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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

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【作者】 平芮巾孙谧刘均忠王跃军郝建华张胜军

【Author】 PING Rui-jin1,2 SUN Mi 1 LIU Jun-zhong1 WANG Yue-jun1 HAO Jian-hua1 ZHANG Sheng-jun3(1 Laboratory of Marine Enzyme and Enzyme Engineering,Yellow Sea Fisheries Research Institute,Chinese Academy of Fishery Sciences,Qingdao 266071)(2 Dalian Fisheries University,116023)(3 Environmental Monitoring Station of Qingdao,266003)

【机构】 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大连水产学院青岛市环境保护监测站

【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。

【Abstract】 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.Co2+,Li+ions were found to activate the esterase,but Ca2+ 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.

【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
  • 【文献出处】 渔业科学进展 ,Progress in Fishery Sciences , 编辑部邮箱 ,2009年02期
  • 【分类号】Q93
  • 【被引频次】7
  • 【下载频次】178
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