Biochemical features of dye-decolorizing peroxidases: Current impact on lignin degradation [PDF]
Biotechnology and Applied Biochemistry, 2020 AbstractDye‐decolorizing peroxidases (DyP) were originally discovered in fungi for their ability to decolorize several different industrial dyes. DyPs catalyze the oxidation of a variety of substrates such as phenolic and nonphenolic aromatic compounds.
Catucci, G. +3 more
core +4 more sources
Application of a novel alkali-tolerant thermostable DyP-type peroxidase from Saccharomonospora viridis DSM 43017 in biobleaching of eucalyptus kraft pulp. [PDF]
PLoS ONE, 2014 Saccharomonospora viridis is a thermophilic actinomycete that may have biotechnological applications because of its dye decolorizing activity, though the enzymatic oxidative system responsible for this activity remains elusive.
Wangning Yu +8 more
doaj +1 more source
Biocatalysis for biorefineries: The case of dye-decolorizing peroxidases
Biotechnology Advances, 2023 Dye-decolorizing Peroxidases (DyPs) are heme-containing enzymes in fungi and bacteria that catalyze the reduction of hydrogen peroxide to water with concomitant oxidation of various substrates, including anthraquinone dyes, lignin-related phenolic and non-phenolic compounds, and metal ions.
Diogo, Silva +4 more
openaire +2 more sources
Comparing Ligninolytic Capabilities of Bacterial and Fungal Dye-Decolorizing Peroxidases and Class-II Peroxidase-Catalases [PDF]
International Journal of Molecular Sciences, 2021 We aim to clarify the ligninolytic capabilities of dye-decolorizing peroxidases (DyPs) from bacteria and fungi, compared to fungal lignin peroxidase (LiP) and versatile peroxidase (VP). With this purpose, DyPs from Amycolatopsis sp., Thermomonospora curvata, and Auricularia auricula-judae, VP from Pleurotus eryngii, and LiP from Phanerochaete ...
Dolores Linde +6 more
openaire +3 more sources
Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II). [PDF]
Appl Microbiol Biotechnol, 2015 Two phylogenetically divergent genes of the new family of dye-decolorizing peroxidases (DyPs) were found during comparison of the four DyP genes identified in the Pleurotus ostreatus genome with over 200 DyP genes from other basidiomycete genomes.
Fernández-Fueyo E +5 more
europepmc +4 more sources
Induction, purification and characterization of a novel manganese peroxidase from Irpex lacteus CD2 and its application in the decolorization of different types of dye. [PDF]
PLoS ONE, 2014 Manganese peroxidase (MnP) is the one of the important ligninolytic enzymes produced by lignin-degrading fungi which has the great application value in the field of environmental biotechnology.
Xing Qin +3 more
doaj +1 more source
Journal of Fungi, 2021 Six fungal strains were isolated from the textile industry effluent in which they naturally occur. Subsequently, the fungal strains were identified and characterized in order to establish their potential decolorizing effect on textile industry effluents.
Juvenal Juárez-Hernández +8 more
doaj +1 more source
Dye decolorization and detoxification potential of Ca-alginate beads immobilized manganese peroxidase [PDF]
BMC Biotechnology, 2015 In view of compliance with increasingly stringent environmental legislation, an eco-friendly treatment technology of industrial dyes and effluents is a major environmental challenge in the color industry. In present study, a promising and eco-friendly entrapment approach was adopted to immobilize purified manganese peroxidase (MnP) produced from an ...
Muhammad Asgher, Muhammad Bilal
core +4 more sources
eLife, 2021 Encapsulin nanocompartments are an emerging class of prokaryotic protein-based organelle consisting of an encapsulin protein shell that encloses a protein cargo.
Katie A Lien +8 more
doaj +1 more source
Protein engineering of Pseudomonas fluorescens peroxidase Dyp1B for oxidation of phenolic and polymeric lignin substrates [PDF]
, 2019 Directed evolution was applied to dye-decolourizing peroxidase Dyp1B from Pseudomonas fluorescens Pf-5, in order to enhance the activity for oxidation of phenolic and lignin substrates.
Ashley, Ben +6 more
core +2 more sources