EC Number |
Application |
Reference |
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4.1.2.10 | agriculture |
hydroxynitrile lyases are involved in the synthesis of enantiomerically pure cyanohydrins which are important intermediates in the production of pharmaceuticals and agrochemicals. The enzyme synthesizes (R)-mandelonitrile in both, batch reaction and fed-batch reaction and can be effectively used in the synthesis of (R)-mandelonitrile |
747466 |
4.1.2.10 | agriculture |
the enzyme has very high potential for synthesis of cyanohydrins and can be used for the production of enantiopure cyanohydrins. Cyanohydrins are important intermediates in the production of pharmaceuticals and agrochemicals |
747465 |
4.1.2.10 | pharmacology |
hydroxynitrile lyases are involved in the synthesis of enantiomerically pure cyanohydrins which are important intermediates in the production of pharmaceuticals and agrochemicals. The enzyme synthesizes (R)-mandelonitrile in both, batch reaction and fed-batch reaction and can be effectively used in the synthesis of (R)-mandelonitrile |
747466 |
4.1.2.10 | pharmacology |
the enzyme has very high potential for synthesis of cyanohydrins and can be used for the production of enantiopure cyanohydrins. Cyanohydrins are important intermediates in the production of pharmaceuticals and agrochemicals |
747465 |
4.1.2.10 | synthesis |
(R)-oxynitrilase immobilized as a cross-linked enzyme aggregate via precipitation with 1,2-dimethoxyethane and subsequent cross-linking using glutaraldehyde is stable and recyclable. Application in microaqueous medium, superior biocatalyst for the enantioselective hydrocyanation of slow-reacting aldehydes |
663008 |
4.1.2.10 | synthesis |
Amygdalus pedunculata hydroxynitrile lyase is an excellent biocatalyst and has very high potential for synthesis of enantiopure cyanohydrins |
747948 |
4.1.2.10 | synthesis |
an easy one-step immobilization of a complex Arabidopsis thaliana hydroxynitrile lyase fusion protein is possible starting from an Escherichia coli crude cell extract (producing a carbohydrate-binding module-containing fusion protein) and cost efficient cellulosic carrier materials. Highly-specific site-selective immobilization of the target protein is achieved by fusing the family 2 carbohydrate-binding module of the exoglucanase/xylanase Cex from Cellulomonas fimi to the target enzyme. This yields a cheap, active, stable and recyclable immobilizate, which can be employed in micro-aqueous reaction systems to enable enantiopure cyanohydrin synthesis |
747367 |
4.1.2.10 | synthesis |
development and validation of a process model for production of (R)-cyanohydrins in an aqueous-organic biphasic-stirred tank reactor with an unknown interfacial area operated in batch mode. The formation of (R)-mandelonitrile from benzaldehyde and cyanide catalyzed by Prunus amygdalus hydroxynitrile lyase is chosen as a model reaction. Methyl tert-butyl ether is selected as the organic solvent and the reaction conditions are 5°C and pH 5.5 at which the nonenzymatic reaction towards rac-mandelonitrile is largely suppressed |
702798 |
4.1.2.10 | synthesis |
fusion of enzyme to different fluorescent reporter proteins. Flavin-based fluorescent reporter fusions convert 95% benzaldehyde to (R)-mandelonitrile within 60 min at pH 4.75, with 96% enantiomeric excess |
726741 |
4.1.2.10 | synthesis |
hydroxynitrile lyases are involved in the synthesis of enantiomerically pure cyanohydrins which are important intermediates in the production of pharmaceuticals and agrochemicals. The enzyme synthesizes (R)-mandelonitrile in both, batch reaction and fed-batch reaction and can be effectively used in the synthesis of (R)-mandelonitrile |
747466 |