Properties of two endoglucanases from a mutant strain Trichoderma sp. M7 |
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Authors: | SD Petrova NG Bakalova DN Kolev |
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Institution: | (1) Department of Biochemistry, Faculty of Biology, University of Sofia `St. Kliment Ohridski', 1164 Sofia, Bulgaria |
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Abstract: | Two endoglucanases (1,4- -d-glucan-4-glucanohydrolase, EC 3.2.1.4) were purified to electrophoretic homogeneity from the culture filtrate of a mutant strain Trichoderma sp. M7. The purified endoglucanases had Mr of 57.4 and 55 kDa, and estimated pI values of 4.1 and 3.95/3.75, respectively. Optimal activity for the first cellulase was at pH 4.5 and 50 °C, and at pH 5.5 and 60 °C for the other. Carbodiimide inactivated the one of the purified endoglucanases, while the other was inhibited by iodoacetamide, indicating the involvement of carboxylic or thiol groups in the catalysis. N-Bromsuccinimide strongly inhibited both endoglucanases, suggesting that tryptophan residues are essential for the activity and binding to the substrate. |
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Keywords: | cellulase cellulose biodegradation endoglucanase Trichoderma |
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