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Plant and Cell Physiology, 2003, Vol. 44, No. 11 1162-1167
© 2003 Oxford University Press

Purification and Characterization of an Antifungal Chitinase in Jelly Fig (Ficus awkeotsang) Achenes

Yu-Ching Li1,2, Chen-Tien Chang3, Eric S. L. Hsiao1, Joyce S. F. Hsu1, Jenn-Wen Huang4 and Jason T. C. Tzen1,5

1 Graduate Institute of Biotechnology, National Chung-Hsing University, Taichung, Taiwan 40227 ROC
2 Department of Medical Technology, Chungtai Institute of Health Sciences and Technology, Taichung, Taiwan 400 ROC
3 Department of Food and Nutrition, Providence University, Shalu, Taiwan ROC
4 Department of Plant Pathology, National Chung-Hsing University, Taichung, Taiwan 40227 ROC

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 Km, kcat, optimal pH and temperature of this putative chitinase were determined to be 0.076 mM, 0.089 s–1, pH 4, and 60°C, respectively. The purified 30-kDa protein was thermostable (retaining activity up to 65°C for several hours) and could be stored at 4°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.

5 Corresponding author: E-mail, TCTZEN{at}dragon.nchu.edu.tw; Fax, +886-4-22853527.


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