嗜热芽孢杆菌高温蛋白酶HS08活性中心研究

运用化学修饰方法对一株嗜热芽孢杆菌所产生的耐高温蛋白酶HS08活性中心的结构进行了研究。结果表明,蛋白酶HS08的活性被酶活性中心丝氨酸残基专一性抑制剂PMSF以及金属离子螯合剂EDTA强烈抑制,色氨酸和精氨酸对酶活性有重要作用,但并不位于酶的活性中心。Zn2+可使该酶活性明显提高,Cu2+对该酶活性有抑制作用。因此,该酶属于金属离子激活的丝氨酸族蛋白酶。

Chemical modification of amino acid side chain groups on protease HS08 secreted by a thermophiric Bacillus strain were investigated, The results indicated that EDTA and PMSF inhibited dramatically the protease activities and serine residue was essential group for the catalytic activity, Tryptophan and arginine residues were important in maintaining the enzyme activity,but not in the activity side of the enzyme,The protease activity was activated by Zn^2＋ but was inhibited by Cu^2＋. So the protease HS08 was belonged to metal-activated serine protease.