高等学校化学学报

高等学校化学学报

• 研究论文 • 上一篇    下一篇

古细菌Aeropyrum pernix K1超嗜热酯酶APE1547的稳定性

解桂秋1,2, 高仁钧1, 毕云枫1, 王中禹1, 刘娜1, 冯雁1, 曹淑桂1   

    1. 吉林大学分子酶学工程教育部重点实验室, 长春 130023;
    2. 吉林大学药学院, 长春 130061
  • 收稿日期:2007-05-16 修回日期:1900-01-01 出版日期:2008-01-10 发布日期:2008-01-10
  • 通讯作者: 曹淑桂

Stability of a Hyperthermophilic Esterase APE1547 from an Archaeon Aeropyrum pernix K1

XIE Gui-Qiu1,2, GAO Ren-Jun1, BI Yun-Feng1, WANG Zhong-Yu1, LIU Na1, FENG Yan1, CAO Shu-Gui1*   

    1. Key Laboratory for Molecular Enzymology and Engineering, Ministry of Education, Jilin University, Changchun 130023, China;
    2. School of Pharmaceutical Sciences, Jilin University, Changchun 130061, China
  • Received:2007-05-16 Revised:1900-01-01 Online:2008-01-10 Published:2008-01-10
  • Contact: CAO Shu-Gui

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摘要： 研究了纯化的超嗜热酯酶APE1547的稳定性. 结果表明, 该酶的稳定性非常好, 蛋白的质量浓度为0.4 mg/mL时, 90 ℃的半衰期为20 h, 0.2 mg/mL时的半衰期为12 h; 而蛋白的质量浓度为0.04 mg/mL时, 保温2.5 h时残余活力仍在50%以上. 同时还研究了热变性时该酶表面疏水氨基酸的变化. 该酶的pH稳定性也很好, pH在6.5-9.0范围内作用24 h, 酶依然很稳定, 残余酶活力大于93％; 同时该酶还具有很强的耐有机溶剂的特性.

关键词: 古细菌, 超嗜热酯酶, 热稳定性, Aeropyrum pernix K1

Abstract: The gene APE1547 from an archeaon Aeropyrum pernix K1 were cloned and expressed in E. coli BL21. The recombinant enzyme shows an esterase activity and its optimum reaction temperature was 90 ℃. In this paper, the stability of a hyperthermophilic esterase APE1547 from an archeaon Aeropyrum pernix K1 was studied. The experimental results indicate that APE1547 was one of the most stable hyperthermophilic enzymes. Its half-life was 20 h at 90 ℃(0.4 mg/mL), and it was stable in an alkalinous environment. At the same time, the change of the fluorescence and the activity was detected when the enzyme was thermally denatured. With the exposure of hydrophobic amino acids, its activity reduced gradually. Furthermore, this enzyme has a good pH stability and shows a good organic solvents resistance. The present results indicate that this enzyme will be useful in specific industry process such as high temperature or organic reaction.

Key words: Archeaon, Hyperthermophilic esterase, Thermostability, Aeropyrum pernix K1

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