高强度超声作用下鲢肌球蛋白的结构及流变学性变化

摘要/Abstract

摘要： 本文以鲢鱼为原料提取纯化肌球蛋白，研究不同高强度超声处理条件下肌球蛋白链构象、二级结构及流变学性能流变学特性的变化。超声处理会降低肌球蛋白的以鲢鱼为原料提取纯化肌球蛋白，研究不同高强度超声处理条件下肌球蛋白链构象、二级结构及流变学特性的变化。超声处理会降低肌球蛋白的低温自组装程度，使样品的零剪切黏度逐渐降低、流动性增大，并诱导肌球蛋白α-螺旋向较为松散的β-折叠和无规卷曲结构转变，促使包埋在分子内部的活性基团暴露出来。该结构变化有利于升温过程中分子间的交联，并降低凝胶化温度，适当的超声条件（100 W和150 W处理12 min）可提高肌球蛋白的凝胶形成能力，而超声功率过大（200 W和250 W处理12 min）则会降低其凝胶形成能力，选择适当的超声条件在鱼糜凝胶的加工中十分重要。

关键词: 关键词：肌球蛋白, 高强度超声, 结构, 流变学特性, 鲢鱼

Abstract: Myosin from silver carp was sonicated with varying power output (100, 150, 200 and 250 W) for 3, 6, 9, 12 min. The changes in the chain conformation，, secondary structure and rheological properties of myosin were evaluated by UV absorption spectrum, circular dichroism and rheometer. The low-temperature self-assembly of myosin was depressed by the high intensity ultrasound (HIU), suggested by the decreased zero shear viscosity and the increased fluidity. The HIU treatment induced a conversion of myosin α-helix to relatively loose β-sheet and random coil. Therefore, some active groups in the molecules were exposed. The structural change was beneficial for forming intermolecular interactions during heating, and reduced the setting temperature of myosin. Furthermore, a suitable ultrasonic treatment (100 W and 150 W for 12 min) could improve the gelation properties of myosin, but an excessive ultrasound power (200 W and 250 W for 12 min) would lead to a decrease in gelation properties. It is important to select a suitable high intensity ultrasound for improving gelation properties of surimi.

Key words: Key words: myosin, high intensity ultrasound, structure, rheological property, silver carp

中图分类号:

谢亚如刘庆尤娟熊善柏刘茹. 高强度超声作用下鲢肌球蛋白的结构及流变学性变化[J]. 食品科学, 0, (): 0-0.

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