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Co-Immobilization of Ketoreductase and Glucose Dehydrogenase

1
Institute of Biotechnology, Faculty of Chemical and Food Technology, Slovak University of Technology, Radlinského 9, 812 37 Bratislava, Slovakia
2
Department of Chemistry, University of Crete, Heraklion 71003, Greece
*
Author to whom correspondence should be addressed.
Catalysts 2018, 8(4), 168; https://doi.org/10.3390/catal8040168
Received: 29 March 2018 / Revised: 12 April 2018 / Accepted: 18 April 2018 / Published: 20 April 2018
(This article belongs to the Special Issue Immobilized Biocatalysts)
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Abstract

A two-enzyme system composed of immobilized ketoreductase (Hansenula polymorpha) and glucose dehydrogenase (Bacillus megaterium) was developed for the asymmetric reduction of keto esters to optically active hydroxy esters via immobilization in polyvinyl alcohol (PVA) gel particles. The concentration of enzymes was optimized, and the final particles were used 18 times in a row in a batch mode to achieve minimal loss of activity and complete conversion of the model substrate, β-ketoester ethyl-2-methylacetoacetate. Excellent stability was also achieved using new storage conditions of PVA particles, with 80% of activity being retained after almost 10 months. View Full-Text
Keywords: ketoreductase; co-immobilization; PVA gel ketoreductase; co-immobilization; PVA gel
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Petrovičová, T.; Markošová, K.; Hegyi, Z.; Smonou, I.; Rosenberg, M.; Rebroš, M. Co-Immobilization of Ketoreductase and Glucose Dehydrogenase. Catalysts 2018, 8, 168.

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