Cross-linked aggregates of (R)-oxynitrilase: a stable, recyclable biocatalyst for enantioselective hydrocyanation.
[Reaction: see text] The (R)-oxynitrilase from almonds was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde. The resulting preparation was a highly effective hydrocyanation catalyst under microaqueous conditions, which suppress the nonenzymatic background reaction. The beneficial effect of these latter conditions on the hydrocyanation of slow-reacting aldehydes is demonstrated. The oxynitrilase CLEA was recycled 10 times without loss of activity.
van Langen
Luuk M
LM
Laboratory of Biocatalysis and Organic Chemistry, Delft University of Technology, Julianalaan 136, 2628 BL Delft, The Netherlands.
Selassa
Rhoderick P
RP
van Rantwijk
Fred
F
Sheldon
Roger A
RA
D000446:Aldehyde-Lyases / Q000737:chemistry*; D002384:Catalysis; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000737:chemistry*; D005019:Ethyl Ethers / Q000737:chemistry; D006856:Hydrogen Cyanide / Q000737:chemistry*; D007218:Industrial Microbiology; D015394:Molecular Structure; D027861:Prunus / Q000201:enzymology*; D013237:Stereoisomerism
D004800:Enzymes, Immobilized; D005019:Ethyl Ethers; D006856:Hydrogen Cyanide; D000446:Aldehyde-Lyases; C021541:mandelonitrile lyase; C024683:1,2-dimethoxyethane