Kinetics and thermodynamics of the Native and Mutated Extracellular Endoglucanases From Cellulomonas Biazotea
The mutation had dramatic effect on the kinetic and thermodynamic parameters inferring thermostability of endo-glucanase from Cellulomonas biazotea mutant 51 SMr .The denaturation activation energies of native and mutated enzymes were 73.3 and 68.8 kJ / mol respectively. They showed compensation effect at 55°C. Both enthalpy and entropy values of irreversible thermal inactivation for mutated enzyme were decreased suggesting that the mutation partly stabilized the enzyme.
Keywords: cellulomonas biazotea; derepressed mutant; endo-glucanase enthalpy; enzyme kinetics; melting point; thermodynamics
Document Type: Review Article
Affiliations: National Institute for Biotechnology and Genetic Engineering, P.O. Box 577, Jhang Road, Faisalabad, Pakistan.
Publication date: 01 December 2003
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