ArticleACS omega2024
Dye-Decolorizing Peroxidases Maintain High Stability and Turnover on Kraft Lignin and Lignocellulose Substrates.
Article in ACS omega, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- Dye-Decolorizing Peroxidase for Lignin Depolymerization: a Comprehensive Review on Enzyme Structural Characteristics, Reaction-Influencing Factors and Efficiency-Enhancing Strategies.Applied biochemistry and biotechnology · 2026Review
- Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase.Applied and environmental microbiology · 2026Article
- Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fungal enzyme systems for the degradation of plant cell wall lignin, consisting of, among others, laccases and lignin-active peroxidases, are well characterized. Additionally, fungi and bacteria contain dye-decolorizing peroxidases (DyP), which are also capable of oxidizing and modifying lignin constituents. Studying DyP activity on lignocellulose poses challenges due to the heterogeneity of the substrate and the lack of continuous kinetic methods. In this study, we report the kinetic parameters of bacterial DyP from
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Registered trials
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