QUANTITATIVE-DETERMINATION OF ALPHA-AMYLASE IN GLUCOAMYLASE PREPARATIONS

被引：7

作者：

MARSHALL, JJ

机构：

[1] UNIV MIAMI,SCH MED,DEPT BIOCHEM,MIAMI,FL 33152

[2] UNIV MIAMI,SCH MED,DEPT MED,MIAMI,FL 33152

来源：

ANALYTICAL BIOCHEMISTRY | 1978年 / 85卷 / 02期

关键词：

D O I：

10.1016/0003-2697(78)90252-X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The use of modified starch substrates for the measurement of α-amylase activity is described. In the presence of excess glucoamylase, the amount of glucose released from substrates containing blockages to exo-enzyme action is proportional to the amount of α-amylase present. The levels of α-amylase in a number of commercial glucoamylase preparations have been determined by this method. The importance of α-amylase in achieving efficient conversion of starch into glucose is illustrated by a comparison of the time courses of degradation of amylopectin by glucoamylase preparations containing low and high levels of α-amylase. © 1978.

引用

页码：541 / 549

页数：9

共 14 条

[1] 2 FORMS OF GLUCOAMYLASE OF ASPERGILLUS NIGER [J].