牙鲆鱼、多宝鱼肌肉蛋白性质比较分析
详细信息 查看官网全文
- 英文论文题名：A comparative study of Japanese flounder(Paralichthys olivaceus)and turbot(Scophthalmus maximus) muscle protein characteristic
- 论文作者：夏俪宁 ; 郝若伊 ; 刘洋 ; 潘锦锋
- 英文论文作者：Xia Lining ; Hao Ruoyi ; Liu Yang ; Pan Jinfeng ; School of Food Science and Technology ; Dalian Polytechnic University ; National Engineering Research Center of Seafood
- 年：2016
- 作者机构：大连工业大学食品学院国家海洋食品工程技术研究中心;
- 论文关键词：肌原纤维蛋白 ; 牙鲆鱼 ; 多宝鱼 ; 流变特性 ; 热变特性
- 英文论文关键词：myofibrillar protein ; japanese flounder ; turbot ; rheological properties ; thermal processing properties
- 会议召开时间：2016-11-09
- 会议录名称：中国食品科学技术学会第十三届年会论文摘要集
- 英文会议录名称：Abstracts of the 13th Annual Meeting of CIFST
- 语种：中文
- 分类号：TS254.1
- 学会代码：ZGSP
- 会议名称：中国食品科学技术学会第十三届年会
- 会议地点：中国北京
- 主办单位：中国食品科学技术学会
- 学会名称：中国食品科学技术学会
- 页数：2
- 文件大小：110k
- 原文格式：O
- 会议级别：全国
摘要
鱼类肌肉蛋白的组成与性质决定了其加工特性和产品的功能特性。本文以牙鲆鱼和多宝鱼为研究对象,分析二者肌肉蛋白组成形式,研究二者肌原纤维蛋白的热变特性、流变特性以及乳化性和起泡性,并对以上性质进行比较。SDS-PAGE电泳分析表明(蛋白浓度7mg/ml)牙鲆鱼和多宝鱼的盐溶性蛋白与水溶性蛋白条带有显著差异,牙鲆鱼肌动蛋白比例低于多宝鱼,水溶性蛋白分子量较低,20.1kDa处水溶性蛋白差异明显。DSC研究表明牙鲆鱼肌原纤维蛋白变性温度为39.976℃,高于多宝鱼肌原纤维蛋白变性温度37.861℃。流变结果显示多宝鱼肌原纤维蛋白储能模量低于牙鲆鱼,牙鲆鱼在40-50℃有一流变特性转折点,多宝鱼在30-40℃有一流变特性转折点,与DSC分析结果相一致。牙鲆鱼与多宝鱼肌原纤维蛋白EAI在5mg/ml分别为3.72 m~2/g与4.16 m~2/g,FC在2mg/ml分别为266.7%与230%,而FS在1 mg/ml分别为178.3%与203.3%。以上结果表明,牙鲆鱼、多宝鱼肌肉蛋白形式、热变特性和流变特性差异较明显,而乳化性和起泡性差异不显著。
Composition and properties of fish muscle protein determines its processing characteristics and product features.This study used Japanese flounder and turbot muscle as research materials,analyzing the muscle protein patterns,thermal response properties of myofibrillar protein(MFP),rheological properties and emulsifying and foaming capability.SDS-PAGE electrophoresis analyses found distinct differences in salt-soluble and water-soluble proteins between Japanese flounder and turbot bar.The former had high proportion of actin than turbot and a 20.1 kDa water soluble protein presented in it.Different scanning calorimetric(DSC) study shows that the denaturation point of flounder MFP was 39.98℃,higher than that of turbot MFP,which was 37.86℃.Rheological result shows that the storage modulus of MFP from turbot was lower than that from flounder.A peak was observed in storage modulus of flounder MFP between 40-50℃ and of turbot MFP at range of 30 to40℃,consistent with the results of DSC.Emulsifying activity index(EAI) of MFP from flounder and turbot at 5 mg/ml were3.72 and 4.16 m~2/g respectively.Foaming capability(FC) of them at 2 mg/ml were 266.7%and 266.7%,and foaming stability(FS) at 1 mg/ml were 178.3%and 203.3%.The above results show that the protein pattern,thermal processing characteristics and rheological properties of flounder and turbot muscle proteins differed,but the emulsifying and foaming capability is similar.
Composition and properties of fish muscle protein determines its processing characteristics and product features.This study used Japanese flounder and turbot muscle as research materials,analyzing the muscle protein patterns,thermal response properties of myofibrillar protein(MFP),rheological properties and emulsifying and foaming capability.SDS-PAGE electrophoresis analyses found distinct differences in salt-soluble and water-soluble proteins between Japanese flounder and turbot bar.The former had high proportion of actin than turbot and a 20.1 kDa water soluble protein presented in it.Different scanning calorimetric(DSC) study shows that the denaturation point of flounder MFP was 39.98℃,higher than that of turbot MFP,which was 37.86℃.Rheological result shows that the storage modulus of MFP from turbot was lower than that from flounder.A peak was observed in storage modulus of flounder MFP between 40-50℃ and of turbot MFP at range of 30 to40℃,consistent with the results of DSC.Emulsifying activity index(EAI) of MFP from flounder and turbot at 5 mg/ml were3.72 and 4.16 m~2/g respectively.Foaming capability(FC) of them at 2 mg/ml were 266.7%and 266.7%,and foaming stability(FS) at 1 mg/ml were 178.3%and 203.3%.The above results show that the protein pattern,thermal processing characteristics and rheological properties of flounder and turbot muscle proteins differed,but the emulsifying and foaming capability is similar.
引文