| METHOD |
developing a high-throughput method that uses an enzyme to selectively transform one enantiomer of a catalytic reaction product. As an example, authors use the addition of diethylzinc to benzaldehyde, producing (R)- or (S)-1-phenyl-1-propanol. An alcohol dehydrogenase from a Thermoanaerobium species oxidizes the S enantiomer to phenyl ethyl ketone, and the rate of this oxidation is a direct measure of ee. One hundred samples can be assayed in 30 minutes, with an accuracy of ±10%. A second assay using an alcohol dehydrogenase from Lactobacillus kefir, which oxidizes the R enantiomer, enables calculation of the extent of conversion. According to authors, alcohol dehydrogenases could be used to analyze alcohol products from a wide variety of reactions, including hydrogenation of ketones, aldol reactions, nucleophilic ring opening of epoxides, and kinetic resolution of alcohols. Other enzymes could be harnessed for other compound types: lipases and esterases for ester products of allylic oxidations with tert-butyl peroxybenzoate, alkene cyclopropanation with alkyl diazoacetate, and the glyoxylate ene reaction; and acylases and proteases for amide products of catalytic hydrogenation of N-acetyleneamines. |
| UPDATE | 06.02 |
| AUTHOR | This data is not available for free |
| LITERATURE REF. | This data is not available for free |
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