The performance of (S)-oxynitrilase from Hevea brasiliensis (HbHNL) has been investigated with several α- and β-substituted alkyl or alkoxy aldehydes and the results have been compared to the data previously obtained with the (R)-specific enzyme from almonds (PaHNL). With both enzymes there was no chiral discrimination between the enantiomers of the racemic substrates, therefore this reaction cannot be used as a preparative method to achieve both the kinetic resolution of the starting racemic aldehyde and the production of diastereomerically pure (or enriched) cyanohydrins. Additionally, in comparison with the (R)-PaHNL the (S)-selective enzyme from Hevea gave products with higher de, but was more negatively effected by oxygenated substituents.
Selectivity of the (S)-oxynitrilase from Hevea brasiliensis towards α- and β-substituted aldehydes / G. Roda, S. Riva, B. Danieli, H. Griengl, U. Rinner, M. Schmidt, A. Mackova Zabelinskaja. - In: TETRAHEDRON. - ISSN 0040-4020. - 58:15(2002), pp. 2979-2983.
Selectivity of the (S)-oxynitrilase from Hevea brasiliensis towards α- and β-substituted aldehydes
G. Roda;B. Danieli;
2002
Abstract
The performance of (S)-oxynitrilase from Hevea brasiliensis (HbHNL) has been investigated with several α- and β-substituted alkyl or alkoxy aldehydes and the results have been compared to the data previously obtained with the (R)-specific enzyme from almonds (PaHNL). With both enzymes there was no chiral discrimination between the enantiomers of the racemic substrates, therefore this reaction cannot be used as a preparative method to achieve both the kinetic resolution of the starting racemic aldehyde and the production of diastereomerically pure (or enriched) cyanohydrins. Additionally, in comparison with the (R)-PaHNL the (S)-selective enzyme from Hevea gave products with higher de, but was more negatively effected by oxygenated substituents.Pubblicazioni consigliate
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