Kinetics of improved production and thermostability of an intracellular beta-glucosidase from a mutant-derivative of Cellulomonas biazotea.
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.
Rajoka
M I
MI
National Institute for Biotechnology and Genetic Engineering, PO. Box 577, Jhang Road, Faisalabad, Pakistan. mirajoka@nibge.org
Durrani
I S
IS
Khalid
A M
AM
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
D014508:Urea; D001617:beta-Glucosidase