摘要
对一种纯化自Bacillus mycoides970发酵上清液的磷脂酶C的部分特性进行了研究。SDS-PAGE检测表明该纯化磷脂酶C由一条多肽链组成,分子量为75.1 kDa。热稳定性实验表明该纯化磷脂酶C对温度敏感,具有热不稳定性。金属离子依赖性检测表明该纯化磷脂酶C属于金属磷脂酶C家族,Ca2+、Mg2+、Zn2+和Ba2+对该磷脂酶C催化活性的发挥必不可少。血平板及卵黄平板检测表明该磷脂酶C没有溶血活性和卵磷脂酶活性。
Some properties of phospholipase C （PLC） from Bacillus rnycoides 970 are studied in this paper. The PLC is indicated to be a single polypeptide and its molecular mass is estimated to be 75.1 kDa by the SDS- PAGE. The PLC is sensitive to temperature and is heat-labile. The PLC belongs to a group of metallophospho-lipase C and Zn^2＋ , Ca^2＋ , Mg^2＋ and Ba^2＋ are essential for its hydrolyzing activity. The enzyme shows no lecithinase activity on egg yolk agar and no hemolytic activity to human erythrocytes on blood agar.
出处
《化学与生物工程》
CAS
2007年第7期52-54,共3页
Chemistry & Bioengineering
基金
湖北省自然科学基金资助项目(2004ABA233)
湖北省教育厅项目(B200514006)
湖北工业大学科技项目(ZZ200303)
