PURIFICATION, CHARACTERIZATION, AND ANTIFUNGAL ACTIVITY OF CHITINASE FROM FUSARIUM-CHLAMYDOSPORUM, A MYCOPARASITE TO GROUNDNUT RUST, PUCCINIA-ARACHIDIS

Chitinase (EC 3.2.1.14) was isolated from the culture filtrate of Fusa rium chlamydosporum and purified by ion-exchange chromatography and ge l filtration. The molecular mass of purified chitinase was 40 kDa as e stimated by sodium dodecyl sulfate - polyacrylamide gel electrophoresi s. Chitinase was optimally active at a pH of 5 and stable from pH 4 to 6 and up to 40 degrees C. Among the metals and inhibitors tested, mer curic chloride completely inhibited the enzyme activity. The activity of chitinase was high on colloidal and pure chitin. The purified chiti nase inhibited the germination of uredospores of Puccinia arachidis an d also lysed the walls of uredospores and germ tubes. The results from these experiments indicated that chitinase of F. chlamydosporum plays and important role in the biocontrol of groundnut rust.