加热温度对鳜鱼肌原纤维蛋白凝胶特性的影响  

Effects of heating temperature on gel properties of mandarin fish(Siniperca chuatsi)myofibrillar protein

作　　者：李苓 杨明柳 周迎芹 殷俊峰[2] 陈小娥 谢宁宁[2] LI Ling;YANG Mingliu;ZHOU Yingqin;YIN Junfeng;CHEN Xiao’e;XIE Ningning(College of Food and Pharmacy,Zhejiang Ocean University,Zhoushan 316022,China;Institute of Agro-products Processing,Anhui Academy of Agricultural Sciences,Hefei 230031,China;Department of Economics and Trade,Chongzuo Preschool Education College,Chongzuo 530022,China)

机构地区：[1]浙江海洋大学食品与药学学院,浙江舟山316022 [2]安徽省农业科学院农产品加工研究所,安徽合肥230031 [3]崇左幼儿师范高等专科学校经济贸易系,广西崇左530022

出　　处：《食品与发酵工业》2023年第19期242-248,共7页Food and Fermentation Industries

基　　金：安徽省重点研究与开发计划项目(202004a06020033);安徽省自然科学基金项目(2108085QC145);安徽省农业科学院畜禽、水产加工创新团队项目(2022YL041);安徽省农业科学院科研团队项目(2022YL030);国家重点研发计划项目(2016YFD0400400);安徽省科技重大专项(202103b06020007)。

摘　　要：通过测定凝胶强度、质构和巯基含量指标,以及运用SDS-PAGE、低场核磁共振和拉曼光谱技术手段,探究加热温度(40~90℃)对鳜鱼肌原纤维蛋白热诱导凝胶的影响。结果表明,温度对该蛋白凝胶特性的影响显著;在整个升温过程中,凝胶强度逐渐增强,从107.19 g·cm增加到422.50 g·cm,巯基含量逐渐降低,α-螺旋结构转变成β-折叠结构,α-螺旋降低了15.30%,β-折叠增加了14.70%;升温至80℃过程中,硬度和弹性逐渐增强,SDS-PAGE中的肌动蛋白和原肌球蛋白条带逐渐加深,而在90℃时,硬度和弹性略有降低,肌动蛋白和原肌球蛋白条带发生降解现象;在70~90℃内,该蛋白凝胶中自由水含量逐渐增多,增加了1.43%,而弛豫时间逐渐变小,减少了5602.917 ms;在80℃时,该热诱导凝胶综合特性最佳。因此,鳜鱼肌原纤维蛋白凝胶具有开发成功能性鱼制品的潜力。To study the effect of heating temperature(40-90℃)on thermally induced gelation of mandarin fish(Siniperca chuatsi)myofibrillar protein,gel strength,texture,and sulfhydryl groups content,sodium dodecyl sulfate-polyacrylamide gel electrophoresis(SDS-PAGE),low-field nuclear magnetic resonance(LF-NMR),and Raman spectroscopy were applied.Results showed that the heating temperature significantly affected the formation of protein gels.With the temperature increased to 90℃,the gel strength gradually increased from 107.19 g·cm to 422.50 g·cm,and the sulfhydryl group content gradually decreased.Besides,the gel’sα-helix structure was converted into aβ-sheet during the period,α-helix decreased by 15.30%,β-sheet increased by 14.7%.As the temperature increased to 80℃,the gel’s hardness and springiness gradually increased,and the actin and tropomyosin bands in SDS-PAGE gradually deepened.In addition,the hardness and springiness slightly decreased,and the actin and tropomyosin bands were degraded at 90℃.Between 70℃and 90℃,free water could be observed and gradually increased by 1.43%,while their relaxation time gradually decreased by 5602.917 ms.At 80℃,the protein exhibited an excellent gel performance.In short,mandarin fish’s myofibrillar protein exerts great potential for developing functional fish products.

关 键 词：鳜鱼 肌原纤维蛋白 温度 凝胶强度 二级结构 水分状态 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]