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Purification and characterization of an endochitinase produced by Colletotrichum gloeosporioides
The phytopathogenic fungus Colletotrichum gloeosporioides was analyzed for chitinase activity, the best production occurring at the fourth day. A 43 kDa endochitinase with specific activity of 413 U μg −1 protein was purified corresponding to a 75% yield. The optima of temperature and pH for the enz...
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Published in: | FEMS microbiology letters 2003-05, Vol.222 (1), p.45-50 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
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Summary: | The phytopathogenic fungus
Colletotrichum gloeosporioides was analyzed for chitinase activity, the best production occurring at the fourth day. A 43 kDa endochitinase with specific activity of 413 U μg
−1 protein was purified corresponding to a 75% yield. The optima of temperature and pH for the enzyme were 50°C and pH 7.0, respectively. The enzyme showed a high stability at 50°C and pH 7.0. Values of pH from 5.0 up to 7.0 gave, at least, 50% of maximum activity, suggesting a biotechnological application. Further studies are in progress to determine the possible use of this endochitinase in biological control. |
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ISSN: | 0378-1097 1574-6968 |
DOI: | 10.1016/S0378-1097(03)00220-9 |