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Please use this identifier to cite or link to this item: http://hdl.handle.net/10204/1390

Title: Characterisation of nitrilase and nitrile hydratase biocatalytic systems
Authors: Brady, D
Beeton, A
Zeevaart, J
Kgaje, C
Van Rantwijk, F
Sheldon, RA
Keywords: Bio-catalysts
Applied microbiology
Rhodococcus strains
Carboxylic acids
Issue Date: Mar-2004
Publisher: Springer-Verlag
Citation: Brady, D, et al. 2004. Characterisation of nitrilase and nitrile hydratase biocatalytic systems. Applied Microbiology and Biotechnology, vol 64(1), pp 76 -85.
Abstract: Bio-catalytic transformations converting aromatic and arylaliphatic nitriles into the analogous related amide or acid were investigated.These studies included synthesis of the beta-substituted nitrile 3-hydroxy-3-phenylpropionitrile, subsequent enrichment and isolation on this substrate of nitrite-degrading micro-organisms 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 beta-hydroxy nitriles (but did not demonstrate enantioselectivity on this substrate). The biocatalysts also mediated the synthesis of a range of alpha-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.
URI: http://hdl.handle.net/10204/1390
ISSN: 0175-7598
Appears in Collections:General science, engineering & technology

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