Enzymatic hydrolysis of cyanohydrins with recombinant nitrile hydratase and amidase from Rhodococcus erythropolis

Biotechnol Lett. 2004 Nov;26(21):1675-80. doi: 10.1007/s10529-004-3521-4.

Abstract

Nitrile hydratase and amidase from Rhodococcus erythropolis CIMB11540 were both cloned and expressed in Escherichia coli. Crude cell free extracts were used for the hydrolysis of different aromatic cyanohydrins. Nitrile hydratase expression was increased up to 5-fold by redesign of the expression cassette. The recombinant enzymes were successfully used for the conversion of several cyanohydrins to the corresponding alpha-hydroxy amides and acids while retaining enantiopurity.

Publication types

  • Comparative Study
  • Evaluation Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / chemistry
  • Amidohydrolases / genetics
  • Amidohydrolases / metabolism*
  • Cloning, Molecular / methods
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Hydro-Lyases / chemistry
  • Hydro-Lyases / genetics
  • Hydro-Lyases / metabolism*
  • Hydrolysis
  • Nitriles / chemistry
  • Nitriles / metabolism*
  • Protein Engineering / methods*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Rhodococcus / classification
  • Rhodococcus / enzymology*
  • Rhodococcus / genetics

Substances

  • Nitriles
  • Recombinant Proteins
  • cyanohydrin
  • Amidohydrolases
  • amidase
  • Hydro-Lyases
  • nitrile hydratase