Bacillus pumilus CN8菌株降解猪血Hb酶的分离纯化及酶学性质研究  

Study on the isolation,purification and zymetology properties of porcine hemoglobin enzyme degraded by Bacillus pumilus CN8

作　　者：李浩丽[1] 马美湖[1] 陈文成[1] 

机构地区：[1]华中农业大学食品科技学院,湖北武汉430070

出　　处：《食品工业科技》2010年第5期171-173,177,共4页Science and Technology of Food Industry

基　　金：国家十一五科技支撑项目(2006BAD05A16)

摘　　要：Bacillus pumilus CN8菌株的发酵液,经离心分离得到粗酶液,再经硫酸铵盐析、透析,DEAE-Cellulose-52离子交换层析等步骤获得电泳纯的中性蛋白酶。得到比活达686.66U/mg的酶蛋白,纯化倍数为13.2,回收率为35.0%。SDS-PAGE测得其分子量大约为97000Da。该酶的最适作用pH为7.4,最适反应温度为42℃,在pH7.0～8.5范围内较稳定,在30～45℃比较稳定。经酶学性质测定,K^＋、Mg^2＋对酶活力具有保护作用,甘油对酶活具有抑制作用。The Bacillus pumilus CN8 protease was purified from liquor to homogeneity by ultrafiltration,ammonium sulfate precipitation,dialysis and DEAE-Cellulose-52 gel filtration. After that the neutral protease（Bacillus pumilus CN8 protease）was collected which was electrophoresis pure. The specific activity of the enzyme was 686.66U/mg. Purification times and recovery rate of the enzyme were 13.2 and 35.0% respectively. The molecular weight of the purified enzyme was estimated to be 97000Da. The optimum pH was 7.4 and the optimum temperature was 42℃. The Bacillus pumilus CN8 protease was stable at pH7.0 to 8.5 and at temperature of 30℃ to 45℃. The effects of metal ions on the enzyme activity of Bacillus pumilus CN8 protease were studied,from the result we could conclude that K^＋,Mg^2＋ strongly activated the enzyme activity,glycerin had inhibitory effect to the enzyme activity.

关 键 词：猪血 血红蛋白 短小芽孢杆菌 分离纯化 酶学特性 

分 类 号：TS201.25[轻工技术与工程—食品科学]