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追踪在长期冷冻储存过程中,普通鲤鱼(Cyprinus carpio)肌原纤维蛋白结构改变引起的蛋白质聚集行为和乳化性质。

Tracking protein aggregation behaviour and emulsifying properties induced by structural alterations in common carp (Cyprinus carpio) myofibrillar protein during long-term frozen storage.

机构信息

School of Food Science and Technology, Dalian Polytechnic University, Dalian 116034, China; College of Food Science and Technology, Guangdong Ocean University, Zhanjiang, Guangdong 524088, China.

College of Food Science, Northeast Agricultural University, Harbin, Heilongjiang 150030, China.

出版信息

Int J Biol Macromol. 2024 Apr;264(Pt 1):130171. doi: 10.1016/j.ijbiomac.2024.130171. Epub 2024 Feb 13.

Abstract

The effect of ultrasound-assisted immersion freezing (UIF), air freezing (AF), and immersion freezing (IF) on the protein structure, aggregation, and emulsifying properties of common carp (Cyprinus carpio) myofibrillar protein during frozen storage were evaluated in the present study. The result showed that, compared with AF and IF samples, UIF sample had higher reactive/total sulfhydryl, protein solubility, and lower protein turbidity (P < 0.05), indicating that UIF was beneficial to inhibit protein oxidation and aggregation induced by frozen storage. UIF inhibited the alteration of secondary structure and tertiary structure during frozen storage. Meanwhile, UIF sample had higher emulsifying activity index, and smaller emulsion droplet diameter than AF and IF samples (P < 0.05), suggesting that UIF was beneficial for maintaining the emulsifying properties of protein during storage. In general, UIF is a potential and effective method to suppress the decrease in protein emulsifying properties during long-term frozen storage.

摘要

本研究评价了超声辅助浸渍冻结(UIF)、空气冻结(AF)和浸渍冻结(IF)对冷冻储存过程中鲤鱼(Cyprinus carpio)肌原纤维蛋白结构、聚集和乳化特性的影响。结果表明,与 AF 和 IF 样品相比,UIF 样品具有更高的反应/总巯基、蛋白质溶解度和更低的蛋白质浊度(P<0.05),表明 UIF 有利于抑制冷冻储存引起的蛋白质氧化和聚集。UIF 抑制了二级结构和三级结构在冷冻储存过程中的变化。同时,UIF 样品的乳化活性指数高于 AF 和 IF 样品,乳液粒径也较小(P<0.05),表明 UIF 有利于在储存过程中保持蛋白质的乳化性能。总的来说,UIF 是一种抑制长期冷冻储存过程中蛋白质乳化性能下降的潜在有效方法。

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