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MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents
Fully exploiting the potential of enzymes in cell‐free biocatalysis requires stabilization of the catalytically active proteins and their integration into efficient reactor systems. Although in recent years initial steps towards the immobilization of such biomolecules in metal–organic frameworks (MO...
Autores principales: | , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9314721/ https://www.ncbi.nlm.nih.gov/pubmed/35133704 http://dx.doi.org/10.1002/anie.202117144 |
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author | Greifenstein, Raphael Ballweg, Tim Hashem, Tawheed Gottwald, Eric Achauer, David Kirschhöfer, Frank Nusser, Michael Brenner‐Weiß, Gerald Sedghamiz, Elaheh Wenzel, Wolfgang Mittmann, Esther Rabe, Kersten S. Niemeyer, Christof M. Franzreb, Matthias Wöll, Christof |
author_facet | Greifenstein, Raphael Ballweg, Tim Hashem, Tawheed Gottwald, Eric Achauer, David Kirschhöfer, Frank Nusser, Michael Brenner‐Weiß, Gerald Sedghamiz, Elaheh Wenzel, Wolfgang Mittmann, Esther Rabe, Kersten S. Niemeyer, Christof M. Franzreb, Matthias Wöll, Christof |
author_sort | Greifenstein, Raphael |
collection | PubMed |
description | Fully exploiting the potential of enzymes in cell‐free biocatalysis requires stabilization of the catalytically active proteins and their integration into efficient reactor systems. Although in recent years initial steps towards the immobilization of such biomolecules in metal–organic frameworks (MOFs) have been taken, these demonstrations have been limited to batch experiments and to aqueous conditions. Here we demonstrate a MOF‐based continuous flow enzyme reactor system, with high productivity and stability, which is also suitable for organic solvents. Under aqueous conditions, the stability of the enzyme was increased 30‐fold, and the space–time yield exceeded that obtained with other enzyme immobilization strategies by an order of magnitude. Importantly, the infiltration of the proteins into the MOF did not require additional functionalization, thus allowing for time‐ and cost‐efficient fabrication of the biocatalysts using label‐free enzymes. |
format | Online Article Text |
id | pubmed-9314721 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-93147212022-07-30 MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents Greifenstein, Raphael Ballweg, Tim Hashem, Tawheed Gottwald, Eric Achauer, David Kirschhöfer, Frank Nusser, Michael Brenner‐Weiß, Gerald Sedghamiz, Elaheh Wenzel, Wolfgang Mittmann, Esther Rabe, Kersten S. Niemeyer, Christof M. Franzreb, Matthias Wöll, Christof Angew Chem Int Ed Engl Communications Fully exploiting the potential of enzymes in cell‐free biocatalysis requires stabilization of the catalytically active proteins and their integration into efficient reactor systems. Although in recent years initial steps towards the immobilization of such biomolecules in metal–organic frameworks (MOFs) have been taken, these demonstrations have been limited to batch experiments and to aqueous conditions. Here we demonstrate a MOF‐based continuous flow enzyme reactor system, with high productivity and stability, which is also suitable for organic solvents. Under aqueous conditions, the stability of the enzyme was increased 30‐fold, and the space–time yield exceeded that obtained with other enzyme immobilization strategies by an order of magnitude. Importantly, the infiltration of the proteins into the MOF did not require additional functionalization, thus allowing for time‐ and cost‐efficient fabrication of the biocatalysts using label‐free enzymes. John Wiley and Sons Inc. 2022-03-09 2022-04-25 /pmc/articles/PMC9314721/ /pubmed/35133704 http://dx.doi.org/10.1002/anie.202117144 Text en © 2022 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Communications Greifenstein, Raphael Ballweg, Tim Hashem, Tawheed Gottwald, Eric Achauer, David Kirschhöfer, Frank Nusser, Michael Brenner‐Weiß, Gerald Sedghamiz, Elaheh Wenzel, Wolfgang Mittmann, Esther Rabe, Kersten S. Niemeyer, Christof M. Franzreb, Matthias Wöll, Christof MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents |
title | MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents |
title_full | MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents |
title_fullStr | MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents |
title_full_unstemmed | MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents |
title_short | MOF‐Hosted Enzymes for Continuous Flow Catalysis in Aqueous and Organic Solvents |
title_sort | mof‐hosted enzymes for continuous flow catalysis in aqueous and organic solvents |
topic | Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9314721/ https://www.ncbi.nlm.nih.gov/pubmed/35133704 http://dx.doi.org/10.1002/anie.202117144 |
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