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- W2085656419 abstract "Abstract Recombinant Escherichia coli strains were constructed which simultaneously expressed the genes encoding the ( S )‐oxynitrilase from cassava ( Manihot esculenta ) together with the wild‐type or a mutant variant of the arylacetonitrilase from Pseudomonas fluorescens EBC191 in a single organism under the control of a rhamnose‐inducible promoter. The whole cell catalysts obtained converted benzaldehyde and potassium cyanide in aqueous media at pH 5.2 mainly to ( S )‐mandelic acid and/or ( S )‐mandelic amide and synthesized only low amounts of the corresponding ( R )‐enantiomers. The conversion of benzaldehyde and potassium cyanide (KCN) by a whole‐cell catalyst simultaneously expressing the ( S )‐oxynitrilase and the wild‐type nitrilase resulted in a ratio of ( S )‐mandelic acid to ( S )‐mandelic amide of about 4:3. This could be explained by the strong nitrile hydratase activity of the wild‐type nitrilase with ( S )‐mandelonitrile as substrate. The relative proportion of ( S )‐mandelic amide formed in this system was significantly increased by coexpressing the ( S )‐oxynitrilase with a carboxy‐terminally truncated variant of the nitrilase. This whole‐cell catalyst converted benzaldehyde and KCN to mandelic amide and mandelic acid in a ratio of about 9:1. The ee of the ( S )‐mandelic amide formed was calculated to be >95%." @default.
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- W2085656419 date "2009-07-01" @default.
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- W2085656419 title "Construction of Recombinant<i>Escherichia coli</i>Catalysts which Simultaneously Express an (<i>S</i>)-Oxynitrilase and Different Nitrilase Variants for the Synthesis of (<i>S</i>)-Mandelic Acid and (<i>S</i>)-Mandelic Amide from Benzaldehyde and Cyanide" @default.
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- W2085656419 doi "https://doi.org/10.1002/adsc.200900087" @default.
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