PSE猪肉肌原纤维蛋白的氧化变性  

Oxidative Denaturation of Myofibril Protein in Pale,Soft and Exudative(PSE)Pork

作　　者：李文采[1] 刘飞[1] 田寒友[1] 邹昊[1] 王辉[1] 张振琪[1] 李家鹏[1] 乔晓玲[1] 

机构地区：[1]中国肉类食品综合研究中心肉类加工技术北京市重点实验室,北京100068

出　　处：《肉类研究》2017年第10期6-11,共6页Meat Research

基　　金：国家公益性行业(农业)科研专项(201303083);"十三五"国家重点研发计划重点专项(2016YFD0401203)

摘　　要：为探讨白肌肉(pale,soft and exudative meat,PSE肉)形成时肌原纤维蛋白结构和功能的变化,以PSE猪肉为研究对象,从氧化还原体系失衡和钙激活蛋白酶活性变化两方面进行研究。结果表明:与正常肉(red,firm and non-exudative meat,RFN肉)相比,PSE肉的超氧化物歧化酶抑制率显著降低(P<0.05),谷胱甘肽过氧化物酶活性显著增加(P<0.01),钙激活蛋白酶活性显著增加(P<0.05);随着氧化还原体系失衡和钙激活蛋白酶活性的增加,PSE肉十二烷基硫酸钠-聚丙烯酰胺凝胶电泳图谱的肌间线蛋白、肌动蛋白和Ⅰ-肌钙蛋白条带变淡、变细;肌原纤维蛋白的表面疏水性显著增大(P<0.05),溶解性显著降低(P<0.01),结构和功能特性发生改变。The objective of this study was to discuss the structural and functional changes of myofibril protein during the formation of pale, soft and exudative （PSE） pork. The focus was on the correlations of these changes with redox imbalance and changes in calpain activity. The results were showed that compared with red, firm and non-exudative （RFN） meat, the activity of superoxide dismutase （SOD） was significantly lower （P 〈 0.05）, while the activities of glutathione peroxidase （GSH-Px） （P 〈 0.01） and calpain （P 〈 0.05） were significantly higher in PSE pork. As redox imbalance occurred and ccalpain activity increased, desmin, actin and troponin I bands became lighter in color and thinner in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis （SDS-PAGE） pattern, the surface hydrophobicity of myofibril protein was significantly increased （P 〈 0.05） and solubility was decreased significantly （P 〈 0.01）, implying the structural and functional changes of myofibril protein in PSE pork.

关 键 词：抗氧化酶 钙激活蛋白酶 肌原纤维蛋白氧化 PSE肉 

分 类 号：TS251.51[轻工技术与工程—农产品加工及贮藏工程]