Abstract
The chitinolytic system of Trichoderma sp. is complex with several types of chitinase working together simultaneously to enhance its mycoparasitism. However, chitinase enzyme has not been studied extensively for Trichoderma longibrachiatum although it has been proven to have significant effect as biocontrol. This study was conducted in the interest to purify chitinase 33kDA from T. longibrachiatum T28 and also to assess chit33 expression patterns. Chitinase activity was determined and the peak of chitinase activity was observed at 36 hours. Chitinase enzyme from the culture filtrate of T. longibrachiatum was precipitated with 80% acetone followed by anion- exchange chromatography using Neobar AQ. Only one chitinase band at 33kDa in size has been detected and analysis of Southern Blotting has confirmed the present of at least a single copy of chitinase 33kDA gene (chit33) for T. longibrachiatum strain T28. Assessment of chit33 expression showed that the expression was strongly affected by substrate specificity; where
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