Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite

Paula Bracco Garcia, Guzman Torrelo Villa, Sander Noordam, Glenn de Jong, Ulf Hanefeld

Research output: Contribution to journalArticleScientificpeer-review

7 Citations (Scopus)
31 Downloads (Pure)

Abstract

The hydroxynitrile lyase from Prunus amygdalus was immobilized on Celite R-633. The immobilized enzyme could successfully be utilized in buffer saturated MTBE and excellent conversions of benzaldehyde to R-mandelonitrile were observed. No leaching occurred. To achieve high enantioselectivities, the suppression of the undesired background reaction was essential. This could be achieved by high enzyme loadings and the tight packing of the immobilized enzymes. When the immobilized enzyme is loosely packed, both the enzyme catalysis and the background reaction accelerates and only a modest enantioselectivity is observed. The enzyme was recycled for up to ten times, with some loss of activity and also enantioselectivity after 5 cycles, independent of packing.
Original languageEnglish
Article number287
Number of pages10
JournalCatalysts
Volume8
Issue number7
DOIs
Publication statusPublished - 17 Jul 2018

Keywords

  • biocatalysis
  • hydroxynitrile lyase
  • Oxynitrilase
  • immobilization
  • Celite
  • diffusion
  • cyanohydrin
  • OA-Fund TU Delft

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