摘要
短小芽孢杆菌(Bacillus pumilus)2080碱性蛋白酶的发酵液经超滤、硫酸铵沉淀、CMSepharose Fast Flow和DEAE Sepharose Fast Flow离子交换层析得到了纯化的组分。SDS-PAGE电泳分析显示其分子量约为61kDa。酶学性质研究表明,该纯化酶的最适pH为10.5,最适温度为50℃。
A high yielding alkaline protease was obtained from Bacillus pumilus 2080 by solid-state fermentation. The alkaline protease from the crude enzyme were purified by ultra-filtration, ammonium sulphate precipitation, CM sepharose fast flow chromatography and DEAE sepharose fast flow chromatography. The purified alkaline protease was demonstrated to be electrophoretic homogeneity by SDS-PAGE, with a molecular weight of about 61 kDa. The optimal pH and temperature for activity of the purified alkaline protease was 10.5 and 50 12 respectively.
出处
《工业微生物》
CAS
CSCD
2009年第3期6-10,共5页
Industrial Microbiology
基金
北京市教委科研计划项目(KM200811417006)
北京市属市管高校人才强教计划资助项目
北京市优秀人才培养资助项目(20061D0502200295)。
关键词
碱性蛋白酶
短小芽孢杆菌
纯化
性质
alkaline protease
Bacillus lmmilus
purification
properties
