Purification and N-terminal sequencing of a 42 kDa Trichoderma viride chitinase isoform effective against Rhizoctonia solani
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Authors
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R. STEPHEN JEBAKUMAR*, GILU LIZY GEORGE, S. BABU*, T. RAGHUCHANDER, G. GOPALASWAY P. VIDHYASEKARAN, R. SAMIYAPPAN, J.A.J. RAJA and P. BALASUBRAMANIAN
Centre for Plant. Molecular Biology and *Department of Plant Pathology, Centre for Plant Protection Studies, Tamil Nadu
Agricultural University, Coimbatore 641 003
Keywords:
Biological control, Trichoderma viride, rice, Rhizoctonia solani, chitinases, mycoparasitsmAbstract
Trichoderma viride extracellular chitinase of molecular weight 42 kDa was purified and its N-terminal sequence was determined. An N-terminal sequence comparison revealed 70-100% similarity to those of already characterised chitinases of similar molecular weight from other fungi. A chitin affinity column fraction that contained the enriched 42 kDa chitinase showed a higher chitinase specific activity. The 42 kDa chitinase purified to homogeneity by electroelution inhibited in vitro the growth of a rice sheath blight isolate of Rhizoctonia solani.
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