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组织蛋白酶L及其酶学特性研究
引用本文:胡庆国,张进杰,纪蓉,顾伟钢.组织蛋白酶L及其酶学特性研究[J].合肥学院学报(自然科学版),2010,20(3):66-71.
作者姓名:胡庆国  张进杰  纪蓉  顾伟钢
作者单位:1. 合肥学院,生物与环境工程系,合肥,230022
2. 浙江大学,食品与营养系,杭州,310029
基金项目:国家自然科学基金,中央高校基本科研业务费专项资金 
摘    要:组织蛋白酶L很难通过常规的肌动球蛋白提取方法完全去除.由琼脂糖凝胶6B凝胶层析图谱显示,组织蛋白酶L的活性主峰明显偏离肌动球蛋白主峰,表明该酶是肌动球蛋白非结合型酶.凝胶柱层析后测定L型组织蛋白酶粗酶液(Lmix)的活性,结果表明Lmix的热稳定性与pH和温度密切相关,其最适pH为5.0,最适温度为45℃.在最适pH5.0时,Lmix的活性随NaCl浓度的增加而增大.专一性底物及酶激活剂、抑制剂影响研究表明,Lmix为内含巯基的半胱氨酸型组织蛋白酶.

关 键 词:鱼糜  组织蛋白酶L  琼脂糖凝胶6B  半胱氨酸蛋白酶

Studies on Cathepsin L and Its Characterization
HU Qing-guo,ZHANG Jin-jie,JI Rong,GU Wei-gang.Studies on Cathepsin L and Its Characterization[J].Journal of Hefei University :Natural Sciences,2010,20(3):66-71.
Authors:HU Qing-guo  ZHANG Jin-jie  JI Rong  GU Wei-gang
Institution:1.Department of Biological and Environmental Engineering,Hefei University,Hefei 230022;2.Department of Food Science and Engineering,Zhejiang University,Hangzhou 310029,China)
Abstract:Cathepsin L could not be removed completely during conventional actomyosin extraction and still remained in the actomyosin of red bulleye surimi.Sepharose 6B gel filtration profile showed that the main peak of cathepsin L was separated from that of actomyosin suggesting the enzyme was non-binding to actomyosin.Optimal pH of cathepsin L in actomyosin and Lmix was 5.0 and the optimal temperature of Lmix was 45℃.Stability of Lmix was closely related to temperature and pH.At optimal pH5.0,activity of Lmix increased with the increase of NaCl concentration.Studies of substrate specificity and effects of activators and inhibitors confirmed Lmix to be a thiol-type cysteine protease.
Keywords:Red bulleye surimi  cathepsin L  sepharose 6B  cysteine protease
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