Enzymatic resolution of 3-butene-1,2-diol in organic solvents and optimization of reaction conditions
Articolo
Data di Pubblicazione:
1999
Citazione:
Enzymatic resolution of 3-butene-1,2-diol in organic solvents and
optimization of reaction conditions / F. Secundo, M.L. Oppizzi, G. Carrea, M. De Amici, C. Dallanoce. - In: BIOCATALYSIS AND BIOTRANSFORMATION. - ISSN 1024-2422. - 17:3(1999), pp. 241-250.
Abstract:
Lipases from different sources were tested in the kinetic resolution of
2-hydroxy-3-butenyl butanoate {[(R,S)-2] carried out by
transesterification of the secondary alcohol. The influence of organic
solvent. acyl donor and temperature on the enantioselectivity and
activity of lipases was also investigated. Our study showed that both
R-(+)-2 and S-(-)-2 could be obtained in high enantiomeric purity (ee
greater than or equal to 99\%) and satisfactory yield (29\% and 27\%,
respectively). Among the enzymes tested, lipase from Candida antarctica
B (CALB) showed the highest preference for the (R)-enantiomer (E = 26 at
-13 degrees C), whereas lipase from Pseudomonas fluorescens (lipase AK)
acylated the (S)-enantiomer preferentially (E = 18 at -9 degrees C).}
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
(R,S)-2-hydroxy-3-butenyl butanoate; (R,S)-3-butene-1,2-diol; Candida antarctica; Kinetic resolution; Lipases; Pseudomonas fluorescens
Elenco autori:
F. Secundo, M.L. Oppizzi, G. Carrea, M. De Amici, C. Dallanoce
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