不同pH和离子强度条件下青鱼(Mylopharyngodon piceus)肌浆蛋白IgG/IgE结合能力的变化  

Effect of different pH and ion strength on IgG/IgE binding capacity of sarcoplasmic protein of black carp( Mylopharyngodon piceus)

作　　者：朱一丹 谢国锦[2] 高岭 杨方 高沛 余达威 姜启兴 许艳顺 夏文水 ZHU Yidan;XIE Guojin;GAO Ling;YANG Fang;GAO Pei;YU Dawei;JIANG Qixing;XU Yanshun;XIA Wenshui(State Key Laboratory of Food Science and Technology,School of Food Science and Technology,Collaborative Innovation Center of Food Safety and Quality Control in Jiangsu Province,Jiangnan University,Wuxi 214122,China;Children′s Hospital of Nanjing Medical University,Nanjing 210000,China)

机构地区：[1]江南大学食品科学与技术国家重点实验室、食品学院、江苏省食品安全与质量控制协同创新中心,江苏无锡214122 [2]南京医科大学附属儿童医院检验科,江苏南京210000

出　　处：《食品与发酵工业》2020年第14期34-39,共6页Food and Fermentation Industries

基　　金：江苏省自然科学青年基金(BK20170185);国家大宗淡水鱼类产业技术体系项目(No.CARS-45);国家食品科学与工程一流学科建设项目(JUFSTR20180201)。

摘　　要：该文以青鱼为研究对象,研究肌浆蛋白在不同p H和离子强度条件下,Ig G/Ig E结合能力及结构的变化。通过间接酶联免疫吸附测定(indirect-enzyme linked immunosorbent assay,间接ELISA)、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(sodium dodecylsulphate polyacrylamide gel electrophoresis,SDS-PAGE)和免疫印迹试验测定肌浆蛋白Ig G/Ig E结合能力的变化,并结合二级结构变化、表面疏水性变化和内源荧光值变化所反映的蛋白结构改变来分析其变化机理。结果表明,p H从4. 0升高到7. 0会小幅度降低肌浆蛋白Ig G/Ig E结合能力,二级结构中α-螺旋增加而不规则卷曲减少,表面疏水性大幅减小且色氨酸疏水基向极性环境暴露。离子强度从0增加到1. 0则不会对Ig G/Ig E结合能力产生显著影响。由此可知,肌浆蛋白Ig G/Ig E结合能力变化与其构象表位有关,初步判断主要由二级结构的改变引起,但仍需要进一步研究。Freshwater fish is the main source of protein for Chinese. The increased fish consumption correlates with increased hypersensitive reactions,which could reduce consumer’s living quality.The aim of this article was to evaluate the Ig G/Ig E binding capacity and structure of sarcoplasmic protein of black carp( Mylopharyngodon piceus) exposed to different p H and ion strength. The Ig G/Ig E binding capacity was determined by indirect ELISA,SDS-PAGE and western blotting. And protein structure was determined by secondary structure,surface hydrophobicity and intrinsic fluorescence intensity. The results showed that the Ig G/Ig E binding capacity of sarcoplasmic protein decreased slightly with p H shifting from 4. 0 to 7. 0,and along with the increased α-helix and decreased random coil in the secondary structure. The surface hydrophobicity decreased significantly and the tryptophan hydrophobic base was exposed to the polar environment. However,the increase of ion strength from 0 to 1. 0 had no significant impact on sensitization. The change of immunological properties of sarcoplasmic protein was related to its conformational epitopes,which was mainly caused by the change of secondary structure.

关 键 词：p H 离子强度 Ig G/Ig E结合能力 青鱼 蛋白结构 

分 类 号：TS254.1[轻工技术与工程—水产品加工及贮藏工程]