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Open AccessArticle

Immobilized Whole-Cell Transaminase Biocatalysts for Continuous-Flow Kinetic Resolution of Amines

1
Department of Organic Chemistry and Technology, Budapest University of Technology and Economics, Műegyetem rkp. 3, 1111 Budapest, Hungary
2
Fermentia Microbiological Ltd., Berlini út 47–49, 1405 Budapest, Hungary
3
Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Science, Magyar tudósok krt. 2, 1117 Budapest, Hungary
4
Institute of Chemistry, University of Graz, NAWI Graz, BioTechMed Graz, BioHealth, Heinrichstraße 28, 8010 Graz, Austria
5
Department of Applied Biotechnology and Food Science, Budapest University of Technology and Economics, Műegyetem rkp. 3, 1111 Budapest, Hungary
6
Biocatalysis and Biotransformation Research Centre, Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University of Cluj-Napoca, Arany János Str. 11, RO-400028 Cluj-Napoca, Romania
7
SynBiocat Ltd., Szilasliget u 3, H-1172 Budapest, Hungary
*
Author to whom correspondence should be addressed.
Catalysts 2019, 9(5), 438; https://doi.org/10.3390/catal9050438
Received: 29 March 2019 / Revised: 25 April 2019 / Accepted: 25 April 2019 / Published: 10 May 2019
(This article belongs to the Special Issue Flow Biocatalysis)
Immobilization of transaminases creates promising biocatalysts for production of chiral amines in batch or continuous-flow mode reactions. E. coli cells containing overexpressed transaminases of various selectivities and hollow silica microspheres as supporting agent were immobilized by an improved sol-gel process to produce immobilized transaminase biocatalysts with suitable stability and mechanical properties for continuous-flow applications. The immobilized cell-based transaminase biocatalyst proved to be durable and easy-to-use in kinetic resolution of four racemic amines 1ad. The batch and continuous-flow mode kinetic resolutions with transaminase biocatalyst of opposite stereopreference provided access to both enantiomers of the corresponding amines. By using the most suitable immobilized transaminase biocatalysts, this study describes the first transaminase-based approach for the production of both pure enantiomers of 1-(3,4-dimethoxyphenyl)ethan-1-amine 1d. View Full-Text
Keywords: stereoselective biocatalysis; transaminase; kinetic resolution; flow chemistry; sol-gel; whole-cell immobilization stereoselective biocatalysis; transaminase; kinetic resolution; flow chemistry; sol-gel; whole-cell immobilization
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MDPI and ACS Style

Molnár, Z.; Farkas, E.; Lakó, Á.; Erdélyi, B.; Kroutil, W.; Vértessy, B.G.; Paizs, C.; Poppe, L. Immobilized Whole-Cell Transaminase Biocatalysts for Continuous-Flow Kinetic Resolution of Amines. Catalysts 2019, 9, 438.

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