小热休克蛋白对牛肉嫩度影响机制的研究进展  

Research progress on the mechanism of the effect of small heat shock protein on the beef tenderness

作　　者：赵妍 罗欣[1] 毛衍伟[1] 杨啸吟[1] 朱立贤[1] 梁荣蓉[1] 成海建 张一敏[1] ZHAO Yan;LUO Xin;MAO Yanwei;YANG Xiaoyin;ZHU Lixian;LIANG Rongrong;CHENG Haijian;ZHANG Yimin(College of Food Science and Engineering,Shandong Agricultural University,Taian 271018,China;National Beef Cattle Industrial Technology System,Jinan 250000,China)

机构地区：[1]山东农业大学食品科学与工程学院,山东泰安271018 [2]国家肉牛牦牛产业技术体系济南站,山东济南250000

出　　处：《食品与发酵工业》2021年第12期294-301,共8页Food and Fermentation Industries

基　　金：现代农业产业技术体系建设专项资金资助(肉牛CARS-37);山东省现代农业产业技术体系创新团队建设专项资金(SDAIT-09-09)。

摘　　要：动物屠宰后,机体会出现缺血、缺氧环境,肌肉内环境胁迫机体发生免疫应答,热休克蛋白首先被激活。热休克蛋白因其具有分子伴侣功能可以起到抗细胞凋亡、维持蛋白质结构稳定等作用,对宰后成熟过程中的肉嫩度产生影响,相关的研究成果亟需总结、归纳。因此,该文首先概述了几种重要的热休克蛋白的分子结构特征和功能,并立足于近年来小热休克蛋白对牛肉嫩度的研究进展,从小热休克蛋白对蛋白质聚合物形成、细胞骨架蛋白降解、阻止细胞凋亡等方面综述了小热休克蛋白对牛肉嫩度的影响机制,同时还概括了pH值、宰前应激等对热休克蛋白表达量的调节及其对嫩度的潜在影响,以期为肉嫩度的改善提供理论参考。After slaughtering,animals appear ischemia,hypoxia,and skeletal muscle cells trigger an immune response to the resistant harmful intramuscular environment.Heat shock proteins(HSPs)are firstly activated.HSPs have the functions of the molecular chaperone,anti-apoptosis,maintaining protein structure stability and so on,which has an impact on the meat tenderness during the post-mortem aging process.In this paper,several important structural features and functions of HSPs were reviewed firstly,and then,the mechanism of sHSPs on red meat tenderness was summarized from the aspects of sHSPs on protein polymer formation,cytoskeleton protein degradation and cell apoptosis prevention.Additionally,the effect of ultimate pH and pre-slaughter stresses on the expression of HSPs,and consequently on the meat tenderness potentially were also summarized.From a practical point of view,the information provided in this review will help to improve meat tenderness.

关 键 词：小热休克蛋白 嫩度 骨架蛋白 μ-钙激活酶 细胞凋亡酶 

分 类 号：TS251.52[轻工技术与工程—农产品加工及贮藏工程]