Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Immobilization of Lipase on Single Walled Carbon Nanotubes in Ionic Liquid

  • Lee, Han-Ki (Department of Chemistry, Pohang University of Science and Technology) ;
  • Lee, Jae-Kwan (Department of Chemistry, Pohang University of Science and Technology) ;
  • Kim, Mahn-Joo (Department of Chemistry, Pohang University of Science and Technology) ;
  • Lee, Cheol-Jin (Nanotube and Nanodevice Laboratory, School of Electrical Engineering and Department of Micro/Nano Systems, Korea University)
  • Published : 2010.03.20
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Abstract

A lipase from Pseudomonas cepacia was immobilized onto single walled carbon nanotubes (SWNTs) in two different ways in each of two solvent systems (buffer and ionic liquid). The most efficient immobilization was achieved in ionic liquid (1-butyl-3-methylimidazolium tetrafluoroborate, BMIM-$BF_4$). In this procedure, carbon nanotubes were first functionalized noncovalently with 1-pyrenebutyric acid N-hydroxysuccinimide ester and then subject to the coupling reaction with the lipase in ionic liquid. The resulting immobilized enzyme displayed the highest activity in the transesterification of 1-phenylethyl alcohol in the presence of vinyl acetate in toluene.

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References

  1. Wong, C.-H.; Whitesides, G. M. Enzymes in Synthetic OrganicChemistry; Pergamon: Oxford, UK, 1994.
  2. Drauz, K.; Waldmann, H. Enzyme Catalysis in Organic Synthesis;VCH: Weinheim, Germany, 1995; Vols. I and II.
  3. Bornscheuer, U. T.; Kazlauskas, R. J. Hydrolases in Organic Synthesis;Wiley-VCH: Weinheim, Germany, 1999.
  4. Koskinen, A. M. P.; Klivanov, A. M. Enzymatic Reactions in OrganicMedia; Blackie Academic ＆ Professional: Glasgow, Scotland,1996.
  5. Kim, M.-J.; Ahn, Y.; Park, J. Curr. Opin. Biotechnol. 2002, 13,578. https://doi.org/10.1016/S0958-1669(02)00347-6
  6. Kim, M.-J.; Ahn, Y.; Park, J. Bull. Korean Chem. Soc. 2005, 26,515. https://doi.org/10.5012/bkcs.2005.26.4.515
  7. Ahn, Y.; Ko, S.-B.; Kim, M.-J.; Park, J. Coord. Chem. Rev. 2008,252, 647. https://doi.org/10.1016/j.ccr.2007.09.009
  8. Dresselhaus, M. S.; Dresselhaus G.; Eklund, P. C. Science of Fullerenesand Carbon Nanotubes; Academic Press: San Diego, 1996;pp 1-985.
  9. Chen, R. J.; Zhang, Y.; Wang, D.; Dai, H. J. Am. Chem. Soc. 2001,123, 3838. https://doi.org/10.1021/ja010172b
  10. Huang, W.; Taylor, S.; Fu, K.; Lin, Y.; Zhang, D.; Hanks, T. W.;Rao, A. M.; Sun, Y.-P. Nano Lett. 2002, 2, 311. https://doi.org/10.1021/nl010095i
  11. Azamian, B. R.; Davis, J. J.; Coleman, K. S.; Bagshaw, C. B.;Green, M. L. H. J. Am. Chem. Soc. 2002, 124, 12664. https://doi.org/10.1021/ja0272989
  12. Rege, K.; Raravikar, N. R.; Kim, D.-Y.; Schadler, L. S.; Ajayan,P. M.; Dordick, J. S. Nano Lett. 2003, 3, 829. https://doi.org/10.1021/nl034131k
  13. Jiang, K.; Schadler, L. S.; Siegel, R. W.; Zhang, X.; Zhang, H.;Terrones, M. Mater. Chem. 2004, 14, 37. https://doi.org/10.1039/b310359e
  14. Yim, T.-J.; Liu, J.; Lu, Y.; Kane, R. S.; Dordick, J. S. J. Am. Chem.Soc. 2005, 127, 12200. https://doi.org/10.1021/ja0541581
  15. Gomez, J. M.; Romero, M. D.; Fernandez, T. M. Catal. Lett. 2005,101, 275. https://doi.org/10.1007/s10562-005-4904-4
  16. Prakash, R.; Superfine, R.; Falvo, M. R. Appl. Phys. Lett. 2006, 88,063102. https://doi.org/10.1063/1.2171802
  17. Heering, H. A.; Williams, K. A.; de Vries, S.; Dekker, C. Chem.Phys. Chem. 2006, 7, 1705.
  18. Reich, S.; Thomsen, C.; Ordejon, P. Phys.Rev. B 2002, 65, 155411. https://doi.org/10.1103/PhysRevB.65.155411
  19. Girifalco, L.; Hodak, M.; Lee, R. S. Phys. Rev. B 2000, 62, 13104. https://doi.org/10.1103/PhysRevB.62.13104
  20. Fukushima, T.; Kosaka, A.; Ishimura, Y.; Yamamoto, T.; Takigawa,T.; Ishii, N.; Aida, T. Science 2003, 300, 2072. https://doi.org/10.1126/science.1082289
  21. Price, B. K.; Hudson, J. L.; Tour, J. M. J. Am. Chem. Soc. 2005,127, 14867. https://doi.org/10.1021/ja053998c
  22. Kragl, U.; Eckstein, M.; Kaftzik, N. Curr. Opin. Biotechnol. 2002,13, 565. https://doi.org/10.1016/S0958-1669(02)00353-1
  23. Park, S.; Kazlauskas, R. J. Curr. Opin. Biotechnol. 2003, 14, 432. https://doi.org/10.1016/S0958-1669(03)00100-9
  24. van Rantwijk, F.; Sheldon, K. R. A. Chem. Rev. 2007, 107, 2757. https://doi.org/10.1021/cr050946x
  25. Cantone, S.; Hanefeld, U.; Basso, A. Green Chem. 2007, 9, 954. https://doi.org/10.1039/b618893a
  26. Lyu, S. C.; Liu, B. C.; Lee, T. J.; Liu, Z. Y.; Yang, C. W.; Park, C.Y.; Lee, C. J. Chem. Commun. 2003, 734.
  27. Liu, B. C.; Lyu, S. C.; Jung, S. I.; Kang, H. K.; Yang, C.-W.; Park,J. W.; Park, C. Y.; Lee, C. J. Chem. Phys. Lett. 2004, 383, 104. https://doi.org/10.1016/j.cplett.2003.10.134

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