Brady, DBeeton, AZeevaart, JKgaje, CVan Rantwijk, FSheldon, RA2007-01-122007-06-072007-01-122007-06-072004-03Brady, D, et al. 2004. Characterisation of nitrilase and nitrile hydratase biocatalytic systems. Applied Microbiology and Biotechnology, vol 64(1), pp 76 -85.0175-7598http://hdl.handle.net/10204/1390http://hdl.handle.net/10204/1390Bio-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.122557 bytesapplication/pdfenCopyright : 2004 Springer-VerlagBio-catalystsBiotechnologyApplied microbiologyRhodococcus strainsNitrilesCarboxylic acidsAmidesCharacterisation of nitrilase and nitrile hydratase biocatalytic systemsArticleBrady, D., Beeton, A., Zeevaart, J., Kgaje, C., Van Rantwijk, F., & Sheldon, R. (2004). Characterisation of nitrilase and nitrile hydratase biocatalytic systems. http://hdl.handle.net/10204/1390Brady, D, A Beeton, J Zeevaart, C Kgaje, F Van Rantwijk, and RA Sheldon "Characterisation of nitrilase and nitrile hydratase biocatalytic systems." (2004) http://hdl.handle.net/10204/1390Brady D, Beeton A, Zeevaart J, Kgaje C, Van Rantwijk F, Sheldon R. Characterisation of nitrilase and nitrile hydratase biocatalytic systems. 2004; http://hdl.handle.net/10204/1390.TY - Article AU - Brady, D AU - Beeton, A AU - Zeevaart, J AU - Kgaje, C AU - Van Rantwijk, F AU - Sheldon, RA AB - 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. DA - 2004-03 DB - ResearchSpace DP - CSIR KW - Bio-catalysts KW - Biotechnology KW - Applied microbiology KW - Rhodococcus strains KW - Nitriles KW - Carboxylic acids KW - Amides LK - https://researchspace.csir.co.za PY - 2004 SM - 0175-7598 T1 - Characterisation of nitrilase and nitrile hydratase biocatalytic systems TI - Characterisation of nitrilase and nitrile hydratase biocatalytic systems UR - http://hdl.handle.net/10204/1390 ER -