anthraquinone dyes
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Chemosphere ◽  
2022 ◽  
Vol 287 ◽  
pp. 131845
Author(s):  
Jonathan M. Dilger ◽  
Todd M. Martin ◽  
Benjamin P. Wilkins ◽  
Brian C. Bohrer ◽  
Kelly M. Thoreson ◽  
...  
Keyword(s):  

2021 ◽  
Vol 22 (22) ◽  
pp. 12524
Author(s):  
Anna Masek ◽  
Angelika Plota ◽  
Julia Chrzastowska ◽  
Małgorzata Piotrowska

This study aimed to present the influence of bio-based and anthraquinone dyes and their combinations on the optical properties of ethylene-propylene (EPM) composites after thermo-oxidative and climatic aging. Therefore, the chosen polymer was filled with a natural, plant-origin flavonoid—quercetin, and with two commercial anthraquinone dyes (C.I. Solvent Yellow 163 and C.I. Solvent Red 207). The manufactured polymer composites were subjected to accelerated aging tests: weathering and thermo-oxidation, respectively. Examination of the materials’ properties indicated that the combination of synthetic and natural dyes can result in better resistance to oxidizing agents and higher thermal stability of ethylene-propylene products. Moreover, color change of quercetin-containing samples due to exposure to simulated atmospheric conditions could be a promising solution for use as aging indicators in intelligent packaging materials that will inform about the ongoing degradation process. Another interesting finding is that these samples exhibited good fungistatic activity against Candida albicans yeast and Aspergillus niger mold. Overall, this novel solution based on hybrid polymer composites containing natural and commercial dyes is a more environmentally friendly alternative to traditional materials used in the plastic packaging industry with better and more desirable properties.


Author(s):  
Sanket Borad

Abstract: Textile industries produce large amounts of waste water. Presence of various dyes like reactive dyes, azo dyes, anthraquinone dyes, etc.is noted in textile industry effluent. In this work we intend to target azo dyes and anthraquinone dyes which has various colouring and toxic effects. Literature review shows that there are various sustainable wastewater treatments namely adsorption, electro-coagulation, ultrasonic treatment, etc. The present investigation intends to discuss the adsorption method for the treatment of industrial wastewater using metal oxide nanoparticles. Literature review supports the use of synthesized porous MgO powder at Nanoscale for the removal of dyes from aqueous solution. Results indicate that the MgO powder can remove more than 98% of both dyes under optimum operational conditions. At various MgO dosages, dye concentrations, solution pH and contact time in a batch reactor are studied. The analysis is followed by FTIR & XRD. Keyword: Waste-water, MgO, Nano particle, Adsorption, Congo red


Materials ◽  
2021 ◽  
Vol 14 (20) ◽  
pp. 6030
Author(s):  
Agnieszka Kołodziejczak-Radzimska ◽  
Joanna Zembrzuska ◽  
Katarzyna Siwińska-Ciesielczyk ◽  
Teofil Jesionowski

A TiO2/ZnO oxide system was proposed as a support for the immobilization of laccase from Trametes versicolor (LTV). The obtained TiO2/ZnO/LTV biocatalytic system was then applied in the decolorization/degradation of C.I. Reactive Black 5 and C.I. Acid Green 25 dyes. The efficiency of immobilization was evaluated based on catalytic properties (Bradford method, oxidation reaction of 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)) and physicochemical (spectroscopic, porous, electrokinetic) analysis. The immobilization process was carried out with high performance (99.4%). Immobilized laccase retained about 40% of its activity in the whole analyzed temperature range and after 10 reaction cycles. Immobilization efficiency was also indirectly confirmed by the presence of characteristic functional groups (–C–H and –C–O), nitrogen and carbon on the TiO2/ZnO/LTV biocatalytic surface, identified by spectroscopic analyses. The increase in the surface area to 126 m2/g, change of isoelectric point (2.0) and zeta potential ranges (from +12.0 to −20.0 mV) after the immobilization process were also observed. The results show that the designed biocatalytic system enables the removal of acid dyes (C.I. Reactive Black 5 and C.I. Acid Green 25) with high efficiency (99% and 70%, respectively). Mass spectroscopy analysis indicated possible degradation products formed by the cleavage of N=N and C–N bonds.


2021 ◽  
Vol 2049 (1) ◽  
pp. 012046
Author(s):  
Raja Ifriadi ◽  
Miranti ◽  
Yuana Nurulita ◽  
Andi Dahliaty ◽  
Yanti ◽  
...  

Abstract One major concern of the textile industry waste is the health hazard imposed by textile dye waste effluents. Anthraquinone dyes are the second largest group of dyes produced and used annually worldwide, that is difficult to degrade naturally. Biological methods using enzymes for waste treatment is gaining popularity due to its eco-friendliness. Laccase is an enzyme with potential to degrade textile dyes, due to its wide ability to oxidize a wide range of substrates. The aim of this study was to evaluate the ability of T. asperellum LBKURCC1 laccase crude extract to decolorize the anthraquinone anionic dye Acid Blue 25 (AB25). A solution of 50 ppm AB25, pH 5.5, was treated with T. asperellum LBKURCC1 laccase crude extract and incubated at room temperature. Absorbance of the solution at 603 nm was measured daily and compared to buffer and heat denatured enzyme controls. No decolorization of AB25 was observed up to 6 days incubation in the enzyme treated samples, as well as the controls. Addition of 0.1 to 5 mM of 1-hydroxybenzotriazole hydrate (HBT) to the decolorization assay did not succeed in mediating the redox reaction of AB25 oxidation by the T. asperellum LBKURCC1 laccase.


2021 ◽  
Vol 22 (16) ◽  
pp. 8683
Author(s):  
Kanako Sugawara ◽  
Toru Yoshida ◽  
Rena Hirashima ◽  
Ryoko Toriumi ◽  
Hotaka Akiyama ◽  
...  

DyP-type peroxidases are a family of heme peroxidases named for their ability to degrade persistent anthraquinone dyes. DyP-type peroxidases are subclassified into three classes: classes P, I and V. Based on its genome sequence, Streptomyces avermitilis, eubacteria, has two genes presumed to encode class V DyP-type peroxidases and two class I genes. We have previously shown that ectopically expressed SaDyP2, a member of class V, indeed has the characteristics of a DyP-type peroxidase. In this study, we analyzed SaDyP1, a member of the same class V as SaDyP2. SaDyP1 showed high amino acid sequence identity to SaDyP2, retaining a conserved GXXDG motif and catalytic aspartate. SaDyP1 degraded anthraquinone dyes, which are specific substrates of DyP-type peroxidases but not azo dyes. In addition to such substrate specificity, SaDyP1 showed other features of DyP-type peroxidases, such as low optimal pH. Furthermore, immunoblotting using an anti-SaDyP2 polyclonal antibody revealed that SaDyP1 and/or SaDyP2 is expressed in mycelia of wild-type S. avermitilis.


2021 ◽  
Vol 22 (12) ◽  
pp. 6265
Author(s):  
Amrita Rai ◽  
Johann P. Klare ◽  
Patrick Y. A. Reinke ◽  
Felix Englmaier ◽  
Jörg Fohrer ◽  
...  

A novel cytoplasmic dye-decolorizing peroxidase from Dictyostelium discoideum was investigated that oxidizes anthraquinone dyes, lignin model compounds, and general peroxidase substrates such as ABTS efficiently. Unlike related enzymes, an aspartate residue replaces the first glycine of the conserved GXXDG motif in Dictyostelium DyPA. In solution, Dictyostelium DyPA exists as a stable dimer with the side chain of Asp146 contributing to the stabilization of the dimer interface by extending the hydrogen bond network connecting two monomers. To gain mechanistic insights, we solved the Dictyostelium DyPA structures in the absence of substrate as well as in the presence of potassium cyanide and veratryl alcohol to 1.7, 1.85, and 1.6 Å resolution, respectively. The active site of Dictyostelium DyPA has a hexa-coordinated heme iron with a histidine residue at the proximal axial position and either an activated oxygen or CN− molecule at the distal axial position. Asp149 is in an optimal conformation to accept a proton from H2O2 during the formation of compound I. Two potential distal solvent channels and a conserved shallow pocket leading to the heme molecule were found in Dictyostelium DyPA. Further, we identified two substrate-binding pockets per monomer in Dictyostelium DyPA at the dimer interface. Long-range electron transfer pathways associated with a hydrogen-bonding network that connects the substrate-binding sites with the heme moiety are described.


Author(s):  
Amrita Rai ◽  
Johann P. Klare ◽  
Patrick Y.A. Reinke ◽  
Felix Englmaier ◽  
Jörg Fohrer ◽  
...  

A novel cytoplasmic dye decolorizing peroxidase from Dictyostelium discoideum was investigated that oxidizes anthraquinone dyes, lignin model compounds and general peroxidase substrates like ABTS efficiently. Unlike related enzymes, an aspartate residue replaces the first glycine of the conserved GXXDG motif in Dictyostelium DyPA. In solution, Dictyostelium DyPA exists as a stable dimer with the side chain of Asp146 contributing to the stabilization of the dimer interface by extending the hydrogen bond network connecting two monomers. To gain mechanistic insights, we solved the Dictyostelium DyPA structures in the absence of substrate as well as in the presence of potassium cyanide and veratryl alcohol to 1.7, 1.85, and 1.6 Å resolution, respectively. The active site of Dictyostelium DyPA has a hexa-coordinated heme iron with a histidine residue at the proximal axial position and either an activated oxygen or CN- molecule at the distal axial position. Asp149 is in an optimal conformation to accept a proton from H2O2 during the formation of compound I. Two potential distal solvent channels and a conserved shallow pocket leading to the heme molecule were found in Dictyostelium DyPA. Further, we identified two substrate-binding pockets per monomer in Dictyostelium DyPA at the dimer interface. Long-range electron transfer pathways associated with a hydrogen-bonding network that connects the substrate-binding sites with the heme moiety are described.


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