一种共固定化酶-介体系统，用于在不含二价锰离子的溶液中促进锰过氧化物酶的催化作用。

A Co-Immobilized Enzyme-Mediator System for Facilitating Manganese Peroxidase Catalysis in Solution Free of Divalent Manganese Ions.

机构信息

Department of Civil and Environmental Engineering, University of Pittsburgh, 709 Benedum Hall, 3700 O'Hara St., Pittsburgh, PA 15261, USA.

Department of Civil and Environmental Engineering, University of California, Los Angeles, 580 Portola Plaza, Los Angeles, CA 90095, USA.

出版信息

Bioresour Technol. 2023 Dec;390:129897. doi: 10.1016/j.biortech.2023.129897. Epub 2023 Oct 19.

DOI:10.1016/j.biortech.2023.129897

PMID:37863333

Abstract

Manganese peroxidase (MnP) offers significant potential in various environmental and industrial applications; however, its reliance on Mn ions for electron shuttling limits its use in Mn-deficient systems. Herein, a novel approach is presented to address this limitation by co-immobilizing MnP and Mn in silica gels. These gels were synthesized following the standard sol-gel method and found to effectively immobilize Mn ions, primarily through electrostatic interactions. The MnP co-immobilized with Mn ions in the silica gel exhibited 4-5 times higher activity than the MnP immobilized alone in activity assays, and generated Mn within the gel, indicating the immobilized Mn ions remain capable of shuttling electrons to the co-immobilized MnP. In decolorization tests with two organic dyes, the co-immobilized system also outperformed the MnP immobilized without Mn ions, resulting in 2-4 times higher dye removals. This study will enable a broader application of MnP enzymes in sustainable environmental remediation and industrial catalysis.

摘要

锰过氧化物酶（MnP）在各种环境和工业应用中具有重要的应用潜力；然而，其对 Mn 离子的电子穿梭依赖性限制了其在缺 Mn 系统中的应用。本文提出了一种新的方法来解决这一限制，即将 MnP 和 Mn 共同固定在硅胶中。这些凝胶是通过标准的溶胶-凝胶法合成的，发现它们能够有效地固定 Mn 离子，主要通过静电相互作用。在活性测定中，与单独固定的 MnP 相比，在硅胶中共固定 Mn 离子的 MnP 表现出 4-5 倍的更高活性，并且在凝胶中产生 Mn，表明固定的 Mn 离子仍然能够将电子转移到共固定的 MnP。在两种有机染料的脱色测试中，共固定系统的表现也优于没有 Mn 离子固定的 MnP，染料去除率提高了 2-4 倍。这项研究将使 MnP 酶在可持续环境修复和工业催化中的应用更加广泛。