Laccase-Catalyzed Removal of Phenol and Benzenediols from Wastewater

Saha, Beeta; Taylor, Keith E.; Bewtra, Jatinder K.; Biswas, Nihar

doi:10.1061/(asce)hz.1944-8376.0000050

Cited by 14 publications

(3 citation statements)

References 37 publications

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“…This ability to easily oxidize phenols has allowed laccase to find a possible niche for environmental cleanup from wastewaters of phenolic substances, such as phenol and catechol, and synthetic dyes. 7 − 9 Laccases have also found use as catalysts for oxidative transformations of nonphenolic small molecules, especially in the presence of radical mediators. Such reactions include oxidation of alcohols to aldehydes and ketones, coupling of phenols and steroids, and carbon–nitrogen bond formation.…”

Section: Introductionmentioning

confidence: 99%

“…Synthetically, laccases are well-known for their ability to polymerize phenol and phenol derivatives via oxidizing the phenol substrate with the concomitant reduction of oxygen to water. , This polymerization occurs through the production of phenoxy radicals which can then undergo C–C or C–O coupling at the ortho- and/or para-position. This ability to easily oxidize phenols has allowed laccase to find a possible niche for environmental cleanup from wastewaters of phenolic substances, such as phenol and catechol, and synthetic dyes. − Laccases have also found use as catalysts for oxidative transformations of nonphenolic small molecules, especially in the presence of radical mediators. Such reactions include oxidation of alcohols to aldehydes and ketones, coupling of phenols and steroids, and carbon–nitrogen bond formation. − …”

Section: Introductionmentioning

confidence: 99%

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Polymer-Assisted Biocatalysis: Effects of Macromolecular Architectures on the Stability and Catalytic Activity of Immobilized Enzymes toward Water-Soluble and Water-Insoluble Substrates

Scheibel

Gitsov

2018

ACS Omega

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The aim of this study is to develop efficient enzyme immobilization media that will enable the reuse of the biocatalysts over multiple cycles, increase their thermal stability, and attenuate their activity toward hydrophobic substrates for “green” transformations in aqueous media. For this purpose, amphiphilic AB and ABA block copolymers were synthesized and tested with laccase (a multicopper oxidase). In all cases, the hydrophilic B block consisted of poly(ethylene glycol), PEG, with molecular masses of 3, 5, 13, 20, or 13 kDa poly(ethylene oxide). The hydrophobic A blocks were made of linear poly(styrene), PS; hyperbranched poly(p-chloromethyl styrene); or dendritic poly(benzyl ether)s of generations 2, 3, and 4 (G2, G3, and G4) with molecular masses ranging from 1 to 24 kDa. A total of 23 different copolymers (self-assembling into micelles or physical networks) were evaluated. Notable activity enhancements were achieved with both micelles (up to 253%) and hydrogels (up to 408%). The highest enzymatic activity and thermal stability were observed with laccase immobilized in hydrogels consisting of the linear ABA block copolymer PS2.7k–PEG3k–PS2.7k (13 290 μkat/L, 65 °C, ABTS test). This represents a 1245% improvement over native laccase at the same conditions. At 25 °C, the same complex showed a 1236% higher activity than the enzyme. The highest polymerization yield for a water-insoluble monomer was achieved with laccase immobilized in hydrogels composed of linear–dendritic ABA copolymer G3–PEG5k–G3 (85.5%, 45 °C, tyrosine monomer). The broad substrate specificity and reusability of the immobilized laccase were also demonstrated by the successful discoloration of bromophenol blue, methyl orange, and rhodamine B over eight repetitive cycles.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Polymer-Assisted Biocatalysis: Effects of Macromolecular Architectures on the Stability and Catalytic Activity of Immobilized Enzymes toward Water-Soluble and Water-Insoluble Substrates

Scheibel

Gitsov

2018

ACS Omega

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“…The oxidation of catechol using laccase as catalyst has been studied. Saha et al investigated a two-step treatment method for the removal of phenol, benzenediols, and an equimolar mixture of phenol and benzenediols from water and demonstrated that the proposed enzymatic method is a viable alternative means to remove phenol and benzenediols from industrial wastewaters (Saha et al, 2011). Tu sek et al tested two different methods to immobilize laccase from Trametes versicolor and compared them for the catechol polymerization using different reactors (Tu sek et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

Enzymatic polymerization of catechol under high-pressure homogenization for the green coloration of textiles

Noro

et al. 2018

Journal of Cleaner Production

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a b s t r a c tLaccase from Myceliophthora thermophila was used to catalyze the polymerization of catechol under high-pressure homogenization for the green coloration of textile substrates. The oxidation reactions were conducted using different forms of laccase, namely native laccase, PEGylated laccase and PEGylated laccase immobilized onto an epoxy resin. The three enzyme forms were deposited inside a polyester fabric bag during the experiments. The amount of polymer obtained was similar when using the three enzyme forms and its dispersion in water/DMSO mixture lead to powder particles of about 30e60 nm. The immobilized and PEGylated enzymes lead to poly(catechol) with 13 and 10 units, respectively, while the native form gave rise to shorter polymers (DP ¼ 8). We have shown that the oxidation of catechol conducted under high-pressure homogenization can be an efficient methodology for the in situ coloration of textiles. The polymers produced by this methodology stained strongly the textile container, revealing this experimental set-up as a promising greener coloration/coating methodology involving milder conditions than the normally used in textile processes.

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Stimulation of Phenol Removal Efficiency of Aspergillus versicolor by Surfactants, a Promising Way to Treat Phenol‐Containing Waste Waters

Karatay

Gül

Dönmez

2014

J Surfact & Detergents

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The effect of the cationic surfactant, dodecyl trimethyl ammonium bromide (DTAB), on phenol bioremoval efficiency of an Aspergillus versicolor strain was examined. The strain was grown in mineral salt (MS) medium and the effect of DTAB was investigated as a function of different pH values, phenol and surfactant concentrations. The effect of pH was tested within the range of 4–7 and the maximum bioremoval was found at pH 4. Initial phenol concentrations investigated ranged from 100 to 600 mg/L, and the effects of surfactant concentrations on the removal were tested with 0, 0.25, 0.5 and 1 mM DTAB, which showed that 0.5 mM surfactant was the most effective concentration. The maximum bioremoval rates found after 72 h incubation were 99.48 and 99.15 % in 100 and 200 mg/L initial phenol‐containing samples, respectively, where the phenol removal capacity of the fungus was only 142.373 mg/g in the DTAB blank samples. The maximum phenol uptake capacity of 267.162 mg/g was measured in the presence of 0.5 mM DTAB at 200 mg/L initial phenol concentration. These results showed that DTAB considerably increased the bioremoval efficiency of the strain tested at relatively lower phenol concentrations. The feasibility of this bioremoval method for industrial wastewater treatment is discussed.

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Laccase-Catalyzed Removal of Phenol and Benzenediols from Wastewater

Cited by 14 publications

References 37 publications

Polymer-Assisted Biocatalysis: Effects of Macromolecular Architectures on the Stability and Catalytic Activity of Immobilized Enzymes toward Water-Soluble and Water-Insoluble Substrates

Polymer-Assisted Biocatalysis: Effects of Macromolecular Architectures on the Stability and Catalytic Activity of Immobilized Enzymes toward Water-Soluble and Water-Insoluble Substrates

Enzymatic polymerization of catechol under high-pressure homogenization for the green coloration of textiles

Stimulation of Phenol Removal Efficiency of Aspergillus versicolor by Surfactants, a Promising Way to Treat Phenol‐Containing Waste Waters

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