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Open AccessArticle

Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite

Biokatalyse, Afdeling Biotechnologie, Technische Universiteit Delft, Van der Maasweg 9, 2629 HZ Delft, The Netherlands
Author to whom correspondence should be addressed.
Catalysts 2018, 8(7), 287;
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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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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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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