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Keywords = benzaldehyde lyase

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17 pages, 948 KiB  
Article
Rigorous Model-Based Design and Experimental Verification of Enzyme-Catalyzed Carboligation under Enzyme Inactivation
by Dominik Hertweck, Victor N. Emenike, Antje C. Spiess and René Schenkendorf
Catalysts 2020, 10(1), 96; https://doi.org/10.3390/catal10010096 - 9 Jan 2020
Cited by 1 | Viewed by 2877
Abstract
Enzyme catalyzed reactions are complex reactions due to the interplay of the enzyme, the reactants, and the operating conditions. To handle this complexity systematically and make use of a design space without technical restrictions, we apply the model based approach of elementary process [...] Read more.
Enzyme catalyzed reactions are complex reactions due to the interplay of the enzyme, the reactants, and the operating conditions. To handle this complexity systematically and make use of a design space without technical restrictions, we apply the model based approach of elementary process functions (EPF) for selecting the best process design for enzyme catalysis problems. As a representative case study, we consider the carboligation of propanal and benzaldehyde catalyzed by benzaldehyde lyase from Pseudomonas fluorescens (PfBAL) to produce (R)-2-hydroxy-1-phenylbutan-1-one, because of the substrate dependent reaction rates and the challenging substrate dependent PfBAL inactivation. The apparatus independent EPF concept optimizes the material fluxes influencing the enzyme catalyzed reaction for the given process intensification scenarios. The final product concentration is improved by 13% with the optimized feeding rates, and the optimization results are verified experimentally. In general, the rigorous model driven approach could lead to selecting the best existing reactor, designing novel reactors for enzyme catalysis, and combining protein engineering and process systems engineering concepts. Full article
(This article belongs to the Special Issue Biocatalytic Applications in Biotechnology)
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10 pages, 2057 KiB  
Article
Immobilization of Prunus amygdalus Hydroxynitrile Lyase on Celite
by Paula Bracco, Guzman Torrelo, Sander Noordam, Glenn De Jong and Ulf Hanefeld
Catalysts 2018, 8(7), 287; https://doi.org/10.3390/catal8070287 - 17 Jul 2018
Cited by 12 | Viewed by 4987
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Immobilized Biocatalysts)
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