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SURIMI WASH-WATERjfq_424 43..50J.J. STINE1,4, L. PEDERSEN2, S. SMILEY3 and P.J. BECHTEL1

1USDA-ARS, Subarctic Agricultural Research Unit, 118 Trident Way, Kodiak AK 996152Dantec Engineering, Danville, CA3University of Alaska, Fishery Industrial Technology Center, Kodiak, AK

4Corresponding author. TEL: 907-486-1534;

FAX: 907-486-1540; EMAIL:

[email protected]

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.Theobject of this study wasto recover protein from pollock surimiprocessingwash-water using membrane filtration and characterize properties of the recovered mate-rial. A pilot unit equipped with membrane elements concentrated protein from thesurimi wash-water. Membrane concentrate and control surimi samples were ana-lyzed for proximate composition, lipid oxidation, color, sodium dodecyl sulfate gelelectrophoresis,amino acids and minerals.Membrane concentrate,membrane con-centrate plus surimi and control surimi were monitored for 180 days of storage at-20C. The membrane concentrate had significantly higher moisture and lipid, butlower protein content than surimi. As determined by sodium dodecyl sulfate poly-acrylamide gel electrophoresis, membrane concentrate proteins displayed a greateramount of lower molar mass molecules compared with surimi. The amino acidprofile was comparable to control surimi and the recovered membrane concentrateproteins had similar nutritional valuesto that of surimi. Theresults indicate that theaddition of 5% membrane concentrate to surimi willnotadversely affect thestorageat -20C and that the recovered wash-water protein could be used to obtain a fishprotein 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 andother material from the wastewater. Membrane filtration is a promising option forthe concentration of wastewater. This study was conducted to determine the recov-ery and characterize the material recovered from surimi wash-water using a com-mercial membrane filtration unit.It was demonstrated that the recoverable materialis nutritionally similar to the final surimi product and that the overall yield can beincreased using membrane technology. In addition to the benefit of recoveringprotein, the membrane filtration can reduce the amount of material in the waste

stream.

INTRODUCTION

Surimi is basicallyconcentrated myofibrillarproteinobtainedfrom fish flesh that has been extensively washed with coldwater.Surimi isa raw foodingredientusedin a varietyof prod-

uctsthathavebecomeincreasinglypopularduetotheiruniquetextural properties, storage properties and high nutritionalvalue (Akilet al. 2008; Park and Morrissey 2000; Bourtoomet al. 2009). In the industrial surimi manufacturing process,mincedfleshisrepeatedlywashedwithchilledwatertoremove

Journal of Food Quality ISSN 1745-4557

43Journal of Food Quality35(2012) 4350 2012 Wiley Periodicals, Inc.

RECOVERY AND UTILIZATION OF PROTEIN DERIVED FROM


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sarcoplasmic proteins, lipids and lower molar mass watersoluble materials,leaving a tasteless and odorless myofibrillarproteinproduct.

Although this washing process effectively lowers manyenzymes associated with muscle protein degradation, theprotein material washed-free has a number of potential uses.

Surimi wash-water typically contains 0.52.3% protein (Linet al. 1995; Morrisseyet al. 2000; Park and Morrissey 2000).However, new and different technologies are needed torecover these proteins economically.

In the seafood industry, solidwaste from surimi processingis usually converted to fishmeal. However, liquid waste withlow solids content is often discarded into the plants wastestream (Chang-Leeet al. 1989; Linet al. 1995). The process-ing of Pacificwhiting,Alaskan pollock andshrimp in Oregon,Alaska andWashingtongenerates 20 million tons/year of pro-cessing water (Park and Morrissey 2000). Increasing concernsover the negative impact of wastewater discharge have led toresearch in protein recovery from surimi wash-water. Aneffective method to recover fish proteins from surimi wash-water would not only reduce the negative environmentalimpact and the cost of waste disposal, but could also lead tonew ways to generate profit. Recovered protein could bereturned to the process to increase final surimi yield.Figure 1illustrates a mass balance for fish solids in a typical surimi

processing facility, including an alternative membrane filtra-tion concentration for press-water. Overall, the mass balancewill vary depending on species, harvesting season and plantoperations. In all cases, the loss of fish solids in wash-waterduring surimi washing remains significant.

There have been several studies on recovering proteins

from surimi processing wash-waters. Ultrafiltration has beenused to produce protein concentrates with good functionalproperties via myofibrillar proteins recovered from surimiwash-water (Morr 1976; Chang-Lee et al. 1989; Lin et al.1995; Morrisseyet al. 2000). Severe fouling of the membraneshas been a frequent problem (Morr 1976). Huang and Mor-rissey (1998) evaluatedthe microfiltrationmembranefoulingby surimi wash-water andreported that fouling occurred ini-tially as a result of pore blocking resistance followed by cakeresistance. Jaouen and Quenmeneur (1992) noted that pro-cessing of surimi wash-water by ultrafiltration without pre-treatment was not practical. However, Mireles Dewitt andMorrissey (2001) showed that large molar mass proteins thatinterfered with ultrafiltration could be removed by firstadjusting wash-water acidity to pH 6 and then applying arapid heat treatment to raise the temperature to 60C.

Attempts to combine ohmic heat treatments with ultrafil-tration on surimi wash-water were also investigated. Huanget al. (1997, 1998) studied the effect of ohmic heating (70C)on protein coagulation in surimi wash-water and found thatthe wash-water-soluble protein could be removed; however,an important consideration was the possibility of retainingproteolytic activity after mild heat treatment. Some proteasestend to be stable, so there is a likelihood of recovered undena-tured enzymes adversely affecting the final product (Scopes

1994).Many proteins have been employed to improve the

mechanical properties of surimi gels. The most frequentlyused are egg white and whey protein concentrates; othersources such as leguminous extracts and porcine plasmaprotein have also been proposed. These proteins are added toinhibit the proteolytic degradation of fish myosin when gelsare incubated at 60C, and to favor gel setting by the action ofendogenous 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 (Afonsoet al. 2004). If the recovered protein was added back to thesurimi cake it would increase productivity and generategreater revenues (Afonsoet al. 2004). The objectives of thisproject were: (1) evaluation of the potential for applyingmembrane filtrationtechnology to the recovery of the proteinfrom surimi wash-water; (2) the chemical characterization ofthe recoveredprotein;and(3) the evaluationof the propertiesof the concentrated recovered protein when added back tosurimi prior to a 180-day frozen storage study.

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.).

RECOVERY OF PROTEIN FROM SURIMI WASH-WATER J.J. STINEET AL.

44 Journal of Food Quality35(2012) 4350 2012 Wiley Periodicals, Inc.


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MATERIALS AND METHODS

Membrane Filtration Unit and Samples

Membrane filtrationwas conducted on wash-water generatedby the standardsurimi processing technology usedin Alaskan

seafood processing plants. The tests were initiated immedi-ately after collection of samples, and the filtration test wascarried out maintaining the wash-water temperature (4C).

For this study, a spiral wound 8-in. filtration modulemanufactured by Kelitec Engineering (Laguna Hills, CA) wasused. Tests were carried out at Westward Seafoods Unalaska,Dutch Harbor, AK plant during the Pollock(Theragra chalco-

gramma) B season utilizing the pilot plant-sized membranefiltration unit equipped with two membrane elements. Themembranes had a nominal pore size of 80 kDa,and themem-brane substratewas polyacrylicnitrile (PAN).This configura-tion provides a compact, cost-effective membrane systemwhere high cross flow rates are required while avoiding pre-mature protein-induced fouling.

Samples obtained from Westward Seafoods Inc. in DutchHarbor, AK, were shipped frozen to Fairbanks,AK, for analy-sis. The five composite samples were (1) pollock surimiserving as a negative control; (2) pollock surimi with 5%membrane concentrate (MC) added; (3) pollock surimi with7% sorbitol and 0.25% polyphosphate added as a cryopro-tectant control; (4) pollock surimi with 7% sorbitol and0.25% polyphosphate as cryoprotectants and 5% MC added;and (5) 100% MC. Samples were stored at -20C until evalu-ated. Three subsamples were taken for each analysis.

Proximate Analysis

Proximate composition was determined in quadruplicate foreach sample. Moisture and ash content were determinedusingAOAC methods 952.08 and 938.08, respectively (AOAC1980). Nitrogen content was determined by pyrolysis with aRapid N3 (Elementar America Inc., Mt. Laurel, NJ) nitrogenanalyzer. Protein content was calculated as 6.25 times %N.Total lipid content was determined gravimetrically by theFolch method (Folch et al. 1957). After lipid extraction, thesolvent was removed at 50C under a N2gas stream using aTurboVap LV (Caliper Life Sciences, Hopkinton, MA).

Electrophoresis

The sodium dodecyl sulfate polyacrylamide gel electrophore-sissystem(SDS-PAGE)wasusedwithaPhotodyneFoto/Force300 electrophoresis apparatus under reducing conditionsaccording to SchaggerandVon Jagow (1987).Precast1020%Tricine gels (Novex, Invitrogen, Carlsbad, CA) were used andmolar mass standards were purchased from Sigma-Aldrich.

The protein bands were visualized from the gels stained withCoomassieblue(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 with6 N HCl and 2% phenol at 110C for 22 h. Amino acids werequantified using the Beckman 6300 analyzer with postcol-umn ninhydrin derivatization. Tryptophan and cysteinecontent were not determined.

Samples for mineral analysis were sent to the University ofAlaska Fairbanks School of Natural Resources and Agricul-tural Sciences Palmer Research Center (Palmer, AK). Thesamples were ashed overnight at 550C. Ashing residues weresubsequentlydigestedovernight in aqueous solutioncontain-ing 10% (v/v) hydrochloric acid and 10% (v/v) nitric acid.Digested solutions were diluted as needed and analyzed forCa, Cu, Fe, K, Mg, Mn, Na, P and Zn by inductively coupled

plasma optical emission spectroscopy on a Perkin ElmerOptima 3000 Radial ICP-OES (Perkin Elmer, Boston,MA).

Whiteness

Surimi color and whiteness are important factors affectingproduct quality and,ultimately, price. Cookedsurimi sampleswere chopped with a spatula, placed on a Hunter Lab Color-flex instrument, and L*(lightness), a*(red-green color),b*(yellow-bluecolor) values were recorded.Four replicates ofeach 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,whichnwas: day 0=2, day 30=2, day 90=4, day 180=3.

Lipid Oxidation

The procedure was modified from Siu and Draper (1978).TBAreagentwas prepared by adding 300 mg 2-thiobarbituricacid (TBA,MP Biomedical,Solon,OH) into 100 mL DI.Five-grams of sample was mixed with 20 mL of 6% TCA (Fisher

Scientifics, Fairlawn, NJ), homogenized using a Turrax for90 s at 11,000 rpm then centrifuged at 10,000 g for 15 min.The supernatant was filtered through Whatman #4 filterpaper. Two milliliters of the filtrate was mixed with 2 mL TBA

reagent, heated for 20 min at 94C, cooled to room tempera-ture, and the absorbance was measured at 531 nm. Sampleswere compared with a standard curve of malonaldehyde bis-(dimethyl acetal) (MDA, ACROS, Geel, Belgium). Values areexpressed 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

J.J. STINE ET AL. RECOVERY OF PROTEIN FROM SURIMI WASH-WATER



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samples, a small amount was removed for day 0 analysis. Theremaining sample was placed inside whirl pack bags andstored in a commercial freezer at -20C until analysis.

Statistical Analysis

The averages and standard deviations were calculated usingExcel (Microsoft). For tests of statistical difference betweendata sets, the data were subjected to analysis of variance fol-lowed 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

Selectionof the filter membranemolecular cutoff determinesthepercentageand typeof product recovered as well as thefil-tration rate. Small-scale preliminary tests carried out at theFishery Industry Technology Center in Kodiak, AK, foundthatmembranes with a molecularcutoff of 50 kDa resultedin

recovery of approximately 80% of the protein contained inthe wash-water while salts andsmaller organic molecules stillpassed through the membrane. Experiments indicated thatmembranes with a molecular cutoff between 50 and 100 kDaachieved a good balance between recovery andfiltration rates(flux). Selection of the appropriate membrane material alsodetermines the methods required to clean the membraneeffectively between runs. Ceramic and polymeric PAN Mseries (polyacrylic nitrile) membranes were found to havesuperior performance under the conditions employed here.

The filtration rate obtained for two consecutive days ofoperation in a commercial surimi plant is shown in Fig. 2. Intest 1, the initial feed volume was 2,850 L concentrated to420 L over an 8-h period. In test 2, the initial volume was also2,850 L, this time concentrated to approximately 200 L over a7-h period, which resulted in a highly viscous concentrate.

The test showed that high cross flow rates (340 L/min perelement) 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 withoutshowing any noticeable degradation.

The viscosity of the recovered product increased rapidly atconcentrations greater than 10% solids. At 14% solids, therecovered product became very thick and difficult to pump.The upper concentration limit with the applied membranesystem was approximately 12% solids. The solids content ofboth the feed and the concentrate is shown in Table 1.

With the 80 kDa cutoff, product recovery was approxi-mately 75% of the solids. This resulted in the recovery of theproduct containing the higher molar mass molecules, whilethe salts and smaller organic molecules still pass through this

type of membrane. The protein content in the recoveredproduct wassimilar to that of surimiwhenadjustedfor differ-ent moisture content.

Proximate Analysis

The initial proximate analyses of the five surimi samples arepresented in Table 2.Thecomposition of MC wasverysimilarto previously published results for recovered protein fromsurimi wastewater (Lin et al. 1995).The MC hadsignificantly

0

2

4

6

8

10

12

0 2 4 6 8 10 12 14 16 18Flux(liters/squaremeter/hour(lmh)

Time (1 unit = 0.5 hrs)

Dehydator/Screw press water concentration by

membrane filtration

Flux 1A

Flux 2A

Flux 1B

Flux 2BToo viscous

to pump

PAN membranes

Two8" modules operated in series

Transmembrane pressure 8 psi

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/m 2/h). PAN, polyacrylic nitrile.




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higher moisture and lipid content, and lower protein contentthan the surimi samples. There was no difference in the ashcomposition of the samples.

Electrophoresis

The SDS-PAGE analysis of surimi samples is presented inFig. 3A,B. The banding pattern for the gels analyzing storageday 0 for cryoprotected surimi and cryoprotectedsurimi+5%MC agreeswellwithpreviously publishedgels ofsurimianalog crabstick product prepared withAlaska pollocksurimi (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 chainbands located between 20 and 13 kDa, while the MC showedonly trace amounts of protein at these molar masses. Theabundance of low molar mass bands in the MC is in agree-mentwith previously publishedresults (Linet al. 1995; Bour-toomet al. 2009). Few differences were seen between the gelsloaded with samples from day 0 (Fig. 3A) and day 180(Fig. 3B), indicating protein stability.

Mineral Analysis and Amino Acid Analysis

The amino acid profile of normal surimi (1a) and MC (3) ispresented in Table 3.Values for three of the basic amino acidswere 9.0% for lysine, 6.1% for arginineand 2.9% for histidine.Methionine (3.5%) and phenylalanine (6.8%) concentra-tionsinMCwerehigherthaninpreviouslypublishedfishandsoy meal analyses (Ohshimaet al. 1993; Wibowoet al. 2005).Theseresults indicate theMC, in termsof aminoacid compo-sition, has values comparable with surimi. The percentage oftotal essential amino acids andtotal nonessential amino acidsin MC was 45.0 and 55.0%, respectively.

TABLE 1. ANALYTICAL RESULTS OF FILTRATION TESTS

Feed Concentrate Init vol. Final vol. Concentration

factor

Solids feed Solids conc. Solids recovered

(% solids) (% solids) (L) (L) (kg) (kg) (% of start)

Test 1 2.1 10.5 2,843 416.9 6.8 226.2 165.9 73.3

Test 2 1.3 13.7 2,843 208.5 13.6 140.0 108.2 77.3

Thesolids content in thefeedand concentrate is shown in Table 1. Duringthe test thevolume was reduced by a factorof 6.8- and13.6-fold,respectively.

TABLE 2. DAY 0 PROXIMATE COMPOSITION

OF SURIMI SAMPLES Sample Moisture (%) Ash (%) Lipid (%) Protein (%)

Surimi control 81.12 0.75a 0.35 0.06a 0.13 0.04a 18.38 0.17a

Surimi+ 5% MC 80.70 0.60a 0.30 0.10a 0.12 0.02a 20.58 0.89b

Cryoprotected surimi 75.76 0.43b 0.28 0.24a 0.05 0.03a 18.10 0.65a

Cryo + 5% MC 75.39 0.23b 0.44 0.11a 0.10 0.08a 18.50 0.64ab

MC 86.70 1.31c 0.59 0.12a 1.09 0.27b 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.

A B

210KDa

90KDa

65KDa

30KDa

8KDa

13KDa

20KDa

40KDa

Lane 1 2 3 Lane 1 2 3

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).




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The mineral composition of normal surimi, cryoprotectedsurimi and MC is presented in Table 4. The mineral concen-trations were similar for surimi and MC; however, higherlevels of Fe, Zn and Cu were present in MC.

Whiteness and Lipid Oxidation

Whiteness data are reported at storage time points over the180 days in Fig. 4. The color of the MC appeared slightlydarker than the other surimi samples for all storage with

values ranging from 55 to 60. The darker color was also con-sistent with the higher Fe values for MC. Whiteness in surimiandsurimi withadded MC didnot decreasedramatically overthe 180 days of storage (P< 0.05).

Theextent of lipid oxidation over thestoragetime is shownin Fig. 5. At day 180, the TBA values in all samples are higherthanthosefoundinallprevioussamplings.Also,theMChasahigher amountof MDA present in all samples compared withtheothertreatments. This canbe explained bythe higherlipidcontent in the MC and possibly the increased Fe in this frac-tion. The results indicate that lipid oxidation increases withtime and samples with higher lipid levels show greater lipidoxidation. TBA values did increase in most treatments withstorage time although generally not significant. There was atrend for higher TBA values in surimi with added MC thansamples where MC was absent.

TABLE 3. COMPARISON OF AMINO ACID PROFILE OF POLLOCK SURIMI

AND MEMBRANE CONCENTRATE

Surimi MC

Ave. SD Ave. SD

ALA 5.8 0.10 6.3 0.16

ARG 7.7 0.04 6.1 0.01

ASP 11.1 0.03 12.6 0.17

GLU 15.4 0.21 11.2 0.13

GLY 3.6 0.04 4.45 0.06

HIS 2.4 0.01 2.9 0.03

ILE 5.6 0.04 5.6 0.01

LEU 9.3 0.09 9.2 0.02

LYS 10.4 0.10 9.1 0.02

MET 3.8 0.02 3.5 0.02

PHE 4.3 0.02 6.8 0.15

PRO 1.8 0.09 3.5 0.01

SER 3.9 0.11 4.0 0.04

THR 4.7 0.06 4.5 0.03

TYR 4.6 0.03 3.9 0.02

VAL 5.7 0.09 6.5 0.08

TEAA % 43.7 45.0TNEAA % 56.2 55.0

wt/wt % total amino acids measured.TEAA is total essentialamino acids.

TNEAA is total nonessential amino acids.

MC, membrane concentrate; Ave., average; SD, standard deviation.

TABLE 4. MINERAL COMPOSITION OF SURIMI SAMPLES

Minerals

Surimi Surimi + Cryo + 5% MC MC

Average SD Average SD Average SD

P (%) 0.26a 0.01 0.36b 0.01 0.70c 0.03

K (%) 0.23a 0.03 0.18a 0.02 0.39b 0.03

Ca (%) 0.15a 0.01 0.12b 0.01 0.22c 0.01

Mg (%) 0.14a 0.00 0.11b 0.01 0.17c 0.01

Na (ppm) 2,724a 45 3,473b 144 3,791b 245

Cu (ppm) 0.95a 0.26 0.56a 0.16 4.35b 0.08

Zn (ppm) 19a 1.73 14b 0.00 39.33c 2.08

Mn (ppm) 1.33 0.58 ND ND 1 0

Fe (ppm) 8a 5.66 1.5a 0.71 47.33b 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.

Day0

Day0

Day

0

Day

0

Day0

Day30

Day30

Day30

Day30

Day30

Day90

Day90

Day90

Day90

Day90

Day180

Day180

Day180

Day180

Day180

0

10

20

30

40

50

60

70

80

C C+MC Cryo Cryo+MC MC

Whiteness

Whiteness During 180 Storage Days at 20C

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

TIME

Whiteness calculated as described in METHODS section. C, control

surimi; MC, membrane concentrate.

0

2

4

6

8

10

12

14

16

C C+MC Cryo Cryo+MC MC

M

DA(mg/g)

Lipid Oxidation versus Storage Days

Day 0

Day 30

Day 90

Day 180

a a a aa a a a

a a a aa a a a

b b b

b

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.




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Storage Study

There were no dramatic changes in proximate composition,minerals, amino acids or whiteness over the 180 days of thestudy. There was however noticeable increase in lipid oxida-tion at day 180 as determined by TBA values, especially inthe MC. This is consistent with previous results demonstrat-ing that higher lipid values result in increased oxidation(Matsushitaet al. 2010). However, the results indicate thatthe addition of MC to surimi will not adversely affect thestorage at -20C.

CONCLUSIONS

Solids from surimi wash-water were successfully recoveredusing an ultrafiltration system. Protein concentrates recov-ered in these experiments had a significantly higher mois-ture and lipid content when compared with surimi. The

proteins concentrated by membrane filtration displayed alarger number of lower molar mass compared with surimi.The amino acid profiles of the MC were comparable to thatof surimi. The results indicate that the addition of 5% MCto surimi will not adversely affect the storage at -20C. Fromthe results of this study, it is possible that the recoveredwash-water protein could be used to obtain a fish proteiningredient or added back at a low percentage to surimiproducts.

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