Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite

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

doi:10.3390/catal8070287

Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite

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

BT/Biocatalysis

Research output: Contribution to journal › Article › Scientific › peer-review

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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 language	English
Article number	287
Number of pages	10
Journal	Catalysts
Volume	8
Issue number	7
DOIs	https://doi.org/10.3390/catal8070287
Publication status	Published - 17 Jul 2018

Keywords

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

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title = "Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite",

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.",

keywords = "biocatalysis, hydroxynitrile lyase, Oxynitrilase, immobilization, Celite, diffusion, cyanohydrin, OA-Fund TU Delft",

author = "{Bracco Garcia}, Paula and {Torrelo Villa}, Guzman and Sander Noordam and {de Jong}, Glenn and Ulf Hanefeld",

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doi = "10.3390/catal8070287",

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AU - Bracco Garcia, Paula

AU - Torrelo Villa, Guzman

AU - Noordam, Sander

AU - de Jong, Glenn

AU - Hanefeld, Ulf

PY - 2018/7/17

Y1 - 2018/7/17

N2 - 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.

AB - 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.

KW - biocatalysis

KW - hydroxynitrile lyase

KW - Oxynitrilase

KW - immobilization

KW - Celite

KW - diffusion

KW - cyanohydrin

KW - OA-Fund TU Delft

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