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

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

Volume: 10 Issue: 6

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

Affiliation:

Keywords: cellulomonas biazotea, derepressed mutant, endo-glucanase enthalpy, enzyme kinetics, melting point, thermodynamics

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.

Cite this article as:

Rajoka I. M., Ashraf Yasmin, Rashid Hamid and Khalid M. A., Kinetics and thermodynamics of the Native and Mutated Extracellular Endoglucanases From Cellulomonas Biazotea, Protein & Peptide Letters 2003; 10 (6) . https://dx.doi.org/10.2174/0929866033478609