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.     

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     

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。     

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.     

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.     

不同食用蛋白的添加对鲤鱼鱼糜流变和凝胶特性的影响

目的:研究大豆分离蛋白(soybean protein isolated,SPI)、乳清分离蛋白(whey protein isolate,WPI)、花生分离蛋白(peanut protein isolate,PPI)的添加对鲤鱼鱼糜流变和凝胶性质的影响。方法:利用流变仪、质构仪、色差计等对添加不同蛋白鱼糜的弹性模量、黏性模量、凝胶强度、破断强度、凹陷深度、持水性以及白度进行测定,并采用相关性分析法研究各指标之间的相互关系。结果:不同添加量的SPI、WPI和PPI均能有效地改善鱼糜的弹性模量、黏性模量、破断强度、凝胶强度和持水性,但会降低破断深度和白度,但各测定指标间存在显著相关(p<0.05)。SPI和PPI的添加对鱼糜的流变性、破断强度、凝胶强度的提高效果更好,添加量为8%时,鱼糜的凝胶强度均达到最大值,其中SPI组可达3806.70 g·mm,比对照组增加了34.63%;WPI对鱼糜的保水性效果最好,添加量为8%时,失水率仅为12.6%;白度随着蛋白添加量的增加而降低,其中PPI组与WPI组引起的白度降低较少,且差异不显著(p>0.05)。结论:在实际鱼糜制品的生产中,应根据产品的特征选择适合的蛋白种类和合理的添加量,来提高鱼糜制品的品质。     

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.     

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     

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.     

乳清浓缩蛋白对竹荚鱼鱼糜凝胶化和凝胶劣化的影响

采用质构分析法、扫描电子显微镜等方法研究乳清浓缩蛋白对竹荚鱼鱼糜凝胶劣化的抑制作用。结果表明：添加乳清浓缩蛋白(WPC)能显著改善竹荚鱼鱼糜在30℃凝胶化时的凝胶特性,并且添加量为5%(质量分数),加热时间为5h时,竹荚鱼鱼糜的凝胶特性最佳;添加WPC能显著抑制竹荚鱼鱼糜在50℃凝胶劣化现象,WPC的添加量为5%时,抑制效果显著,添加量为10%时,抑制效果最佳;WPC的添加量低于0.5%时,对竹荚鱼鱼糜凝胶色泽的影响不明显;添加量超过1%时,竹荚鱼鱼糜凝胶的白度显著降低。微观结构的观察表明,添加WPC使鱼糜凝胶的结构变得更加致密,因而能增强竹荚鱼鱼糜的凝胶强度。     

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.     

ɛ-POLYLYSINE IMPROVES THE QUALITY OF SURIMI PRODUCTS

To apply ɛ-polylysine (PL) as a natural food preservative for the preparation of surimi products, effects of added PL on the textural properties and shelf-life of kamaboko gels were investigated. Kamaboko gels were prepared by setting at 30C for 1 h, then heating at 80C for 20 min. Breaking force and breaking strain of kamaboko gels increased slightly with increasing PL concentration up to 0.2% and decreased at 0.4%. However, the protein subunit component composition of kamaboko gels did not vary with the amount of PL added, indicating that PL did not promote the polymerization of myosin heavy chain. The increased pH value of surimi to around 7.6 as the result of the incorporation of 0.2% PL was found to be attributable to the increased textural properties of kamaboko gels. The shelf-life of kamaboko gels was significantly extended by the addition of 0.2% PL in surimi, especially at 5C and 10C storage.     

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     

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.     

Effects of konjac glucomannan on physicochemical properties of myofibrillar protein and surimi gels from grass carp (Ctenopharyngodon idella)

The cryoprotective effect of konjac glucomannan (KGM) on myofibrillar protein from grass carp (Ctenopharyngodon idella) during frozen storage at −18 °C and the influence of five levels of KGM (0%, 0.5%, 1%, 1.5%, and 2%) on texture properties, water-holding capacity, and whiteness of grass carp surimi gels were investigated. KGM as a novel cryoprotectant could significantly mitigate the decrease in salt extractable protein (SEP), Ca²⁺-ATPase activity, and total sulphydryl and active sulphydryl contents of myofibrillar protein during frozen storage. KGM at the level of 1% showed the same good cryoprotective effect as a conventional cryoprotectant (10% sucrose–sorbitol, 1:1, w/w). As the levels of KGM increased, breaking force and deformation of grass carp surimi gels increased significantly. Water-holding properties of the surimi gels are improved with the increasing addition of KGM, but the whiteness decreased and the colour became darker. The optimum addition level of KGM was suggested to be 1%.     

Chemical Interactions and Protein Conformation Changes During Silver Carp (Hypophthalmichthys Molitrix) Surimi Gel Formation

Chemical interactions and protein conformations changes during the formation of silver carp surimi gel were studied by textural analysis, chemical methods, laser Raman spectroscopy, and circular dichrosim. The optimum setting time at 40°C was 60 min. During surimi gel formation, ionic bonds and hydrogen bonds decreased significantly (P ≤ 0.05), while hydrophobic interactions, disulfide bonds, and non-disulfide covalent bonds increased significantly (P ≤ 0.05). Hydrophobic interactions, disulfide bonds, and non-disulfide covalent bonds were the main chemical interactions maintaining the stable structure of surimi gel. Secondary structural analysis of surimi protein showed that 94.11% α-helix existed in native myosin and it partly changed into β-turn and random coil during heating. Myosin gel was made up of 33.70% α-helix, 12.40% β-turn and 53.90% random coil. These three kinds of secondary structures were the main protein conformations in surimi gel.     

The Pepsin Digestibility of Thermal Gel Products Made from White Croaker (Pennahia argentata) Muscle in Associating with Myosin Polymerization Levels

Thermal gels were made from white croaker (Pennahia argentata) surimi at various polymerization levels of myosin heavy chains induced by suwari treatment at 38 °C for various time periods and subsequently heated at 85 °C for 20 min. Myosin heavy chain polymerization levels were also achieved in the presence of microbial transglutaminase (MTG) added at various concentrations in the surimi. The breaking strength and breaking strain rate were markedly increased during suwari treatment up to 60 min in accordance with the increased levels of myosin heavy chain polymerization. MTG enhanced myosin heavy chain polymerization during suwari treatment for 15 and 30 min, resulting in the increase of breaking strength. The solubilization in 8 M urea and pepsin digestibility of these gels as well as angiotensin I‐converting enzyme (ACE) inhibitory activity of their pepsin digests were decreased with the increased levels of myosin heavy chain polymerization. These results suggest that myosin heavy chain polymerization affects not only rheological properties of thermal gels but also their functional properties for human health.     

Strength of Protein Gels Prepared with Microbial Transglutaminase as Related to Reaction Conditions

Influence of gelling reaction conditions on the strength of several protein gels prepared with microbial transglutaminase (TGase) was investigated. A method was developed to gel proteins and measure gel breaking strength in a micro well plate. Enzyme concentration range for maximum gel breaking strength varied from 10 to 40 units/g protein. Maxima gel breaking strengths were achieved at 50°C for SPI, caseinate and gelatin and 65°C for egg yolk and egg white proteins. Optimum pH resulting in strong gels was pH 9 for SPI, caseinate, and egg yolk, and pH 6 for gelatin and egg white. Adjusting pH was promoted in egg white the formation of ?-(γ-glutamyl)lysine crosslinks and increased its gel breaking strength.