JOURNAL ARTICLE
RESEARCH SUPPORT, NON-U.S. GOV'T
RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
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Enhanced Arylamine N-Oxygenase Activity of Polymer-Enzyme Assemblies by Facilitating Electron-Transferring Efficiency.

Biomacromolecules 2018 March 13
A novel N-oxygenase-coated core-shell nanoparticle was generated through the coassembly of poly(4-vinylpyridine) (P4VP) and arylamine N-oxygenase CmlI. The resulting enzyme-hybridized particles, P4VP-CmlI, showed excellent catalytic activities on the oxidation of two arylamine substrates, i.e., p-aminophenol ( pAP) and p-aminobenzoic acid ( pABA), using a surrogate redox system or a peroxide shunt as co-oxidants. In comparison with the free enzyme, P4VP-CmlI particles exhibited a significantly enhanced catalytic efficiency when using pyridine nucleotide (NADH) and proper redox mediators. Products at different oxygenation stages were observed. On the contrary, the activity of the enzyme-containing nanoparticles was very similar to the free enzyme when using the peroxide shunt. The enhanced catalytic efficiency of the P4VP-CmlI assemblies is attributed to a more efficient electron delivery.

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