Lipase Mediated Resolution of γ-Branched Chain Fatty Acid Methyl Esters

Autor:	A. de Sousa Teixeira, N.W.J.T. Heinsman, Maurice C. R. Franssen, Jaap A. Jongejan, A. van der Padt, Ae. de Groot, S.C. Orrenius, C.L.M. Marcelis
Rok vydání:	1998
Předmět:	biology Stereochemistry Rhizomucor miehei Transesterification biology.organism_classification Biochemistry Catalysis Kinetic resolution chemistry.chemical_compound chemistry biology.protein Organic chemistry Candida antarctica Ethyl group Lipase Enantiomer Biotechnology
Zdroj:	Scopus-Elsevier
ISSN:	1029-2446 1024-2422
DOI:	10.3109/10242429809003618
Popis:	Kinetic resolution of the branched chain fatty acid (BCFA) esters 4-methylhexanoic acid methyl ester (4) and 4-methyloctanoic acid methyl ester (5) was investigated using a series of hydrolases as catalysts. In the transesterification of these methyl esters to their butyl esters, two enzymes showed good conversion and a moderate enantiomeric ratio (E). In the transesterification of 4, an E of 2 was obtained for the reaction catalysed by Rhizomucor miehei lipase, whereas Candida antarctica lipase B (CALB) showed an E of 5. In the conversion of 5 to the butyl ester, Rhizomucor miehei lipase was unselective whereas CALB gave an E of 8. Apparently, changing from an ethyl group to a butyl group at the chiral centre leads to an improved chiral recognition by CALB. The lipases displayed complementary enantiomeric preference. Rhizomucor miehei lipase favours the S-enantiomer of 4 while CALB preferentially transforms the R-cnantiomer of both substrates. Molecular modelling studies supported the measured stereochem...
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::985f2ae88ca6058f9da6a5b27701b1b0 https://doi.org/10.3109/10242429809003618 Zobrazit plný text záznamu