1. Enzymatic epoxidation of cyclohexene by peroxidase immobilization on a textile and an adapted reactor design.
- Author
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Wunschik DS, Ingenbosch KN, Süss P, Liebelt U, Quint S, Dyllick-Brenzinger M, Zuhse R, Menyes U, Hoffmann-Jacobsen K, Opwis K, and Gutmann JS
- Subjects
- Biocatalysis, Coloring Agents, Glutaral metabolism, Oxidation-Reduction, Solvents metabolism, Cyclohexenes metabolism, Enzymes, Immobilized metabolism, Peroxidases metabolism, Textiles
- 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 g
enzyme /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., Competing Interests: Declaration of Competing Interest There are no conflicts to declare., (Copyright © 2020 Elsevier Inc. All rights reserved.)- Published
- 2020
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