Absolute configurations of monoesters produced by enzyme catalyzed hydrolysis of DIETHYL 3-HYDROXYGLUTARATE (cas 18373-31-4)

Add time:08/28/2019    Source:sciencedirect.com

Biocatalytic asymmetrizations of diethyl 3-hydroxyglutarate furnish a route to the enantiomers of ethyl 4-cyano-3-hydroxybutanoate. The enantiopreference of different enzymes has been established by chiral chromatography. Conclusive evidence for absolute configurations has been provided by X-ray crystallographic structure determination of co-crystals of the predominant monoester with (R)-phenylethylamine. The predominant enantiopure monoester produced by ammonolysis of diethyl 3-hydroxyglutarate catalyzed by immobilized lipase B from Candida antarctica (Novozym 435) was ethyl (3S)-4-carbamoyl-3-hydroxybutanoate. This was converted to ethyl (3S)-4-cyano-3-hydroxybutanoate in high yield and enantiomeric excess. Growing cells of Acinetobacter lwoffii gave low ee and predominance of the (S)-enantiomer when used for hydrolysis of diethyl 3-hydroxyglutarate as opposed to previous reports. When Novozym 435 was used for hydrolysis it could be re-used 10 times without loss of activity and selectivity.

We also recommend Trading Suppliers and Manufacturers of DIETHYL 3-HYDROXYGLUTARATE (cas 18373-31-4). Pls Click Website Link as below: cas 18373-31-4 suppliers

Prev:Enantioselective hydrolysis of DIETHYL 3-HYDROXYGLUTARATE (cas 18373-31-4) to ethyl (S)-3-hydroxyglutarate by immobilized Candida antarctica lipase B
Next:Bifunctional chiral synthons via biochemical methods. 5. Preparation of (S)-ethyl hydrogen-3-hydroxyglutarate, key intermediate to (R)-4-amino-3-hydroxybutyric acid and L-carnitine.)