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Catalysts 2018, 8(7), 287; https://doi.org/10.3390/catal8070287

Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite

Biokatalyse, Afdeling Biotechnologie, Technische Universiteit Delft, Van der Maasweg 9, 2629 HZ Delft, The Netherlands
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Received: 29 June 2018 / Revised: 12 July 2018 / Accepted: 13 July 2018 / Published: 17 July 2018
(This article belongs to the Special Issue Immobilized Biocatalysts)
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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. View Full-Text
Keywords: biocatalysis; hydroxynitrile lyase; Oxynitrilase; immobilization; Celite; diffusion; cyanohydrin biocatalysis; hydroxynitrile lyase; Oxynitrilase; immobilization; Celite; diffusion; cyanohydrin
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Bracco, P.; Torrelo, G.; Noordam, S.; De Jong, G.; Hanefeld, U. Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite. Catalysts 2018, 8, 287.

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