冻融次数迫使镜鲤鱼肌原纤维蛋白功能和结构特性变化的研究

摘要/Abstract

摘要： 摘要：通过测定肌原纤维蛋白溶解性、乳化性、δ-电势、巯基含量、自由氨基酸、二聚酪氨酸、表面疏水性和α-螺旋含量的变化，探究反复冻融过程引起镜鲤鱼肌原纤维蛋白功能特性和结构特性的变化。结果表明：随着冻融次数增加到第五次时，蛋白的乳化活性、乳化稳定性分别下降至20.67 m2/g、34.83%，溶解性下降了23.23%，且差异显著（p < 0.05），δ-电势不断增加、巯基含量持续下降、二聚酪氨酸含量不断上升、α-螺旋含量不断下降。冷冻-解冻循环破坏了蛋白质的完整结构，使其功能特性明显降低（p < 0.05）。

关键词: 关键词：冷冻-解冻循环, 镜鲤鱼, 肌原纤维蛋白, 功能特性, 结构

Abstract: Abstract: The change of emulsification, solubility, δ-potential, sulfydryl content, free amino acid, dityrosine, surface hydrophobicity and circular dichroism spectrum in myofibrillar protein of specularis cyprinus carpio induced by freeze-thaw cycles(0、1、3、5) were studied, which to explore the effect of freeze-thaw cycles on the functional and structure properties. The results indicated that the emulsifying activity and emulsifying stability of fish protein decreased to 20.67 m2/g and 34.83%, respectively, and the solubility decreased by 23.23%（p < 0.05）, δ-potential was increased constantly with the increase of freeze-thaw times; sulfhydryl content was declined and dityrosine content was increased constantly, free amino acid and surface hydrophobicity increased by 17.43% and 37.11%, respectively, α-helical content was decreased constantly. The freeze-thaw cycles reduced the functional properties of the myofibrillar protein in fish and its structure also changed significantly (p < 0.05).

Key words: Keywords: freeze-thaw cycles, specularis cyprinus carp, myofibrillar protein, functional properties, structure

中图分类号:

TS254.1

邓思杨王博夏秀芳. 冻融次数迫使镜鲤鱼肌原纤维蛋白功能和结构特性变化的研究[J]. 食品科学, 0, (): 0-0.

Si-Yang DENG XIA Xiu-Fang. Change of functional and structural properties in specularis cyprinus carpio myofibrillar protein induced by freeze-thaw cycles[J]. FOOD SCIENCE, 0, (): 0-0.

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