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Antioxidant, angiotensin-converting enzyme inhibitory activity and other

functional properties of egg white proteins and their derived peptides – A


review

E. D. N. S. Abeyrathne,∗ X. Huang,†,‡,1 and D. U. Ahn‡



Department of Animal Science, Uva Wellassa University, Badulla 90000, Sri Lanka; † College of Food Science &
Technology, Huazhong Agricultural University, Egg Processing Technology Local Joint National Engineering
Research Center, National R&D Center for Egg Processing, Wuhan, Hubei 430070, China; and ‡ Department of
Animal Science, Iowa State University, Ames, IA 50010, USA

ABSTRACT Egg white contains many functionally food processing while other properties such as ACE-
important proteins: ovalbumin (54%), ovotransferrin inhibitory activity of the peptides can have important
(12%), ovomucoid (11%), ovoglobulin (G2 and G3, 8%), health-related functionalities. Bioactive peptides can
ovomucin (3.5%), and lysozyme (3.5%) are major pro- be produced from egg white proteins by enzyme hy-
teins, while ovoinhibitors, ovomacroglobulin, ovogly- drolysis, chemical treatments, or thermal treatments at
coprotein, ovoflavoprotein, thiamine-binding proteins, different pH conditions. The effective functional pep-
and avidin are minor proteins present in egg white. tides produced from egg white proteins are usually
These proteins, as well as the peptides derived from the smaller than 2 kDa in molecular size. However, these
proteins, have been recognized for their functional im- peptides are known for their beneficial activities in
portance as antioxidant, antimicrobial, metal-chelating, vitro only, and little work has been done to prove
anti-viral, anti-tumour, and angiotensin-converting en- their beneficial effects in vivo. Therefore, further stud-
zyme (ACE)-inhibitory activities. Among the func- ies are needed to see if the bioactive peptides derived
tional properties of the peptides, antioxidant and an- from egg white proteins are helpful for humans in the
timicrobial activities are important characteristics for future.
Key words: egg white proteins, functional peptides, antioxidant, angiotensin-converting enzyme inhibitory
activity

2018 Poultry Science 0:1–7


http://dx.doi.org/10.3382/ps/pex399

INTRODUCTION Among these functional properties, antioxidant ca-


pacity is an important characteristic for food process-
Chicken egg consists of three main components, in- ing. The production of reactive oxygen species (ROS)
cluding egg white (56%), yolk (33%), and shell (11%). and free radicals is an essential part of the biological
Egg white is the major component of egg and con- processes that are involved in energy production in all
sists of 88% water and 12% solids, of which over living organisms. However, the ROS can also enter our
90% is protein. Ovalbumin, ovotransferrin, and ovo- body through the ingestion of foods and from the en-
mucoid are considered as the major, while ovomucin, vironment. Oxidative damage by free radicals may be
lysozyme, ovoglobulins, ovoinhibitors, ovomacroglobu- related to aging and diseases such as atherosclerosis, di-
lin, ovoglycoprotein, ovoflavoprotein, thiamine-binding abetes, cancer, and cirrhosis. In particular, lipid oxida-
proteins, ficin/papain inhibitor, avidin, and cystatin tion in foods is a serious problem for the food industry
are the minor egg white proteins. These proteins, because it produces off-flavor, off-odor, discoloration,
as well as their peptides, have been recognized and potentially toxic reaction products. Synthetic an-
for their functional importance as antioxidants, an- tioxidants such as butylated hydroxyanisole, and buty-
timicrobials, metal-chelators, anti-viral, anti-tumor, lated hydroxytoluene are added to food products to re-
and angiotensin-converting enzyme (ACE)-inhibitory tard lipid oxidation. Over the past few decades, how-
activities. ever, the demand for natural antioxidants has increased
dramatically because of the negative consumer percep-
tions and the long-term safety concerns about synthetic

C 2017 Poultry Science Association Inc.
antioxidants. Many natural antioxidants have been iso-
Received April 27, 2017.
Accepted November 27, 2017. lated from plant sources to replace the synthetic ones to
1
Corresponding author: huangxi@mail.hzau.edu.cn improve the flavor and quality of food products, and to

1
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2 ABEYRATHNE ET AL.

extend the shelf life of foods (Abeyrathne et al., 2014). redox-dependent process (Ibrahim et al., 2013). OTf
Replacing artificial antioxidants with natural antioxi- is a superoxide dismutase (SOD)-mimicking
r
protein
dant peptides will be beneficial in the food industry be- with a potent superoxide anion (O2 − )-scavenging ac-
cause they not only control the lipid oxidation in foods tivity and showed dramatically higher scavenging ac-
but also supply additional essential amino acids to the tivity than some known antioxidants, such as serum al-
consumers. bumin or ascorbate. Interestingly, metal-bound OTfs
2+
Besides antioxidant activity, ACE-inhibitory activity such as Fe r−
-OTf, Mn2+ -OTf, Cu2+ -OTf exhibited
is another functional property that has been studied greater O2 dismutation capacity than the apoprotein
extensively, because high blood pressure has been con- (Ibrahim et al., 2007). Conjugation of OTf with small
sidered as a well-defined risk factor for cardiovascular molecules such as catechin shows improved antioxidant
diseases. As a multifunctional enzyme, ACE is involved activity (You et al., 2014). The research in our labora-
in several systems that are related to the blood pres- tory found OTf showed certain antioxidant effects dur-
sure through the inactivation of the vasodepressor agent ing in vitro experiments, and its hydrolysates showed
“Bradykinin” and the generation of the vasopressor approximately 3.2 to 13.5 times higher superoxide an-
agent angiotensin II. The separation and preparation of ion scavenging activity and better copper/calcium-
various ACE-inhibitory proteins and peptides from ani- solubililizing activity than OTf (Kim et al., 2012).
mal and vegetable sources have been reported. Peptides Furthermore, autocleaved OTf showed the higher an-
are demonstrated to possess higher ACE-inhibitory ac- tioxidant activity than the natural OTf, and the hy-
tivity than the proteins in vitro (Chen et al., 2012) and drolysates of autocleaved OTf showed stronger antioxi-
in vivo in hypertensive animals and humans (Mizuno dant activity than those of the autocleaved one (Moon
et al., 2005). Interestingly, it is found that the cardio- et al., 2015).
vascular diseases may also be related to the oxidative Ovomucoid, which accounts for 11% of total egg
stress in cells caused by excessive production of free white proteins, is well known as a “trypsin inhibitor”
radicals (You et al., 2010). The aim of this article is to and is considered as the main food allergen present in
review the research progress of functional proteins and egg (Abeyrathne et al., 2014). It is one of the highly
peptides from egg white on antioxidant, ACE inhibitory glycosylated proteins that contains 20 to 25% carbohy-
activity. drates (Nolan, Phillips and Mine, 2005). It has a molec-
ular weight of 28 kDa with an iso-electric point of 4.1,
but it appears in a range between 45 and 50 kDa in
Functional Properties of Egg White Proteins SDS-PAGE. This protein consists of 186 amino acids
that are arranged in three tandem domains (Oliveria et
Ovalbumin, as a major protein in egg white (54%), al., 2009). This protein contains three disulfide bonds,
demonstrated remarkable antioxidant activity after two tyrosine residues, and one active site (Salahuddin
binding covalently with galactomannan or dextran by and Baig, 1985). It is defined as a single headed in-
a controlled Maillard reaction. A Celite powder sys- hibitor of trypsin, meaning each ovomucoid molecule
tem containing methyllinoleate was used as a simu- binds 1:1 with trypsin, and its three-dimensional struc-
lated dried food model to evaluate lipid oxidation by ture is secured with the 3 disulfide bonds in it (Oliveria
measuring peroxide value and thiobarbituric acid val- et al., 2009).
ues. The results indicated that the antioxidation activ- Ovomucin accounts for 2 to 4% of the total egg white
ity of ovalbumin-polysaccharide conjugates were 1.4 to protein (Stadelman and Cotterill, 2001) and is respon-
1.9 times and 1.8 to 2.4 times their mixture by mea- sible for the gel-like structure in egg white. It consists
suring the peroxide value and thiobarbituric acid val- of two subunits with a wide range of molecular weight
ues, respectively. (Nakamura et al., 1992). Similarly, the (220 to 270 kDa) and very high levels of glycosylation
free-radical scavenging activity, hydroxyl-radical scav- (Omana, Wang and Wu, 2010a). Ovomucin mainly con-
enging activity and reducing power of selenized oval- sists of two types of subunits, which are called α and
bumin revealed that the antioxidant activity of ovalbu- β . α-Ovomucin is homogeneous whereas β -ovomucin is
min was improved when selenite was conjugated. The heterogeneous in structure. Furthermore, the α-subunit
enhanced antioxidant activity of selenized ovalbumin is has two subunits, called α1 and α2, which have fewer
ascribed to the conjugated Se and the formation of a carbohydrate groups than β -ovomucin (Hiidenvoi et al.,
molten globule conformation of protein (Li et al., 2014). 1999). Earlier research of ovomucin was mainly focused
The improvement of antioxidant activity has also been on its effect in the thinning of egg white. Recently,
observed when ovalbumin was combined with buck- however, ovomucin was found to possess a variety of
wheat polyphenol rutin (Awatsuhara et al., 2010). bioactivities such as antibacterial, antiviral, and anti-
Ovotransferrin (OTf), which accounts for 12% of the tumor activities, and the suppression of cholesterol ab-
total egg white protein, is known as an iron binder sorption (Omana, Wang and Wu, 2010b; Shan, Xu and
and transporter in animals, and thus can be used as Ma, 2014; Nagaoka et al., 2002). Heating ovomucin un-
an iron supplementing, antimicrobial, or antioxidant der alkaline conditions produced many peptides that
agent. Japanese researchers found that ovotransfer- have ACE-inhibitory, metal chelating, and antioxidant
rin generates observable thiol-linked self-cleavage in a activities (Abeyrathne et al., 2016).
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EGG WHITE PROTEINS AND ANTIOXIDANT PEPTIDES 3
Lysozyme is another important protein found in egg 6.5 and 5.6, respectively, depending upon whether it is
white (3.5% of total egg white proteins) (Ibrahim et al., non-phosphorylated or phosphorylated (Anastasi et al.,
2007). There are many forms of lysozyme found in na- 1983). Cystatin inhibits most of the cysteine proteases,
ture, but the one found in egg is considered as the most including papain and fucin (Huopalahti et al., 2007).
soluble and stable (Benkerroum, 2008). It is a ubiqui-
tous enzyme that can hydrolyze the β -linkage between
N-acetylneuraminic acid and N-acetylglucosamine in Production of Functional Peptides from Egg
bacterial cell walls. Lysozyme is known for its antibac- White Proteins
terial property, especially against Gram-positive bac-
teria (Huopalahti et al., 2007). It was found that the Elias et al. (2008) demonstrated that the antioxi-
modification of lysozyme exhibited an increased effect dant activity of proteins is due to the complex inter-
against Gram-negative bacteria such as Pseudomonas actions with lipids, oxidation catalysts, and free radi-
fluorescens compared with natural lysozyme (lysozyme cals in food systems. Proteins are somewhat different
monomer) (Cegielska-Radziejewska et al., 2009, 2010). from other food antioxidants because they have multi-
Derde et al. (2013) found that lysozyme rapidly in- ple functions that inhibit various oxidation pathways.
creased the permeability of the outer membrane of Es- Both proteins and peptides derived from egg are well
cherichia coli by forming large size pores, which may be known for anti-microbial ant-cancer, metal binding, and
the possible mechanism for its anti-bacterial activity. ACE-inhibitory activity properties.
In addition to the major proteins in egg white, many The egg white or the single protein has been used
other proteins, including ovoglobulin, ovoinhibitors, to produce bioactive peptides. Until recently, however,
ovomacroglobulin, ovoglycoprotein, ovoflavoprotein, most of the functional peptides were produced from
thiamine-binding proteins, avidin, and ficin/papain in- milk and soybean proteins. Peptides produced from
hibitor have been identified as functional proteins ovalbumin were strongly active agents against Bacil-
(Stadelman and Cotterill, 2001). These proteins, as well lus subtilis but lesser active agents against E. coli,
as their peptides, are known to have antioxidant, an- Candida albicans, and Pseudomonas aeruginosa (Pel-
timicrobial, or anti-enzymatic properties. Among them, legrini et al., 2004). Also highly glycosylated ovomucin
flavoprotein is known as a riboflavin-binding protein peptides are active against one of the most problem-
with a single polypeptide chain (Hamazune et al., atic foodborne pathogens E. coli O157:H7 (Kobayashi
1984). Flavoprotein is composed of 219 amino acids et al., 2004). The glycopeptides derived from ovomucin
with several α- and β -helices. Among the helices, 4 α- by pronase digestion showed good antitumor activity
helix (A-D) and 4 β -helix make the riboflavin bind- against double-grafted tumors in mice (Watanabe et al.,
ing sites. Avidin is an alkaline protein composed of 1998).
128 amino acids with the molecular weight of 14.3 kDa The production of bioactive peptides from egg
(Stadelman and Cotterill, 2001). Even though the bi- proteins was mainly performed using enzyme or heat
ological function of avidin is not well understood, it treatment. Hydrolysing egg white proteins improves
strongly binds biotin and acts as an antimicrobial agent their functional properties such as antioxidant, antimi-
(Huopalahti et al., 2007). crobial, metal-binding, and ACE-inhibitory activities
There are several proteases found in egg white, but (Moure et al., 2006; Abeyrathne et al., 2015). Chiang
the identification of these proteins is difficult because et al. (2006) reported that the peptides produced
of the presence of numerous anti-proteases (Rawlings from egg white proteins using thermolysin showed
et al., 2006). Two of the proteases identified in egg ACE-inhibitory activity in strain spontaneously hyper-
white are glutamyl aminopeptidase and aminopeptidase tensive rats. Ding et al. (2014) further demonstrated
with a broad specificity (Huopalahti et al., 2007). Sev- that the ACE-inhibitory peptides of egg white have a
eral proteins in egg white are characterized as “anti- cytoprotective effect and could be transported to hu-
proteases”. Among them ovostatin, ovoinhibitors, and man intestinal Caco-2 cell monolayers. Lin et al. (2013)
cystatin are considered important. Ovostatin is a α2- found that the hydrolysates produced from egg white
macroglobulin with a very high molecular weight with proteins using different enzymes (pepsin, alcalase, and
an isoelectric point of 4.9 (Nagase and Harris, 1983) and trypsin) showed strong antioxidant activity. Among
is known to have numerous biological properties includ- the peptides produced, alcalase hydrolysates showed
ing anti-bacterial and anti-inflammatory properties and the highest antioxidant activity, and the fractions
can be used to treat keratitis (Geng et al., 2013). Ovoin- with a strong antioxidant activity had molecular size
hibitors are multiple anti-protease proteins present in smaller than 1 kDa. Chen and Chi (2012) reported
egg white. They are glycoproteins and are heat stable that hydrolysis of egg white proteins with papain
and inhibit the serine proteases such as trypsin and produced two dominant peptides with the amino acid
chymotrypsin (Huopalahti et al., 2007). Cystatin has sequence of Tyr-Leu-Gly-Ala-Lys and Gly-Gly-Leu-
a molecular weight of 13 kDa with two major isoelec- Glu-Pro-Ile-Asn-Phe-Gln, which had strong antioxi-
tric forms differ in the occurrence of phosphorylation dant activity in DPPH radical scavenging and lipid
on serine (Huopalahti et al., 2007). These two forms of peroxidation inhibition assays. Dávalos et al. (2004)
cystatin show two different isoelectric point values at reported that strong antioxidant peptides with amino
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4 ABEYRATHNE ET AL.

acid sequences of Tyr-Ala-Glu-Glu-Arg-Tyr-Pro- showed protective effects against the oxidative stress-
Ile, Tyr-Arg-Gly-Gly-Leu-Glu-Pro-Ile-Asn-Phe, and induced DNA damage in human leukocytes.
Tyr-Gln-Ile-Gly-Leu were produced by hydrolysing Lysozyme is considered as one of the most impor-
egg white proteins with papain. Their antioxidation tant proteins isolated and industrialized from egg white
was proved by oxygen radical absorbance capacity- (Elias et al., 2008). Both lysozyme and its hydrolysates
fluorescein (ORAC-FL) assay in vitro. Manso et al. have been recognized as multifunctional fractions. Pep-
(2008) also produced peptides with strong antioxidant tides derived from egg white lysozyme ROS generation
activity from egg white proteins using pepsin. These and protected against acute and chronic oxidant inci-
peptides were effective in preventing or reversing the dence (Liu et al., 2006). It is reported that lysozyme
abnormalities associated with metabolic syndromes and the peptides produced by hydrolyzing lysozyme
and their complications such as hypertension, oxida- with 0.5% w/w alcalase at 95◦ C for 10 min showed
tive stress, and hyperlipidemia in hypertensive rats. significantly higher ORAC-FL activity, which was as
Similarly, the hydrolysis of egg white protein powder high as that of the synthetic antioxidants like BHA
with alcalase produced a peptide (His-Cys-Tyr-Tyr- and BHT in foods (You et al., 2010). Memarpoor-
Phe-Met) with a strong antioxidant activity (2011). Yazdi et al. (2012) fractionated a trypsin + papain hy-
Liu et al. (2015) identified three new peptides with drolysate of lysozyme and identified a peptide with the
molecular weights of 628.64, 630.71, and 684.1 Da amino acid sequence of NTDGSTDYGILQINSR (MW:
from the hydrolysates of egg white proteins. They 1,753.98 ± 0.5 Da), which has very high antioxidant
found that these peptides had amino acid sequences of activity. That fraction also had inhibitory effects on
Asp-His-Thr-Glu, Phe-Phe-Glu-Phe-His and Met-Pro- both Gram-negative and Gram-positive bacteria. The
Ala-His-Leu, and had strong oxygen radical absorbance minimal inhibitory concentration values of the peptide
capacities. Among the peptides derived from egg white against E. coli and Leuconostoc mesenteroides bacteria
proteins, the ones with amino acid sequences of were 355.64 (±2.2) and 442.25 (±2.8) μg/mL, respec-
Tyr-Arg-Glu-Glu-Arg-Tyr-Pro-Ile-Leu, Arg-Ala-Asp- tively. Another research study demonstrated that the in
His-Pro-Phe-Ley and Ile-Val-Phe showed positive vitro digestion product (LPH2) of egg white lysozyme
actions on hypersensitive rats (Miguel et al., 2004). Yu was found to have potent ACE-inhibitory and antioxi-
et al. (2012) reported that 11 peptides derived from egg dant activities in vitro. Of the fragments in the LPH,
white using alcalase had ACE-inhibitory, antioxidant, KVF, MKR, AMK, AKF, RGY, WIR, VAW, and GIL
and anticoagulation activities. All 11 bioactive peptides showed great ACE-inhibitory activity. Furthermore, the
contained Thr-Asn-Gly-Ile-Arg in their amino acid peptides RGY, WIR, and VAW showed strong antioxi-
sequences, and the primary and secondary structures dant activity (Rao et al., 2012).
of the peptides showed strong ACE-inhibitory activity. Recently, a few of the major egg white proteins
Individual egg white proteins have also been used (ovalbumin, ovomucoid, and ovomucin) have been
to produce functional peptides. Among the egg white hydrolyzed using combinations of enzymes (trypsin,
protein OTf, ovalbumin, ovomucin, ovomucoid, and pepsin, chymotrypsin, papain, and alcalase) under 37◦ C
lysozyme were widely used to produce bioactive pep- to produce bioactive peptides (Abeyrathne, Lee and
tides. Manso et al. (2008) reported that the peptides Ahn, 2014; Abeyrathne et al., 2015; Abeyrathne et al.,
derived from ovalbumin showed a strong inhibitory ac- 2016). The combination of pepsin, papain, and alcalase
tivity against ROS. They reported that oral intake of treatments of those proteins produced peptides with
these peptides for a short period reduced the blood high antioxidant activity. Among them, ovalbumin hy-
pressure in spontaneously hypertensive rats. Free rad- drolyzed with alcalase + trypsin (OAArTr) and pro-
icals, including ROS, caused lipid oxidation as well as tease + chymotrypsin (OAC), ovomucoid hydrolyzed
protein and DNA oxidation. Ibrahim and Kiyono (2009) with alcalase + trypsin (OMAlTr), and ovomucin dis-
demonstrated that OTf auto-cleaved under reducing solved at pH 12.0 and heated for 15 min at 100◦ C (OM)
conditions exhibited stronger SOD-like activity and an- produced peptides with the highest antioxidant activ-
ticancer effects against human colon and breast can- ity. The LC-nano ESI-MS/MS analysis identified sev-
cer cells than the natural OTf. Also, the auto-cleaved eral tens to hundreds of peptides from each of the hy-
OTf showed stronger Cu2+ - and Ca2+ -binding capac- drolysates, and the majority of the peptides had molec-
ities than the natural OTf (Moon et al., 2015). The ular weight <2 kDa (Table 1). The results showed that
hydrolysis of OTf with the combination of thermolysin, the hydrolysates with small peptides showed stronger
and pepsin produced 14 peptides with strong antioxi- functional activity than those with larger peptides,
dant activity, and the majority of the peptides identified but purification of individual peptides with a spe-
had high ORAC values. However, peptides with amino cific function from the hydrolysates seems not possi-
acid sequences of LSKAQSDFG and LVEKGDVAFI ble or maybe meaningless. Also, recently Nimalaratne
showed pro-oxidant activity (Shen et al., 2010). Kim et al. (2015) produced 16 antioxidant peptides from
et al. (2012) reported that OTf possessed an antiox- ovalbumin, OTf, and cystatin using different proteases
idant effect in a different system, but hydrolysis of and alcalase, and found that two peptides with the
OTf with acid or enzymes improved these abilities. amino acid sequences of ALs-Glu-Glu-Arg-Tyr-Pro and
Also, they found that OTf and its enzyme hydrolysates Asp-Glu-Asp-Thr-Gln-Ala-Met-Pro showed the highest
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EGG WHITE PROTEINS AND ANTIOXIDANT PEPTIDES 5
Table 1. Effects of enzyme treatment on the size and number of peptides of OAPrTr (ovalbumin treated
with protease and trypsin under ambient conditions), OAC (ovalbumin treated under α-chymotrypsin un-
der optimum conditions), OMAlTr (ovomucoid hydrolysed using alcalase and trypsin under optimum con-
ditions), and OM (ovomucin heat at 100◦ C for 15 minutes) (Abeyrathne et al., 2014; Abeyrathne et al.,
2015; Abeyrathne et al., 2016).

Types of peptides
MW of peptides (Da) OAArTr OAC OMAlTr OM

< 700 10 0 0 0
700 to 1,000 28 63 10 4
1,000 to 1,500 52 257 15 24
1,500 to 2,000 47 124 21 33
2,000 to 3,000 23 105 19 33
3,000 to 5,000 21 34 10 55
Total (Prot. Scores) 181 (64.93) 583 (61.25) 75 (6.90) 149 (0.43)

ORAC. The hydrolyzed peptides from separated ovo- of different enzymes or enzyme combinations can diver-
mucoid showed strong biologically important proper- sify the sizes, functions, and the amino acid sequences
ties, including antioxidant, metal-chelating, and ACE- of the peptides produced.
inhibitory activities (Abeyrathne et al., 2015). Over the years, much research has showed strong
Fertilized chicken eggs and unfertilized duck eggs antioxidant activity of peptides from various protein
were also used to produce functional peptides. Duan sources, but the use of peptides in real foods or pro-
et al. (2014) produced many peptides with antioxi- cessed foods is limited. Some of the bioactive peptides
dant activity from the fertilized eggs: a peptide with purified from the enzyme hydrolysates of proteins ex-
HLFGPPGKKDPV (MW 1291.51 Da) was identified hibited potent inhibitory potential, but it is very dif-
in a 15-day-incubated egg and found to have a strong ficult to commercialize those peptides because of low
antioxidant activity. The hydrolysis of duck eggs with yield, high cost, and difficulties in the separation and
SEEP-Alcalase (HSA21 ) produced 5 oligopeptides with purification processes. Therefore, instead of separating
the molecular weights of 202.1, 294.1, 382.1, 426.3, and individual functional peptides from hydrolysates, using
514.4 Da, (Ren et al., 2014). These peptides showed sta- the whole enzyme hydrolysate of a protein with potent
ble antioxidant activity after in vtiro digestive simula- ACE-inhibitory and antioxidant activities in food pro-
tion. The antioxidant activity of the peptides showed a cessing would be more desirable because it can directly
close relationship with their sizes. Most of the peptides add antioxidant, antimicrobial, or ACE-inhibitory func-
with a strong antioxidant capacity contained either one tions to the product. For example, nitrite used in cured
or few of the amino acids, including Cys, Met, Trp, Tyr, meat is considered as a carcinogenic agent but could
Phe, and His in their peptide sequences. Thus these be replaced with hydrolysate containing functional egg
amino acids were called as antioxidant amino acids be- white peptides (Demeyer et al., 2008).
cause they increased the antioxidant activity of the pep-
tides (Elias et al., 2008).
Future of the Use of Functional Proteins and
Peptides Derived from Egg White Proteins
Strategies for the Practical Application of
the Functional Peptides from Egg Proteins Most of the individual egg white proteins separated
and the peptides derived from them are known to have
Functional food is an emerging area in the food indus- biomedical importance. The peptides that are known
try. Functional food sales topped $55.1 billion in 2015, to reduce ROS activity can be used as a drug or in
up 7.7%, and are projected to reach $63.3 billion by therapeutic activities to control the aging process in
2017 (NBJ, 2016). The derived egg peptides have mul- humans. Also, the peptides derived from egg proteins
tiple functional properties, giving them strong poten- are known to have antioxidant activity, and thus they
tial to be used as natural antioxidant, antimicrobial, or can be used as natural antioxidant agents in most of
metal-chelating agents because the peptides have multi- the processed food products like sausages and cheese.
functional properties. The functional peptides from egg Some of the proteins and peptides can be used as an-
proteins can replace synthetic antioxidants, and there is timicrobial agents since lysozyme, OTf, and the pep-
no upper limit to the addition of the functional peptides tides derived from the egg white proteins have shown
in the processed foods. Although the industrial appli- strong growth suppressing abilities against E. coli and
cations of the peptides from egg proteins are limited, other foodborne pathogens (Masschalck and Michiels,
some of the egg white proteins and their peptides are 2003). Peptides derived from ovalbumin are known to
already used as antimicrobial and antioxidant agents in have ACE-inhibitory activity, and thus may be used
some foods, including cheese, wine, and processed meat to lower high blood pressure. Most of the peptides de-
(Abeyrathne et al., 2013; Herath et al., 2015). The use rived from egg white proteins are proven to have strong
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6 ABEYRATHNE ET AL.

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Dávalos, A., M. Miguel, B. Bartolome, and R. Lopez-Fandino. 2004.
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ACKNOWLEDGMENTS Elias, R. J., S. S. Kellerby, and E. A. Decker. 2008. Antioxidant ac-
tivity of proteins and peptides. Crit. Rev. Food Sci. Nutr. 48:430–
This study was supported by the National Institute of 441.
Food and Agriculture/USDA (Award No. 2015–67018- Geng, F., X. Huang, N. Yam, L. Jia, and M. Ma. 2013. Purification of
hen egg white ovomacroglobulin using one-step chromatography.
23081), Washington, DC, and the National Natural Sci- J. Purif. Sci. 36:3717–3722.
ence Foundation of China (Project No. 31471602). Herath, A. H. M. I. E., J. M. P. Jayasinghe, D. U. Ahn, and E. D. N.
S. Abeyrathne. 2015. Use of lysozyme from chicken egg white as
a nitrite replacer in an Italian-type chicken sausage. Funct. Food
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