Full Thermal Switching of Enzymes by Thermoresponsive Poly(2-oxazoline)-Based Enzyme Inhibitors.
| Autor: | Hijazi M; Department of Bio- and Chemical Engineering, TU Dortmund, Emil-Figge-Str. 66, 44227, Dortmund, Germany., Türkmen E; Department of Bio- and Chemical Engineering, TU Dortmund, Emil-Figge-Str. 66, 44227, Dortmund, Germany., Tiller JC; Department of Bio- and Chemical Engineering, TU Dortmund, Emil-Figge-Str. 66, 44227, Dortmund, Germany. |
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| Jazyk: | angličtina |
| Zdroj: | Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2020 Oct 21; Vol. 26 (59), pp. 13367-13371. Date of Electronic Publication: 2020 Sep 23. |
| DOI: | 10.1002/chem.202001909 |
| Abstrakt: | 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. (© 2020 The Authors. Published by Wiley-VCH GmbH.) |
| Databáze: | MEDLINE |
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