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http://dx.doi.org/10.1007/s11814-008-0051-0

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)
Publication Information
Korean Journal of Chemical Engineering / v.25, no.2, 2008 , pp. 291-294 More about this Journal
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.
Keywords
Ionic Liquid; Lipase; (R,S)-1-Phenylethanol; Reuse; Stability
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
Times Cited By Web Of Science : 9  (Related Records In Web of Science)
Times Cited By SCOPUS : 7
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1 R. A. Sheldon, R. M. Lau, M. J. Sorgedrager and F. van Rantwijk, Green Chem., 4, 147 (2002)   DOI   ScienceOn
2 A. Zaks and A. M. Klibanov, J. Biol. Chem., 263, 3194 (1988)   PUBMED
3 M. Freemantle, Chem. Eng. News, 76, 32 (1998)
4 S. H. Lee, T. T. N. Doan, S. H. Ha and Y.-M. Koo, J. Mol. Catal. B: Enzym., 45, 57 (2007)   DOI   ScienceOn
5 S. H. Schofer, N. Kaftzik, P. Wasserscheid and U. Kragl, Chem. Commun., 425 (2001)
6 S. Park and R. J. Kazlauskas, Curr. Opin. Biotechnol., 14, 432 (2003)   DOI   ScienceOn
7 U. Kragl, M. Eckstein and N. Kaftzik, Curr. Opin. Biotechnol., 13, 565 (2002)   DOI   ScienceOn
8 O. Ulbert, K. Bélafi-Bakó, K. Tonova and L. Gubicza, Biocatal. Biotrans., 23, 177 (2005)   DOI   ScienceOn
9 T. Itoh, Y. Nishimura, N. Ouchi and S. Hayase, J. Mol. Catal. B: Enzym., 26, 41 (2003)   DOI   ScienceOn
10 T. Welton, Chem. Rev., 99, 2071 (1999)   DOI   PUBMED   ScienceOn
11 M. Persson and U. T. Bornscheuer, J. Mol. Catal. B: Ezym., 22, 21 (2003).   DOI   ScienceOn
12 Y. H. Moon, S. M. Lee, S.H. Ha and Y.-M. Koo, Korean J. Chem. Eng., 23, 247 (2006)   DOI   ScienceOn
13 T. de Diego, P. Lozano, M. Vaultier and J. L. Iborra, Biomacromol., 6, 1457 (2005)   DOI   ScienceOn
14 K.W. Kim, B. Song, M.Y. Choi and M.-J. Kim, Org. Lett., 3, 1507 (2001)   DOI   ScienceOn
15 P. Lozano, T. de Diego, D. Carrie, M. Vaultier and J. L. Iborra, Biotechnol. Lett., 23, 1529 (2001)   DOI   ScienceOn