脱毛碱性蛋白酶的纯化及其生化特性研究

Purification and characterization of the denude alkaline protease

采用CM-阳离子交换层析和凝胶过滤层析分离碱性蛋白酶,得到了碱性蛋白酶的单一组分。对枯草芽孢杆菌(Bacillussubtilis)碱性蛋白酶SDS-聚丙烯酰胺电泳进行了分析。结果表明:其亚基分子量约为28kD,等电点约为8 4。并对其生化特性质进行研究,结果表明:酶活最适温度为45℃,最适pH值为10 5,在0 5mol L的Na+对酶活有较大的促进作用。

The alkaline protease from the crude culture filtrate of Bacillus subtilis was purified by means of ction exchange cellulose, and gel filtration chromatography. The single band has been got. The sub-group molecular weight of alkaline protease was about 28 kD by SDS-PAGE electrophoresis. The IEF of the enzyme is about 8.4. The research of property Alkaline Protease showed that the optimal pH is 10.5; the optimal temperature is 45℃; and the 0.5 mol/L Na^+ has promoter of the enzyme's activity.