Enzymatic resolution of 3-butene-1,2-diol in organic solvents and optimization of reaction conditions

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 invest...

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Bibliographic Details
Published in:Biocatalysis and Biotransformation
Main Authors: F. Secundo, M. L. Oppizzi, G. Carrea, M. De Amici, C. Dallanoce
Other Authors: M.L. Oppizzi
Format: Article in Journal/Newspaper
Language:English
Published: HARWOOD ACAD PUBL GMBH 1999
Subjects:
(R,S)-2-hydroxy-3-butenyl butanoate
(R,S)-3-butene-1,2-diol
Candida antarctica
Kinetic resolution
Lipase
Pseudomonas fluorescens
Settore CHIM/08 - Chimica Farmaceutica
Antarc*
Antarctica
Online Access:http://hdl.handle.net/2434/183359
https://doi.org/10.3109/10242429909040117
Description
Summary: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).}

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