Results 31 to 40 of about 335,447 (176)

Biocatalysis for biorefineries: The case of dye-decolorizing peroxidases

open access: yesBiotechnology 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

Genomic Diversity and Phenotypic Variation in Fungal Decomposers Involved in Bioremediation of Persistent Organic Pollutants

open access: yesJournal of Fungi, 2023
Fungi work as decomposers to break down organic carbon, deposit recalcitrant carbon, and transform other elements such as nitrogen. The decomposition of biomass is a key function of wood-decaying basidiomycetes and ascomycetes, which have the potential ...
Jiali Yu   +5 more
doaj   +1 more source

Isolation and Characterization of Dye Decolorizing Bacteria from The Textile Dye Effluents [PDF]

open access: yes, 2023
The most significant challenge confronted by the textile industries is the discharge of dye effluents which contains toxic chemicals posing a considerable threat to environmental pollution. Biological method of treating effluents using bacteria is one of
Queen rosary Sheela   +3 more
core   +1 more source

Application of a novel alkali-tolerant thermostable DyP-type peroxidase from Saccharomonospora viridis DSM 43017 in biobleaching of eucalyptus kraft pulp. [PDF]

open access: yesPLoS 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

Radical transfer but not heme distal residues is essential for pH dependence of dye-decolorizing activity of peroxidase from Vibrio cholerae [PDF]

open access: yes, 2021
Dye-decolorizing peroxidase (DyP) is a heme-containing enzyme that catalyzes the degradation of anthraquinone dyes. A main feature of DyP is the acidic optimal pH for dye-decolorizing activity.
Uchida, Takeshi   +3 more
core   +1 more source

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]

open access: yesPLoS 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

Isolation of Fungi from a Textile Industry Effluent and the Screening of Their Potential to Degrade Industrial Dyes

open access: yesJournal 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

Roles of distal aspartate and arginine of B-class dye-decolorizing peroxidase in heterolytic hydrogen peroxide cleavage. [PDF]

open access: yesJ Biol Chem, 2018
Dye-decolorizing peroxidases (DyPs) represent the most recently classified hydrogen peroxide dependent heme peroxidase family. Although widely distributed with more than 5000 annotated genes and hailed for their biotechnological potential detailed ...
Pfanzagl V   +10 more
europepmc   +2 more sources

In Vitro Heme Coordination of a Dye-Decolorizing Peroxidase— The Interplay of Key Amino Acids, pH, Buffer and Glycerol - Open Data

open access: yes, 2021
Data of In Vitro Heme Coordination of a Dye-Decolorizing Peroxidase— The Interplay of Key Amino Acids, pH, Buffer and Glycerol Authors: Kevin Nys, Vera Pfanzagl, Jeroen Roefs, Christian Obinger and Sabine Van Doorslaer Manuscript ID: ijms-1302052
Kevin Nys   +3 more
core   +1 more source

High overexpression of dye decolorizing peroxidase TfuDyP leads to the incorporation of heme precursor protoporphyrin IX [PDF]

open access: yes, 2016
Highlights • Dye decolorizing peroxidase TfuDyP binds heme and protoporphyrin IX in vivo. • The activity of TfuDyP is dependent on the expression level in E. coli.
Colpa, Dana I.   +2 more
core   +2 more sources

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