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• W2097421027 startingPage "715" @default.
• W2097421027 abstract "The bacterial strain Rhodococcus butanica (ATCC 21197), which exhibits nitrilase and nitrile hydratase/amidase activities, catalyses the enantioselective hydrolysis of racemic naproxen nitrile (R/S)-1 to furnish a moderate enantiomeric excess of (S)-naproxen (S)-3. Racemic naproxen amide (R/S)-2 is not a good substrate for this strain. Resting cells of the newly selected bacterial strain Rhodococcus sp. C3II catalyse the enantioselective hydrolyses of racemic naproxen nitrile (R/S)-1 and naproxen amide (R/S)-2 as well, to give (S)-3 in excellent optical (99 % e.e.) and good chemical yields in aqueous medium and in the biphasic system of phosphate buffer/hexane." @default.
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• W2097421027 date "1994-07-01" @default.
• W2097421027 modified "2023-10-10" @default.
• W2097421027 title "Enzyme-catalysed enantioselective hydrolysis of racemic naproxen nitrile" @default.
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• W2097421027 doi "https://doi.org/10.1016/0968-0896(94)85022-4" @default.
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