Oligomerization of 3-substituted quinolines by catalytic activity of soybean peroxidase as a wastewater treatment. Product formation and computational studies

Mashhadi, Neda; Taylor, Keith E.; Biswas, Nihar; Meister, Paul; Gauld, James W.

doi:10.1016/j.cej.2019.01.184

Cited by 17 publications

(6 citation statements)

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“…7(e)], corresponding to the loss of ‐SO 2 group from MO or loss of ‐SO 3 group from oxygenated MO. Previous researchers also have reported oxygenation in the MS environment 19,22 . The fragmentation products were consistent with similar products detected during analysis of MO by Baiochhi et al .…”

Section: Resultssupporting

confidence: 88%

“…6(e)]. A possible pathway for the formation of an azo‐dimer is through the intermediate N‐N‐coupling product, a hydrazine, which was not detected owing to its rapid oxidation to the azo‐compound 19,22 . An oxidative trimer and its fragmentation product, with the loss of ‐OCH 2 was observed, as shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…In peroxidase reactions H 2 O 2 is a stoichiometric co‐substrate; thus, insufficient peroxide would limit the substrate conversion but an excess could irreversibly inactivate the enzyme by conversion of Compound II to Compound III [peroxy‐iron (III) free radical] 19 . Optimization of H 2 O 2 was done at the pH optima established above.…”

Section: Resultsmentioning

confidence: 99%

“…Enzyme activity was measured as U mL –1 : one unit is defined as the number of micromoles of H 2 O 2 converted per minute at pH 7.4 and room temperature (23 °C). The activity was determined through the rate of formation of pink chromophore (quinoneimine) at 510 nm and an extinction coefficient of 6000 mol L −1 cm −1 , by reaction of 4‐aminoantipyrine and phenol in the presence of H 2 O 2 with the enzyme as a catalyst 19 . The stock solution used here had an activity of 50 U mL –1 and a molar concentration from the A 403 of 33.6 μmol L –1 (i.e.−1.0 U mL –1 corresponds to 0.67 μmol L –1 ).…”

Section: Experimental Protocolmentioning

confidence: 99%

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Soybean peroxidase‐catalyzed degradation of a sulfonated dye and its azo‐cleavage product

Kaur

Taylor

Biswas

2020

J of Chemical Tech & Biotech

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BACKGROUNDThe presence of azo dyes in wastewater from the textile industry is a major environmental concern. The dyes not only make water aesthetically unacceptable, but also have severe toxicological concerns. Research into treatment processes for removal of dyes has focused primarily on decolourization and little attention has been focused on analysis of the degradation products, that could plausibly be more toxic than the parent compound. This study focusses on soybean peroxidase (SBP)‐catalyzed treatment of two azo dyes, Methyl Orange (MO) and CI Direct Yellow 12 (DY12) in water, chosen because they lack phenolic and primary anilino functional groups, which are usually expected to form free radicals under peroxidase catalysis.RESULTSDY12 was found not to be a substrate of SBP, but optimized reaction conditions for 0.50 mmol L–1 MO and 1.0 mmol L–1 p‐anisidine (structurally analogous to 4‐ethoxyaniline, a possible azo‐cleavage product of DY12) achieved ≥95% conversion at exceptionally low minimum effective SBP activities (0.0070 and 0.0018 U mL–1) at pH optima of 4.0 and 5.5 and [hydrogen peroxide]/[substrate] of 2 and 1, respectively.CONCLUSIONSMass spectrometric (MS) analysis for the substrates revealed formation of dimers and trimers for p‐anisidine. For MO, high‐performance liquid chromatography, UV‐visible spectrophotometry and MS provided evidence of azo‐bond cleavage, hetero‐coupling of the dye with the cleavage product and also self‐coupling of the dye through tertiary amine activation. © 2020 Society of Chemical Industry (SCI)

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Section: Resultssupporting

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Experimental Protocolmentioning

confidence: 99%

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Soybean peroxidase‐catalyzed degradation of a sulfonated dye and its azo‐cleavage product

Kaur

Taylor

Biswas

2020

J of Chemical Tech & Biotech

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“…Also, it is easy to cause an acidification and eutrophication of water [8]. Furthermore, its toxicity [9] includes causing cancer, teratogenesis and mutagenicity of animals and human [8,10]. Overall, it has posed a threat to water ecological security and human health.…”

Section: Introductionmentioning

confidence: 99%

Application of copper sulfate based fenton-like catalyst in degradation of quinoline

Jiao

Gong

Peng

et al. 2021

Environmental Engineering Research

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In the practical application of water treatment, the Fenton reaction usually works at a lower pH. To overcome the above shortcomings, a Fenton-like reaction system with copper sulfate as a catalyst was proposed. In this paper, quinoline was used as the target pollutant and the effects of catalyst dosage, H 2 O 2 dosage, reaction temperature, and initial concentration of quinoline and pH on the removal effect were investigated, and the evolution in pH and hydroxyl radical concentration during reaction, as well as the possible catalytic mechanism and degradation pathway were clarified. The results show that under a catalyst dosage of 0.4 gL -1 , a H 2 O 2 dosage of 196 mmolL -1 , a quinoline concentration of 100 mgL -1 and a temperature of 75°C, the removal of quinoline and total organic carbon (TOC) reaches 99.5% and 87.2% in 65 min, respectively. Furthermore, the copper sulfate-driven homogeneous Fenton system exhibits a superior adaptability to pH in the range of 3.8 to 8.8. In the degradation of quinoline, •OH radicals may attack the nitrogen ring and the benzene ring in sequence. The work provides a technical support for the treatment of organic wastewater, and shows promising in practical applications.

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Peroxidases: Role in Bioremediation

Afreen,

Singh,

Kumar

2024

Microbial Enzymes

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Oligomerization of 3-substituted quinolines by catalytic activity of soybean peroxidase as a wastewater treatment. Product formation and computational studies

Cited by 17 publications

References 50 publications

Soybean peroxidase‐catalyzed degradation of a sulfonated dye and its azo‐cleavage product

Soybean peroxidase‐catalyzed degradation of a sulfonated dye and its azo‐cleavage product

Application of copper sulfate based fenton-like catalyst in degradation of quinoline

Peroxidases: Role in Bioremediation

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