Dezembro 2013 vol. 1 num. 2 - Brazilian Meeting on Organic Synthesis 2013

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Enzymatic kinetic resolution of methyl 2-methyl-4-oxopentanoate

Ferreira, Edgard A. ; Omori, Álvaro T. ; Cunha, Rodrigo L. O. R. ;

Abstract:

The stereoselectivity of enzyme catalyzed reactions can be tuned by changing reaction conditions such as pH, temperature and with addition of co-solvents. Other alternatives for the modulation of the affinity and specificity between enzyme and extraneous organic compounds have been developed. In special, addition of salts can promote changes in enzyme solvatation which leads to changes in its interaction with the substrate. However, this approach is scarcely considered in biocatalytic reactions for preparative purposes. Herein, we describe the enzymatic kinetic resolution of methyl (RS)-2-methyl-4-oxopentanoate by a series of changes in the medium with merit to salt effect.

Abstract:

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Palavras-chave: Ester hydrolysis, remote resolution, salt effect, enzymatic kinetic resolution.,

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DOI: 10.5151/chempro-15bmos-BMOS2013_201381614738

Referências bibliográficas
  • [1] 1K. Faber. Biotransformations in Organic Chemistry, 5th ed.; Springer, 2004.
  • [2] 2Collins, K. D. Methods. 2004, 34, 300.
  • [3] 3Escalante, J. and F. Díaz-Coutiño. Molecules. 2009, 14 (4): 159.
Como citar:

Ferreira, Edgard A.; Omori, Álvaro T.; Cunha, Rodrigo L. O. R.; "Enzymatic kinetic resolution of methyl 2-methyl-4-oxopentanoate", p. 40 . In: In Blucher Chemistry Proceedings, São Paulo, v. 1, n. 2, Dezembro.2013. São Paulo: Blucher, 2013.
ISSN 2318-4043, DOI 10.5151/chempro-15bmos-BMOS2013_201381614738

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