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2,268 results on '"Bornscheuer, Uwe"'

4. Alpha-glucans from bacterial necromass indicate an intra-population loop within the marine carbon cycle

Author

Beidler, Irena, Steinke, Nicola, Schulze, Tim, Sidhu, Chandni, Bartosik, Daniel, Zühlke, Marie-Katherin, Martin, Laura Torres, Krull, Joris, Dutschei, Theresa, Ferrero-Bordera, Borja, Rielicke, Julia, Kale, Vaikhari, Sura, Thomas, Trautwein-Schult, Anke, Kirstein, Inga V., Wiltshire, Karen H., Teeling, Hanno, Becher, Dörte, Bengtsson, Mia Maria, Hehemann, Jan-Hendrik, Bornscheuer, Uwe. T., Amann, Rudolf I., and Schweder, Thomas

Published
2024
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6. Optimization of Enzymes

Author

Böttcher, Dominique, Bornscheuer, Uwe T., Bosserhoff, Anja K., Series Editor, Berenjian, Aydin, Series Editor, Carbonell, Pablo, Series Editor, Levite, Mia, Series Editor, Roig, Joan, Series Editor, Turksen, Kursad, Series Editor, Jaeger, Karl-Erich, editor, Liese, Andreas, editor, and Syldatk, Christoph, editor

Published
2024
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22. Strukturaufklärung einer metagenomischen Urethanase und Verbesserung des Hydrolyseprofils durch Protein Engineering.

Author

Bayer, Thomas, Palm, Gottfried J., Berndt, Leona, Meinert, Hannes, Branson, Yannick, Schmidt, Louis, Cziegler, Clemens, Somvilla, Ina, Zurr, Celine, Graf, Leonie G., Janke, Una, Badenhorst, Christoffel P. S., König, Stefanie, Delcea, Mihaela, Garscha, Ulrike, Wei, Ren, Lammers, Michael, and Bornscheuer, Uwe T.

Abstract

Copyright of Angewandte Chemie is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
2024
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23. Structural Elucidation of a Metagenomic Urethanase and Its Engineering Towards Enhanced Hydrolysis Profiles.

Author

Bayer, Thomas, Palm, Gottfried J., Berndt, Leona, Meinert, Hannes, Branson, Yannick, Schmidt, Louis, Cziegler, Clemens, Somvilla, Ina, Zurr, Celine, Graf, Leonie G., Janke, Una, Badenhorst, Christoffel P. S., König, Stefanie, Delcea, Mihaela, Garscha, Ulrike, Wei, Ren, Lammers, Michael, and Bornscheuer, Uwe T.

Subjects
PLASTICS, ENGINEERING plastics, CIRCULAR economy, URETHANE, VIRTUAL economy
Abstract

While plastics like polyethylene terephthalate can already be degraded efficiently by the activity of hydrolases, other synthetic polymers like polyurethanes (PUs) and polyamides (PAs) largely resist biodegradation. In this study, we solved the first crystal structure of the metagenomic urethanase UMG‐SP‐1, identified highly flexible loop regions to comprise active site residues, and targeted a total of 20 potential hot spots by site‐saturation mutagenesis. Engineering campaigns yielded variants with single mutations, exhibiting almost 3‐ and 8‐fold improved activity against highly stable N‐aryl urethane and amide bonds, respectively. Furthermore, we demonstrated the release of the corresponding monomers from a thermoplastic polyester‐PU and a PA (nylon 6) by the activity of a single, metagenome‐derived urethanase after short incubation times. Thereby, we expanded the hydrolysis profile of UMG‐SP‐1 beyond the reported low‐molecular weight carbamates. Together, these findings promise advanced strategies for the bio‐based degradation and recycling of plastic materials and waste, aiding efforts to establish a circular economy for synthetic polymers. [ABSTRACT FROM AUTHOR]

Published
2024
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29. From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets

Author

Jäckering, Anna, Göttsch, Frederike, Schäffler, Moritz, Doerr, Mark, Bornscheuer, Uwe T., Wei, Ren, and Strodel, Birgit

Abstract

Plastic-degrading enzymes facilitate the biocatalytic recycling of poly(ethylene terephthalate) (PET), a significant synthetic polymer, and substantial progress has been made in utilizing PET hydrolases for industrial applications. To fully exploit the potential of these enzymes, a deeper mechanistic understanding followed by targeted protein engineering is essential. Through advanced molecular dynamics simulations and free energy analysis methods, we elucidated the complete pathway from the initial binding of two PET hydrolases─the thermophilic leaf-branch compost cutinase (LCC) and polyester hydrolase 1 (PES-H1)─to an amorphous PET substrate, ultimately leading to a PET chain entering the active site in a hydrolyzable conformation. Our findings indicate that initial PET binding is nonspecific and driven by polar and hydrophobic interactions. We demonstrate that the subsequent entry of PET into the active site can occur via one of three key pathways, identifying barriers related to both PET–PET and PET–enzyme interactions, as well as specific residues highlighted through in silicoand in vitromutagenesis. These insights not only enhance our understanding of the mechanisms underlying PET degradation and facilitate the development of targeted enzyme enhancement strategies but also provide a novel framework applicable to enzyme studies across various disciplines.

Published
2024
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30. LibGENiE : a bioinformatic pipeline for the design of information-enriched enzyme libraries

Author

Patsch, David, Eichenberger, Michael, Voss, Moritz, Bornscheuer, Uwe T., Buller, Rebecca M., Patsch, David, Eichenberger, Michael, Voss, Moritz, Bornscheuer, Uwe T., and Buller, Rebecca M.

Abstract

Enzymes are potent catalysts with high specificity and selectivity. To leverage nature's synthetic potential for industrial applications, various protein engineering techniques have emerged which allow to tailor the catalytic, biophysical, and molecular recognition properties of enzymes. However, the many possible ways a protein can be altered forces researchers to carefully balance between the exhaustiveness of an enzyme screening campaign and the required resources. Consequently, the optimal engineering strategy is often defined on a case-by-case basis. Strikingly, while predicting mutations that lead to an improved target function is challenging, here we show that the prediction and exclusion of deleterious mutations is a much more straightforward task as analyzed for an engineered carbonic acid anhydrase, a transaminase, a squalene-hopene cyclase and a Kemp eliminase. Combining such a pre-selection of allowed residues with advanced gene synthesis methods opens a path toward an efficient and generalizable library construction approach for protein engineering. To give researchers easy access to this methodology, we provide the website LibGENiE containing the bioinformatic tools for the library design workflow.

Published
2024

33. Effiziente enzymatische Synthese von Carbamaten in Wasser durch promiskuitive Esterasen/Acyltransferasen.

Author

Meinert, Hannes, Oehlschläger, Florian, Cziegler, Clemens, Rockstroh, Jan, Marzuoli, Irene, Bisagni, Serena, Lalk, Michael, Bayer, Thomas, Iding, Hans, and Bornscheuer, Uwe T.

Abstract

Copyright of Angewandte Chemie is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
2024
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34. Biocatalytic approaches for plastic recycling.

Author

Branson, Yannick, Wei, Ren, and Bornscheuer, Uwe T.

Subjects
PLASTIC recycling, POLYMER degradation, WASTE recycling, PLASTIC scrap recycling, BIOCATALYSIS, INDUSTRIAL applications
Abstract

Copyright of Automatisierungstechnik is the property of De Gruyter and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Published
2024
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35. Enzymatic Synthesis of Hydroxycinnamic Acid Amides in Water Using the Promiscuous Hydrolase/Acyltransferase PestE from Pyrobaculum calidifontis VA1.

Author

Baumert, Benjamin, Terholsen, Henrik, Cziegler, Clemens, Thier, Isabel, Badenhorst, Christoffel P. S., Siems, Karsten, and Bornscheuer, Uwe T.

Subjects
ACYLTRANSFERASES, SUSTAINABLE chemistry, WATER use, ORGANIC solvents, AMIDES, ARAMID fibers, HYDROXYCINNAMIC acids
Abstract

The article explores the use of the enzyme PestE from Pyrobaculum calidifontis VA1 for the enzymatic synthesis of hydroxycinnamic acid amides (HCAAs). HCAAs are natural compounds with potential applications in various industries. The current methods for synthesizing HCAAs are not environmentally friendly, so enzymatic methods are being explored as a greener alternative. The study focuses on the synthesis of N-trans-feruloyltyramine using PestE and found that the reaction was most efficient at 60 °C with a specific molar ratio. The use of acetonitrile as a cosolvent posed challenges, but ascorbic acid could be added to prevent substrate oxidation. PestE was also found to catalyze the formation of other hydroxycinnamic acid amides. Overall, this enzymatic method offers a more sustainable approach to HCAA synthesis. [Extracted from the article]

Published
2024
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36. Identification and expression of MarCE, a marine carboxylesterase with synthetic ester‐degrading activity.

Author

Carr, Clodagh M., Göttsch, Frederike, de Oliveira, Bruno Francesco Rodrigues, Murcia, Pedro A. Sánchez, Jackson, Stephen A., Wei, Ren, Clarke, David J., Bornscheuer, Uwe T., and Dobson, Alan D. W.

Subjects
CARBOXYLESTERASES, CARBOXYLIC acids, BIODEGRADATION, MARINE toxins, SPONGES (Invertebrates), MOLECULAR docking, BIOCHEMICAL substrates, POLYMERS
Abstract

Carboxylic ester hydrolases with the capacity to degrade polyesters are currently highly sought after for their potential use in the biological degradation of PET and other chemically synthesized polymers. Here, we describe MarCE, a carboxylesterase family protein identified via genome mining of a Maribacter sp. isolate from the marine sponge Stelligera stuposa. Based on phylogenetic analysis, MarCE and its closest relatives belong to marine‐associated genera from the Cytophaga–Flavobacterium–Bacteroides taxonomic group and appear evolutionarily distinct to any homologous carboxylesterases that have been studied to date in terms of structure or function. Molecular docking revealed putative binding of BHET, a short‐chain PET derivative, onto the predicted MarCE three‐dimensional structure. The synthetic ester‐degrading activity of MarCE was subsequently confirmed by MarCE‐mediated hydrolysis of 2 mM BHET substrate, indicated by the release of its breakdown products MHET and TPA, which were measured, respectively, as 1.28 and 0.12 mM following 2‐h incubation at 30°C. The findings of this study provide further insight into marine carboxylic ester hydrolases, which have the potential to display unique functional plasticity resulting from their adaptation to complex and fluctuating marine environmentsw. [ABSTRACT FROM AUTHOR]

Published
2024
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44. Engineering the protein dynamics of an ancestral luciferase

Author

Schenkmayerova, Andrea, Pinto, Gaspar P., Toul, Martin, Marek, Martin, Hernychova, Lenka, Planas-Iglesias, Joan, Daniel Liskova, Veronika, Pluskal, Daniel, Vasina, Michal, Emond, Stephane, Dörr, Mark, Chaloupkova, Radka, Bednar, David, Prokop, Zbynek, Hollfelder, Florian, Bornscheuer, Uwe T., and Damborsky, Jiri

Published
2021
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45. MIXed plastics biodegradation and UPcycling using microbial communities: EU Horizon 2020 project MIX-UP started January 2020

Author

Ballerstedt, Hendrik, Tiso, Till, Wierckx, Nick, Wei, Ren, Averous, Luc, Bornscheuer, Uwe, O’Connor, Kevin, Floehr, Tilman, Jupke, Andreas, Klankermayer, Jürgen, Liu, Luo, de Lorenzo, Victor, Narancic, Tanja, Nogales, Juan, Perrin, Rémi, Pollet, Eric, Prieto, Auxiliadora, Casey, William, Haarmann, Thomas, Sarbu, Alexandru, Schwaneberg, Ulrich, Xin, Fengxue, Dong, Weiliang, Xing, Jiamin, Chen, Guo-Qiang, Tan, Tianwei, Jiang, Min, and Blank, Lars M.

Published
2021
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48. Optimierung von Enzymen

Author

Böttcher, Dominique, Bornscheuer, Uwe T., Jaeger, Karl-Erich, editor, Liese, Andreas, editor, Syldatk, Christoph, editor, and Lay, Martin, Illustrations by

Published
2018
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50. Preface

Author

Weber, Gert, primary, Bornscheuer, Uwe T., additional, and Wei, Ren, additional

Published
2021
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