174849-22-0Relevant academic research and scientific papers
Linum usitatissimum hydroxynitrile lyase cross-linked enzyme aggregates: A recyclable enantioselective catalyst
Cabirol, Fabien L.,Pei, Loo Tan,Tay, Benson,Cheng, Shiryn,Hanefeld, Ulf,Sheldon, Roger A.
, p. 2329 - 2338 (2008)
An immobilized form of the hydroxynitrile lyase from Linum usitatissimum (LuHNL) as cross-linked enzyme aggregate (CLEA) with high specific activity (303.5 U/g) and recovery (33%) was developed. Molecular imprinting using 2-butanone as additive in the immobilization process improved the synthetic activity of the biocatalyst. LuCLEA could be partially recycled for the synthesis of (R)-2-butanone cyanohydrin on a preparative scale over two batches. The enantioenriched cyanohydrin obtained was further hydrolyzed to give (R)-2-hydroxy-2-methylbutyric acid in 85% yield (from 2-butanone) and 87% ee.
Enzyme-catalyzed synthesis of (R)-ketone-cyanohydrins and their hydrolysis to (R)-α-hydroxy-α-methyl-carboxylic acids
Effenberger,Horsch,Weingart,Ziegler,Kuhner
, p. 2605 - 2608 (2007/10/02)
(R)-Ketone-cyanohydrins (R)-2 are obtained with high enantioselectivity from aliphatic ketones 1 and HCN in organic solvents using (R)-oxynitrilase ( EC 4.1.2.10) as catalyst. Acid catalyzed hydrolysis of the cyanohydrins (R)-2 affords the corresponding (R)-α-hydroxy-α-methyl-carboxylic acids (R)-3 without measurable racemization.
