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.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
H.H. Kinfe, V. Chhiba, J. Frederick, M.L. Bode, K. Mathiba, P.A. Steenkamp, D. Brady,