Odd–even effect for efficient bioreactions of chiral alcohols and boosted stability of the enzyme
| dc.contributor.author | Bülow, Mark | |
| dc.contributor.author | Schmitz, Alexa | |
| dc.contributor.author | Mahmoudi, Termeh | |
| dc.contributor.author | Schmidt, Dana | |
| dc.contributor.author | Junglas, Fabian | |
| dc.contributor.author | Janiak, Christoph | |
| dc.contributor.author | Held, Christoph | |
| dc.date.accessioned | 2020-08-18T11:11:50Z | |
| dc.date.available | 2020-08-18T11:11:50Z | |
| dc.date.issued | 2020-07-29 | |
| dc.description.abstract | We describe a holistic approach for achieving a nearly quantitative conversion for an enzymatic reaction while simultaneously increasing the long-term stability of the enzyme. The approach provided chemical control of bioreactions by utilizing newly synthesized tetrahydrothiophene-based ionic liquids (THT ILs). We showcased its power by using THT-ILs as additives at a low concentration (only 10 mmol L−1) in the alcohol dehydrogenase (ADH)-catalyzed synthesis of methylated 1-phenylethanol (Me-PE). We discovered an “odd–even” effect of the IL-cation chain length: Me-PE displayed beneficial interactions with THT ILs having odd-numbered chain lengths and deleterious interactions with those having even-numbered chain lengths. An intermolecular thermodynamic simulation of the bulk phase and critical micelle concentration investigations of the local surroundings of the THT-ILs proved the occurrence of these interactions, and these two methods confirmed the odd–even effect from different perspectives. Additionally, storing the ADH enzyme in pure THT IL at room temperature allowed for a boosted long-term stability of the enzyme (500 times greater than that in aqueous buffer) without the need for freezing. | en |
| dc.identifier.uri | http://hdl.handle.net/2003/39239 | |
| dc.identifier.uri | http://dx.doi.org/10.17877/DE290R-21156 | |
| dc.language.iso | en | de |
| dc.relation.ispartofseries | RSC Advances;10(47) | |
| dc.rights.uri | https://creativecommons.org/licenses/by/3.0/ | |
| dc.subject.ddc | 660 | |
| dc.title | Odd–even effect for efficient bioreactions of chiral alcohols and boosted stability of the enzyme | en |
| dc.type | Text | de |
| dc.type.publicationtype | article | de |
| dcterms.accessRights | open access | |
| eldorado.secondarypublication | true | de |
| eldorado.secondarypublication.primarycitation | Bülow, M, Schmitz, A, Mahmoudi, T, Schmidt, D, Junglas, F, Janiak, C, Held, C. Odd–even effect for efficient bioreactions of chiral alcohols and boosted stability of the enzyme. RSC Adv., 2020, 10, 28351-28354 | de |
| eldorado.secondarypublication.primaryidentifier | https://doi.org/10.1039/D0RA05406B | de |