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鲢肌球蛋白热诱导的凝胶化温度 被引量：6

Studies on heat-induced setting temperature of myosin from silver carp
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摘要 为了研究鲢鱼糜凝胶化温度与肌球蛋白热稳定性的关系,测定经不同凝胶化温度处理的鱼糜凝胶特性,利用浊度法检测鲢肌球蛋白溶液聚集体的形成过程,并采用圆二色谱仪、差式量热扫描仪分别对鲢肌球蛋白溶液的α-helix结构变化和热变性温度进行测定。结果表明,鲢鱼糜的适宜凝胶化温度为40℃,肌球蛋白的聚集速率在39℃、51℃、54℃3个温度点时出现大幅度增加,其中39℃时聚集速率最快;肌球蛋白α-helix在40℃、55℃时大量解旋成无规卷曲结构,40℃时解旋速率最快;肌球蛋白存在两个变性温度43.32℃和51.59℃。鲢鱼糜凝胶化温度与肌球蛋白α-helix的第一个解旋温度和第一个变性峰值温度点相对应,凝胶化温度实质上是肌球蛋白的第一个变性峰值温度点。 In order to study the relationship between silver carp surimi gelling temperature and thermal stability of myosin,surimi gel properties treated with different gelling temperature,formation of myosin solution aggregates,α-helix structure change and thermal denaturation temperature of myosin solution were determined respectively.The results were as follows：The suitable gelling temperature of silver carp surimi was 40 ℃.The aggregation rate of myosin increased greatly at 39 ℃,51 ℃,54 ℃,and the maximum aggregation rate was at 39 ℃.Myosin α-helix unwinded largely to random crimp structure at 40 ℃ and 54 ℃,and the maximum unwinding rate was at 40 ℃.There are two myosin denaturation temperatures of 43.32 ℃ and 51.59 ℃.Silver carp surimi gelling temperature was relative to the first unwinding temperature and denaturing peak temperature of myosin α-helix.The gelling temperature is essentially the first denaturing peak temperature of myosin.
作者 刘海梅 熊善柏 张丽 彭鸽
机构地区 鲁东大学食品工程学院 华中农业大学食品科技学院 鲁东大学生命科学学院
出处 《水产学报》 CAS CSCD 北大核心 2010年第4期643-647,共5页 Journal of Fisheries of China
基金 现代农业产业技术体系建设专项资金资助(NYCYTX-49) 国家"十一五"科技支撑计划(2006BAD05A18)
关键词 鲢 肌球蛋白 凝胶化温度 变性 构象 Hypophthalmichthys molitrix myosin setting temperature denaturation conformation
分类号 TS254 [轻工技术与工程—水产品加工及贮藏工程] S917 [农业科学—水产科学]
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参考文献14

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二级参考文献25

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水产学报
2010年 第4期

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