 241–247.
Raghukumar, C., D’Souza, T.M., Thorn, R.G., Reddy, C.A., 1999. Lignin modifying en-
zymes of Flavodon flavus, a basidiomycete isolated from a coastal marine environ-
ment. Appl. Environ. Microbiol. 65, 2103–2111.
Raghukumar, C., Muraleedharan, U., Gaud, V.R., Mishra, R., 2004. Xylanases of marine
fungi of potential use for biobleaching of paper pulp. J. Ind. Microbiol. Biotechnol. 31
(9), 433–441.
Rahman, R.N.Z.A., Razak, C.N., Ampon, K., Basri, M., Yunus, W.M.Z.W., Salleh, A.B.,
1994. Purification and characterization of a heat-stable alkaline protease from
Bacillus stearothermophilus F1. Appl. Microbiol. Biotechnol. 40, 822–827.
Ramakrishnan, V., Goveas, L.C., Suralikerimath, N., Jampani, C., Halami, P.M., Narayan,
B., 2016. Extraction and purification of lipase from Enterococcus faecium MTCC5695
by PEG/phosphate aqueous-two phase system (ATPS) and its biochemical char-
acterization. Biocatal. Agric. Biotechnol. 6, 19–27.
Ramani, K., Saranya, P., Jain, S.C., Sekaran, G., 2013. Lipase from marine strain using
cooked sunflower oil waste: production optimization and application for hydrolysis
and thermodynamic studies. Bioprocess Biosyst. Eng. 36 (3), 301–315.
Ramos, K.R.M., Valdehuesa, K.N.G., Cabulong, R.B., Moron, L.S., Nisola, G.M., Hong, S.K.,
Chung, W.J., 2016. Overexpression and secretion of AgaA7 from Pseudoalteromonas
hodoensis sp. nov in Bacillus subtilis for the depolymerization of agarose. Enzym.
Microb. Technol. 90, 19–25.
Rasmussen, R.S., Morrissey, M.T., 2007. Marine biotechnology for production of food
ingredients. Adv. Food Nutr. Res. 52, 237–292.
Rattray, F.P., Bockelmann, W., Fox, P.F., 1994. Purification and characterization of an
extracellular proteinase from Brevibacterium linens ATCC 9174. Appl. Environ.
Microbiol. 61, 3454–3456.
Raval, V.H., Pillai, S., Rawal, C.M., Singh, S.P., 2014. Biochemical and structural char-
acterization of a detergent-stable serine alkaline protease from seawater haloalk-
aliphilic bacteria. Process Biochem. 49 (6), 955–962.
Renge, V.C., Khedkar, S.V., Nandurkar, N.R., 2012. Enzyme synthesis by fermentation
method. Sci. Rev. Chem. Commun. 2, 585–590.
Renner, M.J., Breznak, J.A., 1998. Purification and properties of ArfI, an alpha-L-arabi-
nofuranosidase from Cytophaga xylanolytica. Appl. Environ. Microbiol. 64 (1),
43–52.
Ricca, E., Calabro, V., Curcio, S., Iorio, G., 2007. The state of the art in the production of
fructose from inulin enzymatic hydrolysis. Crit. Rev. Biotechnol. 27 (3), 129–145.
Roberts, J.N., Christopher, B.B., Cynthia, D.T., Rhonda, K., Marcelino, B., Peter, L.C.,
Douglas, R.L., John, T., 2007. Genital transmission of HPV in a mouse model is po-
tentiated by nonoxynol-9 and inhibited by carrageenan. Nat. Med. 13, 857–861.
Roberts, R.L., Cabib, E., 1982. Serratia marcescens chitinase: one-step purification and
use for the determination of chitin. Anal. Biochem. 127, 402–412.
Rochima, E., Sekar, N., Buwono, I.D., Afrianto, E., Pratama, R.I., 2016. Isolation and
Characterization of Collagenase from Bacillus subtilis (Ehrenberg, 1835); ATCC 6633
for Degrading Fish Skin Collagen Waste from Cirata Reservoir.
Roseline, T.L., Sachindra, N.M., 2016. Characterization of extracellular agarase produc-
tion by Acinetobacter junii PS12B, isolated from marine sediments. Biocatal. Agric.
Biotechnology 6, 219–226.
Rouzbahan, S., Moein, S., Homaei, A., 2016. Total antioxidant capacities and reduction of
ferric ions by extracts of three medicinal plants and their fractions. Bimon. J.
Hormozgan Univ. Med. Sci. 20 (4), 245–254.
Rouzbehan, S., Moein, S., Homaei, A., Moein, M.R., 2017. Kinetics of α-glucosidase in-
hibition by different fractions of three species of Labiatae extracts: a new diabetes
treatment model. Pharm. Biol. 55 (1), 1483–1488.
Sabu, A., Keerthi, T.R., Kumar, S.R., Chandrasekaran, M., 2000. L-Glutaminase produc-
tion by marine Beauveria sp. under solid state fermentation. Process Biochem. 35,
705–710.
Sabu, A., Pandey, A., Daud, M.J., G, S, 2005. Tamarind seed powder and palm kernel
cake: two novel agro residues for the production of tannase under solid state fer-
mentation by Aspergillus niger ATCC 16620. Bioresour. Technol. 96 (11), 1223–1228.
Sadati, R., Barghi, A., 2014. Urmia hypersaline lake: a potential source of actinomycets
possessing. Iran. J. Public Health 43 (2), 149.
Santorelli, M., Maurelli, L., Pocsfalvi, G., Fiume, I., Squillaci, G., La Cara, F., del Monaco,
G., Morana, A., 2016. Isolation and characterisation of a novel alpha-amylase from
the extreme haloarchaeon Haloterrigena turkmenica. Int. J. Biol. Macromol. 92,
174–184.
Sapelli, P.L., Baldassarre, V., Muzzarelli, R.A.A., Emanuelli, M., 1986. Chitosan in den-
tistry. In: Muzzarelli, R., Jeuniaux, G., Gooday, G.W. (Eds.), Chitin in Nature and
Technology. Springer, US, pp. 507–512.
Sarethy, I.P., Saxena, Y., Kapoor, A., Sharma, M., Sharma, S.K., Gupta, V., Gupta, S., 2011.
Alkaliphilic bacteria: applications in industrial biotechnology. J. Ind. Microbiol.
Biotechnol. 38 (7), 769–790.
Sarwar, G., Matayoshi, S., Oda, H., 1987a. Purification of a kappa-carrageenase from
A. Beygmoradi, A. Homaei
marine Cytophaga species. Microbiol. Immunol. 31 (9), 869–877.
Sarwar, G., Matoyoshi, S., Oda, H., 1987b. Purification of a α-carrageenan from marine
Cytophaga species. Microbiol. Immunol. 31, 869–877.
Sathishkumar, R., Ananthan, G., Iyappan, K., Stalin, C., 2015. A statistical approach for
optimization of alkaline lipase production by ascidian associated—Halobacillus true-
peri RSK CAS9. Biotechnol. Rep. 8, 64–71.
Sawabe, T., Ohtsuka, M., Ezura, Y., 1997. Novel alginate lyases from marine bacterium
Alteromonas sp. strain H-4. Carbohydr. Res. 304, 69–76.
Sawant, R., S, N, 2014. Protease: an enzyme with multiple industrial applications. World
J. Pharm. Pharm. Sci. 3 (6), 568–579.
Saxena, R.K., Ghosh, P.K., Gupta, R., Davidson, W.S., Bradoo, S., Gulati, R., 1999.
Microbial lipases: potential biocatalysts for the future industry. Curr. Sci. 77 (1),
101–115.
Sayali, K., Sadichha, P., Surekha, S., 2013. Microbial esterases. Int. J. Curr. Microbiol.
Appl. Sci. 2 (7), 135–146.
Sen, S.K., Jana, A., Bandyopadhyay, P., Das Mohapatra, P.K., Raut, S., 2016.
Thermostable amylase production from hot spring isolate Exiguobacterium sp: a
promising agent for natural detergents. Sustain. Chem. Pharm. 3, 59–68.
Seo, Y.B., Lu, Y., Chi, W.J., Park, H.R., Jeong, K.J., Hong, S.K., Chang, Y.K., 2014.
Heterologous expression of a newly screened -agarase from Alteromonas sp. GNUM1
in Escherichia coli and its application for agarose degradation. Process Biochem. 49,
430–436.
Seol, Y.J., Lee, J.Y., Park, Y.J., Lee, Y.M., Young, K., Rhyu, I.C., Lee, S.J., Han, S.B.,
Chung, C.P., 2004. Chitosan sponges as tissue engineering scaffolds for bone for-
mation. Biotechnol. Lett. 26 (13), 1037–1041.
Shahidi, F., JanakKamil, Y.V.A., 2001. Enzymes from fish and aquatic invertebrates and
their application in the food industry. Trends Food Sci. Technol. 12, 435–464.
Shanmughapriya, S., Kiran, G.S., Selvin, J., Thomas, T.A., Rani, C., 2010. Optimization,
purification, and characterization of extracellular mesophilic alkaline cellulase from
sponge-associated Marinobacter sp. MSI032. Appl. Biochem. Biotechnol. 162 (3),
625–640.
Sharifian, S., Homaei, A., Hemmati, R., Khajeh, K., 2017. Light emission miracle in the sea
and preeminent applications of bioluminescence in recent new biotechnology. J.
Photochem. Photobiol. B: Biol. 172, 115–128.
Sharma, S., Agarwal, L., Saxena, R.K., 2008. Purification, immobilization and char-
acterization of tannase from Penicillium variable. Bioresour. Technol. 99, 2544–2551.
Shimogaki, H., Takeuchi, K., Nishino, T., Ohdera, M., Kudo, T., Ohba, K., Iwama, M., Irie,
M., 1991. Purification and properties of a novel surface-active agent- and alkaline-
resistant protease from Bacillus sp. Y. Agric. Biol. Chem. 55 (9), 2251–2258.
Shuai, Y., Zhang, T., Jiang, B., Mu, W., 2010. Development of efficient enzymatic pro-
duction of theanine by gamma-glutamyltranspeptidase from a newly isolated strain of
Bacillus subtilis, SK11.004. J. Sci. Food Agric. 90 (15), 2563–2567.
Simpson, H., Denis, M., Malatesta, F., 1997. The terminal oxidase in the marine bacterium
Pseudomonas nautica 617. Biosci. Rep. 17 (3), 343–346.
Song, Q., Wang, Y., Yin, C., H., Z.X., Laa, A., 2016. A novel high-active alkalophilic alpha-
amylase from deep-sea bacterium Luteimonas abyssi XH031. Enzym. Microb.
Technol. 90, 83–92.
Song, Q., Zhang, X., 2008. Characterization of a novel non-specific nuclease from ther-
mophilic bacteriophage GBSV1. BMC Biotechnol. 8, 43.
Songsiriritthigul, C., Buranabanyat, B., Haltrich, D., Yamabhai, M., 2010. Efficient re-
combinant expression and secretion of a thermostable GH26 mannan endo-1,4-beta-
mannosidase from Bacillus licheniformis in Escherichia coli. Microb. Cell Fact. 9, 20.
Sowell, S.M., Norbeck, A.D., Lipton, M.S., Nicora, C.D., Callister, S.J., Smith, R.D.,
Barofsky, D.F., Giovannoni, S.J., 2008. Proteomic analysis of stationary phase in the
marine bacterium "Candidatus Pelagibacter ubique". Appl. Environ. Microbiol. 74
(13), 4091–4100.
Spök, A., 2006. Safety regulations of food enzymes. Food Technol. Biotechnol. 44,
197–209.
Stach, J.E., Maldonado, L.A., Ward, A.C., Goodfellow, M., Bull, A.T., 2003. New primers
for the class Actinobacteria: application to marine and terrestrial environments.
Environ. Microbiol. 5 (10), 828–841.
Stickforth, P., Steiger, S., Hess, W.R., Sandmann, G., 2003. A novel type of lycopene ε-
cyclase in the marine cyanobacterium Prochlorococcus marinus MED4. Arch.
Microbiol. 179 (6), 409–415.
Strom, T., Raa, J., 1993. Marine biotechnology in Norway. J. Mar. Biotechnol. 1, 3–7.
Subramani, R., Aalbersberg, W., 2012. Marine actinomycetes: an ongoing source of novel
bioactive metabolites. Microbiol. Res. 167 (10), 571–580.
Sugano, Y., Matsumoto, T., Kodama, H., Noma, M., 1993a. Cloning and sequencing of
agaA, a unique agarase 0107 gene from a marine bacterium, Vibrio sp. strain JT0107.
Appl. Environ. Microbiol. 59 (11), 3750–3756.
Sugano, Y., Terada, I., Arita, M., Noma, M., Matsumoto, T., 1993b. Purification and
characterization of a new agarase from a marine bacterium, Vibrio sp. strain JT0107.
Appl. Environ. Microbiol. 59 (5), 1549–1554.
Sukharnikov, L.O., Cantwell, B.J., Podar, M., Zhulin, I.B., 2011. Cellulases: ambiguous
nonhomologous enzymes in a genomic perspective. Trends Biotechnol. 29, 473–479.
Suolow, T.V., Jones, J., 1988. Chitinase-producing bacteria. In US Patent.
Suzuki, H., Sawai, Y., Suzuki, T., Kawai, K., 2003. Purification and characterization of an
extracellular beta-agarase from Bacillus sp. MK03. J. Biosci. Bioeng. 95 (4), 328–334.
Takii, Y., Kuriyama, N., Suzuki, Y., 1990. Alkaline serine protease produced from citric
acid by Bacillus alcalophilus subsp. halodurans KP 1239. Appl. Microbiol. Biotechnol.
34 (1), 57–62.
Tong, C.C., Cole, A.L., Shepherd, M.G., 1980. Purification and properties of the cellulases
from the thermophilic fungus Thermoascus aurantiacus. Biochem. J. 191 (1), 83–94.
Trachoo, N., Mistry, V.V., 1998. Application of ultrafiltered sweet buttermilk and sweet
buttermilk powder in the manufacture of nonfat and low fat yogurts. J. Dairy Sci. 81,
3163–3171.
151
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
Tramice, A., Pagnotta, E., Romano, I., Gambacorta, A., Trincone, A., 2007.
Transglycosylation reactions using glycosyl hydrolases from Thermotoga neapolitana,
a marine hydrogen-producing bacterium. J. Mol. Catal. B Enzym. 47, 21–27.
Trincone, A., 2011. Marine biocatalysts: enzymatic features and applications. Mar. Drugs
9 (4), 478–499.
Trincone, A., 2013. Angling for uniqueness in enzymatic preparation of glycosides.
Biomolecules 3 (2), 334–350.
Tsuchiya, K., Nakamura, Y., Sakashita, H., Kimura, T., 1992. Purification and char-
acterization of a thermostable alkaline protease from alkalophilic
Thermoactinomyces sp. HS682. Biosci. Biotechnol. Biochem. 56 (2), 246–250.
Tsugawa, W., Horiuchi, S., Tanaka, M., Wake, H., Sode, K., 1996. Purification of a marine
bacterial glucose dehydrogenase from Cytophaga marinoflava and its application for
measurement of 1,5-anhydro-d-glucitol. Appl. Biochem. Biotechnol. 56 (3), 301–310.
Tsugawa, W., Ogasawara, N., Sode, K., 1998. Fluorescent measurement of 1, 5-anhydro-
D-glucitol based on a novel marine bacterial glucose dehydrogenase. Enzym. Microb.
Technol. 22 (4), 269–274.
Tsujibo, H., Yoshida, Y., Miyamoto, K., Imada, C., Okami, Y., Inamori, Y., 1992.
Purification, properties, and partial amino acid sequence of chitinase from a marine
Alteromonas sp. strain O-7. Can. J. Microbiol. 38, 891–897.
Turkiewicz, M., Gromek, E., Kalinowska, H., Zielińska, M., 1999. Biosynthesis and
properties of an extracellular metalloprotease from the Antarctic marine bacterium
Sphingomonas paucimobilis. J. Biotechnol. 70, 53–60.
Turkiewicz, M., Kur, J., Białkowska, A., Cieśliński, H., Kalinowska, H., Bielecki, S., 2003.
Antarctic marine bacterium Pseudoalteromonas sp. 22b as a source of cold-adapted β-
galactosidase. Biomol. Eng. 20, 317–324.
Turner, P., Svensson, D., Adlercreutz, P., Karlsson, E.N., 2007. A novel variant of
Thermotoga neapolitana beta-glucosidase B is an efficient catalyst for the synthesis of
alkyl glucosides by transglycosylation. J. Biotechnol. 130 (1), 67–74.
Unanue, M., Ayo, B., Agis, M., Slezak, D., Herndl, G.J., Iriberri, J., 1999. Ectoenzymatic
activity and uptake of monomers in marine bacterioplankton described by a biphasic
kinetic model. Microb. Ecol. 37 (1), 36–48.
Vaidya, S.Y., Vala, A.K., Dube, H.C., 2001. Bactrial indicators of fecal pollution at
Bhavnagar coast. Indian J. Microb. 41, 37–39.
Van de Lagemaat, J., Pyle, D.L., 2006. Tannase. Enzyme Technology. Springer, New York.
Vats, P., Bhushan, B., Banerjee, U.C., 2009. Studies on the dephosphorylation of phytic
acid in livestock feed using phytase from Aspergillus niger van Teighem. Bioresour.
Technol. 100 (1), 287–291.
Venugopal, V., 2016. Enzymes from seafood processing waste and their applications in
seafood processing. Adv. Food Nutr. Res. 78, 47–69.
Vieille, C., Zeikus, G.J., 2001. Hyperthermophilic enzymes: sources, uses, and molecular
mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65 (1), 1–43.
Vijayaraghavan, P., Kalaiyarasi, M., Vincent, S.G.P., 2015. Cow dung is an ideal fer-
mentation medium for amylase production in solid-state fermentation by Bacillus
cereus. J. Genet. Eng. Biotechnol. 13 (2), 111–117.
Vijayaraghavan, R., Rajendran, S., 2012. Identification of a novel agarolytic gamma
-Proteobacterium microbulbifer maritimus and characterization of its agarase. J.
Basic Microbiol. 52 (6), 705–712.
Vishwanatha, K.S., Appu-Rao, A.G., Singh, S.A., 2009. Characterization of acid protease
expressed from Aspergillus oryzae MTCC 5341. Food Chem. 114, 402–407.
Vyas, S., Chhabra, M., 2017. Isolation, identification and characterization of
Cystobasidium oligophagum JRC1: a cellulase and lipase producing oleaginous yeast.
Bioresour. Technol. 223, 250–258.
Wang, J., Xu, A., Wan, Y., Li, Q., 2013. Purification and characterization of a new metallo-
neutral protease for beer brewing from Bacillus amyloliquefaciens SYB-001. Appl.
Biochem. Biotechnol. 170, 2021–2033.
Wang, X., Zhao, Y., Tan, H., Chi, N., Zhang, Q., Du, Y., Yin, H., 2014. Characterisation of a
chitinase from Pseudoalteromonas sp. DL-6, a marine psychrophilic bacterium. Int. J.
Biol. Macromol. 70, 455–462.
Wang, X.H., Li, D.P., Wang, W.J., Feng, Q.L., Cui, F.Z., Xu, Y.X., Song, X.H., van der Werf,
M., 2003. Crosslinked collagen/chitosan matrix for artificial livers. Biomaterials 24
(19), 3213–3220.
Wang, Y., Zhang, C., Li, J., Xu, Y., 2013. Different influences of beta-glucosidases on
volatile compounds and anthocyanins of Cabernet Gernischt and possible reason.
Food Chem. 140 (1–2), 245–254.
Wei, X.H., Niu, Y.P., Xu, Y.Y., Du, Y.Z., Hu, F.Q., Yuan, H., 2010. Salicylic acid-grafted
chitosan oligosaccharide nanoparticle for paclitaxel delivery. J. Bioact. Compat.
Polym. 25 (3), 319–335.
Wells, W., 1999. Extreme chemistry. AB/BA/1297xtremo.html accessed.
Weltrowski, M., Martel, B., Morcellent, M., 1996. Chitosan N-benzyl sulfonate derivatives
as sorbents for removal of metal ions in an acidic medium. J. Appl. Polym. Sci. 59 (4),
647–654.
Willi, P., Sharma, P., 2004. Chitosan and alginate wound dressings. Trends Biomater.
Artif. Organs 18 (1), 18–23.
Wong, T.Y., Preston, L.A., Schiller, N.L., 2000. Alginate lyase: review of major sources and
enzyme characteristics, structure-function analysis, biological roles, and applications.
Ann. Rev. Microbiol. 54, 289–340.
Wu, C., Xu, C., Ni, H., Yang, Q., Cai, H., Xiao, A., 2016. Preparation and characterization
of tannase immobilized onto carboxylfunctionalized superparamagnetic ferroferric
oxide nanoparticles. Bioresour. Technol. 205, 67–74.
Wu, G., Qin, Y., Cheng, Q., Liu, Z., 2014a. Characterization of a novel alkalistable and
salt-tolerant α-amylasefrom marine bacterium Zunongwangia profunda. J. Mol. Catal.
B: Enzym. 110, 8–15.
Wu, G., Yuan, M., Wei, L., Zhang, Y., Lin, Y., Zhang, L., al., e, 2014b. Characterization of a
novel cold-adapted phosphinothricin N-acetyltransferase from the marine bacterium
Rhodococcus sp. strain YM12. J. Mol. Catal. B: Enzym. 104, 23–28.
Wu, Q., Ma, S., Xiao, H., Zhang, M., Cai, J., 2011. Purification and the secondary structure
A. Beygmoradi, A. Homaei
of Fucoidanase from Fusarium sp. LD8. Evid.-Based Complement. Altern. Med.
2011, 8.
Wu, S.J., Chen, J., 2014. Preparation of maltotriose from fermentation broth by hydro-
lysis of pullulan using pullulanase. Carbohydr. Polym. 107, 94–97.
Xia, W., Liu, P., Liu, J., 2008. Advance in chitosan hydrolysis by non-specific cellulases.
Bioresour. Technol. 15, 6751–6762.
Xie, W., Lin, B., Zhou, Z., Lu, G., Lun, J., Xia, C., Li, S., Hu, Z., 2013. Characterization of a
novel beta-agarase from an agar-degrading bacterium Catenovulum sp. X3. Appl.
Microbiol Biotechnol. 97, 4907–4915.
Xiong, A.S., Yao, Q.H., Peng, R.H., Li, X., Fan, H.Q., Guo, M.J., Zhang, S.L., 2004.
Isolation, characterization, and molecular cloning of the cDNA encoding a novel
phytase from Aspergillus niger 113 and high expression in Pichia pastoris. J.
Biochem. Mol. Biol. 37 (3), 282–291.
Xu, J.L., Lu, M.S., Wang, S.J., Li, H.Z., Sun, Y.Y., Fang, Y.W., 2009. Production and
characterization of pullulanase from hyperthermophilic archaeon Thermococcus sp.
HJ21. J. Food Sci. Biotechnol. 2, 243–249.
Yadav, R.P., Saxena, R.K., Gupta, R., Davidson, W.S., 1998. Purification and character-
ization of a regiospecific lipase from Aspergillus terreus. Biotechnol. Appl. Biochem.
28 (Pt 3), 243–249.
Yahata, N., Watanabe, T., Nakamura, Y., Yamamoto, Y., Kamimiya, S., Tanaka, H., 1990.
Structure of the gene encoding beta-1,3-glucanase A1 of Bacillus circulans WL-12.
Gene 86 (1), 113–117.
Yamane, S., Iwasaki, N., Majima, T., Funakoshi, T., Masuko, T., Harada, K., Minami, A.,
Monde, K., Nishimura, S., 2005. Feasibility of chitosan-based hyaluronic acid hybrid
biomaterial for a novel scaffold in cartilage tissue engineering. Biomaterials 26 (6),
611–619.
Yamasaki, M., Moriwaki, S., Miyake, O., Hashimoto, W., Murata, K., Mikami, B., 2004.
Structure and function of a hypothetical Pseudomonas aeruginosa protein PA1167
classified into family PL-7: a novel alginate lyase with a beta-sandwich fold. J. Biol.
152
Biocatalysis and Agricultural Biotechnology 11 (2017) 131–152
Chem. 279 (30), 31863–31872.
Yang, J.S., Xie, Y.J., He, W., 2011. Research progress on chemical modification of algi-
nate: a review. Carbohydr. Polym. 84, 33–39.
Yang, Q., Yang, M., Pritsch, K., Yediler, A., Hagn, A., Schloter, M., Kettrup, A., 2003.
Decolorization of synthetic dyes and production of manganese-dependent peroxidase
by new fungal isolates. Biotechnol. Lett. 25 (9), 709–713.
Yang, S., Fu, X., Yan, Q., Jiang, Z., Wang, J., 2016. Biochemical characterization of a
novel acidic exochitinase from Rhizomucor miehei with antifungal activity. J. Agric.
Food Chem. 64, 461–469.
Yaphe, W., Morgan, K., 1959. Enzymic hydrolysis of fucoidin by Pseudomonas atlantica
and Pseudomonas carrageenovora. Nature 183 (4663), 761–762.
Yin, L.J., Lin, H.H., Chiang, Y.I., Jiang, S.T., 2010. Bioproperties and purification of xy-
lanase from Bacillus sp. YJ6. J. Agric. Food Chem. 58 (1), 557–562.
Zeinali, F., Homaei, A., Kamrani, E., 2015. Sources of marine superoxide dismutases:
characteristics and applications. Int. J. Biol. Macromol. 79, 627–637.
Zhang, C., Kim, S., 2008. Research and application of marine microbial enzymes: status
and prospects. Mar. Drugs 8 (6), 1920–1934.
Zhang, C., Kim, S.K., 2010. Research and application of marine microbial enzymes: status
and prospects. Mar. Drugs 8 (6), 1920–1934.
Zhang, G.Q., Dong, X.F., Wang, Z.H., Zhang, Q., Wang, H.X., Tong, J.M., 2010.
Purification, characterization, and cloning of a novel phytase with low pH optimum
and strong proteolysis resistance from Aspergillus ficuum NTG-23. Bioresour. Technol.
101 (11), 4125–4131.
Zhang, Z., Marquardt, R.R., Wang, G., Guenter, W., Crow, G.H., Han, Z., Bedford, M.R.,
1996. A simple model for predicting the response of chicks to dietary enzyme sup-
plementation. J. Anim. Sci. 74 (2), 394–402.
Zhao, K., Guo, L.Z., Lu, W.D., 2012. Extracellular production of novel halotolerant,
thermostable, and alkali-stable carboxymethyl cellulase by marine bacterium
Marinimicrobium sp. LS-A18. Appl. Biochem. Biotechnol. 168 (3), 550–567.