Syntheses of enantiopure aliphatic secondary alcohols and acetates by bioresolution with lipase B from Candida antarctica.

Molecules

Institute of Chemistry of São Carlos, University of São Paulo, Av. Trabalhador São-carlense 400, 13560-970 São Carlos, SP, Brazil.

Published: July 2012

AI Article Synopsis

  • The lipase B from Candida antarctica (Novozym 435®) was effective in separating enantiomers of several aliphatic secondary alcohols, showing high selectivity.
  • The enzyme produced enantiopure alcohols and acetates with over 99% enantiomeric excess (ee) and yielded good results.
  • Kinetic resolution was accomplished using straightforward conditions, employing vinyl acetate as the acylating agent and hexane as the solvent.

Article Abstract

The lipase B from Candida antarctica (Novozym 435®, CALB) efficiently catalyzed the kinetic resolution of some aliphatic secondary alcohols: (±)-4-methylpentan-2-ol, (±)-5-methylhexan-2-ol, (±)-octan-2-ol, (±)-heptan-3-ol and (±)-oct-1-en-3-ol. The lipase showed excellent enantioselectivities in the transesterifications of racemic aliphatic secondary alcohols producing the enantiopure alcohols (>99% ee) and acetates (>99% ee) with good yields. Kinetic resolution of rac-alcohols was successfully achieved with CALB lipase using simple conditions, vinyl acetate as acylating agent, and hexane as non-polar solvent.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6268719PMC
http://dx.doi.org/10.3390/molecules17088955DOI Listing

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