Kübelbeck, Sonja ; Mikhael, Jules ; Keller, Harald ; Konradi, Rupert ; Andrieu-Brunsen, Annette ; Baier, Grit (2022)
Enzyme-Polymer Conjugates to Enhance Enzyme Shelf Life in a Liquid Detergent Formulation.
In: Macromolecular Bioscience, 18 (7)
doi: 10.26083/tuprints-00021680
Artikel, Zweitveröffentlichung, Postprint
Kurzbeschreibung (Abstract)
Herein, the synthesis of enzyme–polymer conjugates is reported. Four different activated polymers (mPEG-aldehyde, mPEG-NHS, maltodextrin-aldehyde, carboxymethyl cellulose aldehyde) are conjugated to the surface of protease, α-amylase, and lipase using two different strategies (reductive amination and alkylation with NHS-activated acid). Although the chemical modification of the enzymes is accompanied by losses in enzyme activity (maximum loss 40%), the covalent attachment of polymers increases the thermal stability and the stability in a standard detergent formulation compared to the unmodified enzymes. The enzyme–polymer conjugates are characterized by asymmetrical-flow field-flow fractionation and differential scanning microcalorimetry. Furthermore, it is demonstrated that conjugated enzymes still show performance in a real washing process. Enzyme–polymer conjugates show a potential as a stabilizing system for enzymes in detergents.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2022 |
| Autor(en): | Kübelbeck, Sonja ; Mikhael, Jules ; Keller, Harald ; Konradi, Rupert ; Andrieu-Brunsen, Annette ; Baier, Grit |
| Art des Eintrags: | Zweitveröffentlichung |
| Titel: | Enzyme-Polymer Conjugates to Enhance Enzyme Shelf Life in a Liquid Detergent Formulation |
| Sprache: | Englisch |
| Publikationsjahr: | 2022 |
| Ort: | Darmstadt |
| Verlag: | John Wiley & Sons |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | Macromolecular Bioscience |
| Jahrgang/Volume einer Zeitschrift: | 18 |
| (Heft-)Nummer: | 7 |
| Kollation: | 26 Seiten |
| DOI: | 10.26083/tuprints-00021680 |
| URL / URN: | https://tuprints.ulb.tu-darmstadt.de/21680 |
| Zugehörige Links: | |
| Herkunft: | Zweitveröffentlichungsservice |
| Kurzbeschreibung (Abstract): | Herein, the synthesis of enzyme–polymer conjugates is reported. Four different activated polymers (mPEG-aldehyde, mPEG-NHS, maltodextrin-aldehyde, carboxymethyl cellulose aldehyde) are conjugated to the surface of protease, α-amylase, and lipase using two different strategies (reductive amination and alkylation with NHS-activated acid). Although the chemical modification of the enzymes is accompanied by losses in enzyme activity (maximum loss 40%), the covalent attachment of polymers increases the thermal stability and the stability in a standard detergent formulation compared to the unmodified enzymes. The enzyme–polymer conjugates are characterized by asymmetrical-flow field-flow fractionation and differential scanning microcalorimetry. Furthermore, it is demonstrated that conjugated enzymes still show performance in a real washing process. Enzyme–polymer conjugates show a potential as a stabilizing system for enzymes in detergents. |
| Status: | Postprint |
| URN: | urn:nbn:de:tuda-tuprints-216808 |
| Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 500 Naturwissenschaften und Mathematik > 540 Chemie |
| Fachbereich(e)/-gebiet(e): | Profilbereiche Profilbereiche > Thermo-Fluids & Interfaces 07 Fachbereich Chemie 07 Fachbereich Chemie > Ernst-Berl-Institut > Fachgebiet Makromolekulare Chemie |
| Hinterlegungsdatum: | 20 Jul 2022 12:17 |
| Letzte Änderung: | 21 Jul 2022 05:05 |
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