Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase

-DyP4, encompassing both peroxidase-mediated oxidation and hydrolytic cleavage. Elucidating this dual chemistry not only redefines the catalytic behavior of the DyP family but also provides a mechanistic cornerstone for engineering robust biocatalysts to eliminate recalcitrant dye pollutants in industrial wastewater.

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Publication Details

Journal
Applied and Environmental Microbiology
Published
2026-04-22
DOI
https://doi.org/10.1128/aem.00282-26
Primary Topic
Enzyme-mediated dye degradation
Type
article
Field-Weighted Citation Impact
0.00

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article

Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase

Rong Jia, Yongming Lu, Feng Tian, Hao Chen et al.
Applied and Environmental Microbiology
Enzyme-mediated dye degradation
article

Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase

Rong Jia, Yongming Lu, Feng Tian, Hao Chen, Peilin Lin
article en

Abstract

-DyP4, encompassing both peroxidase-mediated oxidation and hydrolytic cleavage. Elucidating this dual chemistry not only redefines the catalytic behavior of the DyP family but also provides a mechanistic cornerstone for engineering robust biocatalysts to eliminate recalcitrant dye pollutants in industrial wastewater.

Applied and Environmental Microbiology
Anhui University (CN), Anhui Medical University (CN), National Science Centre (PL)
National Natural Science Foundation of China
Clean water and sanitation
Openalex Percentile: Top 10%
Enzyme-mediated dye degradation
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