A study on the enzyme catalysed enantioselective hydrolysis of methyl 2-methyl-4-oxopentanoate, a precursor of chiral γ-butyrolactones
Tipo
Artigo
Data de publicação
2019
Periódico
Biocatalysis and Biotransformation
Citações (Scopus)
4
Autores
Ferreira E.A.
Rodezno S.V.A.
Omori A.T.
Cunha R.L.O.R.
Rodezno S.V.A.
Omori A.T.
Cunha R.L.O.R.
Orientador
Título da Revista
ISSN da Revista
Título de Volume
Membros da banca
Programa
Resumo
© 2018, © 2018 Informa UK Limited, trading as Taylor & Francis Group. Porcine pancreas lipase (PPL) resolution of the α-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.
Descrição
Palavras-chave
Assuntos Scopus
Enantiomeric excess , Enantioselective hydrolysis , Enzymatic kinetic resolutions , Hofmeister effects , Marine natural products , Porcine pancreas lipase , Salting out , Synthetic precursors