多粘类芽孢杆菌BRF-1抗菌蛋白的分离纯化

Purification of Antifungal Protein from Paenibacillus polymyxa BRF-1

通过硫酸铵分级沉淀、Sephadex G-50柱层析并采用抑菌活性和SDS-PAGE跟踪检测,从多粘类芽孢杆菌BRF-1菌株代谢产物中分离纯化到一种对大豆立枯丝核菌具有拮抗活性的抗菌蛋白,分子量约35.4kD。

Using （NH4） 2SO4 fractional precipitation, Sephadex G-50 chromatography, followed by tracks of fraction antagonistic assay and SDS-PAGE identification, an antifungal protein peak Ⅱ was purified from metabolic of Paenibacillus polymyxa BRF-1 and was showed to be antagonistic to soybean root rot pathogen, Rhizoctonia solani, on PDA plates. Molecular weight of this protein by SDS-PAGE is about 35.4 kD.