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Journal of Food Quality ISSN 1745-4557

RECOVERY AND UTILIZATION OF PROTEIN DERIVED FROM


SURIMI WASH-WATER
jfq_424

43..50

J.J. STINE1,4, L. PEDERSEN2, S. SMILEY3 and P.J. BECHTEL1


1

USDA-ARS, Subarctic Agricultural Research Unit, 118 Trident Way, Kodiak AK 99615
Dantec Engineering, Danville, CA
3
University of Alaska, Fishery Industrial Technology Center, Kodiak, AK
2

Corresponding author. TEL: 907-486-1534;


FAX: 907-486-1540; EMAIL:
stine.jj@gmail.com
Received for Publication December 8, 2010
Accepted for Publication November 1, 2011
doi:10.1111/j.1745-4557.2011.00424.x

ABSTRACT
Surimi processors are committed to improve utilization of seafood resources,
increase productivity and reduce organic matter discharged into the environment.
The object of this study was to recover protein from pollock surimi processing washwater using membrane filtration and characterize properties of the recovered material. A pilot unit equipped with membrane elements concentrated protein from the
surimi wash-water. Membrane concentrate and control surimi samples were analyzed for proximate composition, lipid oxidation, color, sodium dodecyl sulfate gel
electrophoresis, amino acids and minerals. Membrane concentrate, membrane concentrate plus surimi and control surimi were monitored for 180 days of storage at
-20C. The membrane concentrate had significantly higher moisture and lipid, but
lower protein content than surimi. As determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis, membrane concentrate proteins displayed a greater
amount of lower molar mass molecules compared with surimi. The amino acid
profile was comparable to control surimi and the recovered membrane concentrate
proteins had similar nutritional values to that of surimi. The results indicate that the
addition of 5% membrane concentrate to surimi will not adversely affect the storage
at -20C and that the recovered wash-water protein could be used to obtain a fish
protein ingredient or added back at a low percentage to surimi products.

PRACTICAL APPLICATIONS
In order to increase productivity and improve utilization of seafood resources,
surimi processors are looking into alternative technologies to recover proteins and
other material from the wastewater. Membrane filtration is a promising option for
the concentration of wastewater. This study was conducted to determine the recovery and characterize the material recovered from surimi wash-water using a commercial membrane filtration unit. It was demonstrated that the recoverable material
is nutritionally similar to the final surimi product and that the overall yield can be
increased using membrane technology. In addition to the benefit of recovering
protein, the membrane filtration can reduce the amount of material in the waste
stream.

INTRODUCTION
Surimi is basically concentrated myofibrillar protein obtained
from fish flesh that has been extensively washed with cold
water.Surimi is a raw food ingredient used in a variety of prodJournal of Food Quality 35 (2012) 4350 2012 Wiley Periodicals, Inc.

ucts that have become increasingly popular due to their unique


textural properties, storage properties and high nutritional
value (Akil et al. 2008; Park and Morrissey 2000; Bourtoom
et al. 2009). In the industrial surimi manufacturing process,
minced flesh is repeatedly washed with chilled water to remove
43

RECOVERY OF PROTEIN FROM SURIMI WASH-WATER

sarcoplasmic proteins, lipids and lower molar mass water


soluble materials, leaving a tasteless and odorless myofibrillar
protein product.
Although this washing process effectively lowers many
enzymes associated with muscle protein degradation, the
protein material washed-free has a number of potential uses.
Surimi wash-water typically contains 0.52.3% protein (Lin
et al. 1995; Morrissey et al. 2000; Park and Morrissey 2000).
However, new and different technologies are needed to
recover these proteins economically.
In the seafood industry, solid waste from surimi processing
is usually converted to fishmeal. However, liquid waste with
low solids content is often discarded into the plants waste
stream (Chang-Lee et al. 1989; Lin et al. 1995). The processing of Pacific whiting, Alaskan pollock and shrimp in Oregon,
Alaska and Washington generates 20 million tons/year of processing water (Park and Morrissey 2000). Increasing concerns
over the negative impact of wastewater discharge have led to
research in protein recovery from surimi wash-water. An
effective method to recover fish proteins from surimi washwater would not only reduce the negative environmental
impact and the cost of waste disposal, but could also lead to
new ways to generate profit. Recovered protein could be
returned to the process to increase final surimi yield. Figure 1
illustrates a mass balance for fish solids in a typical surimi

FIG. 1. APPROXIMATE MASS FLOW IN SURIMI PROCESSING. BECAUSE


OF THE VARYING MOISTURE CONTENT THROUGHOUT THE PROCESS A
SOLIDS BALANCE IS ALSO SHOWN
(Solids is defined as fish mass at 0% water or fish mass minus water
mass.).

44

J.J. STINE ET AL.

processing facility, including an alternative membrane filtration concentration for press-water. Overall, the mass balance
will vary depending on species, harvesting season and plant
operations. In all cases, the loss of fish solids in wash-water
during surimi washing remains significant.
There have been several studies on recovering proteins
from surimi processing wash-waters. Ultrafiltration has been
used to produce protein concentrates with good functional
properties via myofibrillar proteins recovered from surimi
wash-water (Morr 1976; Chang-Lee et al. 1989; Lin et al.
1995; Morrissey et al. 2000). Severe fouling of the membranes
has been a frequent problem (Morr 1976). Huang and Morrissey (1998) evaluated the microfiltration membrane fouling
by surimi wash-water and reported that fouling occurred initially as a result of pore blocking resistance followed by cake
resistance. Jaouen and Quenmeneur (1992) noted that processing of surimi wash-water by ultrafiltration without pretreatment was not practical. However, Mireles Dewitt and
Morrissey (2001) showed that large molar mass proteins that
interfered with ultrafiltration could be removed by first
adjusting wash-water acidity to pH 6 and then applying a
rapid heat treatment to raise the temperature to 60C.
Attempts to combine ohmic heat treatments with ultrafiltration on surimi wash-water were also investigated. Huang
et al. (1997, 1998) studied the effect of ohmic heating (70C)
on protein coagulation in surimi wash-water and found that
the wash-water-soluble protein could be removed; however,
an important consideration was the possibility of retaining
proteolytic activity after mild heat treatment. Some proteases
tend to be stable, so there is a likelihood of recovered undenatured enzymes adversely affecting the final product (Scopes
1994).
Many proteins have been employed to improve the
mechanical properties of surimi gels. The most frequently
used are egg white and whey protein concentrates; other
sources such as leguminous extracts and porcine plasma
protein have also been proposed. These proteins are added to
inhibit the proteolytic degradation of fish myosin when gels
are incubated at 60C, and to favor gel setting by the action of
endogenous and added transglutaminases (An et al. 1996;
Garcia-Carreno 1996; Sanchez et al. 1998; Benjakul et al.
2001).
Previous studies have shown that using ultrafiltration
could enable greater than 65% recovery of proteins (Afonso
et al. 2004). If the recovered protein was added back to the
surimi cake it would increase productivity and generate
greater revenues (Afonso et al. 2004). The objectives of this
project were: (1) evaluation of the potential for applying
membrane filtration technology to the recovery of the protein
from surimi wash-water; (2) the chemical characterization of
the recovered protein; and (3) the evaluation of the properties
of the concentrated recovered protein when added back to
surimi prior to a 180-day frozen storage study.
Journal of Food Quality 35 (2012) 4350 2012 Wiley Periodicals, Inc.

J.J. STINE ET AL.

MATERIALS AND METHODS


Membrane Filtration Unit and Samples
Membrane filtration was conducted on wash-water generated
by the standard surimi processing technology used in Alaskan
seafood processing plants. The tests were initiated immediately after collection of samples, and the filtration test was
carried out maintaining the wash-water temperature (4C).
For this study, a spiral wound 8-in. filtration module
manufactured by Kelitec Engineering (Laguna Hills, CA) was
used. Tests were carried out at Westward Seafoods Unalaska,
Dutch Harbor, AK plant during the Pollock (Theragra chalcogramma) B season utilizing the pilot plant-sized membrane
filtration unit equipped with two membrane elements. The
membranes had a nominal pore size of 80 kDa, and the membrane substrate was polyacrylic nitrile (PAN). This configuration provides a compact, cost-effective membrane system
where high cross flow rates are required while avoiding premature protein-induced fouling.
Samples obtained from Westward Seafoods Inc. in Dutch
Harbor, AK, were shipped frozen to Fairbanks, AK, for analysis. The five composite samples were (1) pollock surimi
serving as a negative control; (2) pollock surimi with 5%
membrane concentrate (MC) added; (3) pollock surimi with
7% sorbitol and 0.25% polyphosphate added as a cryoprotectant control; (4) pollock surimi with 7% sorbitol and
0.25% polyphosphate as cryoprotectants and 5% MC added;
and (5) 100% MC. Samples were stored at -20C until evaluated. Three subsamples were taken for each analysis.

Proximate Analysis
Proximate composition was determined in quadruplicate for
each sample. Moisture and ash content were determined
using AOAC methods 952.08 and 938.08, respectively (AOAC
1980). Nitrogen content was determined by pyrolysis with a
Rapid N3 (Elementar America Inc., Mt. Laurel, NJ) nitrogen
analyzer. Protein content was calculated as 6.25 times %N.
Total lipid content was determined gravimetrically by the
Folch method (Folch et al. 1957). After lipid extraction, the
solvent was removed at 50C under a N2 gas stream using a
TurboVap LV (Caliper Life Sciences, Hopkinton, MA).

Electrophoresis
The sodium dodecyl sulfate polyacrylamide gel electrophoresis system (SDS-PAGE) was used with a Photodyne Foto/Force
300 electrophoresis apparatus under reducing conditions
according to Schagger and Von Jagow (1987). Precast 1020%
Tricine gels (Novex, Invitrogen, Carlsbad, CA) were used and
molar mass standards were purchased from Sigma-Aldrich.
Journal of Food Quality 35 (2012) 4350 2012 Wiley Periodicals, Inc.

RECOVERY OF PROTEIN FROM SURIMI WASH-WATER

The protein bands were visualized from the gels stained with
Coomassie blue (Sigma-Aldrich, St. Louis, MO).

Amino Acid Analysis and Mineral Analysis


Amino acid profiles were determined by the AAA Service
Laboratory Inc., Boring, OR. Samples were hydrolyzed with
6 N HCl and 2% phenol at 110C for 22 h. Amino acids were
quantified using the Beckman 6300 analyzer with postcolumn ninhydrin derivatization. Tryptophan and cysteine
content were not determined.
Samples for mineral analysis were sent to the University of
Alaska Fairbanks School of Natural Resources and Agricultural Sciences Palmer Research Center (Palmer, AK). The
samples were ashed overnight at 550C. Ashing residues were
subsequently digested overnight in aqueous solution containing 10% (v/v) hydrochloric acid and 10% (v/v) nitric acid.
Digested solutions were diluted as needed and analyzed for
Ca, Cu, Fe, K, Mg, Mn, Na, P and Zn by inductively coupled
plasma optical emission spectroscopy on a Perkin Elmer
Optima 3000 Radial ICP-OES (Perkin Elmer, Boston, MA).

Whiteness
Surimi color and whiteness are important factors affecting
product quality and, ultimately, price. Cooked surimi samples
were chopped with a spatula, placed on a Hunter Lab Colorflex instrument, and L*(lightness), a*(red-green color),
b*(yellow-blue color) values were recorded. Four replicates of
each sample were analyzed. Whiteness was calculated as
(100 - [(100 - L*)2 + a*2 + b*2]1/2) in each case and the
average of the 16 replicates was reported except for MC,
which n was: day 0 = 2, day 30 = 2, day 90 = 4, day 180 = 3.

Lipid Oxidation
The procedure was modified from Siu and Draper (1978).
TBA reagent was prepared by adding 300 mg 2-thiobarbituric
acid (TBA, MP Biomedical, Solon, OH) into 100 mL DI. Fivegrams of sample was mixed with 20 mL of 6% TCA (Fisher
Scientifics, Fairlawn, NJ), homogenized using a Turrax for
90 s at 11,000 rpm then centrifuged at 10,000 g for 15 min.
The supernatant was filtered through Whatman #4 filter
paper. Two milliliters of the filtrate was mixed with 2 mL TBA
reagent, heated for 20 min at 94C, cooled to room temperature, and the absorbance was measured at 531 nm. Samples
were compared with a standard curve of malonaldehyde bis(dimethyl acetal) (MDA, ACROS, Geel, Belgium). Values are
expressed in mg MDA per gram of sample.

Storage Study
To examine the effects of storage, the samples were stored at
-20C and examined at days 0, 30, 90 and 180. Upon receipt of
45

RECOVERY OF PROTEIN FROM SURIMI WASH-WATER

J.J. STINE ET AL.

Flux (liters/square meter/hour (lmh)

Dehydator/Screw press water concentration by


membrane filtration
12
10
8
Flux 1A

Flux 2A
4
2
0
0

Flux 1B

PAN membranes
Two8" modules operated in series
Transmembrane pressure 8 psi
2

10

Too viscous
to pump

12

14

16

Flux 2B

18

Time (1 unit = 0.5 hrs)


FIG. 2. FILTRATION RATE (FLUX) DURING CONCENTRATION OF SURIMI WASH-WATER
Filtration rate is expressed in liters per square meter of membrane surface per hour (L/m2/h). PAN, polyacrylic nitrile.

samples, a small amount was removed for day 0 analysis. The


remaining sample was placed inside whirl pack bags and
stored in a commercial freezer at -20C until analysis.

Statistical Analysis
The averages and standard deviations were calculated using
Excel (Microsoft). For tests of statistical difference between
data sets, the data were subjected to analysis of variance followed by a post hoc Tukeys honest significant difference test
(P < 0.05) using Statistica version 6.0 (StatSoft Inc., Tulsa,
OK).

RESULTS AND DISCUSSION


Membrane Filtration
Selection of the filter membrane molecular cutoff determines
the percentage and type of product recovered as well as the filtration rate. Small-scale preliminary tests carried out at the
Fishery Industry Technology Center in Kodiak, AK, found
that membranes with a molecular cutoff of 50 kDa resulted in
recovery of approximately 80% of the protein contained in
the wash-water while salts and smaller organic molecules still
passed through the membrane. Experiments indicated that
membranes with a molecular cutoff between 50 and 100 kDa
achieved a good balance between recovery and filtration rates
(flux). Selection of the appropriate membrane material also
determines the methods required to clean the membrane
effectively between runs. Ceramic and polymeric PAN M
series (polyacrylic nitrile) membranes were found to have
superior performance under the conditions employed here.
46

The filtration rate obtained for two consecutive days of


operation in a commercial surimi plant is shown in Fig. 2. In
test 1, the initial feed volume was 2,850 L concentrated to
420 L over an 8-h period. In test 2, the initial volume was also
2,850 L, this time concentrated to approximately 200 L over a
7-h period, which resulted in a highly viscous concentrate.
The test showed that high cross flow rates (340 L/min per
element) and very low transmembrane pressures (810 psi)
were required to avoid fouling of the membrane surfaces
(Fig. 2). At these settings, the membrane filters maintained
reasonable flux levels during the 78-h test periods without
showing any noticeable degradation.
The viscosity of the recovered product increased rapidly at
concentrations greater than 10% solids. At 14% solids, the
recovered product became very thick and difficult to pump.
The upper concentration limit with the applied membrane
system was approximately 12% solids. The solids content of
both the feed and the concentrate is shown in Table 1.
With the 80 kDa cutoff, product recovery was approximately 75% of the solids. This resulted in the recovery of the
product containing the higher molar mass molecules, while
the salts and smaller organic molecules still pass through this
type of membrane. The protein content in the recovered
product was similar to that of surimi when adjusted for different moisture content.

Proximate Analysis
The initial proximate analyses of the five surimi samples are
presented in Table 2. The composition of MC was very similar
to previously published results for recovered protein from
surimi wastewater (Lin et al. 1995). The MC had significantly
Journal of Food Quality 35 (2012) 4350 2012 Wiley Periodicals, Inc.

J.J. STINE ET AL.

RECOVERY OF PROTEIN FROM SURIMI WASH-WATER

TABLE 1. ANALYTICAL RESULTS OF FILTRATION TESTS

Test 1
Test 2

Feed
(% solids)

Concentrate
(% solids)

Init vol.
(L)

Final vol.
(L)

Concentration
factor

Solids feed
(kg)

Solids conc.
(kg)

Solids recovered
(% of start)

2.1
1.3

10.5
13.7

2,843
2,843

416.9
208.5

6.8
13.6

226.2
140.0

165.9
108.2

73.3
77.3

The solids content in the feed and concentrate is shown in Table 1. During the test the volume was reduced by a factor of 6.8- and 13.6-fold, respectively.

TABLE 2. DAY 0 PROXIMATE COMPOSITION


OF SURIMI SAMPLES

Sample

Moisture (%)

Ash (%)

Lipid (%)

Protein (%)

Surimi control
Surimi + 5% MC
Cryoprotected surimi
Cryo + 5% MC
MC

81.12 0.75a
80.70 0.60a
75.76 0.43b
75.39 0.23b
86.70 1.31c

0.35 0.06a
0.30 0.10a
0.28 0.24a
0.44 0.11a
0.59 0.12a

0.13 0.04a
0.12 0.02a
0.05 0.03a
0.10 0.08a
1.09 0.27b

18.38 0.17a
20.58 0.89b
18.10 0.65a
18.50 0.64ab
14.21 1.79c

Values are averages of four samples along with standard deviations and expressed in percentage.
Different alphabetical letters indicate a significant difference (P < 0.05) within each column.
MC, membrane concentrate.

higher moisture and lipid content, and lower protein content


than the surimi samples. There was no difference in the ash
composition of the samples.

Electrophoresis
The SDS-PAGE analysis of surimi samples is presented in
Fig. 3A,B. The banding pattern for the gels analyzing storage
day 0 for cryoprotected surimi and cryoprotected
surimi + 5% MC agrees well with previously published gels of
surimi analog crabstick product prepared with Alaska pollock
surimi (Reed and Park 2008). As expected, surimi samples
show myosin heavy chain bands at approximately 200 kDa,
actin bands at approximately 40 kDa, and myosin light chain
bands located between 20 and 13 kDa, while the MC showed
only trace amounts of protein at these molar masses. The
abundance of low molar mass bands in the MC is in agreement with previously published results (Lin et al. 1995; Bourtoom et al. 2009). Few differences were seen between the gels
loaded with samples from day 0 (Fig. 3A) and day 180
(Fig. 3B), indicating protein stability.

A Lane 1

Lane 1

210KDa

90KDa
65KDa
40KDa
30KDa
20KDa
13KDa

8KDa

Mineral Analysis and Amino Acid Analysis


The amino acid profile of normal surimi (1a) and MC (3) is
presented in Table 3. Values for three of the basic amino acids
were 9.0% for lysine, 6.1% for arginine and 2.9% for histidine.
Methionine (3.5%) and phenylalanine (6.8%) concentrations in MC were higher than in previously published fish and
soy meal analyses (Ohshima et al. 1993; Wibowo et al. 2005).
These results indicate the MC, in terms of amino acid composition, has values comparable with surimi. The percentage of
total essential amino acids and total nonessential amino acids
in MC was 45.0 and 55.0%, respectively.
Journal of Food Quality 35 (2012) 4350 2012 Wiley Periodicals, Inc.

FIG. 3. SODIUM DODECYL SULFATE POLYACRYLAMIDE GEL


ELECTROPHORESIS PATTERN OF SAMPLES STORED FOR 0 AND
180 DAYS
Lane assignments: 1 = cryoprotected surimi, 2 = cryoprotected
surimi + 5% membrane concentrate (MC), 3 = MC. Gel A: storage day
0, gel B = storage day 180. Colorburst standard (sigma) was used to
identify molar mass (not shown).

47

RECOVERY OF PROTEIN FROM SURIMI WASH-WATER

J.J. STINE ET AL.

TABLE 3. COMPARISON OF AMINO ACID PROFILE OF POLLOCK SURIMI


AND MEMBRANE CONCENTRATE

wt/wt % total amino acids measured. TEAA is total essential amino acids.
TNEAA is total nonessential amino acids.
MC, membrane concentrate; Ave., average; SD, standard deviation.

The mineral composition of normal surimi, cryoprotected


surimi and MC is presented in Table 4. The mineral concentrations were similar for surimi and MC; however, higher
levels of Fe, Zn and Cu were present in MC.

Whiteness and Lipid Oxidation


Whiteness data are reported at storage time points over the
180 days in Fig. 4. The color of the MC appeared slightly
darker than the other surimi samples for all storage with

Average

Average

0.36
0.18a
0.12b
0.11b
3,473b
0.56a
14b
ND
1.5a

0.01
0.02
0.01
0.01
144
0.16
0.00
ND
0.71

Day 90

Day 90

Day 180

Day 30

Day 180

Day 0

Day 0
Day 30

Day 180

values ranging from 55 to 60. The darker color was also consistent with the higher Fe values for MC. Whiteness in surimi
and surimi with added MC did not decrease dramatically over
the 180 days of storage (P < 0.05).
The extent of lipid oxidation over the storage time is shown
in Fig. 5. At day 180, the TBA values in all samples are higher
than those found in all previous samplings. Also, the MC has a
higher amount of MDA present in all samples compared with
the other treatments. This can be explained by the higher lipid
content in the MC and possibly the increased Fe in this fraction. The results indicate that lipid oxidation increases with
time and samples with higher lipid levels show greater lipid
oxidation. TBA values did increase in most treatments with
storage time although generally not significant. There was a
trend for higher TBA values in surimi with added MC than
samples where MC was absent.

14

0.70
0.39b
0.22c
0.17c
3,791b
4.35b
39.33c
1
47.33b

SD
0.03
0.03
0.01
0.01
245
0.08
2.08
0
1.53

Different alphabetical letters indicate a significant difference (P < 0.05)


within each row.
MC, membrane concentrate; SD, standard deviation of the mean; ND,
below detection limit.

48

Day 0

FIG. 4. WHITENESS OF SURIMI SAMPLES DURING 180-DAY STORAGE


TIME
Whiteness calculated as described in METHODS section. C, control
surimi; MC, membrane concentrate.

12
10

Day 0

Day 30
b
b
b

0.01
0.03
0.01
0.00
45
0.26
1.73
0.58
5.66

MC

Lipid Oxidation versus Storage Days


MC

SD

Cryo+MC

16

Surimi + Cryo + 5% MC

Cryo

Day 90

Day 180

C+MC

a
a
a
a

0.26
0.23a
0.15a
0.14a
2,724a
0.95a
19a
1.33
8a

SD

C+MC

a
a
a
a

Day 90

a
a
a
a

P (%)
K (%)
Ca (%)
Mg (%)
Na (ppm)
Cu (ppm)
Zn (ppm)
Mn (ppm)
Fe (ppm)

Average

30

10

MDA (mg/g)

Minerals

40

20

TABLE 4. MINERAL COMPOSITION OF SURIMI SAMPLES


Surimi

50

Day 30

60

Day 180

0.16
0.01
0.17
0.13
0.06
0.03
0.01
0.02
0.02
0.02
0.15
0.01
0.04
0.03
0.02
0.08

Day 0

6.3
6.1
12.6
11.2
4.45
2.9
5.6
9.2
9.1
3.5
6.8
3.5
4.0
4.5
3.9
6.5
45.0
55.0

Day 30

0.10
0.04
0.03
0.21
0.04
0.01
0.04
0.09
0.10
0.02
0.02
0.09
0.11
0.06
0.03
0.09

Day 90

5.8
7.7
11.1
15.4
3.6
2.4
5.6
9.3
10.4
3.8
4.3
1.8
3.9
4.7
4.6
5.7
43.7
56.2

Day 180

SD

Day 0

Ave.

Day 30

SD

Day 90

70

Ave.

a
a
a
a

ALA
ARG
ASP
GLU
GLY
HIS
ILE
LEU
LYS
MET
PHE
PRO
SER
THR
TYR
VAL
TEAA %
TNEAA %

80

MC

Whiteness

Surimi

Whiteness During 180 Storage Days at 20C

2
0

Cryo

Cryo+MC

MC

FIG. 5. LIPID OXIDATION DURING STORAGE, MEASURED AS MDA-TBA


COMPLEX
Different alphabetical letters indicate a significant difference (P < 0.05)
between samples. C is control surimi; MC is membrane concentrate;
MDA-TBA, malonaldehyde bis(dimethyl acetal)-thiobarbituric acid.

Journal of Food Quality 35 (2012) 4350 2012 Wiley Periodicals, Inc.

J.J. STINE ET AL.

Storage Study
There were no dramatic changes in proximate composition,
minerals, amino acids or whiteness over the 180 days of the
study. There was however noticeable increase in lipid oxidation at day 180 as determined by TBA values, especially in
the MC. This is consistent with previous results demonstrating that higher lipid values result in increased oxidation
(Matsushita et al. 2010). However, the results indicate that
the addition of MC to surimi will not adversely affect the
storage at -20C.

CONCLUSIONS
Solids from surimi wash-water were successfully recovered
using an ultrafiltration system. Protein concentrates recovered in these experiments had a significantly higher moisture and lipid content when compared with surimi. The
proteins concentrated by membrane filtration displayed a
larger number of lower molar mass compared with surimi.
The amino acid profiles of the MC were comparable to that
of surimi. The results indicate that the addition of 5% MC
to surimi will not adversely affect the storage at -20C. From
the results of this study, it is possible that the recovered
wash-water protein could be used to obtain a fish protein
ingredient or added back at a low percentage to surimi
products.

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Journal of Food Quality 35 (2012) 4350 2012 Wiley Periodicals, Inc.