Results 141 to 150 of about 335,447 (176)

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

FEBS 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. We have determined the crystal structures of DyP with ascorbic acid and 2,6‐dimethoxyphenol at 1.5 and 1.4 Å, respectively.
Yasushi Sugano, Toru Yoshida, Hideaki Tsuge   +2 more
exaly   +5 more sources

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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).
Ashwani Kumar Sharma, Shailly Tomar, Vikram Dalal   +2 more
exaly   +3 more sources

Immobilized dye-decolorizing peroxidase (DyP) and directed evolution variants for hydrogen peroxide biosensing

Biosensors and Bioelectronics, 2020
Immobilized dye-decolorizing peroxidase from Pseudomonas putida MET94 (PpDyP) and three variants generated by directed evolution (DE) are studied aiming at the design of a biosensor for H2O2 detection. Structural properties of the enzymes in solution and
Smilja Todorović, Celia M Silveira, Vania Brissos   +2 more
exaly   +2 more sources

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, Lindsay D. Eltis
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, M T, Moreira, G, Feijoo, J M, Lema   +3 more
openaire   +2 more sources

Role of H164 in a unique dye-decolorizing heme peroxidase DyP

Biochemical and Biophysical Research Communications, 2004
The expression system of a unique dye-decolorizing peroxidase DyP in Escherichia coli has been constructed. The molecular mass of the expressed DyP (eDyP) is 47kDa, indicating no any modification with saccharides. The characteristics of eDyP were almost the same as those of native DyP from a fungus Thanatephorus cucumeris Dec 1 and recombinant DyP with
YASUSHI SUGANO, Yosuke Ishii, MAKOTO SHODA   +2 more
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Contribution of manganese peroxidase and laccase to dye decoloration by Trametes versicolor

Applied Microbiology and Biotechnology, 2005
During dye decoloration by Trametes versicolor ATCC 20869 in modified Kirk's medium, manganese peroxidase (MnP) and laccase were produced, but not lignin peroxidase, cellobiose dehydrogenase or manganese-independent peroxidase. Purified MnP decolorized azo dyes [amaranth, reactive black 5 (RB5) and Cibacron brilliant yellow] in Mn(2+)-dependent ...
Paul-Philippe, Champagne, Juliana Akit, Ramsay   +1 more
openaire   +2 more sources

Exploitation of neglected horseradish peroxidase izoenzymes for dye decolorization

International Biodeterioration & Biodegradation, 2015
Abstract Horseradish peroxidase (HRP) is enzyme first described more than 200 years ago and yet there are still some aspects of this potent enzyme to be tackled. Researchers were focused on most abundant isoenzyme HRP C1A while remaining, particularly anionic isoenzymes were discarded in purification process. This work describes exploitation of those
Vujčić, Zoran, Janović, Barbara, Lončar, Nikola, Margetić, Aleksandra, Božić, Nataša, Dojnov, Biljana, Vujčić, Miroslava   +6 more
openaire   +3 more sources

Evaluation of a dye-decolorizing peroxidase from Comamonas serinivorans for lignin valorization potentials

International Journal of Biological Macromolecules, 2023
Although dye-decolourising peroxidases (DyPs) are well-known for lignin degradation, a comprehensive understanding of their mechanism remains unclear. Therefore, studying the mechanism of lignin degradation by DyPs is necessary for industrial applications and enzyme engineering.
Sivasamy, Sethupathy, Rongrong, Xie, Nian, Liang, Raja Mohamed Beema, Shafreen, Mohamed Yassin, Ali, Zhipeng, Zhuang, Liang, Zhe, , Zahoor, Yang-Chun, Yong, Daochen, Zhu   +9 more
openaire   +2 more sources

A bacterial cold-active dye-decolorizing peroxidase from an Antarctic Pseudomonas strain

Applied Microbiology and Biotechnology, 2023
DyP (dye-decolorizing peroxidase) enzymes are hemeproteins that catalyze the H2O2-dependent oxidation of various molecules and also carry out lignin degradation, albeit with low activity. We identified a dyp gene in the genome of an Antarctic cold-tolerant microbe (Pseudomonas sp. AU10) that codes for a class B DyP.
Célica Cagide, Juan José Marizcurrena, Diego Vallés, Beatriz Alvarez, Susana Castro-Sowinski   +4 more
openaire   +2 more sources