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Subtilisin-Catalyzed Transesterifications in the Presence of Iron Oxide Nanoparticles in Organic Solvent: Dramatic Catalytic Improvement

  • Bang, Jong-Kyung (Department of Chemistry, Pohang University of Science and Technology) ;
  • Jung, Sang-Oh (Department of Chemistry, Pohang University of Science and Technology) ;
  • Kim, Yun-Woong (Department of Chemistry, Pohang University of Science and Technology) ;
  • Kim, Mahn-Joo (Department of Chemistry, Pohang University of Science and Technology)
  • 투고 : 2011.03.09
  • 심사 : 2011.03.29
  • 발행 : 2011.08.20

초록

키워드

참고문헌

  1. Klibanov, A. M. Acc. Chem. Res. 1990, 23, 114. https://doi.org/10.1021/ar00172a004
  2. Dordick, J. S. Biotechnol. Prog. 1992, 8, 259. https://doi.org/10.1021/bp00016a001
  3. Klibanov, A. M. Nature 2001, 409, 241. https://doi.org/10.1038/35051719
  4. Serdakowski, A. L.; Dordick, J. S. Trends Biotechnol. 2008, 26, 48. https://doi.org/10.1016/j.tibtech.2007.10.007
  5. Mateo, C.; Palomo, J. M.; Fernandez-Lorente, G.; Guisan, J. M.; Fernandez-Lafuente, R. Enz. Microb. Technol. 2007, 40, 1451. https://doi.org/10.1016/j.enzmictec.2007.01.018
  6. Betancor, L.; Luckarift, H. R. Trends Biotechnol. 2008, 26, 566. https://doi.org/10.1016/j.tibtech.2008.06.009
  7. Affleck, R.; Xu, Z. F.; Suzawa, V.; Focht, K.; Clark, D. S.; Dordick, J. S. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 1100. https://doi.org/10.1073/pnas.89.3.1100
  8. Khmelnitsky, Y. L.; Welch, S. H.; Clark, D. S.; Dordick, J. S. J. Am. Chem. Soc. 1994, 116, 2647. https://doi.org/10.1021/ja00085a066
  9. Paradkar, V. M.; Dordick, J. S. J. Am. Chem. Soc. 1994, 116, 5009. https://doi.org/10.1021/ja00090a065
  10. Hutcheon, G. A.; Parker, M. C.; James, A.; Moore, B. D. Chem. Commun. 1997, 931.
  11. Rich, J. O.; Dordick, J. S. J. Am. Chem. Soc. 1997, 119, 3245. https://doi.org/10.1021/ja9637715
  12. Bedell, B. B.; Mozhaev, V. V. ; Clark, D. S.; Dordick, J. S. Biotechnol. Bioeng. 1998, 58, 654. https://doi.org/10.1002/(SICI)1097-0290(19980620)58:6<654::AID-BIT12>3.0.CO;2-7
  13. Ru, M. T.; Wu, K. C.; Lindsay, J. P.; Dordick, J. S.; Reimer, J. A.; Clark, D. S. Biotechnol. Bioeng. 2001, 75, 187. https://doi.org/10.1002/bit.1178
  14. Eppler, R. K.; Hudson, E. P.; Chase, S. D.; Dordick, J. S.; Reimer, J. A.; Clark, D. S. Proc. Natl. Acad. Sci. USA 2008, 105, 15622.
  15. Kazlauskas, R. J.; Weissfloch, A. N. E. J. Mol. Catal. B: Enzym. 1997, 3, 65. https://doi.org/10.1016/S1381-1177(96)00040-9
  16. Kim, M.-J.; Chung, Y. I.; Choi, Y. K.; Lee, H. K.; Kim, D.; Park, J. J. Am. Chem. Soc. 2003, 125, 11494. https://doi.org/10.1021/ja036766r
  17. Boren, L.; Martin-Matute, B.; Xu, Y.; Cordova, A.; Backvall, J-E. Eur. J. Org. Chem. 2006, 12, 225. https://doi.org/10.1002/chem.200500758
  18. Kim, M.-J.; Lee, H.; Park, J. Bull. Korean Chem. Soc. 2007, 28, 2096. https://doi.org/10.5012/bkcs.2007.28.11.2096
  19. Blidi, L. E.; Nechab, M.; Vanthuyne, N.; Gastaldi, S.; Bertrand, M. P.; Gil, G. J. Org. Chem. 2009, 74, 2901. https://doi.org/10.1021/jo900074w
  20. Dyal, A.; Loos, K.; Noto, M.; Chang, S. W.; Spagnoli, C.; Shafi, K. V. P. M.; Ulman, A.; Cowman, M.; Gross, R. A. J. Am. Chem. Soc. 2003, 125, 1684. https://doi.org/10.1021/ja021223n
  21. Huang, S. H.; Liao, M. H.; Chen, D. H. Biotechnol. Prog. 2003, 19, 1095. https://doi.org/10.1021/bp025587v
  22. Naik, R. R.; Tomczak, M. M.; Luckarift, H. R.; Spain, J. C.; Stone, M. O. Chem. Commun. 2004, 1684.
  23. Kim, J.; Lee, J.; Na, H. B.; Kim, B. C.; Youn, J. K.; Kwak, J. H.; Moon, K.; Lee, E.; Kim, J.; Park, J.; Dohnalkova, A.; Park, H. G.; Gu, M. B.; Chang, H. N.; Grate, J. W.; Hyeon, T. Small 2005, 12, 1203.
  24. Herdt, A. R.; Kim, B. S.; Taton, T. A. Bioconjugate Chem. 2007, 18, 183. https://doi.org/10.1021/bc060215j
  25. Abu-Reziq, R.; Wang, D.; Post, M. L.; Alper, H. Adv. Synth. Catal. 2007, 349, 2145 https://doi.org/10.1002/adsc.200700129

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