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 1999, Vol.17 (3), p.241-250
Main Authors: Secundo, Francesco, Oppizzi, Maria LUISA, Carrea, Giacomo, Amici, Marco DE, Dallanoce, Clelia
Format: Article
Language:English
Subjects:
(R, S)-2-Hydroxy-3-butenyl butanoate
(R, S)-3-butene-1,2 diol
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Candida aniarctica
Fundamental and applied biological sciences. Psychology
Kinetic resolution
Lipases
Methods. Procedures. Technologies
Pseudomonas fluorescens
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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 ≥ 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°C), whereas lipase from Pseudomonas fluorescens (lipase AK) acylated the (S)-enantiomer preferentially (E= 18 at -9°C).
ISSN:1024-2422
1029-2446
DOI:10.3109/10242429909040117