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Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Kinetics and thermodynamics of the Native and Mutated Extracellular Endoglucanases From Cellulomonas Biazotea

Author(s): M. I. Rajoka, Yasmin Ashraf, Hamid Rashid and A. M. Khalid

Volume 10, Issue 6, 2003

Page: [561 - 568] Pages: 8

DOI: 10.2174/0929866033478609

Price: $65

Abstract

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


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