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 glucoamylase indicated that immobilization decreased the entropy and enthalpy of deactivation by magnitudes and made the immobilized glucoamylase thermodynamically more stable.
Perveen
Raheela
R
Industrial Biotechnology Division, National Institute for Biotechnology and Genetic Engineering, P.O. Box 577, Jhang Road, Faisalabad, Pakistan. raheela@nibge.org; raheela_ibd@yahoo.com
Rashid
Muhammad Hamid
MH
Saleem
Muhammad
M
Khalid
Ahmad Mukhtar
AM
Rajoka
Muhammad Ibrahim
MI
D001203:Ascomycota / Q000201:enzymology*; D004800:Enzymes, Immobilized; D005087:Glucan 1,4-alpha-Glucosidase / Q000502:physiology*; D007700:Kinetics; D013816:Thermodynamics
D004800:Enzymes, Immobilized; D005087:Glucan 1,4-alpha-Glucosidase