Oxidative degradation of Remazol Turquoise Blue G 133 by soybean peroxidase

Marchis, Tatiana; Avetta, Paola; Bianco-Prevot, A.; Fabbri, Debora; Viscardi, G.; Laurenti, Enzo

doi:10.1016/j.jinorgbio.2010.11.009

Cited by 67 publications

(46 citation statements)

References 38 publications

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“…During decolorization of Orange T4LL, a significant induction in the activities of lignin peroxidase, tyrosinase and reductases (NADH-DCIP, azo and riboflavin) was observed (Dawkar et al, 2010). Dye degrading peroxidase degrades typical peroxidase substrates, but also degrades hydroxyl free anthraquinone, which is not transformed by other peroxidases (Marchis et al, 2011;Sugano et al, 2006). Likewise, a combination of lignin peroxidases and veratyl alcohol also enhances decolorization of azo and anthraquinone dyes (Joshi et al, 2010).…”

Section: Oxidative Enzymesmentioning

confidence: 99%

“…Redox mediators play an important role in oxidative degradation by Streptomyces laccases, primarily by facilitating the movement of electrons in the system (Gonzalez et al, 2009). Dye-degrading peroxidases are reported to degrade hydroxyl-free anthraquinone dyes (Marchis et al, 2011;Sugano et al, 2006). A combination of lignin peroxidases and veratyl alcohol was found to enhance the decolorization of azo and anthraquinone dyes (Joshi et al, 2010).…”

Section: Oxidative Enzymesmentioning

confidence: 99%

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Bacterial diversity and composition in major fresh produce growing soils affected by physiochemical properties and geographic locations

Ibekwe

Yang

et al. 2016

Science of The Total Environment

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Azo dyes and their intermediate degradation products are common contaminants of soil and groundwater in developing countries where textile and leather dye products are produced. The toxicity of azo dyes is primarily associated with their molecular structure, substitution groups and reactivity. To avoid contamination of natural resources and to minimize risk to human health, this wastewater requires treatment in an environmentally safe manner. This manuscript critically reviews biological treatment systems and the role of bacterial reductive and oxidative enzymes/processes in the bioremediation of dye-polluted wastewaters. Many studies have shown that a variety of culturable bacteria have efficient enzymatic systems that can carry out complete mineralization of dye chemicals and their metabolites (aromatic compounds) over a wide range of environmental conditions. Complete mineralization of azo dyes generally involves a two-step process requiring initial anaerobic treatment for decolorization, followed by an oxidative process that results in degradation of the toxic intermediates that are formed during the first step. Molecular studies have revealed that the first reductive process can be carried out by two classes of enzymes involving flavin-dependent and flavin-free azoreductases under anaerobic or low oxygen conditions. The second step that is carried out by oxidative enzymes that primarily involves broad specificity peroxidases, laccases and tyrosinases. This review focuses, in particular, on the characterization of these enzymes with respect to their enzyme kinetics and the environmental conditions that are necessary for bioreactor systems to treat azo dyes contained in wastewater.

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Section: Oxidative Enzymesmentioning

confidence: 99%

Section: Oxidative Enzymesmentioning

confidence: 99%

Bacterial diversity and composition in major fresh produce growing soils affected by physiochemical properties and geographic locations

Ibekwe

Yang

et al. 2016

Science of The Total Environment

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“…Such mechanism allows the oxidation of inorganic and organic substrates, including important environmental pollutants such as dyes or polychlorophenols [17][18][19]. In addition, SBP shows a remarkable thermal stability, works well in a wide pH range and has a low sensitivity to various organic solvents [20][21].…”

Section: Introductionmentioning

confidence: 99%

TiO2-soybean peroxidase composite materials as a new photocatalytic system

Calza

Avetta

Rubulotta

et al. 2014

Chemical Engineering Journal

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“…A related PC dye, reactive blue 21 (RB21), is also extensively used and has been reported to be decolorized by horseradish peroxidase (10). Although the degradation of this dye by soybean peroxidase to the extent of 95% has been reported (11), the products of degradation were recognized only recently as metabolite I (m/z ϭ 437) and metabolite II (m/z ϭ 524) (3). Apart from peroxidases, no other enzymatic method has been reported until now for degradation of RB21.…”

mentioning

confidence: 99%

Structural Insights into 2,2′-Azino-Bis(3-Ethylbenzothiazoline-6-Sulfonic Acid) (ABTS)-Mediated Degradation of Reactive Blue 21 by Engineered Cyathus bulleri Laccase and Characterization of Degradation Products

Kenzom

Srivastava

Mishra

2014

Appl Environ Microbiol

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Advanced oxidation processes are currently used for the treatment of different reactive dyes which involve use of toxic catalysts. Peroxidases are reported to be effective on such dyes and require hydrogen peroxide and/or metal ions. Cyathus bulleri laccase, expressed in Pichia pastoris, catalyzes efficient degradation (78 to 85%) of reactive azo dyes (reactive black 5, reactive orange 16, and reactive red 198) in the presence of synthetic mediator ABTS [2,2=-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)]. This laccase was engineered to degrade effectively reactive blue 21 (RB21), a phthalocyanine dye reported to be decolorized only by peroxidases. The 816-bp segment (toward the C terminus) of the lcc gene was subjected to random mutagenesis and enzyme variants (Lcc35, Lcc61, and Lcc62) were selected based on increased ABTS oxidizing ability. Around 78 to 95% decolorization of RB21 was observed with the ABTS-supplemented Lcc variants in 30 min. Analysis of the degradation products by mass spectrometry indicated the formation of several low-molecular-weight compounds. Mapping the mutations on the modeled structure implicated residues both near and far from the T1 Cu site that affected the catalytic efficiency of the mutant enzymes on ABTS and, in turn, the rate of oxidation of RB21. Several inactive clones were also mapped. The importance of geometry as well as electronic changes on the reactivity of laccases was indicated.

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Oxidative degradation of Remazol Turquoise Blue G 133 by soybean peroxidase

Cited by 67 publications

References 38 publications

Bacterial diversity and composition in major fresh produce growing soils affected by physiochemical properties and geographic locations

Bacterial diversity and composition in major fresh produce growing soils affected by physiochemical properties and geographic locations

TiO2-soybean peroxidase composite materials as a new photocatalytic system

Structural Insights into 2,2′-Azino-Bis(3-Ethylbenzothiazoline-6-Sulfonic Acid) (ABTS)-Mediated Degradation of Reactive Blue 21 by Engineered Cyathus bulleri Laccase and Characterization of Degradation Products

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