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Bacillus pumilus CN8菌株降解猪血Hb酶的分离纯化及酶学性质研究
引用本文:李浩丽,马美湖,陈文成.Bacillus pumilus CN8菌株降解猪血Hb酶的分离纯化及酶学性质研究[J].食品工业科技,2010(5).
作者姓名:李浩丽  马美湖  陈文成
作者单位:华中农业大学食品科技学院,湖北武汉,430070
基金项目: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+、Mg2+对酶活力具有保护作用,甘油对酶活具有抑制作用。

关 键 词:猪血  血红蛋白  短小芽孢杆菌  分离纯化  酶学特性  

Study on the isolation,purification and zymetology properties of porcine hemoglobin enzyme degraded by Bacillus pumilus CN8
LI Hao-li,MA Mei-hu,CHEN Wen-cheng.Study on the isolation,purification and zymetology properties of porcine hemoglobin enzyme degraded by Bacillus pumilus CN8[J].Science and Technology of Food Industry,2010(5).
Authors:LI Hao-li  MA Mei-hu  CHEN Wen-cheng
Affiliation:LI Hao-li,MA Mei-hu,CHEN Wen-cheng(College of Food Science , Technology,Huazhong Agricultural University,Wuhan 430070,China)
Abstract: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 ...
Keywords:porcine blood  hemoglobin  Bacillus pumilus  purification  zymetology properties  
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