High-throughput enzymatic method for enantiomeric excess determination of O-acetylated cyanohydrins

J Am Chem Soc. 2006 Feb 22;128(7):2234-5. doi: 10.1021/ja058474r.

Abstract

The reaction yield and enantiomeric excess of O-acetylated cyanohydrin reaction products from a library of chiral catalysts can be analyzed by a three-step screening method. Alcohol dehydrogenase and NADH are used to analyze unreacted substrate. A lipase with absolute specificity converts one enantiomer to a quantifiable product before the remaining enantiomer is hydrolyzed with an unspecific esterase and quantified.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Benzaldehydes / chemistry
  • Esterases / chemistry*
  • Fungal Proteins
  • Hydrolysis
  • Lipase / chemistry*
  • Liver / enzymology
  • NAD / chemistry
  • Nitriles / analysis
  • Nitriles / chemistry*
  • Stereoisomerism
  • Swine

Substances

  • Benzaldehydes
  • Fungal Proteins
  • Nitriles
  • cyanohydrin
  • NAD
  • Esterases
  • Lipase
  • lipase B, Candida antarctica
  • benzaldehyde