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|標題:||Purification and characterization of an antifungal chitinase in jelly fig (Ficus awkeotsang) achenes||作者:||Li, Y.C.
|關鍵字:||achene;antifungal;chitinase;jelly fig;pericarp;acidic pectin methylesterase;ripening tomato fruits;expression;cloning;proteins||Project:||Plant and Cell Physiology||期刊/報告no：:||Plant and Cell Physiology, Volume 44, Issue 11, Page(s) 1162-1167.||摘要:||
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 60degreesC, respectively. The purified 30-kDa protein was thermostable (retaining activity up to 65degreesC for several hours) and could be stored at 4degreesC 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.
|Appears in Collections:||生物科技學研究所|
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