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Enzymatic kinetic resolution of methyl 2-methyl-4-oxopentanoate
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.
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.
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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-40-40.
In: In Blucher Chemistry Proceedings, São Paulo, v. 1, n. 2, Dezembro.2013.
São Paulo: Blucher,
2013.
ISSN 23184043,
DOI 10.5151/chempro-15bmos-BMOS2013_201381614738
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TY - CONF T1 - Enzymatic kinetic resolution of methyl 2-methyl-4-oxopentanoate JO - Blucher Chemistry Proceedings VL - 1 IS - 2 SP - 40 EP - 40 PY - 2013 T2 - Brazilian Meeting on Organic Synthesis 2013 AU - , , SN - 23184043 DO - http://dx.doi.org/10.5151/chempro-15bmos-BMOS2013_201381614738 UR - www.proceedings.blucher.com.br/article-details/enzymatic-kinetic-resolution-of-methyl-2-methyl-4-oxopentanoate-8260 KW - ER -
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@article{Ferreira20144,
title="Enzymatic kinetic resolution of methyl 2-methyl-4-oxopentanoate",
journal="Blucher Chemistry Proceedings",
volume="1",
number="2",
pages="40 - 40",
year="2013",
note="",
issn="23184043",
doi="http://dx.doi.org/10.5151/chempro-15bmos-BMOS2013_201381614738",
url="www.proceedings.blucher.com.br/article-details/enzymatic-kinetic-resolution-of-methyl-2-methyl-4-oxopentanoate-8260",
author="Edgard A. Ferreira", "Álvaro T. Omori", "Rodrigo L. O. R. Cunha",
keywords="",
}
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Edgard A. Ferreira, Álvaro T. Omori, Rodrigo L. O. R. Cunha, Enzymatic kinetic resolution of methyl 2-methyl-4-oxopentanoate, Blucher Chemistry Proceedings, Volume 1, 2013, Pages 40-40, ISSN 23184043, http://dx.doi.org/10.5151/chempro-15bmos-BMOS2013_201381614738 (www.proceedings.blucher.com.br/article-details/enzymatic-kinetic-resolution-of-methyl-2-methyl-4-oxopentanoate-8260) Palavras-chave:: ;