Enzymatic synthesis of a chiral chalcogran intermediate

Abstract Two lipases, Novozyme 435 (lipase B from Candida Antarctica) and Lipozyme TL IM (Thermomyces lanuginosus) were used successfully for the kinetic resolution of racemic 1-(2-furyl)-3-pentanol, the key intermediate in synthesis of the bark beetle pheromone, chalcogran. The desired S-(+)-enanti...

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Bibliographic Details
Published in:Chemical Papers
Main Authors: Mastihuba, Vladimír, Čepec, Pavel, Vlčková, Silvia, Farkašová, Erika, Mastihubová, Mária, Bobal, Pavel
Format: Article in Journal/Newspaper
Language:unknown
Published: Springer Science and Business Media LLC 2014
Subjects:
Materials Chemistry
Industrial and Manufacturing Engineering
General Chemical Engineering
Biochemistry
General Chemistry
Antarc*
Antarctica
Online Access:http://dx.doi.org/10.2478/s11696-013-0523-5
http://link.springer.com/content/pdf/10.2478/s11696-013-0523-5
Description
Summary:Abstract Two lipases, Novozyme 435 (lipase B from Candida Antarctica) and Lipozyme TL IM (Thermomyces lanuginosus) were used successfully for the kinetic resolution of racemic 1-(2-furyl)-3-pentanol, the key intermediate in synthesis of the bark beetle pheromone, chalcogran. The desired S-(+)-enantiomer was prepared in enantiomeric excesses higher than 98 % and with yields of 26.3 % and 32.5 %, respectively. Methyl tert-butyl ether and vinyl acetate were found to be the best reaction media and the acetyl donor to achieve fast and effective resolution.

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