Results 191 to 200 of about 2,410 (230)

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, Miho, Sasaki, Yoshikazu, Tanaka, Koichiro, Ishimori   +3 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, M T, Moreira, G, Feijoo, J M, Lema   +3 more
openaire   +2 more sources

Characterization of Dye-Decolorizing Peroxidases from Rhodococcus jostii RHA1

Biochemistry, 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. Steady-state kinetic studies of these enzymes revealed that they have much lower peroxidase activities than C- and D-type DyPs ...
Joseph N, Roberts, Rahul, Singh, Jason C, Grigg, Michael E P, Murphy, Timothy D H, Bugg, Lindsay D, Eltis   +5 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

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

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
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 ...
Christoph J, Behrens, Kateryna, Zelena, Ralf G, Berger   +2 more
openaire   +2 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 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

Enhanced dye decolorization efficiency by citraconic anhydride-modified horseradish peroxidase

Journal of Molecular Catalysis B: Enzymatic, 2006
Abstract Bromophenol blue and methyl orange removal capabilities of citraconic anhydride-modified horseradish peroxidase were compared with those of native horseradish peroxidase. Citraconic anhydride-modified horseradish peroxidase showed higher decolorization efficiencies for both dyes than native horseradish peroxidase.
Jian-Zhong Liu, Teng-Li Wang, Liang-Nian Ji   +2 more
openaire   +1 more source