Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite

Journal Article (2018)
Author(s)

Paula Bracco (TU Delft - BT/Biocatalysis)

G Torrelo Villa (TU Delft - BT/Biocatalysis)

Sander Noordam (Student TU Delft)

Glenn de Jong

Ulf Hanefeld (TU Delft - BT/Biocatalysis)

Research Group
BT/Biocatalysis
Copyright
© 2018 M.P. Bracco Garcia, G. Torrelo Villa, Sander Noordam, Glenn de Jong, U. Hanefeld
DOI related publication
https://doi.org/10.3390/catal8070287
More Info
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Publication Year
2018
Language
English
Copyright
© 2018 M.P. Bracco Garcia, G. Torrelo Villa, Sander Noordam, Glenn de Jong, U. Hanefeld
Research Group
BT/Biocatalysis
Issue number
7
Volume number
8
Reuse Rights

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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.