Subsite mapping of Aspergillus niger glucoamylases I and II with malto- and isomaltooligosaccharides

Glucoamylase, industrially derived from Aspergillus niger, was chromatographically separated into forms I and II and purified to near homogeneity. Preparations were proved to be free of D‐glucosyltransferase by electrophoretic and differential inhibition tests. Maximum rates and Michaelis constants...

Full description

Saved in:
Bibliographic Details
Published in:Biotechnology and bioengineering 1989-08, Vol.34 (5), p.681-688
Main Authors: Meagher, M.M. (University of Nebraska-Lincoln, Lincoln, NE), Nikolov, Z.L, Reilly, P.J
Format: Article
Language:English
Subjects:
active sites
ACTIVIDAD ENZIMATICA
ACTIVITE ENZYMATIQUE
Analytical, structural and metabolic biochemistry
ASPERGILLUS NIGER
BINDING SITE
Biological and medical sciences
Enzymes and enzyme inhibitors
ENZYMIC ACTIVITY
Fundamental and applied biological sciences. Psychology
GLUCAN 1,4-ALPHA-GLUCOSIDASE
GLUCOSA
GLUCOSE
Hydrolases
ISOENZIMAS
ISOENZYME
ISOENZYMES
KINETICS
OLIGOSACARIDOS
OLIGOSACCHARIDE
OLIGOSACCHARIDES
SEPARACION
SEPARATING
SEPARATION
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Glucoamylase, industrially derived from Aspergillus niger, was chromatographically separated into forms I and II and purified to near homogeneity. Preparations were proved to be free of D‐glucosyltransferase by electrophoretic and differential inhibition tests. Maximum rates and Michaelis constants were obtained for both glucoamylases I and II with maltooligosaccharides from maltose to maltoheptaose and with isomaltooligosac‐charides from isomaltose to isomaltohexaose. Subsite maps were calculated from these kinetic data and were not significantly different for the two forms. Subsites in both forms had lower affinities for D‐glucosyl residues contained in isomaltooligosaccharides than for D‐glucosyl residues in maltooligosaccharides.
ISSN:0006-3592
1097-0290
DOI:10.1002/bit.260340512