鲢肌球蛋白热诱导的凝胶化温度

Study on heat induced setting temperature of myosin from silver carp

  • 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。

     

    Abstract: 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 39 ℃. Myosin α-helix unwinded largely to random crimp structure at 40 ℃ and 54 ℃, and the maximum unwinding rate was 40℃. There are two myosin denaturation temperature 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.

     

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