Applied Microbiology and Biotechnology

, Volume 64, Issue 1, pp 76–85

Characterisation of nitrilase and nitrile hydratase biocatalytic systems

Authors

    • CSIR Bio/Chemtek
  • A. Beeton
    • CSIR Bio/Chemtek
  • J. Zeevaart
    • CSIR Bio/Chemtek
  • C. Kgaje
    • CSIR Bio/Chemtek
  • F. van Rantwijk
    • Laboratory of Organic Chemistry and CatalysisDelft University of Technology
  • R. A. Sheldon
    • Laboratory of Organic Chemistry and CatalysisDelft University of Technology
Original Paper

DOI: 10.1007/s00253-003-1495-0

Cite this article as:
Brady, D., Beeton, A., Zeevaart, J. et al. Appl Microbiol Biotechnol (2004) 64: 76. doi:10.1007/s00253-003-1495-0

Abstract

Biocatalytic transformations converting aromatic and arylaliphatic nitriles into the analogous related amide or acid were investigated. These studies included synthesis of the β-substituted nitrile 3-hydroxy-3-phenylpropionitrile, subsequent enrichment and isolation on this substrate of nitrile-degrading microorganisms from the environment, and a comparative study of enzymatic reactions of nitriles by resting cell cultures and enzymes. Each biocatalyst exhibited a distinctive substrate selectivity profile, generally related to the length of the aliphatic chain of the arylaliphatic nitrile and the position of substituents on the aromatic ring or aliphatic chain. Cell-free nitrilases generally exhibited a narrower substrate range than resting whole cells of Rhodococcus strains. The Rhodococcus strains all exhibited nitrile hydratase activity and converted β-hydroxy nitriles (but did not demonstrate enantioselectivity on this substrate). The biocatalysts also mediated the synthesis of a range of α-hydroxy carboxylic acids or amides from aldehydes in the presence of cyanide. The use of an amidase inhibitor permits halting the nitrile hydratase/amidase reaction at the amide intermediate.

Copyright information

© Springer-Verlag 2004