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Abstract

PURIFICATION AND CHARACTERIZATION OF CHITINASE FROM TRICHODERMA VIRIDE N9 AND ITS ANTIFUNGAL ACTIVITY AGAINST PHYTOPATHOGENIC FUNGI

Dr. S. Jenifer*, J.Jeyasree, D. Kezia Laveena and K.Manikandan

ABSTRACT

A chitinase produced by Trichoderma viride N9 isolated from a soil sample collected from Nallamala forest, India, was purified and characterized. The enzyme was purified by ammonium sulphate precipitation, DEAE-cellulose ion-exchange chromatography and sephadex G-100 gel filtration. The molecular mass of the purified chitinase was estimated to be 46 kDa by SDS-PAGE. It was optimally active at pH of 4 and at 40°C. The enzyme was stable from pH 3 to 6, and up to 50°C. Among the metals that were tested, the Fe2+, Hg2+, Mn2+ and Co2+ completely inhibited the enzyme activity. The enzyme was less sensitive to Al3+, Ca2+, Cu2+, and Zn2+. The purified chitinase showed antifungal activity against phytopathogenic fungi

Keywords: Chitinase, Trichoderma viride, ion-exchange chromatography, Nallamala forest.


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