ArticleAMB Express2018
Comprehensive investigation of a dye-decolorizing peroxidase and a manganese peroxidase from Irpex lacteus F17, a lignin-degrading basidiomycete.
Article in AMB Express, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 59 citations in OpenAlex.
- Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase.Applied and environmental microbiology · 2026Article
- Whole-genome sequencing and comparative genomic analysis ofMicrobial genomics · 2025Article
- Pure mycelium materials production from agri-processing water: Effects of feedstock composition on material properties for packaging applications.Water environment research : a research publication of the Water Environment Federation · 2025Article
- Degradation and detoxification of aflatoxin B1 by two peroxidase enzymes from Irpex lacteus F17.Bioprocess and biosystems engineering · 2025Article
- Characterization of theInternational journal of molecular sciences · 2024Article
- Structure-function characterization of two enzymes from novel subfamilies of manganese peroxidases secreted by the lignocellulose-degrading Agaricales fungi Agrocybe pediades and Cyathus striatus.Biotechnology for biofuels and bioproducts · 2024Article
- Dye-Decolorizing Peroxidase ofACS omega · 2024Article
- Relationship between fruiting body development and extracellular laccase production in the edible mushroomBiochemistry and biophysics reports · 2022Article
- Endophytes in Lignin Valorization: A Novel Approach.Frontiers in bioengineering and biotechnology · 2022Review
- Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases.PloS one · 2022Article
- Trends and Applications of Omics Technologies to Functional Characterisation of Enzymes and Protein Metabolites Produced by Fungi.Journal of fungi (Basel, Switzerland) · 2021Review
- Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase.The FEBS journal · 2021Article
- Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17.Biotechnology for biofuels · 2021Article
- DyP-Type Peroxidases: Recent Advances and Perspectives.International journal of molecular sciences · 2021Review
- A multi-omics approach to lignocellulolytic enzyme discovery reveals a new ligninase activity fromProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Characterization of a Dye-Decolorizing Peroxidase fromJournal of fungi (Basel, Switzerland) · 2021Article
- A DyP-Type Peroxidase ofMolecules (Basel, Switzerland) · 2020Article
- Article
- Linking Enzymatic Oxidative Degradation of Lignin to Organics Detoxification.International journal of molecular sciences · 2018Review
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Authors and funding
5 authors at 1 institution in 1 country.
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Abstract
Irpex lacteus F17 is well-known for its ability to degrade recalcitrant aromatic pollutants, which mainly results from the action of the manganese peroxidase (MnP) that it is able to produce. Recently, the genome sequencing and annotation of this strain provided comprehensive picture of the ligninolytic peroxidase gene family. In addition to revealing the presence of 13 MnPs, genes for five dye-decolorizing peroxidases (DyPs) were also discovered in the I. lacteus F17 genome, which are unrelated to the fungal class II peroxidases. In the present study, amino acid sequences of five DyPs and 13 MnPs, representing two different families of heme peroxidases, were analyzed. Of these, two enzymes, a DyP (Il-DyP4) and a MnP (Il-MnP6) were expressed respectively in Escherichia coli, and were characterized by comparing their molecular models, substrate specificities, and catalytic features. The results showed that Il-DyP4 possessed a higher catalytic efficiency for some representative substrates, and a stronger decolorizing ability to a wide range of synthetic dyes in acidic conditions. Based on electrochemical measurements, Il-DyP4 was found to have a high redox potential of 27 mV at pH 3.5, which was superior to that of Il-MnP6 (- 75 mV), thereby contributing to its ability to oxidize high redox potential substrates, such as veratryl alcohol and polymeric dye Poly R-478. The results highlighted the potential of Il-DyP4 for use in industrial and environmental applications.
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