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 language | English |
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Article number | 287 |
Number of pages | 10 |
Journal | Catalysts |
Volume | 8 |
Issue number | 7 |
DOIs | |
Publication status | Published - 17 Jul 2018 |
Keywords
- biocatalysis
- hydroxynitrile lyase
- Oxynitrilase
- immobilization
- Celite
- diffusion
- cyanohydrin
- OA-Fund TU Delft