Kinetic studies of the native and mutated intracellular beta-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 beta-glucosidase from mutant 51 SM(r) 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.
Rajoka
M I
MI
National Institute for Biotechnology and Genetic Engineering, P.O. Box 577, Jhang Road, Faisalabad, Pakistan. mirajoka@nibge.org
Durrani
I S
IS
Khalid
A M
AM
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D040143:Cellulomonas / Q000201:enzymology*; D004795:Enzyme Stability; D005947:Glucose / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D009154:Mutation; D013696:Temperature; D013816:Thermodynamics; D001617:beta-Glucosidase / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D001617:beta-Glucosidase; D005947:Glucose