title: Kinetic and thermodynamic properties of an immobilized glucoamylase from a mesophilic fungus, Arachniotus citrinus.
abstract: 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.
authors.affiliation: 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
authors.forename: Raheela
authors.initials: R
authors.lastname: Perveen
authors.forename: Muhammad Hamid
authors.initials: MH
authors.lastname: Rashid
authors.forename: Muhammad
authors.initials: M
authors.lastname: Saleem
authors.forename: Ahmad Mukhtar
authors.initials: AM
authors.lastname: Khalid
authors.forename: Muhammad Ibrahim
authors.initials: MI
authors.lastname: Rajoka
mesh_terms: D001203:Ascomycota / Q000201:enzymology*; D004800:Enzymes, Immobilized; D005087:Glucan 1,4-alpha-Glucosidase / Q000502:physiology*; D007700:Kinetics; D013816:Thermodynamics
chemical_list: D004800:Enzymes, Immobilized; D005087:Glucan 1,4-alpha-Glucosidase