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     

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.     

Gel properties of surimi from silver carp (Hypophthalmichthys molitrix) as affected by heat treatment and soy protein isolate

The effects of setting conditions and soy protein isolate (SPI) on textural properties of surimi produced from silver carp were investigated. Effects of setting temperature, setting time and protein concentration on the gel strength were evaluated and compared utilizing response surface methodology. Models for breaking force and breaking distance of silver carp surimi were established. The total protein content was 13.4% in all experimental samples. Setting temperature and protein concentration were the major factors affecting the gel strength. In the range of the additive SPI protein (10–40%), breaking force and distance of silver carp surimi gels decreased when the protein ratio of SPI was increased in the total protein at 30 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.     

Gel Strength Enhancement by Addition of Microbial Transglutaminase during Onshore Surimi Manufacture

Surimi from Alaska pollock flesh was manufactured onshore with Microbial transglutaminase (MTGase). Effect of MTGase was investigated by evaluating breaking strength and deformation of gels from MTGase-treated surimi with and without setting at 30°C. Quantitative analysis of ε-(γ-glutamyl)lysine (GL) crosslink was also carried out to monitor the MTGase reaction. In set gels, breaking strength and GL crosslink increased, and myosin heavy chain decreased correspondingly with MTGase concentration. These changes were smaller in gels prepared without setting. Results suggest that surimi gel could be improved through the formation of GL crosslinks by added MTGase in surimi.     

Microbial Transglutaminase and ε-(γ-Glutamyl)lysine Crosslink Effects on Elastic Properties of Kamaboko Gels

Kamaboko gels from Alaska pollock surimi (SA? and 2nd? grades) were prepared by setting at 10 or 45°C with Microbial transglutaminase (MTGase) and its effect on gel properties was investigated. At 10 and 45°C, gels from 2nd? grade surimi paste showed increases in breaking strength, without decline in deformation. Gel from SA? graded surimi paste showed an increase in breaking strength with no changes in deformation in 45°C setting, up to 0.03% MTGase. Crosslinking of myosin heavy chains through ε-(γ-glutamyl)lysine bonds was observed and a possible correlation was shown between ε-(γ-glutamyl)lysine content and gel strength (breaking strength X strain). ε-(γ-Glutamyl)lysine content up to 3 μmol/100g or MTGase 0.03% or higher improved gel properties.     

Linear Heating Rate Affects Gelation of Alaska Pollock and Pacific Whiting Surimi

Shear stress of Alaska pollock surimi gels with and without beef plasma protein (BPP) increased as heating rate decreased, but shear strain was unaffected. An increase in shear stress was accompanied by an increase of cross-linked myosin heavy chain. Slow heating rates increased proteolysis in Pacific whiting surimi as shown by degradation of myosin heavy chain and low shear stress and shear strain. Proteolysis of whiting surimi was lessened by BPP to a greater extent at rapid heating rates (20 and 30°C/min) than at slow heating rates (1 and 5°C/min).     

Comparison of Gel Properties of Surimi from Alaska Pollock and Three Freshwater Fish Species: Effects of Thermal Processing and Protein Concentration

ABSTRACT The gel strength of surimi made from Alaska pollock, common carp, grass carp, and silver carp was determined and compared for different incubation temperatures and periods. Gel strength and setting of the 3 freshwater fish species were inferior to that of Alaska pollock. Effects of the protein concentration, heating temperature and heating period on the gel strength were evaluated and compared utilizing the response surface methodology. Models for the breaking force and breaking distance of the surimi of the 4 species were established. Protein concentration was the major factor affecting the gel strength. Effects of heating temperature and heating period had differed somewhat among the surimi of the 4 species.     

Optimum chopping conditions for Alaska pollock, Pacific whiting, and threadfin bream surimi paste and gel based on rheological and Raman spectroscopic analysis

Rheological and Raman spectroscopic properties of surimi from three species [Alaska pollock (AP) (cold water), Pacific whiting (temperate water), and threadfin bream (warm water)] were investigated as affected by various chopping conditions. Comminuting Alaska pollock surimi at 0 °C demonstrated superior gel hardness and cohesiveness when chopping time was extended to 15-18 min; however, long chopping time at higher temperatures resulted in a significantly decreased gel texture particularly at 20 °C. Warm water fish threadfin bream exhibited higher gel texture when chopping was done longer at higher temperature. Rheological properties were significantly affected by both chopping time and temperature. Species effect, based on their thermal stability, was readily apparent. Raman spectroscopy revealed a significant change in disulfide linkage and the reduction of secondary structure upon extended chopping. Dynamic oscillation rheology demonstrated the damage of light meromyoisn and lowering of onset of gelling temperature as the chopping time was extended. PRACTICAL APPLICATION: Chopping conditions to determine gel quality and manufacture surimi seafood are varied by all manufacturers. This paper covering three primary species for surimi with their suggested optimum chopping conditions: 15 min for Alaska pollock when chopped at 0 °C, 15 min for Pacific whiting at 15-20 °C, and 18 min for threadfin bream at 25-30 °C. The use of optimum chopping condition should maximize the value of each surimi and provide consistent quality to the end users.     

不同加热条件对复合鱼糜凝胶特性的影响

本研究考察了鲢鱼鱼糜和带鱼鱼糜形成的复合鱼糜的破断力和凹陷深度在不同凝胶化条件下的变化规律。实验中各处理组的蛋白含量均为12%,其中蛋白比例为100%鲢鱼鱼糜,100%带鱼鱼糜,以及鲢鱼鱼糜和带鱼鱼糜的蛋白含量比例为9:1,8:2,7:3和6:4。结果表明:在凝胶化温度为30℃时,复合鱼糜的破断力均高于鲢鱼鱼糜,在鲢鱼鱼糜和带鱼鱼糜比例为7:3时破断力和凹陷深度均达到最大值,此时也高于带鱼鱼糜;而在凝胶化温度为40℃时,带鱼鱼糜添加量为40%时,破断力和凹陷深度达到最大,此时的凝胶特性优于带鱼鱼糜。带鱼鱼糜和鲢鱼鱼糜在50℃时均出现凝胶劣化现象。当带鱼鱼糜添加量为10%时,复合鱼糜对鲢鱼鱼糜和带鱼鱼糜的凝胶劣化均有显著的抑制作用。     

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     

Temperature and pH Affect Transglutaminase-Catalyzed "Setting" of Crude Fish Actomyosin

Dynamic rheological properties of actomyosin from two species (Alaska pollock, Atlantic croaker) were monitored during preincubation (setting) at 25°C and 37°C. followed bv nronrammed (l°C/min) cookinn to 77°C. Added guinea pig liver transgluianase enhanced gelation, as indicated by increases in both storage modulus (G′) and percentage of polymerized myosin heavy chain (MHC). In the presence of added transglutaminase maximum G′ and MHC polymerization occurred at the same conditions of pH and temperature which were optimum for setting of surimi pastes. This suggested that the transglutaminase-mediated setting reaction in surimi was constrained more by the conformation of the substrate (i.e., myosin) than by that of the enzyme.     

Effect of rainbow trout (Oncorhynchus mykiss) plasma protein on the gelation of Alaska pollock (Theragra chalcogramma) Surimi

ABSTRACT:  The effect of rainbow trout plasma protein (RPP) on the gelation of Alaska pollock surimi was determined to evaluate the possibility of its commercialization as a new protein additive. For modori gel, the breaking force, deformation, whiteness, and water holding capacity increased as the addition amount of RPP (0 to 0.75 mg/g) increased, and decreased at higher concentration of RPP (0.75 to 1.50 mg/g) ( P < 0.05). Protein solubility of modori gel in the mixture of SDS, urea, and β-mercaptoethanol decreased as the addition amount of RPP increased up to 0.75 mg/g, and increased at higher concentration of RPP (0.75 to 1.50 mg/g) ( P < 0.05). The contents of trichloroacetic acid-soluble peptide decreased as the addition amount of RPP (0 to 1.50 mg/g) increased ( P < 0.05). Based on the result of sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE), most myosin heavy chain of surimi was not degraded when RPP was added. Thus, RPP was supposed to act as a protease inhibitor in the gelation of Alaska pollock surimi. An RPP of 0.75 mg/g was the optimal concentration to prevent the gel weakening of Alaska pollock surimi. Compounds with molecular weights less than 10 kDa in RPP had no significant effect on the gelation of Alaska pollock surimi based on the result of the dialyzed RPP.     

Application of recombinant chum salmon cystatin to Alaska pollock (Theragra chalcogramma) surimi to prevent gel weakening

ABSTRACT:  Recombinant chum salmon cystatin (RC) expressed in Saccharomyces cerevisiae was purified by His-select nickel affinity chromatography. The specific inhibitory activities of RC against papain and cathepsin L were 7.45 and 10.24 U/mg, respectively. RC was stable over pH 5.0 to 7.0 and at temperature below 65 °C. RC was used to prevent the gel weakening of Alaska pollock surimi. RC at 100 μg/g showed the highest inhibitory activity against the autolysis of surimi based on the analysis of TCA-soluble peptides. As the concentration of RC increased, both the breaking force and deformation of modori gel greatly increased ( P < 0.05). The addition of RC resulted in less expressible drip, which coincided with the increase of whiteness. More myosin heavy chain (MHC) was retained as the addition of RC increased. Therefore, RC could prevent the degradation of proteins in Alaska pollock surimi and was better than egg white (EW). Thus, RC could be applied to Alaska pollock surimi to prevent gel weakening and RC at 100 μg/g was the optimal concentration.     

Original article: Gel properties of red tilapia surimi: effects of setting condition,fish freshness and frozen storage

This study aimed to determine effects of setting condition, fish freshness and storage time of frozen surimi on properties of red tilapia surimi gel. To investigate the effect of setting condition, a combination of eight setting temperatures (35–70 °C) and four setting times (30–120 min) was used. Maximum breaking force, deformation and gel strength were obtained after the gel had been set at 40 °C for 90 or 120 min. Setting at 65 °C resulted in the lowest obtained gel strength, because of proteolytic degradation of myosin heavy chain. Increasing storage time of raw fish material in ice caused a significant decrease in gel strength of the resultant surimi gel (P < 0.05). Gels produced from surimi kept in frozen storage for up to 9 months also exhibited reduced gel strength, with a concomitant increase in the expressible drip, with increasing storage time (P < 0.05).     

鲢鱼鱼糜蛋白质凝胶特性的研究

研究了鲢鱼鱼糜在不同的加热条件下 ,其凝胶的色泽、强度及显微结构的变化。结果表明 ,鲢鱼鱼糜在 60℃时达到较理想的色泽 (白色 ) ,较佳的凝胶条件为 ,先经过 3 5～ 40℃、60min的凝胶化 ,再经过 85℃、3 0min加热。在 5 0℃加热时 ,出现凝胶劣化现象     

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.     

超高压耦合热处理对鳙鱼鱼糜凝胶特性和水分迁移的影响

研究不同压力（100~500 MPa）耦合热处理（40 ℃/30 min,90 ℃/20 min）对鳙鱼（Aristichthys nobilis）鱼糜凝胶特性及水分迁移的影响,考察了不同处理条件下鳙鱼鱼糜的凝胶强度、持水性（WHC）、白度、质构、微观结构、SDS-PAGE电泳及水分迁移的变化,并进行相关性分析。研究发现,超高压耦合热处理能显著改善鳙鱼鱼糜的凝胶特性。超高压条件为300 MPa/15 min的压力耦合热处理（记为300PH）样品的凝胶强度和不易流动水单位质量峰面积（A22）显著性高于其他处理组（p<0.05）。与传统二段热处理样品相比,300PH样品的凝胶强度和WHC分别提高了88.40%、4.75%。与鱼糜凝胶的凝胶强度具有高度相关性的指标分别是破断强度、凹陷深度、硬度、弹性、胶着性、咀嚼性和A22。结合水单位质量峰面积（A21）与鱼糜凝胶强度具有中度相关性,这些表明300PH样品形成致密的凝胶网络结构,锁住更多结合水,限制不易流动水向自由水迁移,从而改善鱼糜凝胶的凝胶特性。该研究旨在为超高压技术鱼糜凝胶制品加工中的产业化应用、优质淡水鱼鱼糜制品的加工提供数据参考。     

Viscoelastic Characterization of Surimi Gel: Effects of Setting and Starch

Rheological properties of Alaska pollock surimi gels were affected by setting and addition of corn starch. Setting increased (p < 0.05) both elastic and loss moduli of gel in the absence of starch. However, in the presence of corn starch, setting decreased (p < 0.05) the elastic and loss moduli of the gels. In stress relaxation, the residual forces increased from 37.1 Newton (N) (nonsetting) to 51.8N (setting) in the absence of starch. However, in the presence of starch, the residual force decreased from 49.1N (nonsetting) to 39.0N (setting) which indicated an antagonistic effect between corn starch and setting. A Maxwell model was useful to quantify relaxation behavior of surimi gel and to evaluate the effects of changes in processing conditions.     

Effect of microbial transglutaminase and setting condition on gel properties of blend fish protein isolate recovered by alkaline solubilisation/isoelectric precipitation

The effect of microbial transglutaminase (M-TGase) (0–0.6 units g⁻¹ sample) and setting condition (25 °C/180 min, 30 °C/120 min, 35 °C/60 min and 40 °C/30 min) on gel properties of blend protein isolate of gutted kilka and silver carp was studied. The protein isolate provided a good substrate for M-TGase activity so that a low amount of M-TGase (0.2 unit g⁻¹ sample) substantially improved textural properties and water holding capacity (WHC) of the gels. Breaking force of the gels was positively affected by M-TGase up to 0.6 unit g⁻¹ sample, but it negatively affected their WHC. Prior setting at 25–35 °C increased the breaking force of proteins compared to directly heated gel, resulting in maximum breaking force at 35 °C/60 min. However, the setting at 40 °C/30 min caused proteolysis, which was reflected in higher amounts of TCA-soluble peptides and gel weakening. Denser microstructure and higher myosin heavy chain polymerisation observed in the gels which experienced the setting was well correlated with improvement in textural properties.     

Thermal syneresis affected by heating schedule and moisture level in surimi gels

ABSTRACT:  The extent of thermal syneresis in protein gelation is indicative of thermal and freeze-thaw stability as well as the network integrity of a protein gel. Thermal syneresis in Alaska pollock surimi gels was examined under different heating schedules (40 °C/20 min to 90  °C/30 min, 60 °C/20 min to 90 °C/30 min, and 90 °C/20 min to 90 °C/20 min) at varying moisture levels (80%, 82%, and 84%). The extent of syneresis and gel firming was monitored by centrifugation expressible moisture and penetration force, respectively. The occurrence of 2 distinct peaks as a function of time for both thermal syneresis and gel firming suggests that a multistage aggregation is involved in the formation of gel network. All syneresis preceded gel firming upon protein aggregation. Increasing the moisture content in the gel delayed the 2nd stage of protein aggregation. The 60 °C/20 min preheating followed by 90 °C/30 min postheating resulted in significantly greater thermal syneresis and gel weakening compared to 40 and 90 °C preheating. Changes of gel structure clearly reflected thermal syneresis when the size of water pores became smaller with initiation of network formation and progressively larger upon further heating. Thermal syneresis history during protein gelation can be used to predict thermal and freeze-thaw stability.