Results 11 to 20 of about 248,013 (170)

Dye-Decolorizing Peroxidases Maintain High Stability and Turnover on Kraft Lignin and Lignocellulose Substrates [PDF]

open access: yesACS Omega
10 p.-5 fig.-1 graph. abst.Fungal enzyme systems for the degradation of plant cell wall lignin, consisting of, among others, laccases and lignin-active peroxidases, are well characterized.
Silja Välimets   +8 more
doaj   +3 more sources

Characterization of Two Hydrogen Peroxide Resistant Peroxidases from Rhodococcus opacus 1CP [PDF]

open access: yesApplied Sciences, 2021
The dye-decolorizing peroxidases (DyP) are a family of heme-dependent enzymes present on a broad spectrum of microorganisms. While the natural function of these enzymes is not fully understood, their capacity to degrade highly contaminant pigments such ...
Anna Christina R. Ngo   +5 more
doaj   +8 more sources

Characterization of a Dye-Decolorizing Peroxidase from Irpex lacteus Expressed in Escherichia coli: An Enzyme with Wide Substrate Specificity Able to Transform Lignosulfonates

open access: yesJournal of Fungi, 2021
A dye-decolorizing peroxidase (DyP) from Irpex lacteus was cloned and heterologously expressed as inclusion bodies in Escherichia coli. The protein was purified in one chromatographic step after its in vitro activation.
Laura Isabel de Eugenio   +6 more
doaj   +2 more sources

Mutational and structural analysis of an ancestral fungal dye‐decolorizing peroxidase [PDF]

open access: yesThe FEBS Journal, 2020
Dye-decolorizing peroxidases (DyPs) constitute a superfamily of heme-containing peroxidases that are related neither to animal nor to plant peroxidase families. These are divided into four classes (types A, B, C, and D) based on sequence features.
Habib, Mohamed H   +17 more
core   +6 more sources

Accelerated directed evolution of dye-decolorizing peroxidase using a bacterial extracellular protein secretion system (BENNY) [PDF]

open access: yesBioresources and Bioprocessing, 2019
Background Dye-decolorizing peroxidases (DyPs) are haem-containing peroxidases that show great promises in industrial biocatalysis and lignocellulosic degradation.
Abdulrahman H. A. Alessa   +7 more
doaj   +2 more sources

Crystal structures of dye-decolorizing peroxidase with ascorbic acid and 2,6-dimethoxyphenol [PDF]

open access: yesFEBS Letters, 2012
The structure of dye-decolorizing peroxidase (DyP)-type peroxidase differs from that of other peroxidase families, indicating that DyP-type peroxidases have a different reaction mechanism.
Sugano, Yasushi   +3 more
core   +4 more sources

Characterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1

open access: yesBiochemistry, 2011
The soil bacterium Rhodococcus jostii RHA1 contains two dye-decolorizing peroxidases (DyPs) named according to the subfamily they represent: DypA, predicted to be periplasmic, and DypB, implicated in lignin degradation.
Lindsay D. Eltis   +11 more
core   +3 more sources

Regulation of dye-decolorizing peroxidase gene expression in Pleurotus ostreatus grown on glycerol as the carbon source [PDF]

open access: yesPeerJ
Dye-decolorizing peroxidases (DyPs) (E.C. 1.11.1.19) are heme peroxidases that catalyze oxygen transfer reactions similarly to oxygenases. DyPs utilize hydrogen peroxide (H2O2) both as an electron acceptor co-substrate and as an electron donor when ...
Jorge Cuamatzi-Flores   +6 more
doaj   +3 more sources

Engineering a Hybrid Heme Pathway for Hemoprotein‐Based Dye‐Decolorizing Peroxidase in Escherichia coli

open access: yesFood Bioengineering
Dye‐decolorizing peroxidases (DyPs) are heme‐dependent oxidoreductases with promising applications in mycotoxin detoxification by acting on the oxidizable conjugated structures of aflatoxin B1 (AFB1).
Yue Sun   +7 more
doaj   +2 more sources

Plastics and Bioplastics End of Life: A Biocatalytic Perspective. [PDF]

open access: yesMicrob Biotechnol
Biocatalysis links selected conventional plastics and bioplastics to biological routes for polymer transformation, product recovery and end‐of‐life management. Enzymes and microbes enable depolymerisation, upcycling and recovery of monomers, platform chemicals and new materials.
de Eugenio LI, Pardo I, Prieto MA.
europepmc   +2 more sources

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