Purification and characterization of two distinct carboxymethylcellulases of Paecilomyces sp
Two distinct forms of carboxymethylcellulase (CMCases) were produced by Paecilomyces sp. in a medium containing 5% (w/v) rice hull as the carbon source. CMCases I and II were purified 13·2- and 127·3-fold, respectively, by acetone precipitation, ion-exchange chromatography on DEAE-Sephadex A-50 and...
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Published in | Bioresource technology Vol. 66; no. 3; pp. 231 - 234 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Oxford
Elsevier Ltd
01.12.1998
Elsevier Science |
Subjects | |
Online Access | Get full text |
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Summary: | Two distinct forms of carboxymethylcellulase (CMCases) were produced by
Paecilomyces sp. in a medium containing 5% (w/v) rice hull as the carbon source. CMCases I and II were purified 13·2- and 127·3-fold, respectively, by acetone precipitation, ion-exchange chromatography on DEAE-Sephadex A-50 and gel filtration on Sephadex G-200. Both enzymes were optimally active at 60°C and retained 100% of their original activity at 50°C for 2 h. They were also maximally active at pH 4·0 and stable between pH 4 and 5. CMCase I was activated by Ca
2+, while CMCase II was activated by Ba
2+. Both enzymes were, however, totally inhibited by Zn
2+, Hg
2+, glycine and EDTA. CMCase I and II had
K
m values of 1·42 and 0·91%, respectively, for carboxy-methylcellulose. The relative molecular weights were 55 and 42 KDa for CMCases I and II, respectively. |
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ISSN: | 0960-8524 1873-2976 |
DOI: | 10.1016/S0960-8524(98)00053-4 |