Kinetic Studies of the Native and Mutated Intracellular ß-Glucosidases from Cellulomonas biazotea

Title: Kinetic Studies of the Native and Mutated Intracellular ß-Glucosidases from Cellulomonas biazotea

Volume: 12 Issue: 3

Author(s): M. I. Rajoka, I. S. Durrani and A. M. Khalid

Affiliation:

Keywords: cellulomonas biazotea, derepressed mutant, glucosidase, enzyme kinetics, thermodynamics

Abstract: The mutation, conferring streptomycin and deoxyglucose resistance on cells, had profound effect on the kinetic and thermodynamic parameters inferring thermostabilization of ß-glucosidase from mutant 51 SMr of Cellulomonas biazotea. Free energy of activation for substrate binding, enthalpy and entropy of activation for irreversible denaturation of mutant-derived enzyme were decreased compared with enzyme from wild organism suggesting that the mutation partly stabilized the enzyme and that mutation made it more reactive.

Cite this article as:

Rajoka I. M., Durrani S. I. and Khalid M. A., Kinetic Studies of the Native and Mutated Intracellular ß-Glucosidases from Cellulomonas biazotea, Protein & Peptide Letters 2005; 12 (3) . https://dx.doi.org/10.2174/0929866053587183