CHARACTERISTICS OF GLUCOAMYLASE FROM ASPERGILLUS-TERREUS

被引：18

作者：

ALI, S

HOSSAIN, Z

机构：

[1] Department of Biochemistry, University of Dhaka

来源：

JOURNAL OF APPLIED BACTERIOLOGY | 1991年 / 71卷 / 02期

关键词：

D O I：

10.1111/j.1365-2672.1991.tb02970.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：

Glucose was the only product of starch hydrolysis liberated by glucoamylase. The enzyme was a glycoprotein with an isoelectric point at pH 3.4 and was optimally active at pH 4.0 and 60-degrees-C. It was remarkably stable over a wide range of pH and at elevated temperatures. Divalent Mg2+ and Ca2+ slightly stimulated glucoamylase activity. The enzyme exhibited specificity for substrates containing alpha(1 --> 4) glucosidic linkages and the Km for starch hydrolysis was 4.0 g/l.

引用

页码：144 / 146

页数：3

共 15 条

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ALI, S ;

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[2] INDUCTION OF GLUCOAMYLASE PRODUCTION BY NON-STARCHY CARBOHYDRATES IN ASPERGILLUS-TERREUS [J].

ALI, S ;

HOSSAIN, Z ;

MAHMOOD, S ;

ALAM, R .

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