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

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 M...

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Bibliographic Details
Published in:Bioresource technology 2023-12, Vol.390, p.129897, Article 129897
Main Authors: Jiménez Vizcarra, María J, Mahendra, Shaily, Wang, Meng
Format: Article
Language:English
Subjects:
Catalysis
Enzymes, Immobilized
Gels
Manganese
Peroxidases
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Summary: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.
ISSN:0960-8524
1873-2976
1873-2976
DOI:10.1016/j.biortech.2023.129897