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New developments in manufacturing of

Surimi and Surimi seafood
a b c
Jae W. Park , Tein M. Lin & Jirawat Yongsawatdigul
a
Oregon State University Seafood Laboratory , 250 36th Street,
Astoria, OR, 97103
b
Department of Food Science , University of British Columbia ,
Vancouver, B.C., Canada
c
Department of Food Science , Suranaree University of
Technology , Thailand
Published online: 03 Nov 2009.

To cite this article: Jae W. Park , Tein M. Lin & Jirawat Yongsawatdigul (1997) New developments
in manufacturing of Surimi and Surimi seafood, Food Reviews International, 13:4, 577-610, DOI:
10.1080/87559129709541141

To link to this article: http://dx.doi.org/10.1080/87559129709541141

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 Food Rev. Int., 13(4), 577-610 (1997)

NEW DEVELOPMENTS IN
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MANUFACTURING OF SURIMI
AND SURIMI SEAFOOD
JAE W. PARK,1 TEINM. LIN,2 and JIRAWAT YONGSAWATDIGUL3
1
Oregon State University Seafood Laboratory
250 36th Street
Astoria, OR 97103
2
Department of Food Science
University of British Columbia
Vancouver, B.C., Canada
3
Department of Food Science
Suranaree University of Technology
Thailand

ABSTRACT

Manufacturing technology of surimi and surimi seafood has been

developed to keep the balance of the quality and quantity (yield) of
surimi proteins. This review article covers the chemistry of surimi
manufacturing with an emphasis on solubility of myofibrillar proteins
as affected by ionic strength, pH, washing cycles, wash/meat (W/M)
ratio, and proteolysis. In addition, water quality, waste water, and
cryoprotection are reviewed. Ohmic heating and high hydrostatic
pressure in relation to the manufacturing of surimi seafood are
extensively discussed. Ohmic heating is the newest technology ap-
plied in the manufacturing of surimi seafood. High hydrostatic pres-
sure has not been applied in the commercial practices of surimi
seafood manufacturing, however, it has a great potential to make
surimi gels stronger.

577

Copyright © 1997 by Marcel Dekker, Inc.

 578 PARK, LIN, AND YONGSAWATDIGUL

INTRODUCTION

Surimi is stabilized myofibrillar proteins from fish muscle. In other words, it is

mechanically deboned fish flesh, that has been washed with water, and blended
with cryoprotectants to provide a better frozen shelf life. This intermediate prod-
uct is used for a variety of foods from the traditional kamaboko products of Japan
to the recent shellfish substitutes (hereafter surimi seafood). Before 1960, surimi
was manufactured and used as a refrigerated raw material within a few days, be-
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cause freezing commonly deteriorated muscle proteins as well as induced protein

denaturation and poor functionality.
Nishiya et al. (1) at Hokkaido Fisheries Research Station of Japan discovered
a technique by which freeze-induced denaturation in Alaska pollock (Theragra
chalcogrammd) muscle could be prevented. This technique required the addition
of low molecular weight carbohydrates, such as, sucrose and sorbitol in the dewa-
tered myofibrillar proteins prior to freezing. Actomyosin of Alaska pollock, which
is remarkably unstable during frozen storage (2), was protected from the loss of
functional properties by the use of carbohydrates. This discovery revolutionized
the industry. The industry was no longer dependent on the availability of fresh
fish supplies and further increasing production and sales in Japan, as well as other
countries like the United States. Surimi seafood plants in Japan were able to ex-
tend their base beyond local supplies and draw on fish resources which had, until
then, been unavailable because of distance. Alaska pollock from the North Pacific
Ocean and the Bering Sea was a largely unexploited resource and was available
in the quantity required to meet the large expansion of the Japanese kamaboko
industry in the 1960s and 1970s (3,4). In the 1980s, surimi became Americanized
reaching an annual production (pollock) of 150,000 to 180,000 tons. The produc-
tion of Pacific whiting surimi started at sea in 1991 and at shore-side plants in
spring, 1992. The surimi production from Pacific whiting has ranged from 30,000
to 50,000 tons a year.
To a large extent, the history of world surimi started with the Japanese fish
processing industry. However, recent developments in the United States and Ko-
rea have extended the industry beyond that of Japan. In 1992, the growth of the
world surimi industry exceeded 500,000 tons and was created by demand. Japan's
involvement in world surimi production decreased with the increased surimi pro-
duction in the United States. The United States processing technology of surimi
seafood has drawn on the Japanese experience and now is well established with a
75,000 tons annual production in 1995. Surimi seafood consumption proliferated
mainly in cold salads with an annual growth rate of 10-100% in the 1980s. Con-
sumption suffered in 1991, with a negative growth rate, due to the increased price
of surimi.
The surimi industry largely used Alaska pollock, however, since 1991 efforts
to develop surimi from other species have been successful. These developments
have been taking place throughout the world, often in the technical or marketing
 MANUFACTURING TECHNOLOGY OF SURIMI 579

association with Japan. A number of different species of fish are currently being
used for commercial surimi production. The most suitable species for surimi proc-
essing are those with white flesh and low fat contents. They are: Pacific whiting
(Merluccius productus) from the Pacific coast, hoki (Macruronus navaezelandiae)
from New Zealand, Southern blue whiting (Micromesistius australis) from Chile
and Argentina, Northern blue whiting (Micromesistius poutassou) from EEC
waters, threadfin bream (Nemipterus japonicus) from Thailand, yellow croaker
(Pseudosciaena manchurica) from the south of Japan, and yellow sole (Buglos-
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sidium luteum) from Alaska. Even underexploited species which have a higher
portion of red or dark muscle and/or a higher fat content are used for the produc-
tion of low grade surimi, e.g., pink salmon (Oncorhynchus gorbuscha), atka mack-
erel (Pleurogrammus azonus), Japanese sardine (Sardinops melanostrictus), and
Chilean jack mackerel (Trachurus murphyi).
Gelation of surimi proteins is the most important step in forming desired tex-
ture in many food systems. In reaction to consumer acceptance, surimi seafood
has been successful in food service applications as well as in the retail deli and
salad bar. The success of these surimi-based crab, shrimp, lobster, and scallop
meat is mainly due to their low price in relation to the natural counterparts. They
are also convenient to prepare. Nutritionally, they can be fat free unless vegetable
oils are added in the formulation. These surimi-based seafoods do not fluctuate
in availability of supply or quality as with higher-priced natural shellfish.
This review article will cover the chemistry and new technology developments
in manufacturing surimi and surimi seafood.

I. CHEMISTRY IN SURIMI MANUFACTURING

When fish muscle is separated from bone, skin, and entrails and then comminuted,
it is called minced fish. This becomes raw surimi after washing to remove sarco-
plasmic proteins, fat, and other undesirable matters such as blood and pigments
resulting in concentrated myofibrillar proteins. Following the washing and dewa-
tering, the concentration of functional actomyosin increases. This facilitates the
gel-forming ability of surimi seafood. After washing, the mince is subjected to a
refiner to remove connective tissues, bone fragments, and skin pieces. Extra water
is then removed from the washed mince using a screw press prior to adding cryo-
protectants to protect proteins from denaturation during frozen storage. The
overall process of modern surimi production is summarized in Figure 1.
The fish should be handled carefully since freshness plays a crucial role in de-
termining the quality of surimi; fresh fish results in higher-quality products. After
harvest, the fish are usually stored in crushed ice or in refrigerated sea water to
keep the body temperature of the fish just above the freezing point prior to proc-
essing. According to Peters and Morrissey (5), the champagne ice system cools
fish more rapidly than the refrigerated sea water (RSW) system. It takes ~1 h to
 580 PARK, LIN, AND YONGSAWATDIGUL

Whole Fish
100%
Heading/Gutting
t 60%
j Deboning/Mincing
^ 42%
1st Washing
42%
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lstDewatering Frozen Surimi

33% 24%
Water,!
Sarcoplasmic Proteins, Block Forming
NaCl* M 2nd Washing
Myofibrillar Proteins
33% 24%
2nd Dewatering Mixing
28% 22%
Refining Screw Pressing
25%
T
^Connective Tissues^. Water,
\Myofibrillar Proteins/ (Sarcoplasmic Proteins,^
\MyofibriIlar Proteins^

Figure 1. Flow diagram of surimi manufacturing with estimated yield. NaCl*: NaCl can be added
for better removal of water as needed.

cool fish to 1-2°C using champagne ice and more than 20 h using the RSW system.
Caution should be taken to maintain the integrity of the fish. The occurrence of
trauma or broken skin during handling often causes a loss in the yield and quality
of surimi at the subsequent processing.

Meat/Bone Separation

The head, viscera, and backbone are removed with a header and a filleter. Me-
chanical fish meat separators, developed by companies in Japan, Germany, and
the United States, are modern sanitary machines that remove virtually all of the
flesh from the frame of a properly prepared fish. According to Pigott (6), there
are several methods to prepare fish for deboning. One is to remove head, gut and
thoroughly clean the belly walls prior to deboning the carcass. The other is to fillet
the fish and then debone the fillet containing skins and bones. During the debon-
ing step, plenty of water is used to separate fillets from undesirable parts of fish.
Degutting should be completed at this stage since proteolysis by the enzyme found
in viscera reduces the quality of surimi. In recent years, as an attempt to increase
the recovery rate, butterfly fillets with skin on, are commonly used. This stage of
processing accounts for -60% of the raw materials on a wet-mass basis (Fig. 1).
 MANUFACTURING TECHNOLOGY OF SURIMI 581

The fish fillet is then subjected to a mechanical deboner for the separation of meat
from the skin tissue. It is a standard practice in mincing to use roller-type meat
separators. The dressed fish is pressed between a rolling rubber belt and a steel
drum with numerous orifices of 3-5 mm in diameter. The fish meat and other
small inclusions, such as blood and broken bone, are pressed through the orifices
into the interior of the drum, separating skin, bone, and other impurities.
The particle size offish mince is dependent on drum orifice size. Commercially,
opening sizes of 3 or 5 mm are generally used compared to 0.5-2 mm for poultry
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and red meat. The medium orifice size of 3-4 mm appears to be optimal with
respect to quality and yield (7-10). The relatively larger orifice size of 5 mm yields
larger meat particles, most of which are retained during washing operations.
While this results in a higher yield, the product contains more dark and connective
tissue, thus decreasing the quality. Mincing fish with a drum having a relatively
smaller orifice size of 1-2 mm yields small meat particles that are almost free of
dark and connective tissue. However, a substantial quantity of fine meat particles
are lost during washing. A drum with a small orifice causes greater cell disruption
and releases heme pigments. The presence of heme pigments is generally consid-
ered to be the biocatalyst for Iipid oxidation. An increase in thiobarbituric acid
(TBA) values with smaller particle size of deboned meat has been reported (11).
Proper adjustment of the contact between the belt and drum is critical in ob-
taining a high yield with good quality of mince. When the contact is too loose, the
pressure is not sufficient to separate meat from skin well causing a yield loss.
However, if the contact is too tight, part of the skin will be incorporated into the
mince due to the high shear stress induced. The considerable increase in tempera-
ture caused by friction between the deboning drum and flesh will also promote
the initiation of Iipid oxidation (12,13).

Removal of Sarcoplasmic Proteins and Other Impurities

By removing sarcoplasmic proteins and other soluble substances, the concentra-

tion of myofibrillar proteins increases. Gel strength of surimi increases with an
increase in the concentration of myofibrillar proteins especially actomyosin, but
decreases in the presence of sarcoplasmic proteins (14). Sarcoplasmic proteins
bind with actomyosin and impede the cross-linking process which is crucial for the
formation of gel network. This emphasizes the importance of washing process.
The number of washing cycles and water/meat (W/M) ratios employed for
washing vary among surimi processors. A W/M ratio ranging from 4:1 to 8:1 is
often employed by on-shore processors. This washing process is often repeated
3-4 times to ensure sufficient removal of sarcoplasmic proteins. On the other
hand, at-sea processors use a lower W/M ratio (1:1-3:1) with only one or two
washing cycles due to their limited access to fresh water. Generally, the overall
W/M ratio used for the washing ranges from 3:1 to 24:1. Increased water usage
 582 PARK, LIN, AND YONGSAWATDIGUL

for washing usually resulted in more protein loss and waste water disposal (15).
It was estimated that 50% of total proteins were lost during washing (7,16,17), and
30 L of waste water per one kg of surimi produced were generated from on-shore
processing plants (18). The question has been raised as to whether more water
usage guarantees better surimi quality or if it is unnecessary and wasteful. In early
studies, it was shown that the gel strength of surimi continued to increase as the
number of washing cycles increased (19). However, a recent report (20) indicated
that the major portion of sarcoplasmic proteins are fairly soluble and removed
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during the initial washing steps. Subsequent washing removes the residual sarco-
plasmic proteins along with a small amount of myofibrillar proteins. After sarco-
plasmic proteins are completely removed, further washing causes a severe loss of
myofibrillar proteins. Therefore, excessive washing not only increases the cost for
water usage and waste water treatment, but also results in a yield loss. Thus, a
careful control of W/M ratio, washing cycles, and washing time is important for
surimi processors to maximize quality and yield, as well as to minimize water usage
and waste water disposal.
Since proteins are the basic building block used to form the gel matrix, gel
strength can be affected by concentration of proteins present. Moisture content
of mince is notably changed after washing and dewatering processes. It is possible
that differences in gel strength of washed and unwashed mince are due to the
dilution of the protein, especially myofibrillar proteins. Dawson et al. (21) exam-
ined moisture to protein ratio (M:P ratio) for gels from washed and unwashed
mechanically deboned chicken meat (MDCM) and found that M:P ratios for gels
from washed MDCM were slightly diluted. Even with a slightly higher M:P ratio,
the washed gels had a superior strength compared with that of unwashed gels.
This experiment showed that the greater gel strength of washed mince is due to
removal of water-soluble proteins with a relative increase in myofibrillar proteins.
MacDonald et al. (22) also reported that strength and puncture deformation of
gels from washed hoki minces were generally greater than those from correspond-
ing unwashed minces.
Good gels can also be produced from some species of fish without washing as
long as NaCl is used (23). However, this does not imply that commercial products
could be prepared without washing since this step also removes fat, pigments, and
substances that affect the stability of proteins during the subsequent frozen stor-
age. Lin et al. (24) reported that washed mince had lower lipid oxidation and free
fatty-acid content than unwashed mince during a 6-mo frozen study. Washed
mince also exhibited a lower Hunter "a" value and had superior water retention
ability. Brittle texture often occurs in fish muscle with long frozen storage. It is
believed that this undesirable textural change is due to the activity of trimethy-
lamine oxide (TMAO) demethylase that catalyzes the decomposition of TMAO
to form dimethylamine (DMA) and formaldehyde (FA) (25,26). FA in turn in-
duces formation of cross-linkages between adjacent protein molecules leading to
textural hardening. Since most TMAO in fish mince can be removed by washing
 MANUFACTURING TECHNOLOGY OF SURIMI 583

(27), less FA will be formed in surimi. Thus, texture properties of surimi can be
much better than those of mince and fillets during frozen storage.
The fat content of minced fish is significantly reduced after washing. As much
as 40% and 65% of the original lipid can be removed from minced Pacific whiting
and minced rockfish, respectively, according to Chang-Lee et al. (28) and Adu et
al. (7). Separation of fat during washing treatment was attributed to differences
in density and polarity between fat and aqueous solution. Since fat has a lower
density than water and is water-insoluble, part of the fat floated off during wash-
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ing. Since hemoprotein, which accelerates the initiation of oxidation, is removed

by washing, TBA values of washed mince also are reduced significantly (29).

Quality of Leaching Water

The important factors of water quality associated with washing that affect surimi
quality are pH, hardness, salt concentration, and temperature.
pH. Since water content of washed mince flesh is expected to be very low near
the isoelectric point of the myofibrillar protein (pH 5.3), problems associated with
swelling of mince after washing can be avoided by using low-pH water. However,
myofibrillar proteins lose stability at low pH values. In consideration of both de-
sired gel strength and efficiency of washing, the optimum pH value of 6.5 was
suggested by Sonu (30) and Lee (8).
The pH effect of washing water on lipid oxidation was studied by Tseo et al.
(29). These researchers indicated that TBA values appear to be strongly related
to the effect of pH on muscle protein solubility. The TBA values of refrigerated
minced fish increased when the pH of buffer changed from 3 to 5, but decreased
as the pH increased from 5 to 10. When the pH of buffer is close to the isoelectric
point of actomyosin (pH 5.3), washing causes the muscle protein to become ex-
tensively aggregated, with less hemoprotein removed. Therefore, greater lipid
oxidation development occurred in the minced fish flesh. A pH of 6.0 for washing
water was recommended by Tseo et al. (29) to decrease the TBA number.
Hardness. Water hardness affects the swelling tendency of minced flesh. The
swollen mince has two problems: 1) it does not settle readily to the bottom of the
tank, making it difficult to separate from impurities; and 2) the water in swollen
mince cannot be removed satisfactorily resulting in high moisture content and low
gel strength. Softer water has a greater tendency to induce mince swelling (30).
On the other hand, hard water with high levels of Ca and Mg decrease the tem-
perature tolerance of fish mince during washing process and accelerate the de-
naturation of actomyosin during subsequent frozen storage (8,31). High levels of
Fe and Mn could result in undesirable color changes in the mince (8). Therefore,
medium-hard water is often recommended for washing.
Salt Concentration. During the washing cycle, water-soluble salts are re-
moved from the mince, resulting in a low salt content which imparts an increase
 584 PARK, LIN, AND YONGSAWATDIGUL

in hydrophilicity. Consequently, mince flesh tends to hydrate and swell. To facili-

tate the easy removal of water, the salinity of the water for the last washing is
recommended to be between 0.1% to 0.5% (8,14,30,32). Lin and Chen (32) also
reported that washing with a salt solution is more effective than water alone in
extraction of heme pigments from mince flesh. A minimum hydrophilic condition
for washed mince is at an ionic strength between 0.005 and 0.1, while the corre-
sponding salt concentration is between 0.03% and 0.6% (30). With an increase in
salt concentration greater than 0.6%, the hydrophilicity of minced flesh increases.
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Excessive salt may cause solubilization of myofibrillar proteins which result in

premature setting of the protein sol prior to fabrication (8,32).
Temperature. While cold water is desirable for retaining functional properties
of fish proteins, warm water is more conducive to the dewatering process. A wash-
ing temperature of 5°C or less is often applied in commercial operations. Other
effects of washing temperature on minced flesh have been studied by several re-
searchers. Lin and Chen (32) reported that products prepared with a solution at
2-4°C had higher yields than those prepared at 20-22°C. Surimi prepared with
20-22°C wash solution removed more pigments than those prepared with 2-4°C
wash solutions. Tseo et al. (29) indicated that maximum whiteness index, minimal
TBA numbers, and minimal cooking loss were achieved with washing at 29-33°C
for up to 10 min for minced mullet flesh. Similar results were presented by Chao
(33). Watabe et al. (34) also reported that activation of myofibrillar Mg++-ATPase
increased with increased washing temperature, leading to degradation of ATP.

Solubility of Myofibrillar Proteins

According to the classical muscle protein chemistry, sodium chloride (0.3-0.6 M)

is needed to solubilize myofibrillar proteins (35,36). The classic procedure for
solubilization of myofibrillar proteins is to dissolve them in a salt solution varying
from roughly 0.3-0.6 M at neutral or slightly acid or alkaline pH with or without
compounds such as ATP and magnesium salts. Solubilization occurs in two steps:
1) depolymerization of thick filaments, and 2) dissociation of actin from myosin
(37). They showed that at high salt concentrations thick filaments from different
muscle fibers may have different solubility. This is likely due to the different iso-
forms of myosin which are specific to the functions of the muscle. However, the
recent studies indicated that a significant amount of myofibrillar proteins was
solubilized in a solution with very low (near zero) ionic strength (38) and was often
found in surimi processing waste streams (17). Wu et al. (39) indicated that after
washing the minced muscle tissue of 5 species of white-fleshed fish twice with
water and a third time with 0.15% (26 mM) NaCl solution, a considerable portion
of the remaining protein was soluble when extracted with water at a 1:20 ratio.
The amount of protein extracted was 20-36% of the protein extracted by a buffer
of 1 M LiCl solution indicating the extracted proteins were primarily myofibrillar
 MANUFACTURING TECHNOLOGY OF SURIMI 585

proteins. Hennigar et al. (40) also showed that gels could be prepared by fish
muscle without NaCl suggesting that fish muscle myofibrillar proteins could have
sizable amount of solubility in water.
Myofibrillar proteins constitute approximately 66-77% of total proteins in fish
flesh (41). Therefore, recovery of myofibrillar proteins is expected to be in this
range during surimi manufacturing. However, in commercial operations only
about 50% of total proteins are recovered as myofibrillar proteins in surimi. A
large amount of myofibrillar proteins are lost during washing, dewatering, refin-
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ing, and screw pressing (7,16-18).

During surimi processing, minced fish flesh is subjected to the changes of pH
(24,40) and ionic strength (20,30,39,42), proteolysis (43-45), and possible tem-
perature abuse. These processing factors might change the protein structure in
primary sequence, conformation, molecular size and shape, charge distribution,
intra- and inter-molecular bonding. These changes might, in various degrees, af-
fect protein solubility during processing. Reduced particle size (46) and increased
mechanical forces of screening and screw pressing might also cause the loss of
proteins in the form of particulate. Therefore, myofibrillar proteins lost in surimi
waste streams are both soluble proteins and insoluble particulates.

Effects of Ionic Strengths

Muscle of salt-water fish contains a variety of salts, about equivalent to a solution
with ionic strength 0.145 (39). This ionic strength corresponds to 0.85% NaCl.
Extensive washing of muscle causes the loss of salts in the tissue and allows myofi-
brillar proteins to become highly associated with water. Matsumoto (47) reported
that when the protein extracted by salt solution was repeatedly washed with water,
most of the protein was solubilized. Also increased washing time (8) or washing
cycles using the same amount of water (16) resulted in more proteins, possibly
myofibrillar proteins, being solubilized. Presumably, these two factors are crucial
in changing the ionic strength of fish muscle during washing.
The loss of myofibrillar proteins during extensive washing was minimized at
salt concentrations of 0.5-1.0% (20,39) indicating that washing solution with salt
concentration similar to that offish muscle (0.85%) could inhibit the solubility of
myofibrillar proteins. This is confirmed by Sonu (30) showing that a minimum
hydrophilic condition for washed mince is at an ionic strength between 0.005 and
0.1 which corresponds to the salt concentration of 0.03 to 0.6%. A linear relation-
ship of moisture content of the fish paste to the log of the water-soluble protein
concentration was also observed by Wu et al. (39) suggesting a significant rela-
tionship between hydration and solubility. Similar results reported by Trevino et
al. (42) showed that the solubility of protein in sardine surimi was high in water,
rapidly decreased at low salt concentrations, and increased again as the salt
concentration was further increased. These results suggested the possibility of
using a low concentration of salt to prevent the solubilization offish myofibrillar
 586 PARK, LIN, AND YONGSAWATDIGUL

proteins during the washing process. An extensive research project on the solu-
bility of sarcoplasmic proteins and myofibrillar proteins at various salt concentra-
tions was conducted by Lin and Park (20). Sarcoplasmic proteins were readily
soluble in water (0% NaCl) and removed in the initial washing steps. Myofibrillar
proteins became relatively soluble and lost when subjected to extensive washing.
Washing with salt solutions (0.2-1.0% NaCl) reduced the loss of myofibrillar pro-
teins. However, these salt solutions was not very effective in removing sarcoplas-
mic proteins resulting in lower myosin and actin content in the washed mince.
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Severe loss of proteins due to high ionic strength in washing solution has been
reported. Lee (48) reported that solubilization of myofibrillar protein occurred
when too much salt was used during surimi manufacturing. Foegeding (49) indi-
cated that the solubility of salt-soluble proteins increase as the concentration of
NaCl increases from 0.25 to 0.5 M at pH 6.0. However, at pH 5 and 7 there was
no major effects of NaCl on solubility of salt-soluble proteins (SSP). It was also
shown by Wu and Smith (50) that increasing ionic strength (from 0.10 to 0.35 M)
increased myofibrillar solubilization.
The effects of several different chloride salts and one iodide salt on solubility
of proteins from washed cod mince were determined by Stefansson and Hultin
(38). The general patterns of solubility were very similar. The major effect of
different cations was with MgCl2 and CaCl2 which at higher concentrations re-
duced solubility of the muscle proteins (Fig. 2). It is possible that this effect might
have been related to pH. In the unbuffered systems of the final washed meat, small
changes in proton concentrations could cause very large changes in pH. Magne-
sium and calcium chlorides reduced the pH when added at an ionic strength of
0.01 by —0.2 unit, approximately 6.5 compared to 6.7 (38). This difference in pH
is possibly caused by the strong interactions between the muscle protein side
groups and the divalent cations releasing more protons than did the monovalent
cations. This decrease in pH would probably be sufficient to cause the differences
in protein solubility as shown in Figure 3.

Effect of pH
The solubility of myosin changes at various pHs (51) (Fig. 3). As the pH ap-
proaches the isoelectric point of myosin (4.8-6.2), the negative and positive
charges among protein molecules are about equal. Therefore, protein molecules
are strongly associated with each other through ionic linkages. Myofibrillar pro-
teins are insoluble at these pHs because protein-water interaction is replaced by
protein-protein interaction. It is a logical assumption that using washing solutions
with pH near or at the isoelectric point of fish muscle proteins would reduce the
loss of proteins and improve yield. Pacheco-Aguilar et al. (16) showed that at
pH 5.0-5.3, the water requirement was reduced by 80%, and yield was im-
proved by up to 34% over conventional processing at pH 6.5. However, the texture
of gels was poor when prepared from surimi produced under acidic conditions.
 MANUFACTURING TECHNOLOGY OF SURIMI 587

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• •
lifc—- kN
!
i
25
;
• i
1
20
3 i *l
15
o 10
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i ,j
5
0
0.00001 0.0001 0.001 0.01 0.1
Ionic Strength
|-BNaCl LiCl ONal

Figure 2. Effects of ionic strength of various salts on protein solubility. Adapted from Stefansson
and Hultin (38).

Foegeding (49) also indicated that salt soluble proteins have the least solubility at
pH 5.0. The relative amount of myosin heavy chain (MHC) extracted with 0.25 M
NaCl solution, was decreased from 52.0% to 1.6% as pH decreased from 7.0 to
5.0.
At pH above or below the isoelectric point, the net charge of protein becomes
negative or positive. The increased net charge offers more binding sites for water
and causes the repulsion among protein molecules to increase their surface area
for hydration, thus increasing protein solubility.

Figure 3. Effects of pH on solubility of myosin. Adapted from Lin and Park (51).
 588 PARK, LIN, AND YONGSAWATDIGUL

Effects of Washing Cycles

Nishioka (52) indicated that the greater number of washing cycles applied to
mince produced the stronger gel-forming ability of surimi. Our study (20) also
showed that the relative amount of MHC increased as the washing was repeated.
However, this trend was only effective at the lower salt concentration, while 3 and
4 washing cycles negatively affected the relative amount of MHC in the washed
meat at 0.5% or higher salt concentration. However, it should be noted that the
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increased number of washing cycles caused a lower yield and higher loss of MHC
in the washing solution. The most severe loss of MHC (42.9%) occurred when the
fish mince was washed using 0% NaCl solution for 4 washing cycles (Fig. 4). Even
though the equal W/M ratio (5:1) and stirring time (5 min) were maintained
throughout all the washing steps, only 1.1% MHC were lost in the first washing
step, while 21.8% MHC were lost in the last washing step. At the beginning of the
washing, the sarcoplasmic proteins were readily solubilized. At a compact and
higher molecular weight, MHC had less chance to be hydrated by water. As the
washing steps increased, less sarcoplasmic proteins remained and more water be-
came available for MHC to solubilize and more charged amino acids in the MHC
became available to be hydrated by water due to the removal of salts from these
charged amino acids. This may be the reason for the higher solubility of MHC
during the last washing step when plain water was used for washing.

0 0.25 0.5 1 2 0 0.25 0.5 1 2

% NaCl in the washing solutions % NaCl in the washing solutions

Figure 4. Effects of washing cycles and salt concentration in wash water on the loss of myosin heavy
chain. WS: washing steps. Adapted from Lin and Park (20).
 MANUFACTURING TECHNOLOGY OF SURIMI 589

Effects of W/M Ratio

A logical approach to achieve the same washing effect with less water would be
to increase washing time and number of washing cycles with a lower W/M ratio
for each washing step. Theoretically, at a constant W/M ratio, more extractable
proteins will be dissolved in water when a longer washing time is allowed until the
equilibrium stage is reached. To increase washing efficiency, sufficient washing
time should be allowed. Increased washing cycles at a constant overall W/M ratio
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are likely to have a higher dilution factor, i.e., more extractable proteins are re-
moved per unit of water used.
Possible minimization of water usage for leaching was investigated by reduced
W/M ratio with increased washing cycles and washing times (15). The concentra-
tion of total extractable proteins increased when W/M ratio was reduced from 4:1
to 2:1 or 1:1. This was most noticeable during the initial washing steps (Fig. 5). In
the later washing steps, the difference in protein concentration was less affected
by W/M ratio. This data showed that more proteins per unit of water were re-
moved when W/M ratio was reduced. At the W/M ratio of 2:1, the increased
washing time from 5 to 10 min increased the concentration of extractable proteins.
However, effects of washing time were not significant at the W/M ratio of 1:1
suggesting that at this W/M ratio extractable proteins reached equilibrium at or
before the 5 min washing time. Lin and Park (15) suggested the use of a lower
W/M ratio (2:1 or 1:1) with increased washing cycles (3 or 4) and/or washing times
(5 or 10 min) to reduce water usage. The results showed that the usage of leaching
water could be reduced from 12:1 (overall W/M ratio) to 8:1 by using a lower W/M

20
• 1WS S2WS S3WS M4WS

15
t 10
u
.3

5m 5m 10m 5m 10m 5m 10m 5m 10m

4W.1M 2W:1M 1W:1M

Figure 5. Protein concentration of supernatant at various washing conditions. 5 m and 10 m: 5 and

10 min of washing time; 4W:1M, 2W:1M, and 1W:1M: a water/meat ratio at 4:1,2:1, and 1:1; WS:
washing steps. Adapted from Lin and Park (15).
 590 PARK, LIN, AND YONGSAWATDIGUL

ratio with 4 washing cycles and longer washing time (10 min). This washing was
sufficient to remove sarcoplasmic proteins.
With 3 washing cycles and 5 min of washing time, the MHC content in the
washed mince decreased when W/M ratio was reduced from 4:1 to 2:1 or 1:1 (15).
The reduced MHC content in the washed mince was probably due to insufficient
removal of sarcoplasmic proteins. At W/M ratio of 2:1, increased washing cycles
and/or washing times resulted in an increased MHC content.
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Effect of Proteolysis
A significant effect of proteolytic enzymes on surimi processing has not been re-
ported except in Pacific whiting. The loss of myofibrillar proteins in surimi manu-
facturing from Pacific whiting might be due in part to proteolysis before and dur-
ing processing. Evidence has been shown by several researchers that proteolytic
degradation of myofibrils resulted in a low yield of whiting surimi (43). Native
myosin is in filamentous form and insoluble. The increase in protein solubility of
myofibrils is due to the disintegration of myofibrils. Once the myofibrils are dis-
assembled, the proteins can be readily solubilized (44).
In shore-side surimi operations, Pacific whiting are usually delivered to proc-
essing plants within 6-12 h postharvest. Due to the limited capacity of processing
facilities, fish are often kept in holding tanks with ice water for another 6-14 h.
Thus, fish are usually 6-26 h postharvest before they are subjected to surimi proc-
essing. During this holding period, the temperature can rise if fish are not handled
properly. Prolonged holding time and elevated temperatures can cause severe
proteolysis of myofibrillar proteins and consequently affect the processing yield
and gelation properties of surimi.

I
02 6 24 48 72
Storage Time (h))

Figure 6. Effects of storage time and temperatures on MHC degradation. Adapted from Lin and
Park (53).
 MANUFACTURING TECHNOLOGY OF SURIMI 591

As shown in Figure 6, degradation of MHC in whiting muscle is greatly affected

by the storage temperature and time. Fish kept at 5°C showed higher degradation
than those at 0°C (53). When temperatures increased, degradation occurred more
rapidly. Low temperatures slow down proteolysis. However, with prolonged stor-
age time, severe degradation occurred even though the storage temperature was
maintained at 0°C. When proteolytic degradation occurs, the compact, large mo-
lecular weight myofibrillar proteins are hydrolyzed to small molecular weight pro-
teins or peptides. These degraded proteins have relatively higher solubility than
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their native myofibrillar proteins (Fig. 7), resulting in a reduced surimi processing
yield.
Proteolytic activity in Pacific whiting has been related to infection of myxo-
sporian parasites, Kudoa paniformis and K. thyrsitis (43,54). At the early stage,
infected muscle fibers appear to be opaque white and cannot be identified without
the aid of a microscope, while at the later stage, the infected fibers are readily
visible as a dark black streak on the muscle. The former are called white psuedo-
cysts and the latter are called black psuedocysts (55). A hidden stage, the initial
stage of infection, might also exist (56). By surveying 1500 fish in 35 plants, Mor-
rissey et al. (57) indicated that 4-5% of Pacific whiting harvested from the Pacific
Northwest coast contained black psuedocysts. The overall prevalence of infection,
including white and black psuedocysts, was estimated to be about 90-95% of the
fish population (56). The presence of black psuedocysts can be easily identified
and classified into three categories: slight, moderate, and heavy stages. However,
a recent report (58) indicated that proteolytic activity is mainly related to the
presence and intensity of white psuedocysts (R2 = 0.81, P 0.05) and is not corre-
lated to the degree of black psuedocysts (R2 = 0.23, P 0.05).

30 -

25
-1.2 -1 -0.8 -0.6 -0.4 -0.2
Log (% MHC Degradation)

Figure 7. Relationship between MHC degradation and solubility of proteins during washing.
Adapted from Lin and Park (53).
 592 PARK, LIN, AND YONGSAWATDIGUL

An et al. (59) indicated that in whiting fillets, cathepsin B exhibited the highest
peak activity, followed by cathepsins L and H. Cathepsin L and H in fish extract
showed their highest activity at 55 and 20°C, respectively, while the maximum
activity of cathepsin B was between 20 and 37°C. The total cumulative activity of
the three cysteine cathepsins (L, B, and H) was found to be highest at20°C in fish
fillets. In the temperature range for surimi processing (0-5°C), the activity of
cathepsin L is insignificant, while cathepsin B still exhibited half of its maximal
activity, and cathepsin H retained about one fifth of its maximal activity. These
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results suggest that cathepsin B and H might contribute to the degradation of

myofibrillar protein during surimi processing (0-5°C). After extensive washing
and dewatering, the activity of cathepsin B and H is substantially reduced, while
cathepsin L still remains active in surimi. A gradual decrease in protease activity
by washing was also reported by Chang-Lee et al. (60).
In a study of hydrolysis of whiting myofibrils by the protease, An et al. (61)
indicated that MHC was hydrolyzed to smaller molecular weights ranging from
67 to 145 kDa. These bands were also detected in surimi samples suggesting that
a large portion of myosin was hydrolyzed during surimi processing.

Waste Water and Protein Recovery

Although washing and dewatering in surimi manufacturing are indispensable, it

creates a significant problem in the waste stream. The loss of sarcoplasmic pro-
teins and myofibrillar proteins not only leads to an obviously reduced yield, the
forfeiture of some valuable micro-nutrients, but also causes pollution of the water
by increasing its biological oxygen demand (BOD) and chemical oxygen demand
(COD). A recent investigation showed the extensive washing of minced flesh
caused a high loss of organic substances which resulted in extremely high COD
(6,000-27,000 mg/L) in waste water (18). Huang (62) reviewed several methods
of physical treatment for waste water: dissolved air floatation (D AF), heat coagu-
lation, electrocoagulation, centrifugation, and membrane filtration. The DAF
process is very effective, particularly for treating waste water containing fat and
oil. Hopkins (63) investigated the effectiveness of combined chemical coagulation
and DAF operations in treatment of waste water from poultry processing plants;
the removal of about 50-80% solids were achieved among test plants. DAF has
recently been adopted in a surimi processing plant in Oregon. The use of polyacry-
lamide into the DAF unit caused proteins in the waste water to easily flocculate,
thus reducing the consumption of compressed air (62). The reduction of COD
values was also reported using pressure floatation and activated sludge methods
(64). Huang (62) applied ohmic heating to coagulate frozen mince wash water.
33.0% protein, 59.3% COD, 33.3% total solids, and 92.1% total soluble solids
were removed when the waste water was heated to 70°C. Electrocoagulation,
which is a combined physical and chemical process involving alternating or direct
 MANUFACTURING TECHNOLOGY OF SURIMI 593

current that passes through the waste water to initiate a coagulation process, has
also been applied in treating fish processing waste water. Dalrymple (65) showed
electrocoagulation can reduce 93% total soluble solids and 35.5-76.9% COD
from fish processing waste streams. Centrifugation is one of most frequently used
methods for waste water treatment and the recovery of useful particulates. Typi-
cally, a range of 1700-3000 x g centrifugal force is used to recover protein parti-
cles from surimi waste water streams (62).
The use of ultrafiltration (30,000 molecular weight cut-off) resulted in an
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89-94% reduction in COD value (18). Lin et al. (18) investigated effects of
ultrafiltration on other biological properties of surimi waste water. Aerobic
plate count (APC) in every ultrafiltration permeate became insignificant (100
CFU/mL). The protease activity in waste water from Pacific whiting surimi manu-
facturing did not decrease with successive washing processes. However, with ap-
plication of ultrafiltration, a substantial reduction of protease activity was noted.
Clarity of waste water increased to an extremely high percent transmittance of
97.8. This was nearly identical to that of tap water (98.4%) used for processing.
The clarity of ultrafiltration permeate indicated the potential for water recycling
in surimi operations. However, protein concentration by ultrafiltration was con-
siderably dark in color and strong in odor, therefore, was recommended for high
protein animal feeds.
For surimi manufacturing, myofibrillar proteins, which were lost in the form of
particulates in the final watering process, could be successfully recovered and
concentrated using a rotary screen and microfiltration (18). Surimi with 10% re-
placement of microfiltration-recovered protein had the same gel quality as regular
surimi with respect to gel hardness, elasticity, water retention, and color. This
recovered meat could be used as a yield extender without deteriorating surimi
functionality.

Freeze Denaturation of Myofibrillar Proteins and the Functions of

Cryoprotectants

Freeze Denaturation
The optimal way to achieve long term storage of surimi is through freezing which
prevents microbial spoilage and minimizes biochemical reaction, especially oxi-
dative changes in the lipids and pigments, that cause off-flavors and discoloration
of products. Nevertheless, frozen storage is inevitably associated with some dete-
rioration of protein solubility and gel-forming ability caused by denaturation or
conformational changes of myofibrillar proteins. These properties, i.e., protein
solubility and gel-forming ability, are essential for the manufacture of surimi sea-
food.
Although the exact mechanism of denaturation of fish myofibrillar proteins
during frozen storage is not completely understood, a mechanism proposed by
 594 PARK, LIN, AND YONGSAWATDIGUL

Buttkus (66) is widely accepted. In electronphotomicrograph studies he showed

that myosin molecules aggregated during frozen storage for 5 d at -10°C in a
side-by-side manner. The aggregation reactions involve disulfide-sulfhydryl ex-
change reactions between activated myosin molecules and aggregates. The rate
of forming the insoluble high molecular weight protein aggregates in myosin in-
creased as the temperature decreased below the freezing point. This reached a
maximum near the eutectic point of the myosin-potassium chloride water solution
(-11°C) due to concentration effects. As reviewed by Shenouda (67), formation
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of ice crystals, increase in salt concentration, and dehydration offish muscle pro-
tein during frozen storage promote protein aggregation and loss of solubility. A
later study (68) also indicated that the freeze-denaturation of actomyosin was
caused mainly by formation of disulfide, hydrogen, and hydrophobic bonds. Other
researchers, Ang and Hultin (69), suggested it may be possible for formaldehyde
to induce loss of protein solubility and textural toughening in stored fish other
than by the crosslinking of muscle protein. By interacting with the side chain group
on the fish protein, formaldehyde could increase the rate of protein denaturation
during frozen storage. The degree of protein denaturation during frozen storage
is influenced by many factors, i.e., state of rigor at the time of freezing (70-73),
treatment before freezing (74), quantity and composition of free amino acids (75),
and adenosine-nucleotides and their derivatives (76).

Function of Cryoprotectants
The use of anti-denaturant additives (cryoprotectants) was introduced in 1960 to
protect the myofibrillar protein from freeze denaturation (1). Since then, a
number of other chemicals have been identified for their similar functions. Su-
crose and sorbitol are commercially used in surimi manufacturing because of their
excellence in stabilizing proteins during frozen storage as well as competitive price
(77).
Cryoprotective effects of carbohydrates (sucrose, glucose syrup), polyols (sor-
bitol, glycerol), protein hydrolysates (fish protein, casein hydrolysates), and hy-
drocolloids (sodium alginate, carrageenan) in cod surimi were investigated by
Sych et al. (78,79). Salt extractable protein and DSC were used to monitor the
stability of protein functional properties in surimi stored for 16 weeks at -20°C.
The optimal cryoprotection was achieved with sorbitol, sucrose, and sucrose/sor-
bitol 1:1 w/w mixture at 8% w/w in surimi. Similar results were also obtained by
Park and Lanier (80) and Yoon and Lee (81). Several studies have been under-
taken to identify new sources of cryoprotectants for surimi. Recently, Sych et al.
(79) reported that palatinit, lactitol, and polydextrose stabilized cod-surimi pro-
teins as well as a mixture of sucrose/sorbitol. Park et al. (82) also reported that
polydextrose appeared to substitute for the sucrose/sorbitol used in surimi
manufacture. In DSC studies, the addition of phosphate seemed to induce stabi-
lization of myosin but not the actin component of the myofibril. Freeze-induced
 MANUFACTURING TECHNOLOGY OF SURIMI 595

aggregation was reduced effectively by a combination of phosphate and carbohy-

drate (83). Similarly, Krivchenia and Fennema (84) showed that whitefish fillets
(Coregonus cupleaformis) treated with sodium triphosphate showed better texture
properties (reduced centrifugal drip, cook drip and firmness) than untreated con-
trol samples during frozen storage at -12°C for 28 weeks.
Several mechanisms of how cryoprotectants prevent protein denaturation dur-
ing frozen storage have been proposed. Since all substances with cryoprotective
effects on frozen fish actomyosin have more than two functional groups, such as
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-COOH, -OH, -NH2, -SH, -SO3H, and -PO4H2, Tsuchiya et al. (85) suggested
the following mechanism:
1. To show a positive cryoprotective effect, the molecule must have one
essential group, -COOH, -OH, and one or two complementary groups, such as
-COOH, -OH, -NH2, -SH, -SO3H. Di- or tri- PO4H2 groups function as both
essential and complementary groups.
2. A cryoprotective substance might be bound to protein molecules by one of
the functional groups via either ionic, hydrogen or S-S-bonds, while the other
functional group(s) may be hydrated, resulting in an increase in hydration and in
net charge of the protein. This may increase the electrostatic intermolecular re-
pulsion and hydration of protein, and then protect the protein molecules from
dehydration during frozen storage.
Back et al. (86) pointed out that proteins are stabilized by a combination of
hydrogen bonding, electrostatic interactions, and hydrophobic interactions. Their
experiment showed that sugars induce reorientation and rearrangement of the
water molecules that surround them. Their evidence supported the hypothesis
that the dominant mechanism by which sugars and polyols stabilize proteins
against heat denaturation is through their effect on the structure of water. This,
in turn, determines the strength of hydrophobic interactions. They concluded that
hydrophobic interactions make the major contribution to protein structure stabi-
lization, while hydrogen bonding and electrostatic interactions have relatively
small effects. Stabilization of protein in surimi by carbohydrates or polyols may
follow a similar mechanism.
Another mechanism was proposed by Timasheff et al. (87). The denaturation
of protein is usually accompanied by an unfolding of the macromolecules, gener-
ating new surfaces. Addition of sucrose raises the internal pressure of the solvent,
thus impeding such unfolding processes. The exclusion of sugars and polyols
from the protein surface increase intramolecular hydrophobic interactions among
protein.
More recently, a different concept of cryoprotective effects by high molecular
weight polymers has been proposed. This is called "cryostabilization" theory
based on the ability of high molecular weight solutes to raise the glass transition
of a solution (88,89). Cryostabilization of proteins involves addition of a solute to
raise the glass transition temperature to above the storage temperature, ensuring
that the system is in the glass state. This effectively minimizes the freeze-induced
 596 PARK, LIN, AND YONGSAWATDIGUL

deteriorative process including ice crystal formation, since the water is immobi-
lized in the glass structure. Lanier and MacDonald (90) explained there are fun-
damental differences between the mechanisms of cryostabilization by low molecu-
lar weight polymers: ciyoprotectants function by altering the thermodynamics of
the system to favor the native state of the proteins, while cryostabilizers act to
enmesh the protein in a glass where all deteriorative processes are greatly slowed.
Downloaded by [University of Colorado at Boulder Libraries] at 15:38 28 December 2014

II. GELATION OF FISH MUSCLE PROTEINS AND

ITS APPLICATION IN SURIMI SEAFOOD
Muscle Proteins
Muscle proteins can be categorized into three groups (36): (a) sarcoplasmic pro-
teins are globular and soluble in water or dilute salt; (b) myofibrillar proteins are
contractile proteins which are fibrous and soluble in salt solution; (c) stroma pro-
teins are insoluble fractions. As explained in this article, the solubility of myofi-
brillar proteins at low or zero ionic strength must be noted. After being washed
and refined, surimi constitutes mainly myofibrillar proteins. Approximately
55-60% of myofibrillar proteins is myosin (91). Actin is the second major compo-
nent comprising 15-30% of myofibrillar proteins. Monomer form of actin with
molecular weight of 43,000 daltons is called globular actin (G-actin). Actin mole-
cules polymerize together and form actin filament referred to as fibrous actin
(F-actin). Other small fractions of protein associated with either actin or myosin
are tropomyosin, troponin complex, actinins, M-proteins, and C-proteins (92).
Myosin is an elongated molecule with molecular weight of 470,000 daltons (91).
It is composed of two large subunits called heavy chain and four small subunits
called light chain. Each heavy chain consists of a long a-helical and globular region
with a molecular weight of 200,000 daltons. A long a-helix of each MHC are
wound around each other and forms the rod portion (36). The globular regions
are responsible for ATPase activity and contain actin binding site. Molecular
weight of each light chain ranges from 16,000 to 27,500 daltons, depending on the
source of the myosin (91). When myosin is digested with trypsin, two major frag-
ments are obtained (91,92). The largest fragment is commonly known as heavy
meromyosin containing both myosin globular heads and a portion of the myosin
rod. The other major fragment is light meromyosin which is the helical rod portion
of the myosin molecule. Further proteolytic digestion of heavy meromyosin yields
S-l fragment, the individual myosin head, and S-2 fragment, the small portion of
myosin rod.

Gelation of Surimi

According to Mulvihill and Kinsella (93), protein gels can be defined as "three-
dimensional matrices or networks in which polymer-polymer and polymer-sol-
 MANUFACTURING TECHNOLOGY OF SURIMI 597

vent interactions occur in an ordered manner resulting in the immobilization of

large amounts of water by a small proportion of protein." Ferry (94) proposed
that formation of protein gels involves the following mechanisms:

xP«->xPrf ->(P d )x

where x is the number of protein molecules, Pn is the native protein, and Pd is

denatured protein. Based on this mechanism, gelation is a two-stage process in-
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volving denaturation and aggregation. Denaturation is a process in which native

proteins undergo conformational changes, including alterations of hydrogen
bonding, hydrophobic interactions, and ionic linkages (93). The following process
is aggregation in which denatured protein molecules align themselves and interact
each other at specific points to form a three-dimensional network.
In surimi paste preparation, surimi is comminuted with sodium chloride and
water. Addition of salt is required to extract myofibrillar proteins from the fish
muscle (95). This is achieved through disrupting intermolecular electrostatic
forces among myofibrillar proteins (96,97). In addition, salt destabilizes the native
structures of proteins prior to thermal denaturation (98). Interactions between
myosin and actin upon chopping yield a macromolecule called actomyosin (95).
A three-dimensional gel network is formed when the solubilized actomyosin is
heated. Thermal denaturation of actomyosin begins at 30-35°C in which native
tropomyosin and troponin dissociate from F-actin (99). Then, helical structure of
F-actin unravels to form a single chain at 38°C. When temperature reaches
40-45°C, four myosin light chain subunits dissociates from the globular head of
MHC. Concomitantly, conformational changes of globular head occur. As tem-
peratures reaches 45-50°C, actin-myosin complex starts to dissociate from each
other. Helical regions of MHC then unfold and transform to the random coil
structure. Finally, conformation of G-actin monomer alters at temperatures
greater than 70°C.
Myosin normally undergoes multiple conformational changes during thermal
denaturation. DSC thermograms of rabbit myosin reveal that discrete regions of
myosin molecules, namely globular head and rod portions, exhibit different Tmax,
temperature at which the maximum rate of heat input occurs (100-102). Tran-
sition temperature is dependent on pH, ionic strength, and heating rate
(98,100,102). Tmax values decrease as ionic strength increases and as pH decreases
(100-102). This is because hydrogen and monocovalent ions (H+, Na+, K+) des-
tabilize myosin structure by interfering with electrostatic forces that maintain the
native molecules, resulting in a reduced thermostability of myosin molecules (96).
Tmax also decreases with decreasing heating rates (98,102).
Myosin isolated from mammals show different thermal behaviors than from
fish myosin. DSC thermograms indicate that thermal denaturation offish myosin
takes place at lower temperatures than that of rabbit myosin, suggesting the
structure offish myosin is less thermostable (103,104). The variations in thermo-
 598 PARK, LIN, AND YONGSAWATDIGUL

stability of myosin among species are due to differences in habitat temperature

of the animals (103). These studies also indicated that denaturation offish myosin
was mainly attributed to conformational changes of the a-helical structures of
myosin.
According to Ferry (94), the aggregation is the process following denaturation.
However, aggregation of myosin proceeds prior to the final stage of denaturation
(102,105). Sano et al. (97,106) reported that gel formation of carp myosin first
began to develop through interaction of the light meromyosin at 30-45°C. The
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second step of gel formation involved aggregation among heavy meromyosin by

hydrophobic interactions at 50°C. However, Taguchi et al. (107) suggested that
aggregation of heavy meromyosin S-l occurred to a greater extent at 30-40°C.
They proposed that myosin gelation was initiated by interaction of heavy
meromyosin S-l at 30-40°C, followed by thermal unfolding and interaction of
light meromyosin to form the gel network at 50°C. This gelation mechanism is in
agreement with the findings of Gill and Conway (108) who reported that the tail
region of cod myosin, rather than the head, participated in noncovalent interac-
tion at 40-50°C. Chan et al. (109) studied the role of myosin fragments in cod and
herring suggesting that myosin molecules initially aggregated through interaction
of heavy meromyosin S-2, at 30-40°C. Further aggregation at 40-55°C was medi-
ated by interaction of light meromyosin. The results from these studies indicate
the important role of discrete regions of myosin molecules in forming gel net-
works. Discrepancies in the role of myosin fragments between the studies of Sano
et al. (97,106) and the others are probably due to the structural differences in these
discrete portions among different fish species (109).
The synergistic role of actin in gelation of myofibrillar proteins is also observed
(110-112). The optimal weight ratio of myosin to actin that yields the highest shear
modulus is 15:1. Yasui (112) explained that the complex formed between F-actin
and myosin behaved as a cross-linker between the rod portion of myosin mole-
cules, which consequently increased rigidity of the gel. They also reported that
tropomyosin and troponin did not affect gelation of myofibrillar proteins.
Hydrogen bonding and hydrophobic interaction mainly contribute to the gel
structure of surimi, but the role of disulfide bonding is insignificant (113,114). In
contrast, Samejima et al. (115) reported that globular head segments of rabbit
myosin formed disulfide linkages providing extra cross-linking to gel structure.
Hydrophobic interactions are enhanced during heating when myosin structures
unfold and expose their hydrophobic amino acids to the environment (116). The
surimi gel matrix is stabilized and strengthened by hydrogen bonding during the
cooling period (116).
Nondisulfide covalent bonds are also involved in gelation of surimi made from
some fish species. Preincubation of Alaska pollock surimi pastes at 25°C for 1-24
h prior to heating to 90°C improves textural properties of surimi gels (117,118).
This phenomenon is called "setting" and is also observed in surimi made from
other fish species such as Atlantic croaker (119,120) as well as Southern blue
 MANUFACTURING TECHNOLOGY OF SURIMI 599

whiting and hoki (121). The optimum setting temperature is species specific (120).
An improvement in surimi gels is due to polymerization of myosin molecules be-
tween y-carboxylamide groups of glutamine and e-amino groups of lysine residues
(122,123). The cross-linking of myosin is a Ca++-dependent reaction and is cata-
lyzed by endogenous transglutaminase (124,125). Recently, the addition of micro-
bial transglutaminase produced by Streptoverticillium mobaraense also increases
E-(y-glutamyl)lysine crosslinks as well as textural properties of pollock surimi and
surimi seafood (126). A unique characteristic of microbial transglutaminase is its
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Ca++-independent catalytic activity.

Lee and Park (127) reported a different behavior with pollock and whiting
surimi at different incubation conditions. For pollock, stress increased by —45%
when incubated at 25°C and —70% increase with preincubation at 5°C. For whit-
ing, stress increased by —20% when incubated at 25°C, while no changes were
shown with preincubation at 5°C. Effect of preincubation (setting) temperature
was quite different according to species. Pollock gels were more effective at 5°C
setting, while whiting gels at 25°C. This result was likely related to habitat tem-
peratures of these species. Similar studies on gel functionality and its relation to
habitat temperatures were conducted. Kim (119) reported that the strongest pol-
lock gels were obtained with a 4°C setting for 24 h followed by cooking at 90°C for
15 min, while Atlantic croaker performed best at a continuous treatment of 40°C
for 30 min and 90°C for 15 min. Park et al. (114) also found the optimum setting
temperature for Pacific whiting was 25°C instead of 5°C. Misima et al. (128) con-
firmed that Ca++-activated myofibrillar Mg++-ATPase was highest at the habitat
temperature of carp (25.5°C). The study by Lee and Park (127), along with other
literature, supports a possible relationship between water temperature of fish
habitat and the optimum setting temperature to maximize gel strength of surimi.
Alaska pollock surimi from the Bering Sea performs well at 4-5°C, Pacific whiting
and carp at 25°C, and Atlantic croaker at 40°C.

Ohmic Heating and Its Application

Ohmic heating occurs when alternating electric current (50 or 60 Hz) passes
through electrically conducting food product (129). Heat is generated within the
food due to its electrical resistance, resulting in a relatively rapid heating rate. The
rate of temperature increase in the ohmic process ranges from 1 to 5°C/sec (130);
whereas, the surface of a can in conventional sterilization is about 0.2°C/sec (131).
A number of applications have been found, such as blanching (132,133), thawing
(134), and sterilization (135). Most studies have indicated that the ohmic process
reduces processing time and results in superior product quality compared with
those processed by conventional means. However, practical application in such
processes has been very limited due to the problems associated with process and
equipment design (136).
 600 PARK, LIN, AND YONGSAWATDIGUL

Ohmic heating has been introduced commercially as a means of sterilizing par-

ticulate foods (135). In conventional aseptic processing of particulate foods, the
heat is transferred to the solid particles from the heated liquid phase. Heat pene-
tration is relatively slow and non-uniform because heat transfer is controlled by
conduction. Thus, the product is normally overprocessed to ensure commercial
sterility, resulting in destruction of flavors and nutrients, and mechanical damage
to the particulate (136). This problem can be overcome with ohmic heating in
which particulate and liquid portions are simultaneously heated if the electrical
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conductivity of both phases are similar (130). The ohmic heating process devel-
oped by APV Baker consists of a series of cylindrical electrodes connected to a
50-Hz three-phase supply (137). The food is pumped through the electrodes and
is rapidly sterilized. The use of multiple electrodes provides a uniform electric
field in each section.
Inactivation of microorganisms in the ohmic process is mainly attributed to
thermal effect, rather than the nonthermal effect associated with field strength
(138). Rate of heat generation in ohmic heating for a homogenous material can
be written as (130):

Q = aE2

where Q is rate of heat generation per unit volume, a is electrical conductivity

(S/m), and E is voltage gradient (V/m). Electrical conductivity is the critical prop-
erty affecting rate of heat generation. In the case of very low or zero electrical
conductivity (insulator), the resistance of the food will be so high that a desired
heating rate cannot be achieved because of negligible current flow (139). Further-
more, the sample with infinite electrical conductivity cannot be heated due to
insignificant resistance. Thus, a feasible region of electrical conductivity is re-
quired for ohmic operation (130,140).
Besides aseptic processing of particulate foods, several attempts were made to
use ohmic heating in the meat industry, de Alwis and Fryer (129) summarized the
application of ohmic heating in cooking frankfurters, meat patties, and coagulation
of meat products. The design of ohmic heating devices were varied according to
the shape and type of the product. In general, these meat products are packed
into a non-conductive container and are contacted between two electrodes. Lui-
jerink (141) developed the ohmic apparatus to cook non-homogenous meat prod-
ucts. The sample was placed between several adjacent electrode pairs connected
to a temperature sensor. The temperature at each compartment was automatically
controlled accordingly by adjusting a power supply. The use of ohmic heating in solid
foods has been very limited due to contamination problems caused by sparking
and burning of the electrodes. Good contact between the electrode and product,
which minimizes the scorching, has been suggested, such as applying an edible elec-
trical conducting gel at electrode interface (142), using spring-loaded contacts,
and assuring appropriate penetration of the product by the electrode (129).
 MANUFACTURING TECHNOLOGY OF SURIMI 601

Ohmic heating has recently been used in manufacturing surimi seafood (143).
Textural properties of the ohmically heated products are superior to those heated
in a 90°C water bath (144,145). Yongsawatdigul et al. (146) also found that Pacific
whiting surimi heated ohmically from 10 to 90°C within 1 min displayed double
increase in shear stress and shear strain as compared with conventionally-heated
gels (90°C for 15 min) (Fig. 8). In addition, a superior gel quality was accompanied
by minimal loss of MHC.
Degradation of myosin in the conventionally-heated samples is caused by the
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endogenous proteinase identified as cathepsin L (147). The purified enzyme (pH

5.5) exhibits maximal activity at 55°C. Since the endogenous proteinase is heat
stable, the slow heating rate associated with conventional heating methods allows
the proteinase to hydrolyze myosin before it is thermally inactivated. When surimi
packed in a stainless steel tube (i.d. = 1.9 cm) is heated in a 90°C water bath,
temperature at the geometric center gradually increases and remains in the en-
zyme activation ranges, 45-60°C, for about 85 sec (148). This could be ample time
for hydrolytic reaction of myofibrillar proteins, especially myosin.
Yongsawatdigul and Park (149) later found that a fast and linear heating rate
generated by ohmic heating was not beneficial for Alaska pollock surimi. Shear
stress of Alaska pollock surimi treated ohmically at slow heating rate (l°C/min)
was greater than that heated ohmically at 30°C/min. In addition, polymerization
of MHC through nondisulfide covalent bond was also evident in a slow heating
treatment. Transglutaminase, an endogenous enzyme prevalent in Alaska pol-
lock, is reported to catalyze a crosslinking of MHC, resulting in a increased shear
stress during "setting" of Alaska pollock surimi paste at 25°C (120,124,125). A
slow heating regime is likely to prolong myosin crosslinking reaction because

CON OH-0 OH-1 OH-3 OH-5

Heating Methods

Figure 8. Shear stress and shear strain of Pacific whiting surimi gels. CON: gels cooked in water
bath at 90°C for 15 min; OH-0,1,3,5: ohmic heating to 90°C after holding at 55°C for 0,1,3,5 min.
 602 PARK, LIN, AND YONGSAWATDIGUL

transglutaminase is subjected to an optimum temperature range (25-30°C) for a

longer period.

Effect of Heating Rate on Gelation of Surimi

Gelation of food proteins are greatly influenced by heating temperature and time.
A slow heating rate produces strong protein gels made from myofibrillar and sar-
coplasmic proteins (150,151), myosin and fibrinogen (49), as well as vicillin and
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ovalbumin (152). Wu et al. (153) also reported that chicken breast myosin formed
more elastic gel at relatively low temperatures (44-56°C) than at high tempera-
tures (58-70°C). Although the extent of aggregation of fish myosin is species de-
pendent, Chan et al. (109) indicated that the aggregation rate offish myosin through
noncovalent bonds increased rapidly at temperatures between 32 and 50°C. These
phenomena have been explained by gelation kinetic in which aggregation is fa-
vored at slow heating (94). As a result, heat denatured proteins align in an ordered
fashion to form a fine and elastic networks.
The effect of a wide range of linear heating rates on surimi gelation was first
reported by Yongsawatdigul and Park (149). Since water bath heating provides
nonlinear temperature profiles (Fig. 9), the influence of such heating rates on
gelation cannot be validated. Linear heating rates may be achieved using a pro-
grammable water bath only when slow heating rates such as 12-85°C/min are
applied (49,151,152). However, when ohmic heating is applied, a wide range of
linear heating rates can be developed (Fig. 10).
Based on the discussion thus far, inherent characteristics offish such as aggre-
gation behavior, endogenous transglutaminase, and heat-stable proteinase activi-
ties are important factors in determining the heating process. Surimi made from

20
Water Bath O Ohmic Heating
04
6 8 10 12 14 16
Heating Time (min)

Figure 9. Temperature profiles of two heating methods: water bath and ohmic heating.
 MANUFACTURING TECHNOLOGY OF SURIMI 603

100

80
u
60

40

20
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-G30 + 2 0 -MO S 5 *l°C/min|

0
20 40 60 80 100
Time (min)

Figure 10. Development of a wide range of linear heating rates using ohmic heating method.
Adapted from Yongsawatdigul and Park (149).

fish containing high transglutaminase activity, such as Alaska pollock, can form
gels with high shear stress when either slow heating or "setting" is applied (Fig.
11). In contrast, a rapid heating regime is necessary for surimi made from fish
exhibiting high heat-stable proteinases (Pacific whiting, arrowtooth flounder) (Fig.
11). It is important to maximally retain myofibrillar proteins, especially myosin,
so that inter- and intra-molecular interactions of myosin can be achieved.

50
40 JElPoIlock MWhiting [
30
20
10
No Gels No Gels
0
3

0
5 10 20
Heating rate (°C/min)

Figure 11. Textural properties of two species surimi gels as affected by different heating rates.
Adapted from Yongsawatdigul and Park (149).
 604 PARK, LIN, AND YONGSAWATDIGUL

High Hydrostatic Pressure of Surimi

Besides heat-induced gelation, muscle proteins can form gel upon pressurization.
Pressure is known to have an effect on the rearrangement of hydrogen bonds,
hydrophobic interactions, and electrostatic bonds of the tertiary structure of pro-
teins (154,155). At low ionic strength (0.1 M KC1), rabbit myosin existing as fila-
ments forms gel at 200-280 MPa (156). Microstructure and textural properties of
such gels are comparable to those of heat-treated samples. Tumminia et al. (157)
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demonstrated that the length of myosin filament at pH 7.0 decreased with pres-
sure up to 100 MPa due to partial depolymerization of filaments. In addition, the
dissociated myosin molecules reaggregate and form another population of fila-
ments, which are shorter than original myosin filaments.
However, high pressure alone cannot induce gelation of myosin at high ionic
strength (0.5 M KC1) (158). Ishizaki et al. (159) reported that the extent of myosin
denaturation at high ionic strength (0.6 M NaCl) is less than that at low ionic
strength (0.05 M NaCl). At high ionic strength, intramolecular association of two
heads takes place upon pressurization of myosin. However, intermolecular asso-
ciation through entanglement of myosin tails does not occur as in a thermal gela-
tion process, indicating that helix structure in the tail is retained after application
of pressure up to 500 MPa (158,159). Conformational changes of fish myosin
(black marlin and jack mackerel), as assayed by hydrophobicity and a-helix con-
tent, mainly occur at S-l portion, not at myosin rod (159).
As mentioned earlier, myosin exhibited an ATP hydrolytic activity in the pres-
ence of Ca++. Activity of Ca++-ATPase can be used as an index of the extent of
myosin denaturation. It has been reported that thermal inactivation of Ca++-
ATPase of fish myosin follows a first order reaction. However, inactivation of
Ca++-ATPase of various fish myofibrils treated under pressure exhibited a dou-
ble-linear relationship (160). This suggests that the denaturation mechanism of
fish protein by heat is quite different from that by pressure. Hayakawa et al. (161)
reported that denaturation of proteins under high hydrostatic pressure was caused
by structural changes of the water molecule.
F-actin in the absence of ATP undergoes irreversible denaturation at pressure
above 150 MPa, whereas, ATP's presence shows a significantly protective effect
against pressure-induced denaturation of actin (162,163). In actomyosin, a gel to
sol transition is promoted as a result of pressure treatment. In the absence of ATP,
an association remains between myosin and actin of actomyosin under pressure,
whereas in the presence of ATP, actomyosin dissociates into the individual com-
ponents (162). Heat-induced gels of pressurized actomyosin exhibit storage
modulus (G') higher than those of unpressurized actomyosin regardless of salt
concentration (164). Sulfhydryl content and surface hydrophobicity of pressurized
actomyosin are higher than those of unpressurized sample (162). This would en-
hance protein-protein interactions, resulting in an increased gel strength (G', G")
of pressurized actomyosin.
 MANUFACTURING TECHNOLOGY OF SURIMI 605
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Pressure (MPa)/ Temperature (°C)

Figure 12. Textural properties of two species sumiri gels as affected by hydrostatic pressure and
temperatures. 1 MPa equals to 10 bar or 750 mmHg. Adapted from Chung et al. (168).

Gel of Alaska pollock surimi can be produced at 0°C when subjected to 200-400
MPa for 10 min (165). Crosslinking of MHC of the pressure treated samples in-
volves nondisulfide covalent bonds. Okamoto et al. (166) demonstrated that gels
of carp actomyosin exposed to pressure at 196 MPa for 30 min were translucent
as uncooked sample and exhibited lower stress but higher strain than heat-in-
duced gels. Translucency of pressure-treated gels was presumably attributed from
rearrangement of water molecules surrounding amino acid residues upon high
pressure treatment. However, opaqueness of bluefish surimi increased with ap-
plied pressure and resembled that of heated-induced gel at 300 MPa (167).
The use of high pressure in conjunction with heat can provide an adverse affect
on surimi gels. Chung et al. (168) demonstrated that high pressure of 100-240
MPa at 28-35°C increased textural properties of both Alaska pollock and Pacific
whiting surimi (Fig. 12). However, applying high pressure at 50°C resulted in a
decreased shear stress and shear strain of both surimi. The pressure of 100-240
MPa induces the rupture of lysosomal membrane, resulting in a release of lysoso-
mal enzymes, specially cathepsin L which is responsible for proteolysis of myosin
at elevated temperatures (55-60°C). Ohmori et al. (169) also demonstrated that
proteolytic activities of various endogenous proteinases in beef increased with
applied pressure. Aminopeptidase and carboxypeptidase can be completely inac-
tivated at 400-500 MPa in 10 min. Some of lysosomal proteinases, namely, cathep-
sin B, D, and H, still remain activity at 506.6 MPa (170).
 606 PARK, LIN, AND YONGSAWATDIGUL

CONCLUSION

Solubilization of myofibrillar proteins at zero (water) to low salt concentration

was not generally accepted according to classical muscle chemistry. However, it
is true that myofibrillar proteins are soluble in water and become more soluble
with extended washing steps. For surimi processing, myofibrillar proteins which
were lost in the form of particulates in the final dewatering process, could be
successfully recovered and concentrated using a rotary screen and microfiltration.
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The great reduction of APC and COD in waste waters are achievable using ul-
trafiltration. Use of UF equipment provides the possibility of recycling processing
water in the leaching system.
A new technology, ohmic heating appears to have two significant contributions
to the surimi industry. Its extremely rapid heat generation is very effective for
Pacific whiting surimi which often shows weaker gels due to its protease at slow
heating conditions. The other benefit of ohmic heating is its uniform heat genera-
tion. The ohmic heating is very effective in obtaining a wide range of linear heating
rates which plays an important role in the study of surimi gelation. The use of high
hydrostatic pressure to study the gelation of surimi proteins is new, but appears
to be a promising technology in the manufacturing of surimi seafood.

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