Kinetic Studies of the Native and Mutated Intracellular ß-Glucosidases from Cellulomonas biazotea
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.
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Document Type: Review Article
Affiliations: National Institute for Biotechnology and Genetic Engineering, P.O. Box 577, Jhang Road, Faisalabad, Pakistan.
Publication date: 01 April 2005
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