Results 151 to 160 of about 248,013 (170)

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
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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
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Bacterial dye-decolorizing peroxidases: Biochemical properties and biotechnological opportunities

ChemistrySelect, 2016
Chao Chen
exaly   +2 more sources

6. Bacterial dye-decolorizing peroxidases

2016
Chao Chen, Tao Li
exaly   +2 more sources

Structure and Reactivity of the Dye-decolorizing Peroxidase (DyP) Family

2015
The dye-decolorizing peroxidases are a recently discovered family of bacterial and fungal peroxidases that are structurally unrelated to the previously studied mammalian and plant peroxidases, but show novel reactivity for oxidation of anthraquinone dyes, phenolic substrates, Mn(ii) and in some cases polymeric lignin.
Rahman Rahmanpour, Timothy D. H. Bugg
openaire   +1 more source

Identification and structural characterization of heme binding in a novel dye‐decolorizing peroxidase, TyrA

Proteins: Structure, Function, and Bioinformatics, 2007
AbstractTyrA is a member of the dye‐decolorizing peroxidase (DyP) family, a new family of heme‐dependent peroxidase recently identified in fungi and bacteria. Here, we report the crystal structure of TyrA in complex with iron protoporphyrin (IX) at 2.3 Å. TyrA is a dimer, with each monomer exhibiting a two‐domain, α/β ferredoxin‐like fold. Both domains
Chloe, Zubieta, Rosanne, Joseph, S Sri, Krishna, Daniel, McMullan, Mili, Kapoor, Herbert L, Axelrod, Mitchell D, Miller, Polat, Abdubek, Claire, Acosta, Tamara, Astakhova, Dennis, Carlton, Hsiu-Ju, Chiu, Thomas, Clayton, Marc C, Deller, Lian, Duan, Ylva, Elias, Marc-André, Elsliger, Julie, Feuerhelm, Slawomir K, Grzechnik, Joanna, Hale, Gye Won, Han, Lukasz, Jaroszewski, Kevin K, Jin, Heath E, Klock, Mark W, Knuth, Piotr, Kozbial, Abhinav, Kumar, David, Marciano, Andrew T, Morse, Kevin D, Murphy, Edward, Nigoghossian, Linda, Okach, Silvya, Oommachen, Ron, Reyes, Christopher L, Rife, Paul, Schimmel, Christina V, Trout, Henry, van den Bedem, Dana, Weekes, Aprilfawn, White, Qingping, Xu, Keith O, Hodgson, John, Wooley, Ashley M, Deacon, Adam, Godzik, Scott A, Lesley, Ian A, Wilson   +46 more
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A dye-decolorizing peroxidase from Vibrio cholerae can demetallate heme

Journal of Inorganic Biochemistry
Iron is an essential element for bacterial survival. Bacterial pathogens have therefore developed methods to obtain iron. Vibrio cholerae, the intestinal pathogen that causes cholera, utilizes heme as an iron source. DyP from V. cholerae (VcDyP) is a dye-decolorizing peroxidase. When VcDyP was expressed in Escherichia coli and purified, it was found to
Takeshi, Uchida, Sayaka, Umetsu, Miho, Sasaki, Haruka, Yoshimura, Issei, Omura, Koichiro, Ishimori   +5 more
openaire   +2 more sources