Results 171 to 180 of about 17,549 (202)

Structural insights at acidic pH of dye‐decolorizing peroxidase from Bacillus subtilis

Proteins: Structure, Function, and Bioinformatics, 2022
Dye‐decolorizing peroxidases (DyPs), a type of heme‐containing oxidoreductase enzymes, catalyze the peroxide‐dependent oxidation of various industrial dyes as well as lignin and lignin model compounds.
P. Dhankhar, V. Dalal, A. Sharma, Pravindra Kumar   +3 more
semanticscholar   +1 more source

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

Characterization of a novel Dye-Decolorizing peroxidase from Brevibacillus agri and its application in detoxification of textile industry wastewater.

Bioresource Technology
Dye-containing wastewater from the textile industry poses severe ecological and health risks. Here, we identified and characterized a novel dye-decolorizing peroxidase (BaDyP) from Brevibacillus agri, notable for its broad substrate range and catalytic ...
Wenjing Lin, Wei Lin, Lizhen Yang, Chunfang Zhang, Xuehui Li, Jianbin Xiao, Xingtong Chen, Fan Cai, Chao Chen, Mingliang Zhang, Yan Zhang, Li Li   +11 more
semanticscholar   +1 more source

New application of a dye-decolorizing peroxidase immobilized on magnetic nanoparticles for efficient simultaneous degradation of two mycotoxins.

Food Chemistry
Nowadays the enzymatic approaches are the most promising strategies for mycotoxins detoxification in food stuffs. Herein, the dye-decolorizing peroxidase RhDypB from Rhodococcus jostii was studied for its ability to degrade two mycotoxins in both free ...
Xinling Du, M. Zheng, Han Zhang, Yangyu Qiu, Fuchun Ji, Zishen Nie, Huidong Xu, Xiaoxuan Li, Shijia Wu, Zhouping Wang, Fuguo Xing, Yu Xia   +11 more
semanticscholar   +1 more source

Enzyme Cascade Reaction Involving Lytic Polysaccharide Monooxygenase and Dye-Decolorizing Peroxidase for Chitosan Functionalization.

Journal of Agricultural and Food Chemistry, 2021
In situ H2O2 generation systems are efficient for H2O2-dependent biocatalytic oxidation reactions. Here, we report that lytic polysaccharide monooxygenases (LPMOs), copper-dependent polysaccharide monooxygenases, can efficiently supply H2O2 in situ to ...
Fei Li, Ruijian Shao, Yingzheng Mao, Wen Yu, Hongbo Yu   +4 more
semanticscholar   +1 more source

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

Brilliant green decolorization by dye decolorizing peroxidase producing bacterium, Achromobacter insolitus isolated from Forest soils of Similipal Biosphere Reserve, Odisha

Bioremediation Journal
Dye-decolorizing peroxidases (DyPs) are recently identified superfamily of heme-containing peroxidases which has received much attention for its potential application in dye decolourization.
Sovana Dutta, Subhashree Rath, Arpita Sarangi, H. Thatoi   +3 more
semanticscholar   +1 more source

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