10组织蛋白酶L及其酶学特性研究.pdfVIP

ofHefei 备肥学院学报(自然科学版) Journal University(NaturalSciences) 组织蛋白酶L及其酶学特性研究 胡庆国1，张进杰2，纪 蓉2，顾伟钢2 (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) 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．由琼脂耱凝胶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(L曲)的活性，结果表明L出的热稳定性与pH和温度密切相关，其最适pH为5．O，最适温度 为45℃．在最适pH5．0时，L出的活性随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，L。；。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 中图分类号：Q814 文献标识码：A 文章编号：1673—162X(2010)03—0066—06 on LandIts Studies Cathepsin HU Qing．gu01，ZHANGJin-jie2，JIRon92，GUWei．gan92 of andEnvironmental (1．DepartmentBiological Engineering，HefeiUniversity，Hefei230022； ofFoodScienceand University，Hangzhou310029，China) 2．Department En百neering，Zhejiang Lcouldnotberemoved conventional extractionand Abstract：Cathepsin completelyduring actomyosin stillremainedinthe ofred 6B filtration showedthat actomyosinbulleyesurimi．Sepharosegel profile themain of Lwas fromthatof the Wasnon— peakcathepsinseparated actomyosinsuggestingenzyme of in and 5．0andthe to L was bindingactomyosin．OptimalpH cathepsinactomyosinL。i1 optimal of Was of relatedto and temperatureL田ix 45。C．StabilityL晌Wasclosely temperaturepH．Atoptimal of increasedwiththeincreaseofNaClconcentration．Studiesofsubstrate pI-15．0，activityL。iI tobea andeffectsofactivatorsandinhibitorsconfirmed specificity