Purification and characterization of an antifungal chitinase in jelly fig (Ficus awkeotsang) achenes
2003
Li, Y.C. (National Chung Hsing Univ., Taichung (Taiwan)) | Chang, C.T. | Hsiao, E.S.L. | Hsu, J.S.F. | Huang, J.W. | Tzen, J.T.C.
A method was developed to purify a 30-kDa protein from jelly fig (Ficus awkeotsang) pericarp, including preparation of jelly curd from achenes, extraction of proteins from the curd, and isolation of the 30-kDa protein by anion-exchanger and gel filtration. Chitinase activity was detected in the purified 30-kDa protein by activity staining in both non-denaturing gel electrophoresis and SDS-PAGE. Isoelectrofocusing showed that the isoelectric point of the 30-kDa protein was lower than pH 3.5. The K sub (m), k sub (cat), optimal pH and temperature of this putative chitinase were determined to be 0.076 mM, 0.089 s sup (-1), pH 4, and 60 deg C, respectively. The purified 30-kDa protein was thermostable (retaining activity up to 65 deg C for several hours) and could be stored at 4 deg C for a year without apparent loss of chitinase activity. Antifungal activity of this putative chitinase was measured in terms of inhibition of Colletotrichum gloeosporioides spore germination.
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