Isolation, purification and characterization of carboxymethyl cellulase (CMCase) from endophytic Fusarium oxysporum producing podophyllotoxin

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DOI: 10.4236/aer.2013.14010    5,977 Downloads   12,545 Views  Citations

ABSTRACT

Endophytic fungus Fusarium oxysporum is a rich source of cellulases. In the present study, the highest activity was reported at 28 ° C, pH 5.6 with 2% Carboxymethyl cellulose (CMC) as carbon source. CMC was purified using Sephadex G and DEAE cellulose chromatography to 15.9 folds and the molecular weight was determined to be 84 kDa by SDS-PAGE analysis and was subsequently characterized. The purified enzyme was stable over the pH range from 4.0 to 8.0 and at temperatures below 50 ° C. The enzyme was highly active on CMC and reduced or no activity on Avicel, cellobiose and it was suggested to be CMCase/endoglucanase. The activity of endoglucanase was enhanced in the presence of MgCl2, CoCl2, FeCl3, CaCl2, FeCl2 and intensive to HgCl2. The purified enzyme showed its optimum activity at pH 5.0 - 6.0 and was quite stable at 50 ° C for 30 min and retained 45% of original activity.

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Dar, R. , Saba, I. , Shahnawaz, M. , Sangale, M. , Ade, A. , Rather, S. and Qazi, P. (2013) Isolation, purification and characterization of carboxymethyl cellulase (CMCase) from endophytic Fusarium oxysporum producing podophyllotoxin. Advances in Enzyme Research, 1, 91-96. doi: 10.4236/aer.2013.14010.

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