Scocozza Magalí F, Vieyra Francisco, Battaglini Fernando, Martins Ligia O, Murgida Daniel H
Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EGA, Argentina.
Instituto de Química Física de Los Materiales, Medio Ambiente y Energía (INQUIMAE), CONICET-Universidad de Buenos Aires, Buenos Aires C1428EGA, Argentina.
ACS Catal. 2023 May 18;13(11):7437-7449. doi: 10.1021/acscatal.3c01530. eCollection 2023 Jun 2.
Dye decolorizing peroxidases (DyP) have attracted interest for applications such as dye-containing wastewater remediation and biomass processing. So far, efforts to improve operational pH ranges, activities, and stabilities have focused on site-directed mutagenesis and directed evolution strategies. Here, we show that the performance of the DyP from can be drastically boosted without the need for complex molecular biology procedures by simply activating the enzyme electrochemically in the absence of externally added HO. Under these conditions, the enzyme shows specific activities toward a variety of chemically different substrates that are significantly higher than in its canonical operation. Moreover, it presents much broader pH activity profiles with the maxima shifted toward neutral to alkaline. We also show that the enzyme can be successfully immobilized on biocompatible electrodes. When actuated electrochemically, the enzymatic electrodes have two orders of magnitude higher turnover numbers than with the standard HO-dependent operation and preserve about 30% of the initial electrocatalytic activity after 5 days of operation-storage cycles.
染料脱色过氧化物酶（DyP）在含染料废水处理和生物质加工等应用中引起了人们的兴趣。到目前为止，提高操作pH范围、活性和稳定性的努力主要集中在定点诱变和定向进化策略上。在这里，我们表明，通过在不添加外部HO的情况下简单地对酶进行电化学激活，无需复杂的分子生物学程序，就能大幅提高 中DyP的性能。在这些条件下，该酶对多种化学性质不同的底物表现出比其常规操作时显著更高的比活性。此外，它呈现出更宽的pH活性谱，最大值向中性至碱性偏移。我们还表明，该酶可以成功地固定在生物相容性电极上。当进行电化学驱动时，酶电极的周转数比标准的依赖HO的操作高两个数量级，并且在5天的操作-储存循环后仍保留约30%的初始电催化活性。
