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Article

Characterization of an Immobilized Amino Acid Racemase for Potential Application in Enantioselective Chromatographic Resolution Processes

1
Department of Physical and Chemical Foundations of Process Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, Sandtorstraße 1, 39106 Magdeburg, Germany
2
Institute of Chemical Engineering, Otto von Guericke University, 39106 Magdeburg, Germany
*
Authors to whom correspondence should be addressed.
Academic Editors: Aniello Costantini and Valeria Califano
Catalysts 2021, 11(6), 726; https://doi.org/10.3390/catal11060726
Received: 19 May 2021 / Revised: 5 June 2021 / Accepted: 6 June 2021 / Published: 11 June 2021
(This article belongs to the Special Issue Enzyme Immobilization and Biocatalysis)
Enantioselective resolution processes can be improved by integration of racemization. Applying environmentally friendly enzymatic racemization under mild conditions is in particular attractive. Owing to the variety of enzymes and the progress in enzyme engineering, suitable racemases can be found for many chiral systems. An amino acid racemase (AAR) from P. putida KT2440 is capable of processing a broad spectrum of amino acids at fast conversion rates. The focus of this study is the evaluation of the potential of integrating AAR immobilized on Purolite ECR 8309 to racemize L- or D-methionine (Met) within an enantioselective chromatographic resolution process. Racemization rates were studied for different temperatures, pH values, and fractions of organic co-solvents. The long-term stability of the immobilized enzyme at operating and storage conditions was found to be excellent and recyclability using water with up to 5 vol% ethanol at 20 °C could be demonstrated. Packed as an enzymatic fixed bed reactor, the immobilized AAR can be coupled with different resolution processes; for instance, with chromatography or with preferential crystallization. The performance of coupling it with enantioselective chromatography is estimated quantitatively, exploiting parametrized sub-models. To indicate the large potential of the AAR, racemization rates are finally given for lysine, arginine, serine, glutamine, and asparagine. View Full-Text
Keywords: racemization; chiral systems; enantioselective resolution; immobilization; process coupling racemization; chiral systems; enantioselective resolution; immobilization; process coupling
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MDPI and ACS Style

Harriehausen, I.; Bollmann, J.; Carneiro, T.; Bettenbrock, K.; Seidel-Morgenstern, A. Characterization of an Immobilized Amino Acid Racemase for Potential Application in Enantioselective Chromatographic Resolution Processes. Catalysts 2021, 11, 726. https://doi.org/10.3390/catal11060726

AMA Style

Harriehausen I, Bollmann J, Carneiro T, Bettenbrock K, Seidel-Morgenstern A. Characterization of an Immobilized Amino Acid Racemase for Potential Application in Enantioselective Chromatographic Resolution Processes. Catalysts. 2021; 11(6):726. https://doi.org/10.3390/catal11060726

Chicago/Turabian Style

Harriehausen, Isabel, Jonas Bollmann, Thiane Carneiro, Katja Bettenbrock, and Andreas Seidel-Morgenstern. 2021. "Characterization of an Immobilized Amino Acid Racemase for Potential Application in Enantioselective Chromatographic Resolution Processes" Catalysts 11, no. 6: 726. https://doi.org/10.3390/catal11060726

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