Kinetic and thermodynamic properties of an immobilized glucoamylase from a mesophilic fungus, Arachniotus citrinus

Purified glucoamylase from Arachniotus citrinus was immobilized on polyacrylamide gel with 70% yield of immobilization. The immobilization improved the pH optima, temperature optima, values of K(m), V(max), and activation energy. Irreversible thermal denaturation studies of soluble and immobilized g...

Full description

Saved in:
Bibliographic Details
Published inProtein and peptide letters Vol. 13; no. 7; p. 665
Main Authors Perveen, Raheela, Rashid, Muhammad Hamid, Saleem, Muhammad, Khalid, Ahmad Mukhtar, Rajoka, Muhammad Ibrahim
Format Journal Article
LanguageEnglish
Published Netherlands 01.01.2006
Subjects
Ascomycota - enzymology
Enzymes, Immobilized
Glucan 1,4-alpha-Glucosidase - physiology
Kinetics
Thermodynamics
Online AccessGet more information

Cover

More Information
Summary:Purified glucoamylase from Arachniotus citrinus was immobilized on polyacrylamide gel with 70% yield of immobilization. The immobilization improved the pH optima, temperature optima, values of K(m), V(max), and activation energy. Irreversible thermal denaturation studies of soluble and immobilized glucoamylase indicated that immobilization decreased the entropy and enthalpy of deactivation by magnitudes and made the immobilized glucoamylase thermodynamically more stable.
ISSN:0929-8665
DOI:10.2174/092986606777790539