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

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

18 Citations (Scopus)


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
Issue number15
Publication statusPublished - Apr 8 2002


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

ASJC Scopus subject areas

  • Biochemistry
  • Drug Discovery
  • Organic Chemistry


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