Cross-Linked Aggregates of (R)-Oxynitrilase: A Stable, Recyclable Biocatalyst for Enantioselective Hydrocyanation

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 supp...

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Bibliographic Details
Published in:	Organic letters Vol. 7; no. 2; pp. 327 - 329
Main Authors:	van Langen, Luuk M, Selassa, Rhoderick P, van Rantwijk, Fred, Sheldon, Roger A
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 20-01-2005
Subjects:	Aldehyde-Lyases - chemistry Catalysis Enzyme Stability Enzymes, Immobilized - chemistry Ethyl Ethers - chemistry Hydrogen Cyanide - chemistry Industrial Microbiology Molecular Structure Prunus - enzymology Stereoisomerism
Online Access:	Get full text
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Summary:	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.
ISSN:	1523-7060 1523-7052
DOI:	10.1021/ol047647z