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Updated: Dec 23, 2025

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
Enzymatic epoxidation of cyclohexene by peroxidase immobilization on a textile and an adapted reactor design
D S Wunschik1, K N Ingenbosch1, P Süss2
1Niederrhein University of Applied Sciences, Chemistry Department, Adlerstr. 32, 47798 Krefeld, Germany; Deutsches Textilforschungszentrum Nord-West gGmbH, Adlerstr. 1, 47798 Krefeld, Germany; Institute of Physical Chemistry and CENIDE (Center for Nanointegration), University Duisburg-Essen, Universitätsstraße 5, 45117 Essen, Germany.
Abstract:
A textile-based reaction system for new peroxidase reactions in non-native media was implemented. The epoxidation of cyclohexene by the commercial peroxidase MaxiBright® was realized with the textile-immobilized enzyme in an adapted liquid-liquid two-phase reactor. A commercially available polyester felt was used as low-price carrier and functionalized with polyvinyl amine. The covalent immobilization with glutardialdehyde lead to an enzyme loading of 0.10 genzyme/gtextile. The textile-based peroxidase shows a high activity retention in the presence of organic media. This catalyst is shown to enable the epoxidation of cyclohexene in various solvents as well as under neat conditions. A model reactor was produced by 3D printing which places the textile catalyst at the interphase between the liquid reaction phase and the product extracting solvent.
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