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

Authors: Rajoka, M. I.; Ashraf, Yasmin; Rashid, Hamid; Khalid, A. M.

Source: Protein and Peptide Letters, Volume 10, Number 6, December 2003 , pp. 561-568(8)

Publisher: Bentham Science Publishers

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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

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866033478609

Affiliations: National Institute for Biotechnology and Genetic Engineering, P.O. Box 577, Jhang Road, Faisalabad, Pakistan.

Publication date: December 1, 2003

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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