A Review on the Loss of the Functional Properties of Proteins during Frozen Storage and the Improvement of Gel-forming Properties of Surimi
The functional properties of the myofibrillar proteins were protected during frozen storage when a cryoprotectant was added. Some normally used cryoprotectants are sorbitol, sucrose, polydextrose, lactitol, litesse, maltodextrin, trehalose, sodium lactate and mixtures of the above cryoprotectants. Phosphate is normally added to surimi in combination with cryoprotectants to reduce viscosity, increase moisture retention and the proteins ability to reabsorb liquid when the surimi is thawed or tempered and increase the pH slightly, which leads to improved gel-forming ability, gel strength and cohesiveness. Some food additives also can be used to improve the physical properties of and prevent the textural degradation of, surimi gels such as egg whites, Beef Plasma Protein (BPP) and Whey Protein Concentrate (WPC). A new surimi-developing process using an acid and alkaline washing method has shown significant potential for use in increasing the concentration of myofibrillar protein in the surimi.
Received: February 28, 2010;
Accepted: April 11, 2010;
Published: July 05, 2010
In Japan, the term was denoting for a minced fish product, where most of the
water soluble components including sarcoplasmic proteins have been removed by
leaching with potable water. According to Okada (1992),
surimi is the wet concentrate of the myofibrillar proteins of fish muscle that
has been mechanically deboned, water-washed and frozen. The Japanese have been
improving surimi technology for several hundred years. The development of the
industry has recently been supported by an increase in the supply of raw materials,
the development of new products and the development of new technologies for
manufacturing and preserving the products. The surimi industry has spread to
other countries such as Korea, Europe and the United States.
Surimi can be produced from both marine and fresh-water fish, including both
white-muscled and dark-muscled fish, such as alaska pollock, blue whiting, croaker,
lizardfish, sardine, tilapia and bigeye snapper. Commonly, certain species are
used due to their easy capture and low price. The use of alternative species
in order to obtain surimi of good gel-forming ability is one of the aims of
the fishing industry.
Surimi technology has been widely developed. Significant effort has been directed to developing new products, as well as new technologies for waste-water treatment, the utilization of other fish species, preserving surimi-based products, the utilization of some cryoprotectants and improved gel-forming.
THE IMPORTANCE OF SURIMI
Surimi is a Japanese term referring to the ground fish meat paste formed during
the manufacturing process of traditional Japanese product kamaboko.
Introduced more than two decades ago, since 1980s, Surimi is now an important
industry in the Southeast Asian region. A 2006 survey found that a total of
80 surimi processing plants are located in the region; including 26 in Thailand,
15 in Vietnam, 3 in Myanmar, 8 in Indonesia and 15 in Malaysia (SAFDC,
Surimi is the primary ingredient in a variety of processed foods such as kamaboko,
kani (crab)-kamaboko, chikuwa, satsumage, fish sausages and fish balls, contributing
more than 50% to the production yield. Huda and Noryati
(2009) reported most of fish balls manufacturer in Malaysia used surimi
for their production. Similar trend also begin at fish cracker manufacturer
(Huda and Ariffin, 2010). The quality of these products
depends very much on the quality of the surimi used. Surimi gels upon kneading.
Gel is an important characteristic for surimi-based products. However, it soon
loses this ability upon frozen storage. That is to say, the functional properties
of the myofibrillar proteins in the raw surimi deteriorate rapidly during freezing:
the freezing process causes ice crystals to form, which results in the dehydration
of the myofibrillar protein, a pH decrease and a change in salt concentrations.
These three effects, in addition to various hydrophobic interactions, denature
and/or aggregate the frozen myofibrillar proteins in surimi. Furthermore, the
longer the surimi is frozen, the greater is the degree of protein denaturation
(United States Patent 5436024, 1995). The formaldehyde
level in a given fish muscle has been used as an index of frozen storage deterioration.
Myofibril proteins that react with formaldehyde have become denatured and formation
of protein aggregates has occurred. Benjakul et al.
(2004) reported that lizardfish produce high levels of formaldehyde, leading
to high levels of protein aggregation, as shown by the considerable loss of
solubility during 6 months storage at -18°C. Several technologies
have been applied in attempts to prevent the problem, including the use of cryoprotectants
like sugars and sugar alcohols, as well as quick-freezing the surimi into block
form. It is essential to provide a cryprotectant that (1) Maintains the functionality
of proteins in frozen surimi, (2) has a low tendency to cause Maillard browning
during storage of the surimi at freezing temperatures and during the heating
of a surimi-based foodstuff and (3) has a mild taste (United
States Patent 5436024, 1995).
Many techniques for improving the texture of surimi-based products have been
proposed and implemented, including adjusting the pH of the surimi paste (Rawdkuen
et al., 2008; Karayannakidis et al., 2007),
application of temperature setting prior to cooking (Alvarez
et al., 1997) and using additives like polyphosphate and potassium
bromated (Julavittayanukul et al., 2006). Further
improvements in both physical and nutritional quality are anticipated: current
research focuses on the development of low calorie, low cholesterol value-added
products, replacing the cryoprotectants in surimi with low-calorie substitutes.
THE RAW MATERIALS OF SURIMI
The fish normally used for making surimi are alaska pollock or walleye pollock
(Theragra chalcogramma), new zealand hoki (Macruronus novaezelandiae),
southern blue whiting (Micromesistius australis) and northern blue whiting
(Micromesistius poutassou). In Asia, several species, such as the croaker
(Pennahai macrophthalmus), lizardfish (Sauruda micropectoralis),
barracuda (Sphyraena sp.), hairtail (Trichiurus sp.), atka mackerel
(Pleurogrammus azonus), threadfin bream (Nemipterus bleekeri)
and bigeye snapper (Priacanthus tayenus), are commonly used by shore-based
surimi manufacturers (Park, 2005).
Pollock is a small cousin of cod and found throughout the North Pacific, north
of latitude 30°N from the Gulf of Alaska in the East, throughout the Bering
Sea, around the Kamchatka Peninsula in the West Pacific and into the Sea of
Japan. Pollock is chosen because of its abundance, accessibility, subtle flavor
and low odor and low cost, making this species preferable as a raw ingredient
of surimi (Lanier and Lee, 1992).
New Zealand hoki is another popular species used for surimi in Japan and Korea.
Most of the hoki caught is currently processed into surimi or other high-quality
fillet and fillet-based products. Hoki flesh is normally high in protein, up
to 20% and low in oil, at less than 5%. The predominant characteristics of hoki
flesh are a mild, slightly sweet flavor and a moist texture. Recent research
has shown that at the same protein-to-moisture ratio, hoki surimi has similar
functional qualities to the equivalent grades of alaska pollock surimi and that
surimi from these two species could be interchangeable when manufacturing surimi-based
products (Lanier and Lee, 1992).
Southern blue whiting is a member of the true cod family that lives in the
sub-Antarctic waters South of New Zealand. The composition of southern blue
whiting muscle (g/100 g sample) is as follows: 79.35% moisture, 18.57% protein,
1.21% ash, 0.78% fat and 0.78% carbohydrate (Stark et
al., 2009). Southern blue whiting can be made into surimi with a high
functional quality and can form a very firm and cohesive gel. Generally, southern
blue whiting surimi is whiter and has lower fishy flavor and odor scores than
hoki or Alaska pollock surimi. In the Southern Hemisphere, Southern blue whiting
is second only to hoki for use in surimi production (Lanier
and Lee, 1992).
Northern blue whiting occupies the North Atlantic off the coast of Norway and
the Faeroe Islands and is the most commonly used species for surimi production
in this area. Its meat yield rate is 22-27% (Lanier and Lee,
1992). Northern blue whiting offers a high-quality surimi similar to that
from southern blue whiting (Park, 2005).
The use of threadfin bream for surimi production has increased dramatically
over the past decade and will continue to play a major role in surimi markets
in the future. It has been shown to make a high-quality surimi with good gel
strength. These fish are benthic, inhabiting marine waters on sandy or muddy
bottoms, usually at depths of 20 to 50 m and feeding on small benthic invertebrates
and small fish. Because of the white color, smooth texture, strong gel-forming
ability and easy processing, threadfin bream surimi is widely used as raw material
for Japanese kamaboko and surimi-based crabstick or kani-kama (Park,
Croaker is the preferred fish of the traditional kamaboko industry. The croakers
myofibrillar proteins are highly stable in frozen storage, making it a good
candidate for surimi processing. Croaker is one of the most bountiful near-shore
species in Asia. There are more than 60 species of croaker, but the three of
interest to surimi producers are blackmouth croaker (Atrobucca nibe),
white croaker (Argyrosomus argentatus) and yellow croaker (Pseudoscianena
polytis). The meat of blackmouth croaker has a good flavor with a strong
gel-forming ability and is most commonly used in Taiwans croaker surimi.
Average yields are 43%, very high compared to other species used for making
surimi. White croaker meat has only a moderately good flavor, but its meat has
the best gel-forming ability of all the croaker species and is the main species
used in Japanese croaker surimi. Yellow croaker meat has a very good flavor
but is said to have a low gel-forming ability (Lanier and
Lee, 1992). Croaker surimi from these species is generally darker in color
than threadfin bream surimi, but can fetch a high price in Japan (Park,
Lizardfish has long been considered a high-grade surimi fish and is used for
kamaboko processing in Japan. The fresh meat is white in color, has a good flavor
and a very high gel-forming ability. However, the freshness and gel-forming
ability decrease quickly in storage and the stability of the fish is very low
in frozen storage. Thus, the fish must be processed quickly after catching and
at low temperatures. Generally, frozen lizardfish cannot be used for frozen
surimi. Japan is the only country that is currently using lizardfish for surimi
Pike-conger has a rich flavor that demands immediate processing directly into
surimi, without leaching. There are five species of pike-conger; the one most
used for surimi is daggertooth pike-conger (Muraenesox cinereus). Pike-conger
has an extremely high meat-yield rate of 68%. Its fat content is also relatively
high (Lanier and Lee, 1992).
The largehead hairtail has slightly gray flesh and makes a middle-grade surimi.
However, only Japan uses hairtail in surimi. It has a good flavor but a low
gel-forming ability. The meat-yield rate is about 50% and it has a relatively
high fat content (Lanier and Lee, 1992). Although it has
a low gel-forming ability and the surimi is generally darker in color, it is
used in Japan for surimi because of its good flavor (Park,
Atka mackerel is a member of the greenling family and produces a middle-quality
surimi. The Japanese use Atka mackerel for surimi, but use only the small fish.
The meat is slightly yellowish-gray, with about a 45% meat-yield rate. The fat
content of Atka mackerel is relatively high for a surimi fish and has a low
gel-forming ability (Lanier and Lee, 1992).
There are 10 species of bigeye, but the purple-spotted bigeye (Priacanthus
tayenus) is the species most likely to be used for surimi. Bigeye meat is
slightly dark but has a high gel-forming ability (Lanier and
The use of alternative fish species, other than those above, to obtain surimi with a good gel-forming ability is one of the aims of the fishing industry. Pelagic species like sardine, tilapia, rainbow trout, grass carp are now being considered in surimi manufacturing due to their easy capture and low price.
DEVELOPMENT OF SURIMI TECHNOLOGY
Lanier and Lee (1992) assert that surimi is produced
by repeatedly washing mechanically separated fish flesh with chilled water (5-10°C),
until most of the water- soluble protein has been removed. The washing procedure
is key to for the final surimi quality, not only for removing fat and undesirable
materials, such as blood, pigments and odorous substances, but, more importantly,
for increasing the concentration of myofibrillar protein, thereby improving
the gel-forming ability of the surimi. Then, the raw surimi is mixed with cryoprotectants
such as sugars or sugar alcohols. The latter form is quick-frozen into blocks
and becomes frozen surimi.
Many studies have been conducted to improve the technology of surimi-making,
especially to reduce the loss of the functional properties of myofibrillar proteins
during frozen storage and to improve the gel-forming ability. The addition of
cryoprotectants is required to retain the functional properties of the myofibrillar
proteins. The most commonly used cryoprotectant in the surimi industry is a
1:1 mixture of sucrose and sorbitol at a concentration of 8% (MacDonald
and Lanier, 1994). Phosphates have been used as additives for improving
the gel-forming ability of the proteins (Julavittayanukul
et al., 2006), along with the pH-shift process (Karayannakidis
et al., 2007; Rawdkuen et al., 2008),
the addition of whey protein concentrate (Rawdkuen and Benjakul,
2008) and the addition of chitosan (Mao and Wu, 2007).
THE STUDIES OF CRYOPROTECTANTS
The most important step in the making of surimi is the addition of the cryoprotectant.
Cryoprotectants are important to stabilize the surimi and protect it during
freezing and frozen storage. However, the myofibrillar proteins in the raw surimi
lose their functional properties rapidly once they are frozen, a process leading
to protein aggregation, textural changes and the loss of gelling and water-holding
functionality in the fish (Lainer and Lee, 1992). MacDonald
and Lanier (1994) reported that the addition of cryoprotectants is required
in order to retain the fishs functional properties. More over, cryoprotectant
is not only able to retain functional properties of protein during freezing
and frozen storage, but also during drying process (Huda
et al., 2000a, 2001). Surimi powder produced
also showing higher protein quality (Huda et al.,
Many compounds, including some low molecular weight sugars and polyols as well
as many amino acids, carboxylic acids and polyphosphates, have been found to
be cryoprotective (Park et al., 1987; Sych
et al., 1991a). Nevertheless, many of them cannot be used for various
reasons such as high cost, food regulations that prohibit them, or adverse sensory
Sorbitol and sucrose: Surimi freezing is done commercially using incorporation
of sucrose (4%), sorbitol (4%) and polyphosphates (0.2%), which protect fish
myofibrillar protein during long periods of frozen storage (Sultanbawa
and Li-Chan, 1998). However, one disadvantage of the current commercial
cryoprotectant blend is the high level of sucrose and sorbitol, which impart
a sweet taste. Yoon and Lee (1990) showed that 4% sucrose
plus 4% sorbitol in crystalline or liquid form in red hake (Urophysics chuloss)
surimi, when given as extruded gel products to a sensory panel, were judged
to be slightly too sweet. In addition, todays consumer is conscious of
caloric content and a low calorie cryoprotectant may be preferred for surimi.
Lactitol: Lactitol is the product of hydrogenation of lactose, thus
also a disaccharide polyol (Marshall et al., 2003)
and well established as a replacement sweeter for low-calorie foods (MacSweeney,
2009). Lactitol was highly effective in preventing changes from taking place
in frozen-stored natural actomyosin extracts of rainbow trout (Herrera
and Mackie, 2004). A study by Sych et al. (1991a)
showed that lactitol in cod surimi (Godus morhua) could be reduced from
8% to 5.7-6.4% without a significant alteration of the stabilizing effect. Another
study by Sych et al. (1991b) showed that lactitol
at the 8% level or lactitol at the 4% level maintained the functional properties
of the myofibrillar proteins in cod surimi during 4 months of storage at -20°C.
Polydextrose: Polydextrose is an odorless, white-to-light-cream amorphous
powder, with virtually no sweetness and an energy value of only 1 kcal g-1
(Roller and Jones, 1996). The use of polydextrose as a
cryoprotectant has been patented by Lanier and Akahane (1986).
Most of the studies on polydextrose have shown that it is a good cryostabilizer
for surimi (Sych et al., 1990, 1991b;
Herrera and Mackie, 2004). Furthermore, other research
has shown that polydextrose at the 8% level maintained the functional properties
of myofibrillar proteins in cod surimi during 4 months of storage at -20°C
(Sych et al., 1991a). Herrera
and Mackie (2004) reported that polydextrose was highly effective in preventing
changes in frozen stored natural actomyosin extracts of rainbow trout. Park
et al. (1987) reported that polydextrose maintained a high level
of solubility in the myofibrillar proteins at -28°C over several months.
Litesse: Litesse is the brand name for improved forms of polydextrose.
Litesse is produced from polydextrose using additional processing to reduce
the acidity and bitterness, thereby improving the flavor profile (Nabors,
2001). Litesse is not sweet and is less bitter, astringent and acidic than
polydextrose and therefore, in most food systems, litesse does not require neutralization.
Sultanbawa and Li-Chan (2001), claimed that the calorie
utilization of litesse is 1 kcal g-1, which is 25% that of carbohydrates.
Sultanbawa and Li-Chan (2001) reported that 8% litesse
was effective in maintaining the gel strength of surimi after eight freeze-thaw
Maltodextrin: Maltodextrin has the potential to act as cryoprotectant
in fish muscle protein. Maltodextrins of varying mean Molecular Weights (MW)
(M040, M100, M150, M180, M200, M250) stored isothermally at either -8,-14, -20°C
for 3 months were evaluated for cryoprotective ability in alaska pollock surimi.
All maltodextrins at -20°C isothermal storage, irrespective of MW, produced
good cryoprotective qualities, but higher MW maltodextrins at higher isothermal
storage temperatures produced poor cryoprotection. Lower MW maltodextrins likely
cryoprotect by a preferential solute exclusion mechanism, similar to sucrose
and sorbitol. Higher MW maltodextrins presumably cryoprotect at lower storage
temperatures via a reduced water mobility mechanism. The MW of maltodextrins
increase the gelling ability of the surimi (Carvajal et
Trehalose: Trehalose is a well-known non-reducing disaccharide synthesized
by a wide variety of organisms and it is considered a dietetic sugar (Arnoldi,
2004). Recently, trehalose has been found to have properties protective
against thermal inactivation of enzymes; this effectiveness was correlated with
its large hydration volume (MacDonald et al., 2000).
Osako et al. (2005) reported that an addition
of 5.0 to 7.5% concentration of trehalose increased the amount of unfrozen water
and prevented freezing-induced denaturation of proteins. Other research has
shown that trehalose exhibited the greatest protective effects on protein denaturation
as shown by the effectiveness Ca2-ATPase activity and protein solubility
in comparison with sucrose and sorbitol. The greatest breaking force and deformation
were obtained in surimi with 8% trehalose added, in frozen storage for up to
24 weeks (Zhou et al., 2006).
Sodium lactate: Sodium lactate has no sweetness and has a low caloric
value. It is currently Generally Recognized as Safe (GRAS) for use as an emulsifier,
flavor enhancer, flavoring agent, humectant and pH control agent (MacDonald
and Lanier, 1994). Sodium lactate has been demonstrated to be an effective
stabilizer against both freeze-thaw and heat-induced denaturation of tilapia
(Tilapia niloticaxTilapia aurea) actomyosin (MacDonald
and Lanier, 1994). Sodium lactate shows a similar cryprotective effect to
sucrose or a sorbitol blend. Sodium lactate at a level of 8% (w/w) effectively
prevented the protein denaturation of tilapia surimi during storage at -18°C
for 24 weeks (Zhou et al., 2006).
Mixtures of cryoprotectants: Matsumoto reported 4% sucrose and 4% sorbitol
to be the optimum cryoprotectant blend (Yoon and Lee, 1990).
Additionally, Medina and Garrote (2002) discovered that
at 45 and 90 days of frozen storage, surubí (Pseudoplatystome coruscans)
surimi made with the sucrose-sorbitol blend had a higher gel strength than surimi
made with maltodextrin-sorbitol in a ratio 1:1, under different processing temperatures
(2 to 18°C), times (1 to 7 min/cycle) and water-to-mince ratios (2:1 to
8:1). However, such a blend yields a taste that is too sweet. Other research
reported that the commercial mix of 4% sucrose and 4% sorbitol, as well as other
cryoprotectant blends at levels ranging from 4-12%, were all effective in ensuring
good gel formation from ling cod surimi after frozen storage at -18°C for
4 months, with the blend containing 4% cryoprotectants (sucrose, sorbitol, litesse
and lactitol at a ratio of 1:1:1:1) offering advantages of reduction in sweetness
and cost (Sultanbawa and Li-Chan, 1998).
Phosphates are natural compounds; they are salts containing phosphorus and
other minerals. The phosphates usually used in surimi are sodium tripolyphosphate
(STPP), sodium pyrophosphate (SPP), sodium hexametaphospate (SHMP), tetrasodium
pyrophosphate (TSPP), tetrapotassium pyrophosphate, sodium hexametaphosphate
(SHMP) and trisodium phosphate (TSP). The names correspond to the standard system
of nomenclature, outlined below. Members of the series having one phosphorus
atom are called orthophosphates. The dimers (two P atoms) are the pyrophosphates,
followed by the triphosphates, also known as tripolyphosphates (three P atoms)
and by the tetraphosphates (four atoms). The members of the homologous series
having 5-15 P atoms are sometimes referred to as oligophosphates (Molins,
The use of phosphates in surimi reduces the viscocity of the paste, allowing
for better machinability (Park, 2005). Phosphates increase
moisture retention and increase the ability of a protein to reabsorb liquid
when the surimi is thawed or tempered. Phosphates increase the pH slightly,
which will also lead to an improved gel-forming ability, gel strength and cohesiveness,
because of an increase in water-holding capacity at a higher pH. Polyphosphate
added at 0.5% provides the greatest gel strength, but 0.3% is optimal for gel
strength and flavor with sodium tripolyphosphate trisodium pyrophosphate used
in combination (Hui, 2006).
Phosphate is normally added to surimi in combination with cryoprotectants,
such as sugar or sorbitol (Sultanbawa and Li-Chan, 2001).
Julavittayanukul et al. (2006) reported that
the type of phosphate (sodium pyrophosphate, PP; sodium tripolyphosphate, TPP
and sodium hexametaphosphate, HMP) and the concentration of phosphate compounds
(0, 0.05, 0.1, 0.3 and 0.5% w/w) had a varying influence on surimi gels from
bigeye snapper (Priacanthus tayenus). An increased phosphate concentration
generally displays a detrimental effect on gel formation, possibly by chelating
calcium ion, required for endogenous TGase. Sodium pyrophosphate (PP) exhibited
superior gel-strengthening effects, compared to the others, whereas sodium hexametaphosphate
(HMP) was shown to have adverse effects on surimi gelation. The use of PP (0,025%)
in combination with CaCl2 (50 mmol kg-1) at appropriate
levels could effectively improve the gel-forming ability of surimi.
THE STUDY OF GEL-FORMING PROPERTIES
Proteolytic degradation of myofibrillar proteins has an adverse effect on the
gel-forming properties of surimi. Various food-grade inhibitors, such as egg
whites and Beef Plasma Protein (BPP) have been used to improve the physical
properties and prevent the textural degradation of surimi gels (Rawdkuen
et al., 2007; Lou et al., 2000). These
are also known as food additives. However, alternative food-grade proteinase
inhibitors for surimi production are still needed.
Egg whites: Egg whites are frequently used in surimi-derived products.
Egg whites make the partially heat-set analog more elastic and stretchable.
The amount of egg whites added depends upon the fish species used and the quality
of the fish used. Hui (2006) reported, egg whites added
at 10% produces a gel with high yield stress; gels containing up to 20% egg
whites are softer, but there is a decrease in gel strength and the gel becomes
brittle at percentages greater than 20%. Egg whites contribute to the structure
of surimi analog gels by filling interstitial spaces in the fish protein network.
Benjakul et al. (2004) reported that the addition
of egg whites up to 3% increased gelling properties of lizardfish surimi regardless
of the heating conditions (40/90, 60/90 and 90°C).
There are some negative effects of using egg whites in surimi. Egg whites are
an allergen and must therefore appear on the label of surimi analog products.
Class II food recalls of analog products have been initiated in the United States
because of the failure of companies to list egg whites on the ingredient statement
(Hui, 2006). In addition, egg whites must be used carefully
because they often generate off-flavors and react with many of the components
of the flavor, particularly the aldehydes found in the flavor or extract used
Beef Plasma Protein (BPP): Beef plasma protein, which is mostly dried,
is used as a gelling agent and/or protease inhibitor. Plasma constitutes about
two-thirds of the weight of blood and can be separated from red cells by centrifugation.
The liquid plasma is then filtered and spray-dried. Beef plasma, which contains
about 70% protein, is widely used in the meat industry for its high solubility
and excellent gelling properties. The latter is attributed to the presence of
fibrinogen (5%), a superior gelling protein and albumin (65%). Plasma protein
can be dissolved in brine and injected into meat. It will form an elastic, irreversible
gel when cooked to above 650C and therefore is suitable for a variety
of sectioned, formed and restructured meats that require a strong bind between
meat chunks and particles. Another important application of beef plasma is in
surimi products. Beef plasma exhibits a remarkable capability to inhibit modori,
or gel weakening, during the cooking of surimi, when it is prepared from some
fish species or animal by-product meats (Yada, 2004).
Lou et al. (2000) reported that electrophoretic
analysis has shown that myosin degradation, which occurs in control surimi samples
heated to above 45°C, is prevented when as little as 0.5% beef plasma powder
sis added. This strongly suggests that beef plasma contains protease inhibitors,
although the nature of such inhibitors has not been elucidated. The BPP may
act as a gel-forming component because BPP contains multiple polypeptides, which
may facilitate the gelation of surimi proteins. Another potential factor is
that BPP contains active transgulaminase, which catalyzes the formation of covalent
bonds and hence assists the gel network formation. Benjakul
et al. (2004) reported that the addition of BPP, up to 3%, showed
higher gel strengthening of lizardfish surimi than egg whites under a variety
of heating conditions (40/90, 60/90 and 90°C), but resulted in a lower whiteness
in the finished product.
After all of the advantages of BPP, surimi added with BPP is not suitable for
Muslim consumer due to the Halal issue (Huda et al.,
1999). The use of BPP also prohibited in the EU, Japan, Canada and the Unites
States due to the outbreaks of BSE (bovine serum encephalopathy, or mad-cow
disease) (Park, 2005).
Whey protein concentrate: Whey Protein Concentrate (WPC) has commonly
been used as a protein supplement, foam stabilizer, filler/water binder and
as a thickening, emulsifying and gelling agent (Rawdkuen
and Benjakul, 2008). Previous studies have shown that WPC increases the
shear strain of surimi gels prepared from Pacific whiting and alaska pollock
(Chang-Lee et al., 1990; Park,
1994; Piyachomkwan and Penner, 1995; Weerasinghe
et al., 1996). Rawdkuen and Benjakul (2008)
reported that breaking force and deformation of kamaboko gels of all surimi
increased as the levels of WPC added increased (0-3%). The WPC at 3% (w/w) significantly
decreased the whiteness of the gels. However, the water-holding capacity of
kamaboko gels improved with increasing concentrations of WPC. The microstructure
of surimi gels generally became denser with the addition of WPC.
NEW DEVELOPMENTS IN THE SURIMI PROCESS
The washing procedure is very important for the quality of the finished surimi,
not only because it removes fat and undesirable materials, such as blood, pigments
and odorous substances, but more importantly because it increases the concentration
of myofibrillar proteins, improving the gel-forming ability (Lanier
and Lee, 1992). Acid and alkaline-aided solubilization has shown potential
as a new method for maximal protein recovery from muscle foods. Park
(2005) claims that the procedure offers several advantages, including high
yields, high-quality proteins, the improvement of functional properties, pollutant
reduction, the removal of most lipids and the efficient removal of insoluble
impurities. The extraction mechanism of the two processes is to solubilize the
muscle protein at low- and high-pH levels to separate soluble proteins, bone,
skin, connective tissue, cellular membranes and neutral storage lipids through
centrifugation. The proteins recovered by this process have good functionality
and in some cases better gelation properties (Rawdkuen et
al., 2008) than have proteins recovered by conventional surimi processing
(Kristinsson et al., 2005).
In general, lean fish have traditionally been used for surimi production worldwide.
Due to increasingly limited fish resources, dark-muscle fish have been gaining
popularity as an alternative raw material for surimi production. However, one
problem that arises when producing surimi from dark-fleshed fish species is
the high lipid and myoglobin content associated with dark muscle fish, resulting
in difficulties in making high-quality surimi. Due to the lower pH of dark-fleshed
fish, the gel forming ability of the proteins decreases gradually during post
mortem handling or storage. To alleviate this problem, alkaline leaching has
been developed to raise the pH of the muscle and to increase the efficacy in
removing sarcoplasmic protein, lipid and pigments. Balange
and Benjakul (2009) discovered that the alkaline-saline washing process
for surimi with 0.25% oxidized tannic acid added showed increases in breaking
force and deformation in mackerel surimi, improving the gel properties compared
with that of surimi produced using a conventional washing process, without adverse
effects on sensory properties.
Other studies have shown that acidic wash treatments (pH values of 2.50, 4.00
and 5.50) used in products from sardines (Sardina pilchardus) offers
a higher recovery of total solids and proteins, while washing in alkaline (pH
values of 8.50, 10.00 and 11.50) solutions was more effective in removing lipids.
Lightness and whiteness indices improved due to washing and increased further
when a thermal process was applied, particularly in the samples washed under
acidic conditions. Kamaboko gels washed under acidic conditions showed higher
values in firmness as well as cohesive properties and elastic textures. Whiteness
showed the highest values at pH 4.00 and 5.50. Increasing values of lipids and
ash removal were indicative of high pH values (10.00 and 11.50) and of low-firmness
and cohesiveness of the final product. Sardine samples initially washed at pH
5.50 can lead to high-quality kamaboko gels (Karayannakidis
et al., 2007). Rawdkuen et al. (2008)
reported that a higher protein yield and greater lipid- and pigment-reductions
in tilapia muscle were achieved with the acid-alkaline-aided process than with
the conventional washing process.
Surimi is stabilized minced fish meat that is washed with water and blended with cryoprotectants. The enriched myofibrillar fraction of that protein is the starting material for the surimi, which is used for gel-based products. Low-sweetness sugar has been used by some researchers in surimi processing. Cryoprotectants are additionally required in order to retain functional properties of the myofibrillar proteins, such as the gel-forming properties of surimi, since surimi may lose its functional properties because of the denaturation and/or aggregation of myofibrillar proteins during frozen storage. To improve the physical properties and prevent the textural degradation of the proteins, some food additives permitted by food regulation and new processes in washing methods can be used for manufacturing surimi.
The authors would like to acknowledge with gratitude the support given by Universiti Sains Malaysia (USM) for our research in this area. This research was carried out with aid of a research grant from Malayan Sugar Manufacturing Company Berhad through grant 304/PTEKIND/650442/K132.
1: Alvarez, C., I. Couso and M.S.M. Tejada, 1997. Waxy corn starch affecting texture and ultrastructure of sardine surimi gels. J. Zeitschrift fur Lebensmitteluntersuchung und -Forschung A, 204: 121-128.
2: Arnoldi, A., 2004. Functional Foods, Cardiovascular Disease and Diabetes. Woodhead Publishing and CRC Press, England and North America, pp: 465.
3: Balange, A.K. and S. Benjakul, 2009. Effect of oxidised tannic acid on the gel properties of mackerel (Rastrelliger kanagurta) mince and surimi prepared by different washing processes. J. Food Hydrocolloid, 23: 1693-1701.
4: Benjakul, S., W. Visessangua, J. Tueksuban and M. Tanaka, 2004. Effect of some protein additives on proteolysis and gel - forming ability of lizardfish (Saurida tumbil). J. Food Hydrocolloids, 18: 395-401.
5: Carvajal, P.A., G.A. MacDonald and T.C. Lanier, 1999. Cryostabilization mechanism of fish muscle proteins by maltodextrins. J. Cryobiol., 38: 16-26.
6: Chang-Lee, M.V., L.E. Lampila and D.L. Crawford, 1990. Yield and composition of surimi from pacific whiting (Merluccius productus) and the effect of various protein additives on gel strength. J. Food Sci., 55: 83-86.
7: Huda, N., A. Aminah and A.S. Babji, 1999. Halal issues in processing of surimi and surimi-based food product. Info. Fish Int., 5: 45-49.
Direct Link |
8: Huda, N., A. Abdullah and A.S. Babji, 2000. Effects of cryoprotectants on functional properties of dried lizardfish (Saurida tumbil) surimi. Malaysian Applied Biol., 29: 9-16.
9: Huda, N., A. Abdullah and A.S. Babji, 2000. Nutritional quality of surimi powder from Threadfin bream. J. Muscle Foods, 11: 99-109.
10: Huda, N., A. Abdullah and A.S. Babji, 2001. Functional properties of surimi powder from three Malaysian marine fish. Int. J. Food Sci Technol., 36: 401-406.
11: Huda, N. and F. Ariffin, 2010. Production and properties of Malaysian fish crackers. INFOFISH Int., 2: 32-36.
12: Huda, N. and N. Ismail, 2009. Malaysian fishball production then and now. INFOFISH Int., 2: 35-39.
13: Hui, Y.H., 2006. Handbook of Food Science. Vol. 4. Technology and Engineering, CRC Press, UK., ISBN: 9780849398476.
14: Julavittayanukul, O., S. Benjakul and W. Visessanguan, 2006. Effect of phosphate compounds on gel-forming ability of surimi from bigeye snapper (Priacanthus tayenus). J. Food Hydrocoloids, 20: 1153-1163.
15: Karayannakidis, P.D., A. Zotos, D. Petridis and K.D.A. Taylor, 2007. The effect of initial wash at acidic and alkaline pHs on the properties of protein concentrate (kamaboko) products from sardine (Sardina pilchardus) samples. J. Food Eng., 78: 775-783.
16: Kristinsson, H.G., A.E. Theodore, N. Demir and B. Ingadottir, 2005. A comparative study between acid-and alkali-aided processing and surimi processing for the recovery of proteins from channel catfish muscle. J. Food Sci., 70: 298-306.
Direct Link |
17: Lanier, T.C. and T. Akahane, 1986. Methods of retarding denaturation of meat products. United States Patent 4572838. http://www.freepatentsonline.com/4572838.html.
18: Lanier, T.C. and C.M. Lee, 1992. Surimi Technology. 1st Edn., Marcel Dekker, New York.
19: Lou, X., C. Wang, Y.L. Xion, B. Wang and S.D. Mims, 2000. Gelation characteristics of Paddlefish (Polyodon spathula) surimi under different heating conditions. J. Food Sci., 65: 394-398.
20: MacDonald, G.A and T.C. Lanier, 1994. Actomyosin stabilization to freeze-thaw and denaturation by lactate salts. J. Food Sci., 59: 101-105.
21: MacDonald, G.A., T.C. Lanier and P.A. Carvajal, 2000. Stabilization of Proteins in Surimi. In: Surimi and Surimi Seafood, Park, J.W. (Ed.). Marcel Dekker, Inc., New York, pp: 91-125.
22: MacSweeney, P.L.H., 2009. Advanced Dairy Chemistry. Vol. 3. Lactose, Water, Salts and Minor Constituents, Springer, New York, ISBN: 978-0-387-84864-8, pp: 152.
23: Mao, L. and T. Wu, 2007. Gelling properties and lipid oxidation of kamaboko gels from grass carp (Ctenopharyngodon idellus) influenced by chitosan. J. Food Eng., 82: 128-134.
24: Marshall, R.T., H.D. Goff and R.W. Hartel, 2003. Ice Cream. 6th Edn., Kluwer Academic/Plenum Publisher, New York, ISBN: 0-306-47700-9, pp: 78.
25: Medina, J.R. and R.L. Garrote, 2002. Determining washing conditions during the preparation of frozen surimi from Surubi (Pseudoplatystome coruscans) using response surface methodology. J. Food Sci., 67: 1455-1461.
26: Molins, R.A., 1991. Phosphates in Food. CRC Press, Boca Raton, FL., USA., ISBN-13: 9780849345883.
27: Nabors, L.O., 2001. Alternative Sweeteners. 3rd Edn., CRC Press, New York, ISBN: 9780824704377, pp: 502.
28: Okada, M., 1992. History of Surimi Technology in Japan. In: Surimi Technology, Tyre, C.L. and M.L. Chong (Eds.). Marcel Dekker Inc., New York, ISBN: 0-8247-8470-7, pp: 3-21.
29: Osako, K., M.A. Hossain, K. Kuwahara and Y. Nozaki, 2005. Effect of trehalose on the gel-forming ability, state of water and myofibril denaturation of horse mackerel (Trachurus japonicus) surimi during frozen storage. J. Fish. Sci., 71: 367-373.
30: Park, J.W., T.C. Lanier, D.D. Hamann and J.T. Keeton, 1987. Use of cryoprotectants to stabilize functional properties of prerigor salted beef during frozen storage. J. Food Sci., 52: 537-542.
31: Park, J.W., 1994. Functional protein additives in surimi gels. J. Food Sci., 59: 525-527.
32: Park, J.W., 2005. Surimi and Surimi Seafood. 2nd Edn., CRC Press, Florida, USA., ISBN: 9780824726492.
33: Piyachomkwan, K. and M.H. Penner, 1995. Inhibition of pacific whiting surimi-associated protease by whey protein concentrate. J. Food Biochem., 18: 341-353.
34: Rawdkuen, S., S. Benjakul, W. Visessanguan and T.C. Lanier, 2007. Effect of chicken plasma protein and some protein additives on proteolysis and gel-forming ability of Sardine (Sardinella gibbosa) surimi. J. Food Process. Preservation, 31: 492-516.
35: Rawdkuen, S. and S. Benjakul, 2008. Whey protein concentrate: Autolysis inhibition and effects on the gel properties of surimi propared from tropical fish. J. Food Chem., 106: 1077-1084.
36: Rawdkuen, S., S. Sai-Ut, S. Khamsorn, M. Chaijan and S. Benjakul, 2009. Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process. Food Chem., 112: 112-119.
CrossRef | Direct Link |
37: Roller, S. and S.A. Jones, 1996. Handbook of Fat Replacers. CRC Press, Boca Raton, FL, USA., ISBN: 9780849325120.
38: SAFDC, 2009. Information collection for economically important species as surimi raw meterial in the Southeast Asian Region. July 1-2, 2009, SEAFDEC Training Department Samutprakan Thailand, http://map.seafdec.org/downloads/surimi-ws.html.
39: Stark, Y.Y., M. Tsukamoto, K. Futagawa, M. Kubota and M. Oguchi, 2009. Bioactive of surimi from nouthern blue whiting prepared by different ways. J. Food Chem., 113: 47-52.
40: Sultanbawa, Y. and I.M. Li-Chan, 1998. Cryoprotective effects of sugar and polyol blends in ling cod surimi during frozen storage. J. Food Res. Int., 31: 87-98.
41: Sultanbawa, Y. and I.M. Li-Chan, 2001. Structural changes in natural actomyosin and surimi from ling cod (Ophiodon elongatus) during frozen storage in the absence or presence of cryoprotectants. J. Agric. Food Chem., 49: 4716-4725.
42: Sych, J., C. Lacroix, L.T. Adambounou and F. Castaigne, 1990. Cryoprotective effects of lactitol, palanitit and polydextrose on cod surimi proteins during frozen storage. J. Food Sci., 55: 356-360.
43: Sych, J., C. Lacroix and M. Carrier, 1991. Determination of optimal level of lactitol for surimi. J. Food Sci., 56: 285-290.
44: Sych, J., C. Lacroix, L.T. Adambounou and F. Castaigne, 1991. The effect of low-or non-sweet additives on the stability of protein functional properties of frozen cod surimi. Int. J. Food Sci. Technol., 26: 185-197.
45: United States Patent 5436024, 1995. Cryoprotected surimi product. United States Patent 5436024. Access June, 1. http://www.freepatentsonline.com/5436024.html.
46: Yada, R., 2004. Proteins in Food Processing. Woodhead Publishing Ltd., UK.
47: Yoon, K.S. and C.M. Lee, 1990. Cryoprotective effects in surimi and surimi/minced-based extruded products. J. Food Sci., 55: 1210-1216.
48: Zhou, A., S. Benjakul, K. Pan, J. Gong and X. Liu, 2006. Cryoprotective effects of trehalose and sodium lactate on tilapia (Sarotherodon nilotica) surimi during frozen storage. J. Food Chem., 96: 96-103.
49: Weerasinghe, V.C., M.T. Morrissey, Y.C. Chung and H. An, 1996. Whey protein concentrate as a proteinase inhibitor in pacific whiting surimi. J. Food Sci., 61: 367-371.
50: Herrera, J.R. and I.M. Mackie, 2004. Cryoprotection of frozen-stored actomyosin of farmed rainbow trout (Oncorhynchus mykiss) by some sugars and polyols. Food Chem., 84: 91-97.