Print Email Facebook Twitter Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite Title Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite Author Bracco Garcia, M.P. (TU Delft BT/Biocatalysis) Torrelo Villa, G. (TU Delft BT/Biocatalysis) Noordam, Sander (Student TU Delft) de Jong, Glenn Hanefeld, U. (TU Delft BT/Biocatalysis) Date 2018-07-17 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. Subject biocatalysishydroxynitrile lyaseOxynitrilaseimmobilizationCelitediffusioncyanohydrinOA-Fund TU Delft To reference this document use: http://resolver.tudelft.nl/uuid:18c6968c-2def-48cb-a14d-a2871ea973ad DOI https://doi.org/10.3390/catal8070287 ISSN 2073-4344 Source Catalysts, 8 (7) Part of collection Institutional Repository Document type journal article Rights © 2018 M.P. Bracco Garcia, G. Torrelo Villa, Sander Noordam, Glenn de Jong, U. Hanefeld Files PDF catalysts_08_00287.pdf 1.11 MB Close viewer /islandora/object/uuid:18c6968c-2def-48cb-a14d-a2871ea973ad/datastream/OBJ/view