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微生物学通报 1997
PURIFICATION AND SOME PROPERTIES OF ANTIFUNGAL PROTEIN SECRETED FROM ANTAGONISTIC BACILLUS SUBTIL IS BS-98
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Abstract:
The antifungal protein purified by ammonium sulphate precipitation and columnchromatography on Sephadex G-100, and DEAE-Cellulose was demonstrated to be of threeprotein bands by polyacrylamide gel electrophoresis The protein was found to be thermostableand partially sensitive to proteinases. The inhibitory spectum showed that the protein had astrong inhibiting activity against the pathogens of Phoma asparagi,, Fusarium graminearum,Fusarium oxysporum f. sp. vasinfectum, Verticillium, albo-atrum, Botrytis cinerea, Rhizoctoniasolani, Pseudomonas Syringae pv. lachrmans.