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Enhanced stability of Candida antarctica lipase B in ionic liquids

  • Ha, Sung-Ho (ERC for Advanced Bioseparation Technology, Inha University) ;
  • Lee, Sang-Hyun (ERC for Advanced Bioseparation Technology, Inha University) ;
  • Dang, Dung-Thanh (Department of Biological Engineering, Inha University) ;
  • Kwon, Min-Sik (Department of Biological Engineering, Inha University) ;
  • Chang, Woo-Jin (ERC for Advanced Bioseparation Technology, Inha University) ;
  • Yu, Yong-Jae (C-TRI) ;
  • Byun, Il-Suk (C-TRI) ;
  • Koo, Yoon-Mo (ERC for Advanced Bioseparation Technology, Inha University)
  • Published : 20080000

Abstract

The activity and stability of lipase from Candida antarctica were investigated in the kinetic resolution of (R,S)-1-phenylethanol with vinyl acetate using ionic liquids (ILs) as reaction media. Among ILs tested, the highest activity of lipase was observed in [Edmim][$Tf_2N$]. In hydrophobic ILs such as [Edmim][$Tf_2N$], [Emim][$Tf_2N$] and [Pmim] [$PF_6$], lipase could retain its activity after 5 times reuse, while the activity of lipase in hydrophilic ILs and organic solvents was drastically decreased. The activities of lipase in [Edmim][$Tf_2N$], [Emim][$Tf_2N$] and [Pmim][$PF_6$] were also well maintained after 1 day incubation at 80 ℃. The lipase suspended in [Edmim][$Tf_2N$] could be successfully reused 6 times without loss of activity.

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References

  1. R. A. Sheldon, R. M. Lau, M. J. Sorgedrager and F. van Rantwijk, Green Chem., 4, 147 (2002) https://doi.org/10.1039/b110008b
  2. M. Freemantle, Chem. Eng. News, 76, 32 (1998)
  3. Y. H. Moon, S. M. Lee, S.H. Ha and Y.-M. Koo, Korean J. Chem. Eng., 23, 247 (2006) https://doi.org/10.1007/BF02705724
  4. S. Park and R. J. Kazlauskas, Curr. Opin. Biotechnol., 14, 432 (2003) https://doi.org/10.1016/S0958-1669(03)00100-9
  5. K.W. Kim, B. Song, M.Y. Choi and M.-J. Kim, Org. Lett., 3, 1507 (2001) https://doi.org/10.1021/ol015824f
  6. U. Kragl, M. Eckstein and N. Kaftzik, Curr. Opin. Biotechnol., 13, 565 (2002) https://doi.org/10.1016/S0958-1669(02)00353-1
  7. S. H. Schofer, N. Kaftzik, P. Wasserscheid and U. Kragl, Chem. Commun., 425 (2001)
  8. M. Persson and U. T. Bornscheuer, J. Mol. Catal. B: Ezym., 22, 21 (2003). https://doi.org/10.1016/S1381-1177(02)00294-1
  9. P. Lozano, T. de Diego, D. Carrie, M. Vaultier and J. L. Iborra, Biotechnol. Lett., 23, 1529 (2001) https://doi.org/10.1023/A:1011697609756
  10. O. Ulbert, K. Bélafi-Bakó, K. Tonova and L. Gubicza, Biocatal. Biotrans., 23, 177 (2005) https://doi.org/10.1080/10242420500192940
  11. T. Itoh, Y. Nishimura, N. Ouchi and S. Hayase, J. Mol. Catal. B: Enzym., 26, 41 (2003) https://doi.org/10.1016/S1381-1177(03)00147-4
  12. S. H. Lee, T. T. N. Doan, S. H. Ha and Y.-M. Koo, J. Mol. Catal. B: Enzym., 45, 57 (2007) https://doi.org/10.1016/j.molcatb.2006.11.008
  13. A. Zaks and A. M. Klibanov, J. Biol. Chem., 263, 3194 (1988)
  14. T. de Diego, P. Lozano, M. Vaultier and J. L. Iborra, Biomacromol., 6, 1457 (2005) https://doi.org/10.1021/bm049259q
  15. T. Welton, Chem. Rev., 99, 2071 (1999) https://doi.org/10.1021/cr980032t