摘要
对鲤鱼鱼背部白肌中的组织蛋白酶L进行分离纯化并研究了其酶学性质。结果发现,鲤鱼组织蛋白酶L提取液经酸处理、硫酸铵分级沉淀、DEAE-Sepharose F.F.离子交换层析和SephacrylS-100凝胶过滤层析等步骤后得到部分纯化,纯化倍数为16.39。鲤鱼组织蛋白酶L的最适反应温度和pH值分别为40℃和5.0,在20～50℃和pH 4.5～5.5范围内具有较好的稳定性。
Cathepsin L from Carp Cyprinus carpio muscle was isolated through a serious of procedures including acidification,ammonium sulfate fractionation,DEAE-Sepharose F.F.chromatography and Sephacryl S-100 chromatography,and the enzymatic characterization was also studied.The results showed that cathepsin L was partially purified to 16.39 folds.The optimum temperature and pH of the purified enzyme were 5.0 ℃ and 40 ℃,respectively.It was stable between 20～50 ℃ and within a pH range of 4.5～5.5.
出处
《食品科技》
CAS
北大核心
2011年第2期9-12,共4页
Food Science and Technology
基金
国家863项目(2007AA09Z442)
浙江省自然科技基金项目(Y307132)
关键词
鲤鱼
组织蛋白酶L
分离纯化
酶学性质
Carp Cyprinus carpio
Cathepsin L
isolation
characterization
