Results 141 to 150 of about 248,013 (170)

Redox thermodynamics of B-class dye-decolorizing peroxidases [PDF]

open access: yesJournal of Inorganic Biochemistry, 2019
With>5000 annotated genes dye-decolorizing peroxidases (DyPs) represent a heme b peroxidase family of broad functional diversity. Bacterial B-class DyPs are poor peroxidases of unknown physiological function. Hydrogen peroxide efficiently mediates the
Paul G Furtmüller   +2 more
exaly   +5 more sources

Superoxide versus peroxide activation of dye decolorizing peroxidases for bioelectrocatalysis

open access: yesBioresource Technology Reports
Here we show that dye decolorizing peroxidases can be electrochemically activated for substrate oxidation without addition of exogenous H2O2, yielding activities similar or better than in their conventional operation.
Daniel H Murgida   +2 more
exaly   +5 more sources

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.
Patricia Teixeira Borges   +2 more
exaly   +3 more sources
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The multihued palette of dye-decolorizing peroxidases

Archives of Biochemistry and Biophysics, 2015
Dye-decolorizing peroxidases (DyPs; EC 1.11.1.19) are heme enzymes that comprise a family of the dimeric α+β barrel structural superfamily of proteins. The first DyP, identified relatively recently in the fungus Bjerkandera adusta, was characterized for its ability to catalyze the decolorization of anthraquinone-based industrial dyes. These enzymes are
Rahul Singh   +2 more
exaly   +3 more sources

Biochemical features of dye‐decolorizing peroxidases: Current impact on lignin degradation [PDF]

open access: yesBiotechnology 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.
Gianluca Catucci   +2 more
exaly   +3 more sources

Characterization of dye-decolorizing peroxidase from Bacillus subtilis

Archives of Biochemistry and Biophysics, 2020
The dye-decolorizing peroxidases (DyPs) belong to a unique heme peroxidase family for their biotechnological potential to detoxify synthetic dyes. In this work, we have biochemically and structurally characterized the dye-decolorizing peroxidase from Bacillus subtilis (BsDyP).
Poonam Dhankhar   +6 more
openaire   +2 more sources

Dye Decolorization by Manganese Peroxidase in an Enzymatic Membrane Bioreactor

Biotechnology Progress, 2008
In the present work an enzymatic membrane reactor (EMR) for the oxidation of azo dyes by manganese peroxidase (MnP) has been developed. The configuration consisted of a stirred tank reactor coupled with an ultrafiltration membrane. The membrane allowed for most of the enzymatic activity to be recovered while both the parent dye and the degradation ...
C, López   +3 more
openaire   +2 more sources

Comparative Cold Shock Expression and Characterization of Fungal Dye-Decolorizing Peroxidases

Applied Biochemistry and Biotechnology, 2016
Dye-decolorizing peroxidases (DyPs) from Auricularia auricula-judae, Bjerkandera adusta, Pleurotus ostreatus and Marasmius scorodonius (Basidiomycota) were expressed in Escherichia coli using the cold shock-inducible expression system pCOLD I DNA. Functional expression was achieved without the addition of hemin or the co-expression of any chaperones ...
Ralf G Berger
exaly   +3 more sources

A Dye-Decolorizing Peroxidase from Vibrio cholerae

Biochemistry, 2015
The dye-decolorizing peroxidase (DyP) protein from Vibrio cholerae (VcDyP) was expressed in Escherichia coli, and its DyP activity was assayed by monitoring degradation of a typical anthraquinone dye, reactive blue 19 (RB19). Its kinetic activity was obtained by fitting the data to the Michaelis-Menten equation, giving kcat and Km values of 1.3 ± 0.3 s(
Takeshi, Uchida   +3 more
openaire   +2 more sources

Description of the first fungal dye-decolorizing peroxidase oxidizing manganese(II) [PDF]

open access: yesApplied Microbiology and Biotechnology, 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.
Dolores Linde   +2 more
exaly   +3 more sources

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