THERMOSTABILITY OF GLUCOAMYLASE IMMOBILIZED IN DIFFERENT WAYS HAS A CERTAIN LIMIT

被引：11

作者：

KLYOSOV, AA

GERASIMAS, VB

机构：

[1] Laboratory of Chemical Enzymology, Department of Chemistry, Moscow State University, Moscow

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1979年 / 571卷 / 01期

关键词：

Glucoamylase; Immobilized enzyme; Stability limit; Thermostability;

D O I：

10.1016/0005-2744(79)90237-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Thermostability of glucoamylase from Aspergillus niger is increased both by immobilization and substrate binding. However, the total superimposed stabilization effect at a given condition is apparently restricted by a certain limit which hardly depends on the mode of immobilization of the enzyme, and is determined mostly by the enzyme-substrate complex formation. © 1979.

引用

页码：162 / 165

页数：4