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Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors
Controlling the activity of enzymes is an important feature for many processes in medicine, bioanalytics, and biotechnology. So far, it has not been possible to fully switch biocatalysts on and off by thermoresponsive enzyme inhibitors. Herein, we present poly(2‐oxazoline)s with iminodiacetic acid e...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7702056/ https://www.ncbi.nlm.nih.gov/pubmed/32706128 http://dx.doi.org/10.1002/chem.202001909 |
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author | Hijazi, Montasser Türkmen, Esra Tiller, Joerg C. |
author_facet | Hijazi, Montasser Türkmen, Esra Tiller, Joerg C. |
author_sort | Hijazi, Montasser |
collection | PubMed |
description | Controlling the activity of enzymes is an important feature for many processes in medicine, bioanalytics, and biotechnology. So far, it has not been possible to fully switch biocatalysts on and off by thermoresponsive enzyme inhibitors. Herein, we present poly(2‐oxazoline)s with iminodiacetic acid end groups (POx‐IDA) that are lower critical solution temperature (LCST) polymers and thus thermosensitive. They are capable of reversibly inhibiting the activity of horse radish peroxidase and laccase by more than 99 %. Increasing the temperature makes the POx‐IDA precipitate, which leads to 100 % recovery of the enzyme activity. This switching cycle is fully reversible. The LCST of the POx‐IDA can be tuned by varying the polymer composition to generate a wide range of switching windows. |
format | Online Article Text |
id | pubmed-7702056 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-77020562020-12-14 Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors Hijazi, Montasser Türkmen, Esra Tiller, Joerg C. Chemistry Communications Controlling the activity of enzymes is an important feature for many processes in medicine, bioanalytics, and biotechnology. So far, it has not been possible to fully switch biocatalysts on and off by thermoresponsive enzyme inhibitors. Herein, we present poly(2‐oxazoline)s with iminodiacetic acid end groups (POx‐IDA) that are lower critical solution temperature (LCST) polymers and thus thermosensitive. They are capable of reversibly inhibiting the activity of horse radish peroxidase and laccase by more than 99 %. Increasing the temperature makes the POx‐IDA precipitate, which leads to 100 % recovery of the enzyme activity. This switching cycle is fully reversible. The LCST of the POx‐IDA can be tuned by varying the polymer composition to generate a wide range of switching windows. John Wiley and Sons Inc. 2020-09-23 2020-10-21 /pmc/articles/PMC7702056/ /pubmed/32706128 http://dx.doi.org/10.1002/chem.202001909 Text en © 2020 The Authors. Published by Wiley-VCH GmbH This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Communications Hijazi, Montasser Türkmen, Esra Tiller, Joerg C. Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors |
title | Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors |
title_full | Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors |
title_fullStr | Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors |
title_full_unstemmed | Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors |
title_short | Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors |
title_sort | full thermal switching of enzymes by thermoresponsive poly(2‐oxazoline)‐based enzyme inhibitors |
topic | Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7702056/ https://www.ncbi.nlm.nih.gov/pubmed/32706128 http://dx.doi.org/10.1002/chem.202001909 |
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