JFS C: Food Chemistry

Negative Roles of Salt in Gelation

Properties of Fish Protein Isolate

C: Food Chemistry
Y.S. KIM AND J.W. PARK

ABSTRACT: Salt effect on gelling properties of fish protein isolate (FPI) prepared by acid- and alkali-aided extrac-
tion was investigated. Acid- or alkali-extracted FPI formed significantly better gel texture with 0% NaCl than with 3%
NaCl. Texture properties of acid- or alkali-extracted FPI decreased as NaCl content increased, especially at 2% to 3%
salt. Contrarily, salt significantly promoted texture qualities of conventional surimi gels. The effect was highlighted
when they were subjected to low temperature setting. The myofibrillar proteins in FPI were not solubilized when
NaCl was added, perhaps due to protein aggregation caused by acid or alkali extraction. FPI solubility, however, was
not closely related to their texture properties. Cold setting did not promote texture properties of FPI gels as much as
conventional surimi gels. Acid-extracted gels gave the best color properties.
Keywords: Alaska pollock, fish protein isolate, pH shift, salt, texture

Introduction made from Alaska pollock (Theraga chalcogramma) was used as a

F or the conventional method of surimi gel preparation, salt is

required to extract myofiblillar proteins and to obtain desired
texture upon cooking. Almost all surimi seafood are manufactured
with salt at 1% to 2.5% for the purpose of maintaining taste, tex-
ture, and microbial safety. However, 1 undesirable factor in surimi
seafood is its relatively high sodium content. Recent trends indi-
cate many consumers are interested in reducing their sodium in-
take. Thus, the salt content of surimi seafood deserves considerable
attention (Chang and others 2001).
New approaches in isolating fish protein isolate (FPI) using
strong acid and/or alkali have received profound interests (Hultin
1999; Choi and Park 2002; Kim and others 2003, 2005a; Kristinsson
and Hultin 2003a, 2003b; Thawornchinsombut and Park 2005, 2007;
Park and others 2008). These methods, even without salt addition,
induce protein unfolding by pH-driven solubilization and subse-
quent partial refolding by isoelectric precipitation and further pH
adjustment to the neutrality. Consequently, if myofibrillar proteins
are unfolded as shown in our studies on acid- and alkali-extracted
FPI (Choi and Park 2002; Kim and others 2003; Thawornchinsom-
but and Park 2005), salt addition may not be necessary for the ex-
posure of reactive binding sites of myofibrillar proteins.
Our hypotheses in dealing with fish protein isolate (FPI) were:
(1) salt may not be required for the gelation of acid- and alkali-
extracted FPI, and (2) the effect of cold setting may be reduced for
the gelation of FPI because FPI is chemically damaged due to strong
acid or alkali. The resulting objective was to investigate the role
of salt in the gelation and the effect of setting of acid- and alkali-
extracted FPI.
Materials and Methods
Materials and sample preparation
Due to the seasonal availability of fresh fish samples, frozen
surimi (12 mo old) (American Seafoods, Seattle, Wash., U.S.A.)
MS 20080218 Submitted 3/25/2008, Accepted 7/8/2008. Dept. of Food Science
& Technology, Seafood Research and Education Center, Oregon State Univ.,
2001 Marine Dr. #253 Astoria, OR 97103, U.S.A. Direct inquiries to author
Park (E-mail: Jae.Park@oregonstate.edu).
raw material instead fresh fish mince. After partially thawing, the
surimi was homogenized (Power Gen 700, GLH 115, Fisher Scien-
tific Inc., Pittsburgh, Pa., U.S.A.) with distilled water at a 1:9 ratio
for the acid or alkali treatment. The acid or alkali treatment was
obtained using 2N HCl or 2N NaOH to adjust to pH 2 or 11, re-
spectively. Then the pH of the acidic or alkaline homogenates was
readjusted to 5.5. Dewatering was conducted using centrifugation
(4000 × g, 20 min). The precipitate was collected as fish protein iso-
lates (FPI). FPI was then mixed with cryoprotectants (5% sucrose,
4% sorbitol, and 0.3% sodium tripolyphosphate) using a food pro-
cessor (Model 702R, Hamilton Beach, Mexico City, Mexico) and the
pH was adjusted to approximately 7 using 2N NaOH. All samples
were prepared in a walk-in cold room (4 to 5 ◦ C) to avoid pos-
sible protein denaturation caused by high temperature. FPI was
vacuum-packed and stored at –30 ◦ C until used.
Gel preparation and analysis
Conventional surimi and FPI was comminuted with 0%, 1%,
2%, or 3% salt and adjusted to 78% moisture content (Kim and
others 2003). The pH of all samples was adjusted to 7 using 1N
NaOH. The paste was stuffed into stainless steel tubes (2 cm di-
ameter). To observe the setting (suwari) effect, the samples were
divided into 2 parts. One was cooked at 90 ◦ C in a circulating wa-
ter bath for 15 min immediately after stuffing. The other was kept
at 5 ◦ C for 16 to 18 h followed by cooking at 90 ◦ C for 15 min.
Cooked gels, after chilled in ice water for 15 min, were refrigerated
overnight.
Before conducting texture analysis, gel samples were equili-
brated to room temperature after keeping them at room temper-
ature for at least 2 h. Texture properties were measured by the pen-
etration test using a Sintech machine (Sintech 1/G, MTS, Cary, N.C.,
U.S.A.), which was equipped with 5 kg load cell. The test was done
using a 5 mm spherical probe and a crosshead speed of 1 mm/s.
Breaking force (g) and deformation (mm) at fracture were recorded.
A CIE Lab color scale was used to measure the degree of lightness
(L∗ ), redness or greenness (a∗ ), and yellowness or blueness (b∗ ) of
gels using a tristimulus colorimeter (Model CR-300, Minolta, Osaka,
Japan). The instrument was standardized using calibration plates.


C 2008 Institute of Food Technologists
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Vol. 73, Nr. 8, 2008—JOURNAL OF FOOD SCIENCE C585
doi: 10.1111/j.1750-3841.2008.00900.x
Further reproduction without permission is prohibited
 Acid- and alkali-extracted fish protein isolate . . .

Whiteness was calculated using the whiteness index L∗ – 3b∗ (Park or tears of the muscle fibers during comminuting. The dissoci-
1994). ated myosin participates in gel matrix formation and binds water
(Park and others 1996). The greatest gelling effect of Pacific whiting
Solubility measurements surimi at neutral pH was obtained at 2.5% NaCl among the salt con-
Solubility of surimi and FPI was determined in 2 different solu- centrations tested between 0% and 2.5% (Chung and others 1993).
tions; 20 mM tris-HCl (pH 7) and 20 mM tris-HCl (pH 7) containing This phenomenon was not observed at 3% NaCl in this study. It
0.6 M NaCl. Surimi sols (3 g), (moisture content adjusted to 78%) was probably due to the use of aged, frozen surimi (12 mo old).
C: Food Chemistry

was mixed and homogenized with 27 mL of the above solution us- The proteins might have been partially damaged (unfolded) during
ing a homogenizer (Power Gen 700, GLH 115, Fisher Scientific Inc., long term frozen storage. Alterations in myofibrillar proteins (that
Pittsburgh, Pa., U.S.A.). The sample solutions were centrifuged at is, protein solubility) and their functionality have been observed in
27000 × g at 4 ◦ C for 20 min. The supernatant was subjected to the frozen muscle and isolated protein systems, resulting in decreased
Bradford dye binding method for protein determination (Bradford gel-forming ability of Alaska pollock surimi (Park and others 1988).
1976). Unlike CS, both breaking force and deformation values de-
creased in acid-extracted fish protein isolate (FPI) and alkali-
Salinity extracted FPI as NaCl content increased (P < 0.05) (Figures 2 and
3, respectively). These results were in accordance with the study by
Salinity was evaluated to determine the difference between con-
Pérez-Mateos and Lanier (2006). After adding 2% salt, gel strength
ventional surimi gels and acid- or alkali-extracted FPI gels. Salinity
of Atlantic menhaden FPI without setting declined, while gel strain
was measured using a conductivity meter (YSI Model 3100, Yellow
increased. Both acid- and alkali-extracted FPI could be less and
Springs, Ohio, U.S.A.) after homogenizing gels with 20-fold deion-
ized water and filtering through Whatman nr 54 filter paper (Kent,
England). A standard curve was made using 0.005% to 0.05% NaCl
solutions.

Statistical analysis
Data were analyzed for the degree of variation and significance
of difference based on the analysis of variance (ANOVA) with
Tukey’s pair-wise comparison test to determine differences (P ≤
0.05) between treatment means. This was done using S-Plus 2000
Professional Release 3 (MathSoft Inc., Seattle, Wash., U.S.A.).

Results and Discussion

B reaking force indicates the strength of gels, while deforma-
tion denotes the cohesiveness (Kim and others 2005b). The
gel cohesiveness of conventional surimi (CS) without setting was
enhanced when 1% to 3% salt was added (Figure 1). However, the
strength of those surimi gels was not affected by salt addition. The
primary function of salt is actually to solubilize the myofibrillar
proteins and subsequently to induce their bonding to form a gel.
Salt also increases dissociation of actomyosin through physical cuts
Figure 2 --- Texture properties of acid-extracted FPI gel at
various salt concentrations. Nonsetting = 90 ˚C cooking
for 15 min, Setting = set gel at 4 ˚C setting for 16 to
18 h followed by cooking at 90 ˚C for 15 min. Different
upper and lower case letters indicate a significant dif-
ference (P ≤ 0.05) between treatment combinations of
deformation and breaking force, respectively.

Figure 1 --- Texture properties of conventional surimi gel
at various salt concentrations. Nonsetting = 90 ˚C cook-
ing for 15 min, Setting = set gel at 4 ˚C for 16 to 18 h fol-
lowed by cooking at 90 ˚C for 15 min. Different upper and
lower case letters indicate a significant difference (P ≤
0.05) between treatment combinations of deformation
and breaking force, respectively.
Figure 3 --- Texture properties of alkali-extracted FPI gel
at various salt concentrations. Nonsetting = 90 ˚C cook-
ing for 15 min, Setting = set gel at 4 ˚C setting for 16 to
18 h followed by cooking at 90 ˚C for 15 min. Different
upper and lower case letters indicate a significant dif-
ference (P ≤ 0.05) between treatment combinations of
deformation and breaking force, respectively.

C586 JOURNAL OF FOOD SCIENCE—Vol. 73, Nr. 8, 2008

Acid- and alkali-extracted fish protein isolate . . .
more solubilized in tris-HCl buffer with and without 0.6 M NaCl,
respectively, when compared to CS (Table 1). The ratio of pro-
tein solubility in buffer with 0.6 M NaCl to without 0.6 M NaCl
(B/A, Table 1) of CS was larger than both FPI by approximately 4.7
times. Thus, NaCl did not make a large contribution to the solubi-
lization of myofibrillar proteins in both acid- and alkali-extracted
FPI as compared to CS. Studies conducted at our laboratory (Tha-
wornchinsombut and others 2006; Thawornchinsombut and Park
2007) demonstrated that alkali-extracted FPI can form a gel at a
neutral pH without adding salt or at physiological ionic strength
(150 mM NaCl). It is perhaps due to the reorientation of protein
molecules as a result of pH adjustments. A study using Raman spec-
troscopy with globular proteins found that, when a gel is formed,
there is a tendency for the β-sheet content to increase with a si-
multaneous decrease in α-helix content (Clark and others 1981).
The less α-helix and greater β-sheet contents of alkali-treated FPI
than CS may explain its ability to form gels at a neutral pH without
adding salt (Thawornchinsombut and others 2006). Furthermore,
the Raman spectroscopy study also revealed that several amino
acid side chains and peptide backbones of alkali-extracted rock-
fish protein isolates were more exposed in comparison to those of
the CS (Thawornchinsombut and others 2006). As a result, more
protein–protein interactions could be induced. Since salt promotes
the role of hydrophobic interactions (Lanier 2000), acid- and alkali-
extracted FPI would have more hydrophobic residues exposed
upon salt addition. Therefore, the addition of salt into FPI possibly
leads to protein aggregation prior to gel network formation.
Our results showed that the cohesiveness of CS gels increased
when 1% NaCl added and no further increase was observed at 2%
and 3% (Figure 1), while both cohesiveness and strength of FPI gels
decreased as salt addition increased from 0% to 3% (Figures 2 and
3). With 3% salt addition, gel strength was extremely soft (Figures 2
and 3). It indicates that 3% salt addition to FPI, which were chem-
ically unfolded, could have induced salting-out effect at the rela-
tively low salt concentration.
In conventional surimi gel, low temperature setting did not pro-
mote texture qualities of gel when salt is not added. On the other
hand, salt addition induced the setting effect (Figure 1). Niwa
and others (1991) found that gel strength of Alaska pollock surimi
(added salt) set at 10 ◦ C increased by about 3 times after 48 h in-
cubation, but little increase of gel strain was noted. In our current
research, cold setting (4 ◦ C, 16 to 18 h) enhanced breaking force of
salted Alaska pollock gels by approximately 3.5 to 5 times and de-
formation by approximately 1.3 to 1.4 times. In addition to covalent
dipeptide (lysine and glutamic acid) linkages, which were initiated
by endogenous transglutaminase, intermolecular hydrophobic in-
teractions probably contributed to the low temperature setting re-
action (Lanier 2000). Setting induces conformational changes in
Table 1 --- Salinity and solubility of Alaska pollock proteins
in 3 different forms.
Solubility (mg/mL)
Salinity Tris A Tris B
(mM) (0 M NaCl) (0.6 M NaCl) B/A
Conventional 52.1 ± 2.2 0.77 ± 0.01 4.62 ± 0.03 6.00 ± 0.05
surimi
Acid-aided FPI 36.0 ± 0.6 1.39 ± 0.04 1.76 ± 0.00 1.27 ± 0.03
Alkali-aided FPI 29.6 ± 1.4 1.85 ± 0.00 2.39 ± 0.02 1.29 ± 0.01
Salinity measurement was performed using surimi gels prepared without salt.
Solubility measurement was conducted using surimi paste prepared without salt.
Tris A: tris-HCl buffer (pH 7) containing 0 M NaCl; Tris B: tris-HCl containing
0.6 M NaCl.
B/A: The ratio of protein solubility of sample in Tris A to Tris B.
the protein molecules by localized exposure and subsequent inter-
action of hydrophobic amino acid residues, resulting in the forma-
tion of a stronger gel (Park and others 1996). The requirement of salt
addition to surimi paste for inducing setting also supports the role
of hydrophobic interactions because certain salts, such as sodium
chloride, act with water molecules to strengthen the hydrophobic
interactions between proteins (Lanier 2000).
C: Food Chemistry
Gels made from acid- and alkali-extracted FPI were generally
of poorer quality than those made with CS with added salt and
cold setting. However, under nonsetting condition, both acid- and
alkali-extracted FPI without salt exhibited stronger gels (breaking
force of 305 g and 325 g, respectively) than CS with 2% NaCl (230 g
breaking force). This was concomitant with several reports of pH-
shifted protein isolates (Undeland and others 2002; Kristinsson and
Hultin 2003b; Pérez-Mateos and others 2004; Yongsawatdigul and
Park 2004).
The reduced effect of setting was observed in acid- and alkali-
extracted FPI. Comparing to CS, the setting effect was consider-
ably low. This observation indicates that endogenous transglutam-
inases, which play a major role in setting (Pérez-Mateos and Lanier
2006), could have been damaged during acid or alkali extraction.
The least enhancement of gel strength was seen in the FPI without
NaCl (Figures 2 and 3).
During acidic or alkaline treatment, salinity did not increase
(Table 1) indicating that HCl and NaOH were chemically neutral-
ized and salt was released with water. In fact, the salinity values
of FPI were significantly lower than that of surimi. This may be an
added value in preparing low sodium gel products if FPI is used as
a raw material.
Color properties of CS gel and FPI gels are shown in Table 2.
The a∗ values were relatively constant regardless of salt concen-
tration and setting effect in all surimi gels. Park (1994) reported
that a∗ value of pollock and whiting gel was very consistent regard-
less of cooling/setting conditions, moisture content, sample size, or
frozen storage. No significant difference of the L∗ values for acid-
or alkali-extracted FPI was found at various salt concentrations
(P > 0.05). The b∗ values, however, gradually decreased as salt con-
centration increased in acid- or alkali-extracted FPI gels. In addi-
tion, as the b∗ value decreased, whiteness values increased. Acid-
extracted FPI gel gave the highest whiteness values under the same
salt and setting conditions. However, it should be pointed out that
the raw material used to make the acid- and alkali-extracted FPI in
this study was commercial surimi that did not contain sarcoplasmic
proteins washed off thoroughly during processing.
Protein may form a gel that appears either turbid or translucent
depending on the processing conditions. Manipulation of environ-
mental conditions can be used to change the gel properties (Chris-
ten and Smith 2000). For the CS, the lightness of nonset gel in-
creased significantly when 1% salt was added (Table 2). However,
additional salt addition did not change the lightness. In the for-
mation of surimi gel, partially unfolded or solubilized myofibrillar
proteins, which are obtained through comminuting with salt, are
transformed into gel network by cooking immediately or letting set
before cooking. Without suitable time of setting, polypeptides can
form a gel network (Matsumura and Mori 1996) resulting in opaque
gel with high L∗ value. When the optimum level of salts (2% and
3% NaCl) was added, L∗ value of CS gels decreased after setting
(Table 2). This was probably caused by long incubation of salted
surimi paste. Well-organized network resulted in translucency and
gave less light reflectance.
In both setting and nonsetting conditions, whiteness of CS and
FPI gels prepared without salt were not different (P ≥ 0.05). An in-
crease in salt content resulted in greater whiteness values (Table 2).
Vol. 73, Nr. 8, 2008—JOURNAL OF FOOD SCIENCE C587
 Acid- and alkali-extracted fish protein isolate . . .

Table 2 --- Color properties of surimi and FPI gels at various salt concentrations.
Nonsetting Setting
Salt (%) 0 1 2 3 0 1 2 3
Conventional surimi L∗ 73.3c 78.2ab 78.3a 79.1a 74.8bc 79.0a 75.9abc 76.8abc
a∗ −4.9bc −4.6ab −4.5ab −4.2a −5.0bc −4.8ab −5.2c −4.9bc
b∗ 1.0ab 2.2a 2.2a 2.4a 1.1ab 2.3a 0.0b 0.7ab
Whiteness 70.4c 71.7c 71.6c 71.9bc 71.6c 72.0bc 75.9a 74.7ab
C: Food Chemistry

Acid-aided FPI L∗ 75.7a 78.0a 77.9a 77.1a 77.8a 78.1a 77.7a 77.0a
a∗ −4.3ab −4.2ab −4.3ab −4.2ab −4.1a −4.4ab −4.4ab −4.5b
b∗ 1.2a 0.7ab −0.2bc −0.4bc 1.4a 0.4abc −0.7c −0.9c
Whiteness 72.2c 76.0ab 78.3a 78.2a 73.6bc 77.1ab 79.6a 79.6a
Alkali-aided FPI L∗ 75.2a 78.2a 77.3a 76.4a 75.2a 78.5a 77.6a 77.0a
a∗ −4.3ab −4.2a −4.3ab −4.4ab −4.3ab −4.3ab −4.5ab −4.7b
b∗ 1.7a 1.8a 1.0ab 0.3ab 1.5a 1.8a 0.6ab −0.5b
Whiteness 70.2c 72.7bc 74.3abc 75.6ab 70.8c 72.9bc 75.9ab 78.6a
Different letters in the same row (within the boxes of nonsetting or the setting) indicate a significant difference (P ≤ 0.05).

Similar finding was observed by Pérez-Mateos and Lanier (2006) in
acid- and alkali-extracted protein isolates (0% and 2% NaCl) from
Atlantic menhaden with or without setting. This was probably due
to protein aggregates induced by incomplete refolding of FPI as
well as ionic strength effects as previously described. High molec-
ular weight protein aggregates could be formed through protein–
protein interaction (mainly via surface hydrophobic interaction)
enhanced by salt addition, thus yielding a turbid gel with high
reflecting light (L∗ ).
Setting also slightly contributed to an increase in whiteness val-
ues across all treatments (P < 0.05) (Table 2). Park (1995) reported
slightly lighter gels were obtained when surimi was subjected to
setting.
Conclusions
Chung YC, Richardson L, Morrissey MT. 1993. Effect of pH and NaCl on gel strength
of Pacific whiting surimi. J Aquat Food Prod Technol 2(3):19–35.
Clark AH, Saunderson DHP, Suggett A. 1981. Infrared and laser-Raman spectroscopic
studies of thermally induced globular protein gels. Int J Pept Prot Res 17(3):353–
64.
Hultin HO. 1999. Process for isolating a protein composition from a muscle source
and protein composition. U.S. Patent 6,005,073.
Kim YS, Park JW, Choi YJ. 2003. New approaches for the effective recovery of fish pro-
teins and their physicochemical characteristics. J Fish Sci 69:1231–9.
Kim YS, Yongsawatdigul J, Park JW, Thawornchinsombut S 2005a. Characteristics
of sarcoplasmic proteins and their interaction with myofibrillar proteins. J Food
Biochem 29:517–32.
Kim BY, Yoon WB, Park JW. 2005b. Rheology and texture properties of surimi gels.
In: Park JW, editor. Surimi and surimi seafood. Boca Raton, Fla.: CRC Press. p 491–
582.
Kristinsson HG, Hultin HO. 2003a. Changes in conformation and subunit assembly of
cod myosin at low and high pH and after subsequent refolding. J Agric Food Chem
51:7187–96.
Kristinsson HG, Hultin HO. 2003b. Effect of low and high pH treatment on the func-
tional properties of cod muscle proteins. J Food Sci 68:917–22.
Lanier TC. 2000. Surimi gelation chemistry. Park JW, editor. New York: Marcel Dekker
Inc. p 249–50.

S alt addition is not necessary for gel formation of acid or alkali-

extracted fish protein isolate (FPI). In fact, salt reduced the gel
strength. It indicates that salt addition to chemically unfolded FPI
could have induced salting-out effect. This could lead a muscle
food manufacturer to develop no or reduced sodium gel foods by
utilizing acid or alkali-extracted FPI. Low temperature setting does
not significantly enhance gel qualities of acid- or alkali-extracted
FPI.
Acknowledgment
This research was partially funded by the Natl. Sea Grant College
Program of the U.S. Dept. of Commerce’s Natl. Oceanic and At-
mospheric Administration under NOAA grand nr NA76RRG0476
(project nr R/SF-24), and by appropriations made by the Oregon
State Legislature. The views expressed herein do not necessarily re-
flect the views of any of these organizations.
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