产海洋细菌MP-2酯酶菌株的鉴定及酯酶理化性质的研究  

Identification of MP-2 esterase-producing marine Bacillus and study on properties of the esterase

作　　者：平芮巾[1,2] 孙谧[1] 刘均忠[1] 王跃军[1] 郝建华[1] 张胜军 

机构地区：[1]中国水产科学研究院黄海水产研究所海洋酶与酶工程实验室,青岛266071 [2]大连水产学院,116023 [3]青岛市环境保护监测站,266003

出　　处：《渔业科学进展》2009年第2期83-88,共6页Progress in Fishery Sciences

基　　金：国家自然科学基金项目(30571429);国际科技合作重点计划项目(2005DFA30830)共同资助

摘　　要：从渤海海泥样品中分离获得1株新型酯酶菌株,经鉴定为地衣芽孢杆菌Bacillus licheniformis。所得的MP-2酯酶的最适作用温度范围50～70℃,在60℃表现出了最高活性,属于耐热酶;最适作用pH为10,属于碱性酶,其pH值作用范围比较窄;具有良好的热稳定性;金属离子Co2+,Li+对酶具有激活作用,Ca2+对酯酶的活力没有显著影响,化学试剂SDS、EDTA及Tween-20对酯酶的抑制效果显著,对常见有机溶剂具有良好的耐受力;该酯酶对碳链长短不同的底物表现出不同的酶活。A novel marine esterase-producing bacteria isolated from the Bohai Sea sediment was identified as Bacillus licheniformis. The MP-2 esterase was primarily purified and characterized. The optimal range of temperature of the esterase was 50-70 ℃, and the maximum activity was achieved at 60 ℃ and pH10.0. The esterase was alkaline and its optimum range of pH was narrow. The thermal stability of the esterase was good. Co^2＋,Li＋ ions were found to activate the esterase, but Ca^2＋ had no significant effects on the activity of the esterase. While SDS, EDTA and Tween-20 had significantly suppressive effects on the esterase. It showed strong resistance to ordinary organic solvents. The enzyme exhibited different esterase activities towards substrates with different length of carbon chains.

关 键 词：海洋地衣芽孢杆菌 酯酶 鉴定 性质 

分 类 号：Q55[生物学—生物化学]