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
收藏
页码：144 / 146
页数：3
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