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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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Bibliographic Details
Published in:FEMS microbiology letters 2003-05, Vol.222 (1), p.45-50
Main Authors: Souza, R.F., Gomes, R.C., Coelho, R.R.R., Alviano, C.S., Soares, R.M.A.
Format: Article
Language:English
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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.
ISSN:0378-1097
1574-6968
DOI:10.1016/S0378-1097(03)00220-9