Effect of medium temperature setting on gelling characteristics of surimi from some tropical fish

Effects of setting at 25 °C on textural properties and cross-linking of myofibrillar proteins in surimi produced from threadfin bream (Nemipterus bleekeri), bigeye snapper (Priacanthus tayenus), barracuda (Sphyraena jello) and bigeye croaker (Pennahai macrophthalmus) were investigated. Increase in setting time (0–8 h) resulted in a higher breaking force and deformation for all surimi gels tested (P<0.05). Increased gel strength was associated with increase in non-disulfide bond formation and decreased heavy chain myosin. Proteins underwent degradation during setting; however polymerization occurred to a much higher extent, leading to a strengthened gel matrix. Therefore, setting at 25 °C, for an appropriate time, should be a promising means to improve gelling properties of surimi produced from tropical fish.     

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     

Effect of Freezing and Frozen Storage of Alaska Pollock on the Chemical and Gel-Forming Properties of Surimi

Alaska pollock was headed, gutted, and frozen at sea in pre- and postrigor condition. Surimi made from this fish held at - 29°C showed a gradual loss in gel-forming ability with time of storage. This loss in gel-forming ability was accompanied by a loss in viscosity and Ca⁺⁺-ATPase activity of the surimi over the 9-month storage period. The gel strength of kamaboko gels showed an inverse linear relationship with gel moisture over a limited moisture range. Simply freezing and thawing pollock resulted in surimi with significantly lower gel strength than that from fresh pollock.     

Heat-Induced Gelation Properties of Surimi From Mechanically Separated Chicken

Chicken surimi was prepared from fresh mechanically separated chicken meat using a sodium bicarbonate washing process. The heat-induced gelation properties were assessed under different conditions of pH, temperature, heating rate, protein and sodium tripolyphosphate (TPP) concentrations. Surimi gel strength increased (p < 0.05) after: reducing pH from 6.4 to 6.0, increasing temperature from 40°C to 80°C, reducing heating rate from 5°C/min to 1°C/min, increasing protein concentration from 4% (w/w) to 8% (w/w) or addition of 0.3% (w/w) TPP. Freeze thaw stability studies revealed that the gel strength of surimi decreased (p < 0.05) when subjected to frozen storage at – 18°C.     

Effect of soy protein isolate on gel properties of Alaska pollock and common carp surimi at different setting conditions

The effects of soy protein isolate (SPI) on the gel properties of different grade Alaska pollock and common carp surimi at different setting conditions were evaluated and compared. Breaking force and distance of gels decreased with increasing SPI concentrations in direct cook (85 °C for 30 min) and in cook after setting at 30 °C for 60 min conditions. The effect of SPI on gel strength of common carp surimi was less than in Alaska pollock surimi. The breaking force obtained for addition of 10% SPI to Alaska pollock surimi was higher than for surimi alone when cooked after incubation at 50 °C for 60 min. Addition of SPI decreased the whiteness and increased the yellowness of the gel. The gel structure showed that the addition of SPI modified the microstructure of the fish protein gel, thus resulting in surimi with different gelling properties. Copyright © 2004 Society of Chemical Industry     

Gel‐forming ability of surimi from grass carp (Ctenopharyngodon idellus): influence of heat treatment and soy protein isolate

The effects of setting conditions and soy protein isolate (SPI) on textural properties of surimi produced from grass carp were investigated. Effects of setting temperature, setting time and protein concentration on the breaking force and distance were evaluated and compared utilizing response surface methodology. Models for breaking force and breaking distance of grass carp surimi were established. Protein concentration was the major factor affecting the gel strength of grass carp surimi. Breaking force and distance of grass carp surimi gels decreased with increase of protein ratio from SPI at 30 °C and 40 °C for 60 min setting and heating at 85 °C for 30 min, but the breaking force obtained for addition of 100 g kg^?1 SPI protein to grass carp surimi was higher than that for surimi alone at 60 °C for 60 min incubation and heating at 85 °C for 30 min. Copyright © 2005 Society of Chemical Industry     

Physical and Oxidative Stabilization of Omega-3 Fatty Acids in Surimi Gels

ABSTRACT: The objective of the study was to compare the dispersion and oxidative stability of omega-3 fatty acid oil in high- and low-quality surimi gels during 4-mo refrigerated and frozen storage. Low-quality surimi was prepared by subjecting Alaska pollock surimi to 7 freeze–thaw cycles. Surimi gels were prepared with 4% modified starch, 2% salt, and 0.5% or 1% algal DHA or concentrated fish EPA-DHA oil, and stored at −18 or 3 °C for 4 mo after being vacuumed packed and pasteurized. The effect of surimi gel properties on oil dispersion was examined using light microscopy equipped with image process software. The extent of lipid oxidation was monitored by thiobarbituric acid reactive substances (TBARS), peroxide value (PV), and fatty acid methly esters (DHA and EPA). Very fine and uniform oil dispersion was observed in the high-quality surimi gel with the average droplet size of 12.37 μm² and dispersion of 1.73 × 10⁻³ droplets/μm² compared to 84.32 μm² and 0.57 × 10⁻³ droplets/μm² in the low-quality gel. Throughout the 4 mo storage, TBARS and PV of high-quality surimi gel were significantly (P < 0.05) lower than those of low-quality surimi gel. The decreases in omega-3 fatty acids in the high-quality surimi gels were lower than those in the low-quality surimi gels under both storage conditions. Results confirm that a highly cohesive gel matrix is required to have a fine dispersion and oxidative stability of omega-3 fatty acids in the surimi gel system. Practical Application: Uniform dispersion and oxidative stability of omega-3 fatty acid oil can be achieved in the highly cohesive surimi gel system without use of antioxidants. This suggests that surimi can be used as a protein-based carrier in developing high omega-3 fatty acids-containing seafood products.     

Sardine Surimi Gels as Affected by Salt Concentration, Blending, Heat Treatment and Moisture

The effects of simultaneous modification of salt concentration, blending time, moisture content and heat treatment at different setting and cooking temperatures and time on characteristics of sardine (Surdina pilchardus) surimi gels was examined using a randomized incomplete block design. Maximum gel strength (GS) was obtained at highest salt concentrations and 78% moisture. Pre-setting was required to achieve acceptable gel quality. Highest GS values were found in gels set for 30–60 min at 35°C prior to heating at 90°C for 40 min. However, GS decreased after prolonged heating at 90°C. Gels set at 25, 35 and 40°C for 90 min had lower GS values when heated at 90°C for 40 min but were stable during further heating.     

Quality Assessment of Commercially Processed Carbon Monoxide‐Treated Tilapia Fillets

Carbon monoxide (CO) has been used to stabilize the color of fish muscle during frozen storage and distribution. This study compared changes in the quality profiles of CO‐treated and untreated (UT) tilapia fillets stored at 21 to 22 °C (room temperature), 4 to 5 °C (refrigerated), and 0 °C (iced). Samples (n = 3) were analyzed at different time intervals for chemical, lipid oxidation, microbiological, color, and expert sensory profiles. CO samples contained greater (P < 0.05) apparent ammonia and total volatile base nitrogen (TVB‐N) at day 0, with greater (P < 0.05) TVB‐N throughout refrigerated and iced storage. At time 0, peroxide values (POV) and thiobarbituric‐acid‐reactive substances were lower (P < 0.05) for CO samples and continued to have lower trends throughout all storage temperatures. Microbiological analysis at time 0 did not show any differences between UT and CO samples. Redness (a*) color values were greater (P < 0.05) in CO tilapia at time 0; however, treated product showed a more rapid decline in a* throughout all storage temperatures. While expert sensory evaluation showed no statistical differences between UT and CO tilapia at time 0, CO product failed sensory assessment sooner than UT product when stored refrigerated and in ice.     

Setting Response of Alaska Pollock Surimi Compared with Beef Myofibrils

Physicochemical properties of surimi after preincubation at 25–50°C and beef myofibrils at 25–60°C for up to 8 hr prior to cooking at 80°C for 20 min were evaluated by a torsion test and sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. Shear stress and true shear strain of surimi were more sensitive to pH changes than beef myofibrils. Maximum gel strength was found at = pH 7 for surimi and pH 6 for beef myofibrils. The myofibrils showed no setting effect at any preincubation temperatures examined, while surimi showed an optimum setting effect at 25°C. Incorporation of beef myofibrils into surimi resulted in decrease of shear stress and true shear strain values.     

Proteinase inhibitory activity of sarcoplasmic proteins from threadfin bream (Nemipterus spp.)

BACKGROUND: Thailand is the second largest surimi producer in the world and 50% of surimi is produced from threadfin bream. During surimi processing, sarcoplasmic proteins are removed through water washing and discarded in the waste stream. This study was aimed at investigating the proteinase inhibitory activity of sarcoplasmic proteins. RESULTS: Sarcoplasmic proteins from threadfin bream (TBSP) exhibited inhibitory activity toward trypsin but did not inhibit papain and chymotrypsin. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis under non‐reducing condition stained by trypsin inhibitory activity revealed three protein bands of molecular mass of 95, 41 and 37 kDa. Inhibitory activity of TBSP reached a maximum when subjected to 45 °C and completely disappeared at 60 °C. The breaking force and deformation of lizardfish surimi gel with added TBSP and pre‐incubated at 37° for 20 min increased with additional levels of TBSP (P < 0.05). Trichloroacetic acid–oligopeptide content of lizardfish surimi gel with added TBSP decreased with the addition of 4 g kg^?1 TBSP (P < 0.05). Retention of myosin heavy chain (MHC) increased when TBSP concentration was increased. TBSP effectively protected MHC from proteolysis at 37 °C to a similar extent as egg white powder, but efficacy of TBSP was not observed at 65 °C. CONCLUSION: TBSP could be applied to reduce proteolytic degradation of lizardfish surimi or other surimi associated with trypsin‐like proteinase, rendering an improvement in surimi gelation set at 37–40 °C. Copyright © 2009 Society of Chemical Industry     

Effects of Hydrolysates from Silver Carp (Hypophthalmichthys molitrix) Scales on Rancidity Stability and Gel Properties of Fish Products

This study aimed to evaluate the effectiveness of hydrolysates, which were obtained from the scales of silver carp (Hypophthalmichthys molitrix) by papain, flavourzyme, and Alcalase 2.4 L, as natural antioxidants in silver carp mince and surimi gels during storage at 4 °C. The hydrolysates that possess greater in vitro antioxidant activities (DPPH radical-scavenging activity, Fe²⁺-chelating activity, and reducing power), including hydrolysates catalyzed by papain at 10 min (HP), flavourzyme at 5 min (HF), and Alcalase 2.4 L at 5 min (HA), were chosen as additives. Color, cooking loss, conjugated dienes (CDs), thiobarbituric acid reactive substances (TBARS), fatty acids, and sensory scores of mince were measured on days 0, 2, 4, 6, and 8 during 4 °C storage; additionally, whiteness, breaking force, deformation, gel strength, and sensory score of surimi gels were measured on days 1, 3, 5, 7, 9, and 11 during 4 °C storage. The results indicate that HA was conducive to lowering the cooking loss of mince and that HF significantly (P?<?0.05) reduced the CDs value of mince. For surimi gels, HF improved whiteness, deformation, and gel strength. Hence, HF could serve as a natural antioxidant during early oxidation and improve gel formation of silver carp products.     

Gel‐forming properties of surimi produced from bigeye snapper,Priacanthus tayenus and P macracanthus,stored in ice

The influence of iced storage of two species of bigeye snapper, Priacanthus tayenus and P macracanthus, on the gel‐forming ability of the resulting surimi was investigated. Upon iced storage, whole fish underwent deterioration faster than beheaded/eviscerated fish. Total volatile base and trimethylamine contents of whole fish were higher than those of beheaded/eviscerated fish, particularly after 9 days of storage (P < 0.05). P macracanthus muscle was more susceptible to proteolytic degradation than P tayenus muscle. Ca²⁺‐ATPase activity decreased as the storage time increased (P < 0.05), indicating the denaturation of myosin. A marked decrease in Ca²⁺‐ATPase activity was found in whole fish kept for more than 6 days in ice (P < 0.05). Breaking force and deformation of surimi gels from both species decreased, with a concomitant decrease in whiteness, as the storage time increased (P < 0.05). Beheading and evisceration of fish retarded the deterioration. However, the gel‐forming ability of surimi produced from both species decreased continuously throughout iced storage (P < 0.05), probably owing to the denaturation and degradation of myofibrillar proteins. © 2002 Society of Chemical Industry     

Thermal Gel Degradation (Modori) in Sturgeon (Acipenseridae) Surimi Gels

Sturgeon meat has been found to be suitable as surimi raw materials. The present study determined the modori phenomenon in sturgeon surimi gels and identified its relationship with cathepsins. In all heat‐treated gels (25 to 90 °C, at 5 °C intervals), the 40 °C‐incubated sturgeon surimi gel showed the weakest gel properties and water‐holding capacity (P < 0.05), a rough protein gel network under SEM, and the highest protein solubility and trichloroacetic acid‐soluble peptides content (P < 0.05). SDS‐PAGE indicated that the myosin heavy chain band of sturgeon surimi gels was almost completely degraded at 40 °C. Moreover, the highest cathepsin L activity was observed in 40 °C‐treated sturgeon surimi gels (P < 0.05). Our results suggested that the modori phenomenon in sturgeon surimi gels occurred at 40 °C, which was partially attributed to cathepsin L, thereby allowing for the better exploitation and utilization of sturgeon surimi.     

Influence of texture of suwari gels on kamaboko gels made from sardine (Sardina pilchardus) surimi

The textural characteristics and water holding capacity of suwari (set) and kamaboko (set and cooked) sardine surimi gels were examined in order to clarify the influence of the initial network formed in setting conditions (25, 35 and 40°C for 30 and 60 min) on the texture of the kamaboko gels. Although the texture of suwari gels set at 35°C improved with longer setting, both setting times ensured kamaboko gels with the highest gel strength. Suwari gels set at 25°C also improved with longer setting but the gel strength of both suwari and kamaboko gels was lower than at 35°C. For gels set at 40°C prolonged setting weakened the suwari networks formed, leading to kamaboko gels with poorer textural characteristics. ©1997 SCI     

Transglutaminase-mediated setting in bigeye snapper Surimi

Effect of setting induced by endogenous transglutaminase (TGase) in two species of bigeye snapper, Priacanthus tayenus and Priacanthus macracanthus, on gel properties and protein cross-linking was investigated. Setting at either 25 or 40 °C, prior to heating at 90 °C resulted in the increase in both breaking force and deformation of surimi from both species, particularly when setting time increased (P<0.05). A decrease in solubility of surimi gels in a mixture of sodium dodecyl-sulfate, urea and β-mercaptoethanol suggested increased formation of non-disulfide covalent bonding which coincided with increased gel strength and the decrease in myosin heavy chain (MHC) polypeptide. The optimum conditions for setting of surimi sol was found to be 40 °C for 2 h for P. tayenus and 25 °C for 3 h for P. macracanthus. Assayed by monodancylcadaverine (MDC)-incorporation method, TGase from P. tayenus and P. macracanthus exhibited an optimum temperature at 40 and 25 °C, respectively. In addition, the breaking force and deformation of surimi from both species increased markedly with the addition of calcium chloride, while they decreased considerably in the presence of EDTA, N-methylmaleimide and ammonium chloride. The results confirmed that endogenous transglutaminase played an important role in gel enhancement of surimi from both species of bigeye snapper.     

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.     

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.     

Suppression of Surimi Gel Setting by Transglutaminase Inhibitors

Three types of salted meat paste (3% NaCl, 3% NaCl plus 0.66% NH₄Cl or 3% NaCl plus 0.2% EDTA) were prepared from high and second grade surimi, set at 30°C up to 4 br, and subsequently heated at 85°C for 30 min. The gel strength, crosslinking of myosin heavy chain (MHC) and ?-(γ-glutamyl)lysine (?-(γ-Glu)Lys) content were determined. With extended setting time, gel strength, crosslinking of MHC and the content of a crosslinked product, ?-(γ-Glu)Lys, increased markedly in the gel from the high grade surimi. Such changes were suppressed considerably in the presence of NH₄Cl and EDTA and were not observed in the gel prepared from second grade surimi. These results indicated an active participation of intrinsic transglutaminase in the setting process.     

Determining Washing Conditions During the Preparation of Frozen Surimi from Surubí (Pseudoplatystome Coruscans) Using Response Surface Methodology

The effect of process temperature (2 to 18 °C), time (1 to 7 min/ cycle), and water‐mince ratio (2:1 to 8:1) on the quality attributes of surubí (Pseudoplatystoma coruscans) surimi was studied using Response Surface Methodology (RSM). Conditions were identified that allowed to achieve 25% of extracted proteins and a moisture content of 79%, compatible with an acceptable quality of surimi gel. The verification of the prediction models was acceptable. Two cryoprotectant mixtures (sucrose‐sorbitol and maltodextrin‐sorbitol) were also evaluated, with regard to the freezing and frozen storage and the functional quality of the gels. Freezing proved to be an aggressive method, and the 2 mixtures tested showed to be efficient for 6 months of frozen storage.