Zobrazeno 1 - 10
of 80
pro vyhledávání: '"Matthias, Höhne"'
Autor:
Shuke Wu, Chao Xiang, Yi Zhou, Mohammad Saiful Hasan Khan, Weidong Liu, Christian G. Feiler, Ren Wei, Gert Weber, Matthias Höhne, Uwe T. Bornscheuer
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-10 (2022)
Fast screening of enzymes is key for directed evolution of industrial biocatalysts. Here, the authors report a simple, high-throughput, and low-equipment-dependent growth selection system for engineering three enzymes for synthesis of chiral amines.
Externí odkaz:
https://doaj.org/article/daa9820f5ef346a0806e953ac1ba04dc
Autor:
Tobias Heinks, Luisa M. Merz, Jan Liedtke, Matthias Höhne, Luuk M. van Langen, Uwe T. Bornscheuer, Gabriele Fischer von Mollard, Per Berglund
Publikováno v:
Catalysts, Vol 13, Iss 5, p 875 (2023)
Building blocks with amine functionality are crucial in the chemical industry. Biocatalytic syntheses and chemicals derived from renewable resources are increasingly desired to achieve sustainable production of these amines. As a result, renewable ma
Externí odkaz:
https://doaj.org/article/b559d379a8b34402b2834f5acafa4d07
Autor:
Tobias Heinks, Nicolai Montua, Michelle Teune, Jan Liedtke, Matthias Höhne, Uwe T. Bornscheuer, Gabriele Fischer von Mollard
Publikováno v:
Catalysts, Vol 13, Iss 2, p 300 (2023)
Biocatalytic syntheses often require unfavorable conditions, which can adversely affect enzyme stability. Consequently, improving the stability of biocatalysts is needed, and this is often achieved by immobilization. In this study, we aimed to compar
Externí odkaz:
https://doaj.org/article/2540904060c64b508a65d459e9d918db
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 23, p 15347 (2022)
Amine transaminases (ATAs) are powerful biocatalysts for the stereoselective synthesis of chiral amines. However, wild-type ATAs usually show pH optima at slightly alkaline values and exhibit low catalytic activity under physiological conditions. For
Externí odkaz:
https://doaj.org/article/017be38408bd45d6b25b6a799c8bf30b
Publikováno v:
Chemie Ingenieur Technik. 94:1836-1844
Autor:
Yu‐Fei Ao, Shuxin Pei, Chao Xiang, Marian J. Menke, Lin Shen, Chenghai Sun, Mark Dörr, Stefan Born, Matthias Höhne, Uwe T. Bornscheuer
Publikováno v:
Angewandte Chemie. 135
Autor:
Yu‐Fei Ao, Shuxin Pei, Chao Xiang, Marian J. Menke, Lin Shen, Chenghai Sun, Mark Dörr, Stefan Born, Matthias Höhne, Uwe T. Bornscheuer
Amine transaminases (ATAs) are powerful biocatalysts for the stereoselective synthesis of chiral amines. Machine learning provides a promising approach for protein engineering, but activity prediction models for ATAs remain elusive due to the difficu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b52791f4f506e79722b98c0302cd579a
Autor:
Theresa Dutschei, Irena Beidler, Daniel Bartosik, Julia‐Maria Seeßelberg, Michelle Teune, Marcus Bäumgen, Soraia Querido Ferreira, Julia Heldmann, Felix Nagel, Joris Krull, Leona Berndt, Karen Methling, Martin Hein, Dörte Becher, Peter Langer, Mihaela Delcea, Michael Lalk, Michael Lammers, Matthias Höhne, Jan‐Hendrik Hehemann, Thomas Schweder, Uwe T. Bornscheuer
Publikováno v:
Environmental Microbiology.
Autor:
Maika Genz, Clare Vickers, Tom van den Bergh, Henk-Jan Joosten, Mark Dörr, Matthias Höhne, Uwe T. Bornscheuer
Publikováno v:
International Journal of Molecular Sciences, Vol 16, Iss 11, Pp 26953-26963 (2015)
To alter the amine donor/acceptor spectrum of an (S)-selective amine transaminase (ATA), a library based on the Vibrio fluvialis ATA targeting four residues close to the active site (L56, W57, R415 and L417) was created. A 3DM-derived alignment compr
Externí odkaz:
https://doaj.org/article/30fb63db4ccc4d2289130962ef420ad3
Autor:
Tobias Heinks, Jannik Paulus, Simon Koopmeiners, Tobias Beuel, Norbert Sewald, Matthias Höhne, Uwe T. Bornscheuer, Gabriele Fischer von Mollard
Publikováno v:
ChemBioChem. 23
Chiral and enantiopure amines can be produced by enantioselective transaminases via kinetic resolution of amine racemates. This transamination reaction requires stoichiometric amounts of co-substrate. A dual-enzyme recycling system overcomes this lim