Journal Article

Purification and Characterization of an Antifungal Chitinase in Jelly Fig (<i>Ficus awkeotsang</i>) Achenes

Yu-Ching Li, Chen-Tien Chang, Eric S. L. Hsiao, Joyce S. F. Hsu, Jenn-Wen Huang and Jason T. C. Tzen

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 44, issue 11, pages 1162-1167
Published in print November 2003 | ISSN: 0032-0781
Published online November 2003 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcg141
Purification and Characterization of an Antifungal Chitinase in Jelly Fig (Ficus awkeotsang) Achenes

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  • Biochemistry
  • Molecular and Cell Biology
  • Plant Sciences and Forestry

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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.

Keywords: Keywords: Achene — Antifungal — Chitinase — Jelly fig — Pericarp.; Abbreviations: pI, isoelectric point; 4-MU-β-(GlcNAc)3, 4-methylumbelliferyll β-d-N,N′N′′-triacetylchitotrioside.

Journal Article.  4035 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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