Enzymatic Resolution Of 3-Butene-1, 2-Diol In Organic Solvents And Optimization Of Reaction Conditions

• Published in: Biocatalysis and biotransformation Vol. 17; no. 3; pp. 241 - 250
• Main Authors: Secundo, Francesco, Oppizzi, Maria LUISA, Carrea, Giacomo, Amici, Marco DE, Dallanoce, Clelia
• Format: Journal Article
• Language: English
• Published: Abingdon Informa UK Ltd 1999; Taylor & Francis; Taylor and Francis
• 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; Pseudomonadales; Yeast; Enantioselectivity; Enzyme; Triacylglycerol lipase; Environmental factor; Esterases; Pseudomonas fluorescens; Transesterification; Optimization; Carboxylic ester hydrolases; Fungi; Organic solvent; Optical resolution; Bacteria; Hydrolases; Pseudomonadaceae; Fungi Imperfecti; Thallophyta; Enzymatic reaction
• ISSN: 1024-2422; 1029-2446
• DOI: 10.3109/10242429909040117

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).