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Enhanced Arylamine N-Oxygenase Activity of Polymer–Enzyme Assemblies by Facilitating Electron-Transferring Efficiency
Biomacromolecules ( IF 6.2 ) Pub Date : 2018-02-20 00:00:00 , DOI: 10.1021/acs.biomac.7b01706
Libo Zhang 1 , Yanmei Xu 1 , Thomas M. Makris 1 , Qian Wang 1
Affiliation  

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.

中文翻译:

通过促进电子转移效率增强聚合物-酶组装体的芳胺N-氧合酶活性

通过聚(4-乙烯基吡啶)(P4VP)和芳胺N加氧酶CmlI的共组装,产生了一种新型的N加氧酶包覆的核壳纳米粒子。将得到的酶杂化颗粒,P4VP-CmlI,显示出在两个芳基胺底物的氧化,即,优异的催化活性p氨基苯酚(p AP)和对-氨基苯甲酸(pABA),使用替代氧化还原系统或过氧化物分流器作为助氧化剂。与游离酶相比,当使用吡啶核苷酸(NADH)和适当的氧化还原介体时,P4VP-CmlI颗粒显示出显着增强的催化效率。观察到处于不同氧合阶段的产物。相反,当使用过氧化物分流器时,含酶纳米颗粒的活性与游离酶非常相似。P4VP-CmlI组件提高的催化效率归因于更有效的电子传递。
更新日期:2018-02-20
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