Selectivity of the (S)-oxynitrilase from Hevea brasiliensis towards α- and β-substituted aldehydes

Gabriella Roda, Sergio Riva, Bruno Danieli, Herfried Griengl, Uwe Rinner, Michael Schmidt, Antonina Mackova Zabelinskaja

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18 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2979-2983
Number of pages5
JournalTetrahedron
Volume58
Issue number15
DOIs
Publication statusPublished - Apr 8 2002

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Keywords

  • Cyanohydrins
  • Hevea brasiliensis
  • Oxynitrilases
  • Prunus amygdalus
  • Substituted aldehydes

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry

Cite this

Roda, G., Riva, S., Danieli, B., Griengl, H., Rinner, U., Schmidt, M., & Mackova Zabelinskaja, A. (2002). Selectivity of the (S)-oxynitrilase from Hevea brasiliensis towards α- and β-substituted aldehydes. Tetrahedron, 58(15), 2979-2983. https://doi.org/10.1016/S0040-4020(02)00187-4