低温胁迫肌原纤维蛋白结构和热稳定性的变化  

Change of Protein Structure and Thermal Stability of Myofibrillar Protein under Cold Stress

作　　者：李芳菲[1] 王博[1] 石硕 潘男 邓思杨[1] 夏秀芳[1] Li Fangfei;Wang Bo;Shi Shuo;Pan Nan;Deng Siyang(Northeast Agricultural University, College of Food Science , Harbin 150030)

机构地区：[1]东北农业大学食品学院,哈尔滨150030

出　　处：《中国食品学报》2019年第3期232-241,共10页Journal of Chinese Institute Of Food Science and Technology

基　　金：国家自然科学基金面上项目(31571859)

摘　　要：本文研究了冻藏温度(-5,-18,-26,-35,-70℃)、冻藏时间(0,1,3,6,9,12 mon)对猪肉背最长肌中的蛋白质结构(ATPase酶活性、巯基含量、SDS-聚丙烯酰氨凝胶电泳)和热稳定性的影响。结果表明:随着冻藏温度的降低,12 mon蛋白质总巯基含量、活性巯基含量、Ca^(2+)-ATPase活性、K^+-ATPase活性呈递减趋势;通过DSC测定蛋白的热稳定性,冻藏过程中肌肉蛋白的热转变温度和焓值均降低,且冻结温度越高冻藏时间越长,温度和焓值降低得越明显;蛋白的SDS-PAGE电泳图谱结果显示,冻藏时间越长冻藏温度越高,蛋白质分子降解越明显。The effect of freezing temperature(-5,-18,-26,-35 and-70 ℃) and freezing storage time(0, 1,3, 6, 9, 12 mon) on protein structure(ATPase activity, sulfhydryl content, SDS-PAGE) and thermal stability of Myofibrillar protein were studied. The results show that with the decrease of freezing storage temperature, after frozen storage 12 mon, the total sulfhydryl content of MP, the activity sulfhydryl content of MP, the Ca^2+-ATPase activity of MP, the K^+-ATPase activity of MP decreased progressively. Myofibrillar protein thermal stability is determination by DSC during frozen storage. The result is: myofibrillar protein thermal transition temperature and enthalpy values are the lower. Myofibrillar protein thermal transition temperature and enthalpy values significantly decreased;the longer freezing time, the higher freezing temperature, myofibrillar protein thermal transition temperature and enthalpy values are the lower. The protein of SDS-PAGE electrophoresis patterns showed that the course of frozen storage occurred to protein degradation and denaturation.

关 键 词：冻藏时间 冻藏温度 肌原纤维蛋白结构 热稳定性 

分 类 号：TS251.4[轻工技术与工程—农产品加工及贮藏工程]