鱼糜凝胶形成过程中物理化学变化

采用化学法测定鱼糜凝胶形成过程中离子键、氢键、疏水相互作用和二硫键的变化,借助拉曼光谱仪分析草鱼鱼糜凝胶形成过程中鱼糜蛋白质构象的变化,进而研究化学作用力和蛋白质构象对鱼糜凝胶形成的影响。结果表明：在草鱼鱼糜凝胶的形成过程中,离子键、氢键显著减少,疏水相互作用、二硫键和非二硫共价键增加;α- 螺旋结构部分转化为无规卷曲结构。疏水相互作用、二硫键及非二硫共价键是影响凝胶形成的主要作用力,α- 螺旋和无规卷曲是草鱼鱼糜凝胶形成过程中维持鱼糜凝胶稳定结构的主要蛋白质构象。     

Effect of phosphate compounds on gel-forming ability of surimi from bigeye snapper (Priacanthus tayenus)

The properties of surimi gel from bigeye snapper (Priacanthus tayenus) added with various phosphate compounds (sodium pyrophosphate, PP; sodium tripolyphosphate, TPP; and sodium hexametaphosphate, HMP) at different levels (0%, 0.05%, 0.1%, 0.3% and 0.5% w/w) and heated under various conditions were studied. Kamaboko and directly heated gels from bigeye snapper surimi added with 0.05% PP had the increase in breaking force and deformation by 17.35% and 11.52%, and 13.54% and 3.53%, respectively, compared with the control gel (without PP addition). At the same level used (0.05%), TPP had no influence, but HMP exhibited a detrimental effect on kamaboko gel. The addition of PP (0.025%) in combination with 50 mmol CaCl₂/kg increased the breaking force by 38.68% as compared with the control gel (without additives), suggesting that the sufficient amount of CaCl₂ could enhance the setting of the gel. Generally, the marked decrease in breaking force with the coincidental increased expressible moisture was observed when the excessive amount of phosphate compounds was used (p<0.05). Microstructure study revealed that a gel with a fine network was formed with addition of PP. Therefore, the addition of PP in combination with CaCl₂ could increase the gel strength as well as water holding capacity of surimi gel.     

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.     

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.     

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.     

Effect of chitin and chitosan on gelling properties of surimi from barred garfish (Hemiramphus far)

The addition of chitin/chitosan significantly increased the breaking force and deformation of gels prepared from barred garfish surimi (P < 0.05). Addition of 7B chitosan with 65.6% degree of deacetylation (% DD) at the level of 15 mg g⁻¹ resulted in the maximum increases in both breaking force and deformation of suwari and kamaboko gels compared to the control and gels containing chitin or chitosan with other % DD (P < 0.05). A chitosan concentration of 10 mg g⁻¹ was found to render the highest breaking force of kamaboko gel compared to other concentrations tested (P < 0.05). Kamaboko gel containing chitosan had an increased breaking force as the calcium chloride concentration increased (P < 0.05), indicating the role of endogenous transglutaminase in cross‐linking of protein–protein and protein–chitosan conjugates. Therefore the incorporation of chitosan and calcium chloride greatly improved the gelling properties of surimi from barred garfish without changes in colour. © 2000 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     

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.     

草鱼和鲢鱼鱼糕品质及其微冻特性

测定草鱼和鲢鱼鱼糕的营养成分,以及在－2℃贮藏期间的硬度、弹性、持水性、白度、细菌总数、挥发性盐基氮(TVB-N)含量和硫代巴比妥酸还原值(TBARS)的变化。结果表明：鲢鱼鱼糕的蛋白质含量明显高于草鱼鱼糕(P＜0.05),水分、脂肪和灰分含量无显著性差异(P＞0.05);持水性和弹性都随微冻时间的延长而下降,硬度和白度则呈现先上升后下降的趋势;微冻过程中,细菌总数、TVB-N含量、TBARS值逐渐增加。微冻和真空包装相结合可以使草鱼和鲢鱼鱼糕保质期达到56d以上。     

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     

辅料改善草鱼鱼糜凝胶性能的机理

以草鱼为原料,通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳、质构分析和化学作用力测定等方法,研究辅料改善草鱼鱼糜凝胶性能的机理。结果表明：草鱼鱼糜蛋白自溶最适温度和pH值分别为65 ℃和6.5;马铃薯淀粉对鱼糜蛋白交联结构的填充能力强于胶原蛋白,而胶原蛋白对鱼糜组织蛋白酶的抑制效果好于马铃薯淀粉;辅料加入后,改变了鱼糜蛋白间的离子键、氢键、疏水性相互作用和二硫键等化学作用力,从而达到改善鱼糜品质的目的。     

棒状乳杆菌发酵秘鲁鱿鱼糜凝胶特性的变化及其形成机理

为阐明棒状乳杆菌（Lactobacillus coryniformis）Lz153发酵秘鲁鱿鱼糜的凝胶形成机理,通过质构仪测定棒状乳杆菌Lz153发酵秘鲁鱿鱼糜凝胶特性,分析凝胶形成过程中离子键、氢键、疏水相互作用、二硫键及非二硫共价键的变化,并利用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（sodium dodecyl sulfate-polyacrylamide gel electrophoresis,SDS-PAGE）方法观察肌原纤维蛋白变化情况。结果表明,棒状乳杆菌Lz153鱿鱼糜发酵24～36?h阶段凝胶特性最佳;离子键含量在发酵过程中呈逐渐减少趋势,氢键和疏水相互作用含量分别在发酵36?h和30?h达到最大值,二硫键和非二硫共价键含量随发酵时间延长而呈增加的趋势;氢键、疏水相互作用、二硫键和非二硫共价键是形成和维持凝胶网络的主要作用力。SDS-PAGE图谱显示,发酵后肌动蛋白和肌球蛋白重链均开始被降解,同时经发酵24?h后分子质量在100～135?kDa范围出现了新的盐溶性蛋白质条带,发酵至48?h也被降解。研究结果可为开发秘鲁鱿鱼为原料的乳酸菌发酵鱼糜制品加工提供参考依据。     

淡水鱼鱼糕加工适性和微冻特性的研究

测定了草鱼、鲢鱼、鲫鱼、鲈鱼、鲑鱼、黑鱼、鳊鱼、鲶鱼、鳙鱼等9种淡水鱼的采肉率和成本,比较不同淡水鱼鱼糕的营养特性和品质差异,测定鱼糕微冻贮藏过程中细菌总数、挥发性盐基氮(TVB-N)和硫代巴比妥酸还原值(TBARS)的变化。试验结果表明,鲶鱼采肉率最高,所需成本最低。不同淡水鱼鱼糕总蛋白含量有显著差异(p<0.05),而含水量、脂肪和灰分含量差异不显著(p>0.05)。草鱼鱼糕的硬度适中,弹性和凝聚性均优于其他种类淡水鱼鱼糕,咀嚼性和凝胶强度仅次于鲑鱼鱼糕,最适合作为淡水鱼鱼糜制品的加工原料。微冻与真空包装结合能明显延长鱼糕的货架期。草鱼鱼糕、鲢鱼鱼糕、黑鱼鱼糕和鳙鱼鱼糕的微冻保鲜期在56d以上。     

羊血浆蛋白对高温杀菌鱼糜制品凝胶特性的影响

为改善高温杀菌鱼糜制品的品质,研究羊血浆蛋白对121℃处理鱼糜制品凝胶特性的影响。以白鲢鱼糜为原料,测定羊血浆蛋白的添加对鱼糜凝胶质构特性、凝胶强度、持水性、折叠性、白度和流变特性的影响,并通过测定分子间作用力和溶解率的变化探究其影响机制。结果表明,与对照组相比,随着羊血浆蛋白的添加,高温处理鱼糜制品的硬度、弹性、胶粘性和咀嚼性显著增大(P<0.05),持水性显著增强(P<0.05),折叠性能增强,白度降低。当添加量为2%时,鱼糜制品的凝胶强度增加了92.88%。分子间作用力和溶解率分析显示,添加羊血浆蛋白能够提高体系氢键和非二硫共价键含量,从而改善高温处理鱼糜制品凝胶品质。     

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.     

葡萄糖氧化酶对鲢鱼糜凝胶特性的影响

为了研究葡萄糖氧化酶(GOD)诱导的氧化对鲢鱼糜凝胶特性的影响,以冷冻鲢鱼糜为原料,分析在不同的GOD添加量(0、0.1‰、0.3‰、0.5‰、0.7‰、0.9‰)下,鱼糜的弹性模量(G′)、损耗模量(G′′)以及鱼糜凝胶的凝胶强度、白度、微观结构、持水性、水分分布状态和蛋白交联等指标的变化情况.结果表明,随着GOD添...     

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.     

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。     

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.     

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%.