Full thermal switching of enzymes by thermoresponsive poly(2-oxazoline)-based enzyme inhibitors

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dc.contributor.authorHijazi, Montasser
dc.contributor.authorTürkmen, Esra
dc.contributor.authorTiller, Jörg C.
dc.date.accessioned2021-07-19T11:29:07Z
dc.date.available2021-07-19T11:29:07Z
dc.date.issued2020-07-24
dc.description.abstractControlling 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.en
dc.identifier.urihttp://hdl.handle.net/2003/40331
dc.identifier.urihttp://dx.doi.org/10.17877/DE290R-22206
dc.language.isoende
dc.relation.ispartofseriesChemistry - a european journal;Vol. 26. 2020, Issue 59, pp 13367-13371
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectEnzymeinhibitorsen
dc.subjectFunctional polymer end groupsen
dc.subjectLower critical solutiontemperature polymersen
dc.subjectPoly(2- oxazoline)en
dc.subjectThermoresponsiveen
dc.subject.ddc660
dc.titleFull thermal switching of enzymes by thermoresponsive poly(2-oxazoline)-based enzyme inhibitorsen
dc.typeTextde
dc.type.publicationtypearticlede
dcterms.accessRightsopen access
eldorado.secondarypublicationtruede
eldorado.secondarypublication.primarycitationChemistry - a european journal. Vol. 26. 2020, Issue 59, pp 13367-13371de
eldorado.secondarypublication.primaryidentifierhttps://doi.org/10.1002/chem.202001909de

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