Stability of alpha-amylase with immobilization through its different functional groups

The paper deals with stability of Aspergillus aryzae alpha-amylase immobilized on CM- and AE-celluloses using N,N'-dicyclohexylcarbodiimide by means of binding through its amine or carboxylic groups. The binding of the enzyme with CM-cellulose makes its preparations more stable to the effect of...

Full description

Saved in:
Bibliographic Details
Published inUkrainskij biohimičeskij žurnal Vol. 51; no. 2; p. 154
Main Authors Kolesnik, L A, Galich, I P
Format Journal Article
LanguageRussian
Published Ukraine 01.03.1979
Subjects
alpha-Amylases - metabolism
Amylases - metabolism
Aspergillus oryzae - enzymology
Drug Stability
Enzymes, Immobilized - metabolism
Hydrogen-Ion Concentration
Kinetics
Temperature
Online AccessGet more information

Cover

More Information
Summary:The paper deals with stability of Aspergillus aryzae alpha-amylase immobilized on CM- and AE-celluloses using N,N'-dicyclohexylcarbodiimide by means of binding through its amine or carboxylic groups. The binding of the enzyme with CM-cellulose makes its preparations more stable to the effect of EDTA and elevated temperature (50 degrees C) than under fixation on AE-cellulose.
ISSN:0201-8470