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›› 2007, Vol. 7 ›› Issue (1): 141-144.

• 生化工程专栏 • 上一篇    下一篇

Candida sp.脂肪酶的纯化及其性质

秦韶巍,于明锐,谭天伟   

  1. 北京化工大学生命科学与技术学院
  • 出版日期:2007-02-20 发布日期:2007-02-20

Investigation on Purification and Properties of Extracellular Lipase from Candida sp.

QIN Shao-wei,YU Ming-rui,TAN Tian-wei   

  1. Key Lab Bioprocess of Beijing, College of Life Science and Technology, Beijing University of Chemical Technology
  • Online:2007-02-20 Published:2007-02-20

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摘要： 采用简单的两步法-离子交换层析和疏水层析法，对Candida sp. 99-125脂肪酶进行了纯化，比活提高了10.0倍，达到27200 U/mg，回收率为35.5%. SDS-PAGE电泳分析显示该酶的分子量约为38 kDa. 酶学性质研究表明，该酶最适反应温度为40℃，最适反应pH值为8.5，在室温下具有良好的稳定性. 钙离子和Tween80能够促进提高脂肪酶的活性，而铁离子、铜离子和SDS对其有明显的抑制作用.

关键词: 脂肪酶, 纯化, 层析

Abstract: The extracellular lipase from Candida sp. 99-125 was purified by ion exchange chromatography and hydrophobic interaction chromatography. The results showed that the specific activity of the purified enzyme was raised by 10.0 times and the activity recovery was 35.5%. The molecular weight of the purified lipase was determined to be about 38 kDa by SDS-PAGE in Coomassie brilliant blue staining. The optimum pH and temperature of the purified enzyme were 8.5 and 40℃ respectively. The purified lipase remained 95% activity after incubated for 2 d at room temperature (20℃). Fe2+, Cu2+ and SDS had an inhibitory effect on lipase activity, whereas Ca2+ salts and Tween80 increased it.

Key words: lipase, purification, chromatography