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Purification and Modes of Antifungal Action by Vicia faba cv. Egypt Trypsin Inhibitor
Faculty
Agriculture
Year:
2010
Type of Publication:
Article
Pages:
10729-10735
Authors:
Fang, Evandro Fei, Hassanien, Abdallah Abd Elazeem, Wong, Jack Ho, Bah, Clara Shui Fern, Soliman, Saeed Saad, Ng, Tzi Bun
DOI:
10.1021/jf102277k
Journal:
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY AMER CHEMICAL SOC
Volume:
58
Research Area:
Agriculture; Chemistry; Food Science \& Technology
ISSN
ISI:000282545000059
Keywords :
Protease inhibitor, Vicia faba, innate immunity, antifungal protein, Valsa mali
Abstract:
A new 15 kDa Bowman Birk type trypsin inhibitor (termed VFTI-E1) from lava beans ( Vicia faba cv. Egypt 1) was isolated using liquid chromatography. Though it exhibited substantial homology in N-terminal amino acid sequence to other protease inhibitors, VFTI-E1 showed antiproteolytic activity against trypsin (K(i) 11.9 x 10(-9) M) but hardly any activity against chymotrypsin. It demonstrated antifungal activity toward the filamentous fungus Valsa mali with an IC(50) of 20 mu M. The mechanism of its antifungal action toward V. malt included (1) induction of alteration of hyphal morphology, (2) growth inhibition by chitin deposition at hyphal tips, and (3) permeabilization of fungal membrane. The antifungal activity of VFTI-E1 was dependent on the ambient ionic strength as increasing concentrations of NaCl, CaCl(2), and MgCl(2) diminished the activity. The membranolytic action of VFTI-E1 was confined to fungus, but not exerted on human and rabbit erythrocytes. This study sheds light on the mode of hyphal growth inhibitory activity of protease inhibitors with antifungal activity. The antifungal activity of VFTI-E1 amplifies the scope of its potential applications.
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