A study on the enzyme catalysed enantioselective hydrolysis of methyl 2-methyl-4-oxopentanoate, a precursor of chiral gamma-butyrolactones

Author(s)

Ferreira, Edgard A. ^{[1, 2]} ; Rodezno, Sindy V. A. ^[1] ; Omori, Alvaro T. ^[1] ; Cunha, Rodrigo L. O. R. ^[1]

Affiliation

^[1] Univ Fed ABC, Ctr Ciencias Nat & Humanas, Santo Andre - Brazil

^[2] Univ Presbiteriana Mackenzie, Escola Engn, Sao Paulo - Brazil

• Document type: Journal article
• Source: BIOCATALYSIS AND BIOTRANSFORMATION; v. 37, n. 2, p. 115-123, MAR 4 2019.
• Web of Science Citations: 2

Abstract

Porcine pancreas lipase (PPL) resolution of the alpha-methyl group of racemic methyl 2-methyl-4-oxopentanoate, a valuable synthetic precursor of fragrances and marine natural products, was enhanced by salt modulation of the enzymatic hydrolysis. For the enantioselective hydrolysis of the title ester, PPL was selected from a series of esterases and lipases, and its enantioselectivity was evaluated by changing the reaction medium parameters. The use of 1.6 mol L-1 sodium sulfate in phosphate buffer (pH 7.2) improved the enantioselectivity allowing the formation of methyl (2R)-(+)-2-methyl-4-oxopentanoate and (2S)-(-)-2-methyl-4-oxopentanoic acid with an enantiomeric excess of >99% and 71%, respectively. The study showed that a modulation of PPL enantioselectivity could be achieved by using kosmotropic salts in the reaction media. The present method consists of a practical and low-cost option to improve enzymatic kinetic resolution reactions. (AU)

• FAPESP's process: 09/00617-2 - Biocatalysis: the use of plant cells and lipases in organic synthesis - application on asymmetric synthesis of biologically active compounds
• Grantee: Alvaro Takeo Omori
• Support Opportunities: Research Grants - Young Investigators Grants