短小芽孢杆菌2080碱性蛋白酶的纯化与性质  

Purification and properties of alkaline protease from Bacillus pumilus 2080

作　　者：李祖明[1] 李鸿玉[1] 王德良[2] 莫欣[1] 白志辉[3] 李丽云[1] 

机构地区：[1]北京联合大学师范学院,北京100011 [2]中国食品发酵工业研究院,北京100027 [3]中科院生态环境研究中心,北京100085

出　　处：《工业微生物》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)。

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.

关 键 词：碱性蛋白酶 短小芽孢杆菌 纯化 性质 

分 类 号：TQ925[轻工技术与工程—发酵工程]