Axial Compression Properties of Kamaboko

Kamaboko, gelled seafood product from frozen surimi, has distinctive textural properties. Characterization of those properties, using an integrated approach to Theological studies, was accomplished by means of an instrumental texture profile analysis and evaluation of resultant stress-strain relationships. The material had near-ideal area expansion even at compressions of 60% while retaining its highly elastic texture. Apparently the product did not yield through 80% compression. Hardness of the kamaboko at 80% compression was characterized by a local maximum at 37.5°C which may have been related to processing temperature of the initial surimi gel-set used in a double-gel-set procedure. Evaluation of stress-strain relationships confirmed the incompressible nature of the gel and showed relatively slight variations between the Young's modulus and the deformability modulus. The elastic limit of the kamaboko increased significantly as temperature increased from 25 to 50°C.     

Characteristics of surimi and kamaboko from sardines

Sardines of varying freshness (1 to 3 days in ice) were manually or mechanically processed into fish mince and surimi using 1 to 3 washing steps. Standard kamaboko gels were prepared by grinding thawed surimi with 3% NaCl and 5% potato starch, stuffing into sausage casings, holding at 37°C for 30 min and cooking at 90°C for 50 min.
Three washing steps decreased the yield of washed fish mince (21-27 g per 100 g of whole fish), and the protein recovery (50-55% of that present in the unwashed mince), but caused efficient lipid removal (80%) leading to surimi containing only 0.2-1.4% lipid. The texture and colour of the final kamaboko were also improved.
The texture parameters (folding score, rigidity, elasticity index and gel strength) of kamaboko prepared from very fresh sardines were markedly enhanced by gel setting during incubation at 37°C for 30 min or 4°C for 24 hr. Incubation at 60°C for 30 min led to soft, coarse gels. Omitting potato starch or replacement by spray dried egg white had little effect on texture.
The texture of kamaboko prepared from less fresh sardines was less firm and elastic, did not improve when incubation was carried out at 37 or 4°C before cooking, and was softer and coarser after incubation at 60°C. Partial or total replacement of potato starch by egg white, soy protein isolate or bovine serum albumin markedly improved the texture. Egg white also increased the colour lightness.     

Effects of CaCl<Subscript>2</Subscript> on chemical interactions and gel properties of surimi gels from two species of carps

Effects of CaCl₂ on chemical interactions, textural properties and expressible moisture content of suwari and kamaboko gels from yellowcheek carp and grass carp were investigated. And the correlations between the contents of chemical interactions and physical properties of surimi gels were analyzed. The contents of chemical interactions, especially non-disulfide covalent bonds, disulfide bonds and hydrophobic interactions of suwari and kamaboko gels, varied with addition concentration of CaCl₂ and fish species. Suwari and kamaboko gels from yellowcheek carp exhibited higher breaking force, deformation and gel strength than these from grass carp. Surimi gels (suwari and kamaboko gels) from yellowcheek carp and grass carp exhibited their maximum gel strength when 40 mmol/kg and 100 mmol/kg CaCl₂ was added, respectively. Addition of CaCl₂ at high concentration resulted in low water holding capacity of surimi gels. Correlation analysis indicated that the contents of nonspecific associations, ionic bonds, hydrophobic interactions and sulfhydryl groups exhibited significant correlation with breaking force of surimi gels from yellowcheek carp and grass carp. Additionally, the content of non-disulfide covalent bonds had significant positive correlations with breaking force and expressible moisture of surimi gel from yellowcheek carp.     

Whey protein concentrate: Autolysis inhibition and effects on the gel properties of surimi prepared from tropical fish

Effects of whey protein concentrate (WPC) on autolysis inhibition and gel properties of surimi produced from bigeye snapper (Priacanthus tayenus), goatfish (Mulloidichthys vanicolensis), threadfin bream (Nemipterus bleekeri) and lizardfish (Saurida tumbil) were investigated. WPC (0–3%) showed inhibitory activity against autolysis in all surimi at both 60 and 65 °C in a concentration-dependent manner. Myosin heavy chain (MHC) of surimi was more retained in the presence of WPC. Breaking force and deformation of kamaboko gels of all surimi increased as added levels of WPC increased (P < 0.05). This was associated with lower levels of protein degradation, as evidenced by the decrease in trichloroacetic acid-soluble peptide content (P < 0.05). WPC at 3% (w/w) significantly decreased the whiteness of gels. However, water-holding capacity of kamaboko gels was improved with increasing concentration of WPC. The microstructure of surimi gels generally became denser with the addition of WPC.     

GEL PROPERTIES OF BIGEYE SNAPPER (PRIACANTHUS TAYENUS) SURIMI AS AFFECTED BY SETTING AND PORCINE PLASMA PROTEINS

Effects of setting temperature, time, and addition of porcine plasma protein (PPP) on gel properties of surimi from bigeye snapper (Priacanthus tayenus) were investigated. Breaking force and deformation of the surimi gels increased as the setting time and temperature increased. The gel preincubated at 35C for 90 min in the presence of 0.5% PPP, followed by cooking at 90C for 20 min showed the maximum force and deformation. The decrease in solubility of the resultant suwari and kamaboko gels in solution containing sodium dodecyl sulfate, urea and β‐mercaptoethanol suggested that gel enhancement was mainly mediated through the formation of nondisulfide covalent bonds catalyzed by both transglutaminase (TGase) in fish muscle and porcine plasma. Addition of PPP slightly decreased the whiteness of the kamaboko gels.     

Characteristics of Sarcoplasmic Proteins and Their Interaction with Surimi and Kamaboko Gel

ABSTRACT:  This study examined the effect of adding common carp sarcoplasmic proteins (Sp- P) on the gel characteristics of threadfin bream surimi and kamaboko while maintaining constant moisture and myofibrillar levels. Based on the temperature sweep test, which is involved in heating of surimi gel from 10 to 80 °C to monitor the viscoelastic properties, at temperature range of 40 to 50 °C, the decrease level (depth of valley) in storage modulus (G') thermograph was in proportion to the concentration of added Sp- P. Storage modulus (G') showed greater elasticity after adding Sp- P compared with the control without Sp- P. Furthermore, the breaking force and distance and consequently gel strength of the resultant kamaboko were improved significantly ( P > 0.05). Thus, added Sp- P did not interfere with myofibrillar proteins during sol–gel transition phase but associated with textural quality enhancement of resultant kamaboko; however, addition of Sp- P from the dark muscle of the carp decreased the whiteness of the resultant surimi. Furthermore, according to the SEM micrographs, the gel strength could not be associated with either the number of polygonal structures/mm² or the area of the polygonal structures in the kamaboko gel microstructure.     

Alternative Techniques for Producing a Quality Surimi and Kamaboko from Common Carp (Cyprinus carpio)

ABSTRACT: The demand for surimi and kamaboko is increasing in the world at the same time as the supply of the fish traditionally used has declined. In an effort to increase the range and hence supply of fish used, factors increasing the quality of surimi and kamaboko from common carp were investigated. The best surimi and kamaboko characteristics were produced by a modified conventional method (MCM) rather than traditional method (TM), alkaline‐aided method (AAM), and pH modified method (PMM). MCM processing used centrifugation instead of decanting and filtering to optimize dewatering and remove the sarcoplasmic proteins (Sp‐P). The temperature sweep test, at the end of sol–gel transition stage (at 75 °C), showed significantly (P < 0.05) greater G′ for the kamaboko from MCM than that from other methods tested. Furthermore, the greatest and the least gel strengths were obtained with MCM and TM kamaboko, respectively. The protein recovery was about 67%, 74%, 87%, and 92% for TM, AAM, MCM, and PMM, respectively. TM and MCM resulted in the removal of Sp‐P as determined by SDS‐PAGE. The superiority of MCM kamaboko gel characteristics was supported by scanning electron micrographs (SEM) of the gel, which showed a significantly (P < 0.05) greater number of polygonal structures than for the TM kamaboko, which had the fewest and largest polygonal structures. The pH‐shifting methods improved the textural quality of the resultant kamaboko compared with TM. However, a simple modification (centrifugation compared with decanting) by MCM in the surimi process can further improve the quality of the surimi and kamaboko gels. Furthermore, because it removed Sp‐P and still preserved gel strength, it suggests that Sp‐P are not required for gel strength.     

Rheological and Textural Properties of Pacific Whiting Surimi Gels As Influenced by Chicken Plasma

Rheological properties of Pacific whiting surimi, in the absence and presence of chicken plasma (CP) at different levels (0.3–3.0%, w/w), were studied by dynamic rheological (small strain) and torsion fracture measurements, respectively. The surimi paste exhibited two major distinctive rheological transitions during heating (1°C/min) from 20 to 90°C with peaks observed at 33 and 56°C. The abrupt loss of G′ upon heating from 47 to 57°C, and the occurrence of small peak of phase angle at the same temperature range were prevented by the addition of CP. Nevertheless, the final G′ of the surimi paste added with CP was lower than that of the control. But shear fracture stress of both kamaboko and modori gels increased as the CP levels increased and shear strain increased with the addition of CP up to 2% (P < 0.05). CP inhibited the degradation of myosin heavy chains (MHC) caused by endogenous proteinases as indicated by more retained MHC and lowered TCA-soluble peptide content. Whiteness of gels decreased somewhat with increasing CP levels. CP, thus, could be a helpful additive for improving gelling properties of Pacific whiting surimi     

Contribution of sarcoplasmic proteins to myofibrillar proteins gelation

Surimi, a refined protein extract, is produced by solubilizing myofibrillar proteins during the comminuting and salting stages of manufacturing. The resulting paste gels on heating to produce kamaboko or a range of analog shellfish such as crab claw, filament sticks, fish mushroom, and so on. The myosin molecule is the major myofibrillar protein in gelation. It is believed that washing steps during the traditional surimi process play an important role in enhancing the gel properties of the resultant kamaboko by removing water-soluble (sarcoplasmic, Sp-P) proteins. By contrast, some researchers claim that retaining Sp-P or adding it into the surimi gel network not only does not interfere with the action of myofibrillar proteins during the sol-gel transition step but also improves the gel characteristics of the resultant kamaboko. It seems that retention of Sp-P or their addition into raw surimi does enhance the textural properties of kamaboko gel perhaps by functioning as a proteinase inhibitor, particularly against trypsin and trypsin-like proteinases but this depends on the type of applied surimi process. Among different types of Sp-P, it has been claimed that some proteins such as endogenous transglutaminase (TGase) play a more important role than other Sp-P in bond formation, by catalyzing the cross-linking of myosin heavy chain (MHC) molecules during low-temperature setting of surimi, resulting a more elastic kamaboko gel.     

Participation of cysteine protease cathepsin L in the gel disintegration of red bulleye (Priacanthus macracanthus) surimi gel paste

BACKGROUND: Endogenous proteases, among them cysteine‐type proteases, are reported to contribute to gel disintegration, resulting in kamaboko of poor quality. Severe gel disintegration occurs in red bulleye surimi gel paste. The objective of this study was to clarify the participation of cysteine protease cathepsin L in the gel disintegration of red bulleye surimi. The surimi was made into kamaboko with and without cathepsin L inhibitors. To confirm its hydrolysis action, crude cathepsin L was also extracted and added to the surimi to make kamaboko. RESULTS: The gel strength of kamaboko obtained by both one‐step (50 °C, 2 h) and two‐step (50 °C, 2 h + 80 °C, 20 min) heating was very low in the absence of inhibitors. Protease inhibitors E‐64 and leupeptin were found to enhance the gel strength considerably. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that the hydrolysis of kamaboko was promoted by crude cathepsin L and inhibited by E‐64 and leupeptin. The gel strength of two‐step heated kamaboko was increased from 12 to 110 and 130 g cm^?2 by E‐64 and leupeptin respectively at a concentration of 0.2 g kg^?1 surimi. CONCLUSION: Endogenous cathepsin L of red bulleye surimi participates in gel disintegration during kamaboko processing. It does so by degrading the myosin heavy chain of actomyosin and consequently hindering the gelation of red bulleye surimi. Copyright © 2009 Society of Chemical Industry     

Yam affects the antioxidative and gel‐forming properties of surimi gels

The antioxidative activities and textural properties of pollock surimi gels containing four different yams were determined to evaluate the potential of using yam as a health ingredient and an alternative source for starch in surimi‐based seafoods. Surimi gels containing 20% fresh yam showed higher α,α‐diphenyl‐β‐pricryl‐hydrazyl (DPPH) radicals scavenging activities and total phenolic contents than the gels without yam. Two tested cultivars, 70W34 and 70W35, did not show significant reductions in antioxidative activities when used in surimi gel while three other cultivars revealed species‐dependant declines in both the DPPH scavenging activities and total phenolic contents. The surimi gel containing the cultivar 70R20 showed the highest breaking forces and deformations. In general, 20% fresh yam could be used to form a yam‐containing surimi gel having similar textural properties with a potato starch containing pollock surimi gel. The dried yam powders might be used at the amount of 30% fresh yam equivalent without causing significant losses of the textural properties of pollock surimi gels. Copyright © 2005 Society of Chemical Industry     

Rheological characteristics of suwari and kamaboko gels made of surimi from Indian major carps

The gel strength, compressibility and folding characteristic of suwari (set) and kamaboko (set and cooked) gels prepared from rohu ( Labeo rohita ), catla ( Catla catla ) and mrigal ( Cirrhinus mrigala ) surimi were examined to understand the occurrence of suwari and modori phenomena in surimi from major freshwater carps. Suwari setting of gels did not take place at lower temperatures. Suwari gels showed good gel strength at 50 °C for rohu and at 60 °C for catla and mrigal after 30 min setting time. Incubation for 60 min decreased the gel strength at 60 °C for rohu and catla. Setting at 25 °C followed by cooking at 90 °C increased the gel strength. Increased setting temperature, however, decreased the gel strength of cooked gels. Gel strength and compressibility data were supported by folding characteristics. © 2002 Society of Chemical Industry     

Trypsin Inhibitory Activity and Gel‐Enhancing Effect of Sarcoplasmic Proteins from Common Carp

Abstract: Proteinase inhibitory activity of sarcoplasmic protein (SP) extracted from common carp (Cyprinus carpio) muscle and its gel‐improving ability were investigated. SPs displayed 89% and 54% inhibitory activity toward trypsin at 40 and 65 °C, respectively. Protein bands with molecular mass of 69, 50, 44, 41, and 35 kDa appeared on trypsin inhibitory activity staining under nonreducing condition when incubated at 40 °C, while 2 protein bands at 54 and 35 kDa were observed at 65 °C. Addition of SP at 0.18 g protein/100 g increased textural properties of threadfin bream surimi gel. However, when SP was added in combination with various CaCl₂ concentrations (0.1% to 0.5%) it did not further improve textural properties as compared to the addition of SP alone. Retention of myosin heavy chain of threadfin bream surimi was greater with the addition of SP. These results indicated that the gel‐enhancing effect of common carp SP was due to the inhibitory activity toward endogenous trypsin‐like proteinases in threadfin bream surimi. Practical Application: Sarcoplasmic protein from common carp muscle could be used as a functional protein ingredient that minimizes muscle proteolysis and improves textural properties of surimi containing trypsin‐like endogenous proteinases.     

Biochemical and gelling properties of tilapia surimi and protein recovered using an acid-alkaline process

The biochemical and gel properties of tilapia surimi prepared by a conventional washing method and protein isolated using alkaline-acid-aided processes were studied. Solubility and recovery of protein was found to be highest by using a conventional method, followed by an alkaline- and acid-aided process, respectively. Decreases in myoglobin and lipid contents were found in alkaline- or acid-aided process when compared to the conventional process (p < 0.05). The highest breaking force and deformation of kamaboko and modori gels was found in the gels prepared by the conventional washing method. Higher expressible water and whiteness were found in modori gels when compared to kamaboko gels. TCA-soluble peptide contents of conventional surimi gels were lower than those of acid- and alkaline-recovered protein gels. Degradation of myofibrillar protein was observed in acid-isolated protein. Microstructure of kamaboko gels showed more compact network than in modori gels in both conventional surimi and protein recovered using the pH-shift process.     

Effect of high-temperature setting on gelling characteristic of surimi from some tropical fish

The effect of setting at 40 °C on the textural properties and the changes in myofibrillar proteins in surimi produced from threadfin bream (Nemipterus bleekeri), bigeye snapper (Priacanthus tayenus), barracuda (Sphyraena jello) and bigeye croaker (Pennahai macrophthalmus) was investigated. An increase in the time of setting generally resulted in higher breaking force and also the deformation of both suwari and kamaboko gels. Maximum increases in gel‐breaking force were obtained in 1 h for threadfin bream, 2 h for bigeye snapper, 1.5 h for barracuda and 3 h for bigeye croaker. Extended setting time caused decreases in breaking force and deformation in all surimi, except that produced from bigeye croaker. Gel strengthening was associated with an increase in non‐disulphide covalent bond formation. Degradation of proteins occurred with prolonged setting. Therefore, setting at 40 °C for an appropriate time is a promising means to improve the gelling property of surimi produced from tropical fish.     

Gel Properties of Surimi from Bighead Carp (Aristichthys nobilis): Influence of Setting and Soy Protein Isolate

ABSTRACT: The effects of setting conditions and soy protein isolate (SPI) on textural properties and microstructures of surimi produced from bighead carp were investigated. The incubation conditions of bighead carp surimi affected the breaking force and distance. The optimum setting conditions were 35 °C to 40 °C for 60 min. When the surimi was cooked after 50 °C incubation for 30 to 120 min, the breaking force and distance were inferior to that of no incubation. The gel structure showed that the incubation conditions affected the bighead carp surimi gel microstructures, thus producing surimi with different gelling properties. Breaking force and distance of surimi gels decreased when the protein ratio of SPI was increased in the total protein at 30 °C and 40 °C for 60 min setting and heating at 85 °C for 30 min, but the breaking force obtained for 90% surimi protein plus 10% SPI protein was higher than surimi alone at 50 °C for 60 min incubation and heating at 85 °C for 30 min.     

Negative Roles of Salt in Gelation Properties of Fish Protein Isolate

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

Utilization of Surimi-like Products from Pork with Sex-odor in Restructured, Precooked Pork Roast

Surimi-like materials from boar and sow muscle and Alaskan pollack fish surimi were evaluated as binders for sow muscle chunks in restructured roasts. Boar surimi-like material tended to have lower mi-crobial counts and less lipid oxidation than unwashed counterparts. Increasing salt content increased lipid oxidation (P<0.05), degraded color and improved (P<0.05) textural integrity. The surimi-like boar material had equal or better binding properties than fish surimi at a 5% level and did not consistently result in detectable boar odor. Roasts without binder were comparable or better in textural and microbial characteristics than those with binders. Restructured, precooked, pork roasts were successfully produced with 0.2% NaCI.     

The effect of low- or non-sweet additives on the stability of protein functional properties of frozen cod surimi

The cryoprotective effect of low- or non-sweet additives, Palatinit^R, Polydextrose^R, casein hydrolysate and fish protein hydrolysate (at 8% w/w) as well as lactitol (at 4% and 8% w/w) were compared to an industrial control containing sucrose/sorbitol (8% w/w) and a control without additive in cod surimi stored at –20°C for 4 months. Freeze-induced protein denaturation was evaluated monthly by salt extractable protein and differential scanning calorimetry analyses of surimi followed by texture and expressible moisture analyses of surimi cooked gels. Results revealed that protein functionality was similarly maintained during frozen storage by lactitol, Palatinit^R and Polydextrose^R when incorporated in cod surimi at the 8% level. Surimi gels could be produced with textural attributes comparable to 8% w/w sucrose/sorbitol surimi gels, and the level of lactitol in cod surimi could be reduced to 4% w/w without significant alteration of cryoprotection. Some benefits in gel-forming properties were obtained by adding 8% casein hydrolysate to cod surimi.     

Characteristics and gel properties of muscles from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) caught in Thailand

Dark and ordinary muscle from sardine (Sardinella gibbosa) and mackerel (Rastrelliger kanagurta) were characterized. Lipid and myoglobin contents were higher in dark muscle than in ordinary muscle of both species, and higher contents of both constituents were found in sardine muscle than mackerel muscle. The extractable myoglobin contents in sardine dark and ordinary muscle were 14.27 and 2.18 mg/g, while mackerel dark and ordinary muscle contained 4.88 and 1.37 mg myoglobin/g sample, respectively. Alkali-soluble protein and stroma contents were greater in dark muscle than ordinary muscle. Mackerel muscle comprised a higher content of non-protein nitrogenous compounds than sardine muscle. The effect of washing conditions on the myoglobin extractability was investigated. A large amount of myoglobin was removed in the first washing cycle and only a small amount was removed in the second washing cycle. The highest removal of myoglobin from sardine (32.10–46.55%) and from mackerel muscle (103.20–313.66%) was achieved when the mince was washed with 0.2% NaCl and 0.5% NaCl, respectively. Washing media showed the marked effect on the color, expressible drip and textural properties of sardine and mackerel mince gels. The breaking force of directly heated and kamaboko gels from both sardine and mackerel mince washed with NaCl solution was higher than that of unwashed mince and water washed mince. However, no difference in deformation was observed. Washing also resulted in increased whiteness and lowered expressible moisture. In general, sardine surimi showed the superior gel-forming ability and whiteness to mackerel surimi.