| Literature DB >> 17129637 |
Yongfeng Liu1, Zhiyi Chen, T B Ng, Jie Zhang, Mingguo Zhou, Fuping Song, Fan Lu, Youzhou Liu.
Abstract
An antifungal protein, with a molecular mass of 41.9 kDa, and designated as bacisubin, was isolated from a culture of Bacillus subtilis strain B-916. The isolation procedure consisted of ion exchange chromatography on DEAE-Sepharose Fast Flow, and fast protein liquid chromatography on Phenyl Sepharose 6 Fast Flow and hydroxyapatite columns. The protein was adsorbed on all three chromatographic media. Bacisubin exhibited inhibitory activity on mycelial growth in Magnaporthe grisease, Sclerotinia sclerotiorum, Rhizoctonia solani, Alternaria oleracea, A. brassicae and Botrytis cinerea. The IC50 values of its antifungal activity toward the last four fungal species were 4.01 microM, 0.087 microM, 0.055 microM and 2.74 microM, respectively. Bacisubin demonstrated neither protease activity, nor protease inhibitory activity. However, it manifested ribonuclease and hemagglutinating activities.Entities:
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Year: 2006 PMID： 17129637 DOI： 10.1016/j.peptides.2006.10.009
Source DB: PubMed Journal: Peptides ISSN： 0196-9781 Impact factor: 3.750