A highly thermostable, alkaline CMCase produced by a newly isolated Bacillus sp. VG1
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- Singh, J., Batra, N. & Sobti, R. World Journal of Microbiology and Biotechnology (2001) 17: 761. doi:10.1023/A:1013564717107
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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 °C. 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.