| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 71011 | Journal of Molecular Catalysis B: Enzymatic | 2009 | 6 Pages |
Abstract
The kinetic resolution of 3-hydroxy-4-aryloxybutanenitriles and 3-hydroxy-3-arylpropanenitriles by the nitrile biocatalyst Rhodococcus rhodochrous ATCC BAA-870 was attempted. The nitriles were converted to the corresponding carboxyamides and carboxyacids with enantiomeric excesses (ee) of 0.55 to >99% depending on the substrate. The organism expressed nitrile hydratase and amidase activities responsible for these biotransformations.
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Authors
H.H. Kinfe, V. Chhiba, J. Frederick, M.L. Bode, K. Mathiba, P.A. Steenkamp, D. Brady,
