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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...

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Autores principales: Hijazi, Montasser, Türkmen, Esra, Tiller, Joerg C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2020
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.
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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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