Tuning Chemoenzymatic Pd/Laccase Conformation Toward Optimized Heterogeneous Aerobic Oxidation
Abstract: Heterogeneous chemoenzymatic catalysts differing in their spatial organization and relative orientation of their enzymatic laccase and Pd units confined into macrocellular silica foams were tested on veratryl alcohol oxidation. When operating under continuous flow, we show that the catalytic efficiency of hybrids is significantly enhanced when the Pd (II) complex is combined with a laccase exhibiting a surface located lysine next to the T1 oxidation site of the enzyme.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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Tuning Chemoenzymatic Pd/Laccase Conformation Toward Optimized Heterogeneous Aerobic Oxidation ; day:09 ; month:01 ; year:2024 ; extent:8
ChemBioChem ; (09.01.2024) (gesamt 8)
- Creator
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Yang, Fangfang
Rousselot Pailley, Pierre
Backov, Rénal
Courvoisier‐Dezord, Elise
Amouric, Agnès
Tron, Thierry
Mekmouche, Yasmina
- DOI
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10.1002/cbic.202300781
- URN
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urn:nbn:de:101:1-2024011014120880117999
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:38 AM CEST
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Yang, Fangfang
- Rousselot Pailley, Pierre
- Backov, Rénal
- Courvoisier‐Dezord, Elise
- Amouric, Agnès
- Tron, Thierry
- Mekmouche, Yasmina
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