薄荷幼叶蔗糖酶的分离纯化与部分性质  

Isolation and Purification of Invertase from Mentha haplocalyx Briq and Some Its Properties

作　　者：郭小路[1] 张万秋[2] 阙瑞琦[1] 邱慧[1] 唐云明[1] 

机构地区：[1]西南大学生命科学院,重庆400715 [2]成都中医药大学峨眉学院,四川峨眉山614201

出　　处：《西南大学学报（自然科学版）》2008年第2期90-94,共5页Journal of Southwest University(Natural Science Edition)

基　　金：重庆市科委资助项目(CSTC,2004AC1012)

摘　　要：经10 KD的膜超滤,DEAE-Sepharose离子交换柱层析,Sephacryl S-200凝胶过滤纯化,从薄荷(MenthahaplocalyxBriq)幼叶中分离纯化出电泳纯的转化酶,该酶提纯倍数为186.3倍,比活力为67.06 U/mg.酶学性质和动力学性质研究表明:该酶不可逆催化蔗糖生成果糖和葡萄糖,最适pH值为5.0,最适温度为55℃,米氏常数Km值为12.25 mmol/L.Electrophoretically pure invertase was isolated and purified from the young leaves of Mentha haplocalyx Briq by 10 KD membrane ultrafiltration, ion exchange chromatography on DEAE-Sepharose Fast Flow column and gel filtration chromatography on Sephacryl S-200. The preparation was shown to be homogenous on polyacrylamide gel electrophoresis. Its specific activity was 67.06 unit/mg protein and its molecular weight was 130KD. The optimum pH and optimum temperature for the enzyme to catalyze the hydrolysis of sucrose were 5.0 and 55 ℃, respectively. Its Michaelis constant （Km） was determined to be 12.25 mmol/L.

关 键 词：薄荷 蔗糖酶 分离纯化 

分 类 号：Q814[生物学—生物工程]