A highly thermostable, alkaline CMCase produced by a newly isolated Bacillus sp VG1

An extracellular, highly thermostable and alkaline CMCase was purified from Bacillus sp. VG1 using ion exchange and gel filtration chromatography. Enzyme was optimally produced in a medium containing 1.0% CMC and 0.5% tryptone. The purified CMCase had a pH optimum of 9-10 and a half life of 12 min even at 100 degreesC. The enzyme activity was reduced by Hg2+ and stimulated by Co2+, Na+ and K+. Various detergents and proteinases moderately inhibited the CMCase activity. The molecular weight studies showed a single band on SDS-PAGE.