Abstract
A Cysteine protease inhibitor exhibiting antifungal activity from pearl millet seeds has been purified to homogeneity by ammonium sulphate precipitation and chromatographic procedures involving CM- sephadex and SP- sepharose cation exchange columns. The molecular characterization has revealed its molecular mass as 24 kD and isoelectric point 9.8. The amino acid composition data shows presence of high content of serine and glycine (34 residues / mole) and absence of tryptophan. The inhibitor exhibits potent antifungal activity againstTrichoderma reesei,a dead wood fungus with minimum inhibitory dose to inhibit mycelial growth or spore germination is as low as 1μg / ml (250 ng/disc). In addition toTrichoderma reesei,the antifungal activity is observed against some important phytopathogenic fungi, namely,Claviceps, Helminthosporium, Curvularia, AlternariaandFusarium species.To the best of our knowledge, a cysteine protease inhibitor as an antifungal protein is reported for the first time from a plant system.
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