Biocatalytic kinetic resolution of rac‐1‐phenylethanol and rac‐2‐pentanol in hexane medium: ACYL donor and water content effects

Abstract The kinetic resolutions of rac ‐1‐phenylethanol and rac ‐2‐pentanol by transesterification with vinyl esters catalysed by a commercial immobilised Candida antarctica lipase B were successfully carried out in hexane medium. This enzyme showed very high enantioselectivity for both substrates....

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Bibliographic Details
Published in:The Canadian Journal of Chemical Engineering
Main Authors: de los Ríos, A. P., Hernández‐Fernández, F. J., Tomás‐Alonso, F., Gómez, D., Víllora, G.
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2010
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Online Access:http://dx.doi.org/10.1002/cjce.20285
https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fcjce.20285
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cjce.20285
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Summary:Abstract The kinetic resolutions of rac ‐1‐phenylethanol and rac ‐2‐pentanol by transesterification with vinyl esters catalysed by a commercial immobilised Candida antarctica lipase B were successfully carried out in hexane medium. This enzyme showed very high enantioselectivity for both substrates. The influence of the water content of the medium on the synthetic activity, selectivity and enantioselectivity of the enzyme was analysed, with the optimal amount of water about 100 ppm. Our results also showed that the activity per gram enzymatic derivate of CaLB was slightly higher with butyl butyrate as acyl donor.