A novel thermostable and organic solvent-tolerant lipase from Xanthomonas oryzae pv. oryzae YB103: screening, purification and characterization

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• 作者：Qiurun Mo ; Aili Liu ; Hailun Guo ; Yan Zhang ; Mu Li
• 关键词：Biotechnology ; Enzyme stability ; Enzyme application ; Enzyme structure ; Function ; Synthesis in organic solvents ; Protein stability
• 刊名：Extremophiles
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：20
• 期：2
• 页码：157-165
• 全文大小：612 KB
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• 作者单位：Qiurun Mo (3)
  Aili Liu (3)
  Hailun Guo (3)
  Yan Zhang (3)
  Mu Li (1) (2) (3)
  
  3. College of Food Science and Technology, Huazhong Agricultural University, 430070, Wuhan, People’s Republic of China
  1. Key Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, 430070, Wuhan, Hubei, People’s Republic of China
  2. National Key Laboratory of Agro-Microbiology, Huazhong Agricultural University, 430070, Wuhan, Hubei, People’s Republic of China
  
• 刊物类别：Biomedical and Life Sciences
• 刊物主题：Life Sciences
  Microbiology
  Biotechnology
  Ecology
  
• 出版者：Springer Japan
• ISSN：1433-4909

文摘

Thermostable lipases offer major biotechnological advantages over mesophilic lipases. In this study, an intracellular thermostable and organic solvent-tolerant lipase-producing strain YB103 was isolated from soil samples and identified taxonomically as Xanthomonas oryzae pv. oryzae. The lipase from X. oryzae pv. oryzae YB103 (LipXO) was purified 101.1-fold to homogeneity with a specific activity of 373.9 U/mg. The purified lipase showed excellent thermostability, exhibiting 51.1 % of its residual activity after incubation for 3 days at 70 °C. The enzyme showed optimal activity at 70 °C, suggesting it is a thermostable lipase. LipXO retained 75.1–154.1 % of its original activity after incubation in 20 % (v/v) hydrophobic organic solvents at 70 °C for 24 h. Furthermore, LipXO displayed excellent stereoselectivity (e.e._p >99 %) toward (S)-1-phenethyl alcohol in n-hexane. These unique properties of LipXO make it promising as a biocatalyst for industrial processes.