Purification and characterization of an antifungal chitinase in jelly fig (Ficus awkeotsang) achenes.
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(m), k(cat), optimal pH and temperature of this putative chitinase were determined to be 0.076 mM, 0.089 s(-1), pH 4, and 60 degrees C, respectively. The purified 30-kDa protein was thermostable (retaining activity up to 65 degrees C for several hours) and could be stored at 4 degrees 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.[1]References
- Purification and characterization of an antifungal chitinase in jelly fig (Ficus awkeotsang) achenes. Li, Y.C., Chang, C.T., Hsiao, E.S., Hsu, J.S., Huang, J.W., Tzen, J.T. Plant Cell Physiol. (2003) [Pubmed]
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