title: Kinetics of improved production and thermostability of an intracellular beta-glucosidase from a mutant-derivative of Cellulomonas biazotea.
abstract: The highest productivity (20 IU l(-1) h(-1)) of beta-glucosidase by a mutant of Cellulomonas biazotea was 2.5-fold more than that of the parent organism. The enzyme had a lower activation energy (57 kJ mol(-1)) than the native enzyme (68 kJ mol(-1)). The enzyme from the mutant had enthalpy and entropy values for irreversible intactivation of 95.6 kJ mol(-1) and 60 J.mol(-1) K(-1) compared with 108 kJ mol(-1) and 86 J mol(-1) K(-1) for the native enzyme suggesting that the mutation had stabilized the enzyme.
authors.affiliation: National Institute for Biotechnology and Genetic Engineering, PO. Box 577, Jhang Road, Faisalabad, Pakistan. mirajoka@nibge.org
authors.forename: M I
authors.initials: MI
authors.lastname: Rajoka
authors.forename: I S
authors.initials: IS
authors.lastname: Durrani
authors.forename: A M
authors.initials: AM
authors.lastname: Khalid
mesh_terms: D040143:Cellulomonas / Q000201:enzymology*; D019277:Entropy; D006358:Hot Temperature; D007700:Kinetics; D009154:Mutation; D013696:Temperature; D013816:Thermodynamics; D014508:Urea / Q000494:pharmacology; D001617:beta-Glucosidase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
chemical_list: D014508:Urea; D001617:beta-Glucosidase