PURIFICATION AND CHARACTERIZATION OF A THERMOSTABLE GLUCOAMYLASE FROM A MYROTHECIUM ISOLATE

被引：8

作者：

ALI, S ^{[1
]}

MALEK, S ^{[1
]}

HOSSAIN, Z ^{[1
]}

机构：

[1] UNIV DHAKA, DEPT BIOCHEM, DHAKA, BANGLADESH

来源：

JOURNAL OF APPLIED BACTERIOLOGY | 1994年 / 76卷 / 03期

关键词：

D O I：

10.1111/j.1365-2672.1994.tb01618.x

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

TWO glucoamylases, glue I and glue II, were purified to homogeneity from the culture filtrate of a Myrothecium strain M1 by chromatography on DEAE-cellulose and concanavalin A-sepharose. Molecular masses deduced by SDS-PAGE were 72 000 +/- 2500 for glue I and 96 000 +/- 4000 for glue II. The temperature optima of the enzymes were both about 70 degrees C and their pH optima were around 4.0. Both enzymes were glycoprotein and preferentially hydrolysed high molecular mass substrate. Hg2+ was a potent inhibitor of both glucoamylases. Glue II had higher debranching activity than glue I.

引用

页码：210 / 215

页数：6

共 26 条

[1] CHARACTERISTICS OF GLUCOAMYLASE FROM ASPERGILLUS-TERREUS [J].