Abstract
Microbial degradation of cellulose has economic potential in enzyme industry as well as for the production of biofuels from plant biomass. In this study bacteria were isolated from soil sample of Leh region and screened for different hydrolases. The strain Bacillus SL4 was found as potent producer of cellulase. The enzyme from Bacillus SL4 was purified by ion exchange chromatography and characterized. The molecular weight of enzyme was 82kDa. Enzyme showed an optimum activity at pH 6.0 and highly stable between 55-65 °C. The crude cellulase had activity toward CMC, avicell, β- glucan and cellobiose, but there was no detectable activity on xylan and p-nitrophenyl-β-d-glucopyranoside (PNPG). The rate of CMC degradation was higher than any other substrates used in this study. The enzyme reported in this paper was able to hydrolyze both -β-1, 4 and β-1,3 glycosidic linkages and thermostable at high temperature.
Keywords: Cellulases, leh soil, CMCase, hydrolase, thermostable.
Current Biotechnology
Title:Purification and Characterization of Thermostable Cellulase from Soil Bacteria of Northwestern Himalayas
Volume: 2 Issue: 2
Author(s): Sarika Sharma, Kuldeep Kaur, Vikas Sharma and Sandeep Shama
Affiliation:
Keywords: Cellulases, leh soil, CMCase, hydrolase, thermostable.
Abstract: Microbial degradation of cellulose has economic potential in enzyme industry as well as for the production of biofuels from plant biomass. In this study bacteria were isolated from soil sample of Leh region and screened for different hydrolases. The strain Bacillus SL4 was found as potent producer of cellulase. The enzyme from Bacillus SL4 was purified by ion exchange chromatography and characterized. The molecular weight of enzyme was 82kDa. Enzyme showed an optimum activity at pH 6.0 and highly stable between 55-65 °C. The crude cellulase had activity toward CMC, avicell, β- glucan and cellobiose, but there was no detectable activity on xylan and p-nitrophenyl-β-d-glucopyranoside (PNPG). The rate of CMC degradation was higher than any other substrates used in this study. The enzyme reported in this paper was able to hydrolyze both -β-1, 4 and β-1,3 glycosidic linkages and thermostable at high temperature.
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Cite this article as:
Sharma Sarika, Kaur Kuldeep, Sharma Vikas and Shama Sandeep, Purification and Characterization of Thermostable Cellulase from Soil Bacteria of Northwestern Himalayas, Current Biotechnology 2013; 2 (2) . https://dx.doi.org/10.2174/22115501113029990010
DOI https://dx.doi.org/10.2174/22115501113029990010 |
Print ISSN 2211-5501 |
Publisher Name Bentham Science Publisher |
Online ISSN 2211-551X |
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