Triclosan removal by laccase immobilized on mesoporous nanofibers: Strong adsorption and efficient degradation

Xu, Ran; Si, Yifang; Wu, Xuan; Li, Fengting; Zhang, Bingru

doi:10.1016/j.cej.2014.06.060

Cited by 84 publications

(41 citation statements)

References 41 publications

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“…1). Similarly, using a reaction time 120 h, Xu et al [35] observed the laccase-catalysed conversion of triclosan in a pH range 3-7 and an optimum pH in the range 4-6. In the reactions catalysed by HRP, triclosan was converted in the pH range 3.0-9.0 and the highest removal was obtained at pH 7.0, as reported by our group.…”

Section: Effects Of Ph and Temperaturementioning

confidence: 97%

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A comparison between the oxidation with laccase and horseradish peroxidase for triclosan conversion

Melo

Dezotti

Marques

2015

Environmental Technology

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Triclosan is a broad-spectrum biocide used in personal-care products that is suspected to be linked to the emergence of antibiotic-resistant bacteria. In the present work, the enzymes horseradish peroxidase and laccase from Trametes versicolor were evaluated for the conversion of triclosan in an aqueous matrix. The removal of antibacterial activity by the enzymatic processes was evaluated by an assay based on the growth inhibition of Escherichia coli K12. The horseradish peroxidase (HRP) process appears more advantageous than the laccase process in removing triclosan from an aqueous matrix, considering the reaction parameters pH, temperature, catalytic efficiency, and enzyme concentration. The highest conversion of triclosan catalysed by laccase was observed at pH 5.0, that is, lower than the typical pH range (6.5-7.5) of sewage treatment plants' effluents. The efficiency of laccase process was much more impacted by variations in the temperature in the range of 10-40°C. Kinetic studies showed that triclosan is a substrate more specific for HRP than for laccase. The protein content for the HRP-catalysed process was 14 times lower than that for the laccase process. Decay kinetics suggest that reaction mechanisms depend on enzyme concentration and its concentration. Both processes were able to reduce the antibacterial activity, and the residual activity of the treated solution is probably due to non-converted triclosan and not due to the reaction products. The laccase-catalysed conversion of triclosan in an environmental relevant concentration required a higher amount of enzyme than that required in the HRP process.

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Section: Effects Of Ph and Temperaturementioning

confidence: 97%

“…According to Xu et al [35], laccase-catalysed conversion of triclosan showed an optimal temperature of 40 °C and above this value, the conversion gradually decreased. On the other hand, HRP-catalysed conversion of triclosan was less influenced by temperature.…”

Section: Effects Of Ph and Temperaturementioning

confidence: 98%

A comparison between the oxidation with laccase and horseradish peroxidase for triclosan conversion

Melo

Dezotti

Marques

2015

Environmental Technology

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“…The range of compounds oxidized by laccase can be expanded in the presence of appropriate redox mediators such as 1-hydroxybenzotriazole, violuric acid, and ABTS [10,13,14]. In recent studies, laccase was successfully used for the elimination of synthetics dye [15,16], antibiotics [13,17], triclosan [18][19][20], anthracene [21], benzodiazepines [22], pesticide [23], and several other contaminants from aqueous solution.…”

Section: Introductionmentioning

confidence: 98%

Optimization of the enzymatic elimination of flumequine by laccase-mediated system using response surface methodology

Ashrafi

Nasseri

Alimohammadi

et al. 2015

Desalination and Water Treatment

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Response surface methodology (RSM) was applied to optimize the removal of flumequine (FLU) from aqueous solution by laccase from Trametes versicolor. Box-Behnken design (BBD) with four variables namely pH, temperature, FLU initial concentration, and 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid) (ABTS) concentration was used to optimize these factors. The results showed that the predicted values for FLU removal were close to the experimental values, and the R 2 (0.9967) indicated that the regression was able to give a good prediction of response for the FLU removal process in the studied range. Optimization of the factors levels was carried out in two approaches. At first, all factors were set in the studied range. The selected optimal conditions for the maximum removal of FLU (98.27%) were predicted as: temperature of 39.64˚C, pH of 4.06, FLU initial concentration of 90.74 mg L −1 , and ABTS concentration of 1.35 mM. Then, the optimization was carried out by minimizing the amount of ABTS, maximizing the FLU initial concentration, and maximizing the removal efficiency. The recommended optimum conditions are: temperature of 39.19˚C, pH value of 4.32, FLU initial concentration of 125 mg L −1 , and ABTS concentration of 0.28 mM with the percentage FLU removal of 77.76%.

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“…Among these organic pollutants, phenol is well known for its high toxicity in humans and animals (Rangelov and Nicell 2015, Hou et al 2014a, Xu et al 2014. Phenolic pollutants can originate from agricultural and industrial activities, including the partial degradation of phenoxy herbicides, the use of wood preservatives, the generation of wastes by pulp and paper, petrochemicals, dyeing, and other organic chemical and textile industries.…”

Section: Introductionmentioning

confidence: 99%

Characterization and immobilization ofTrametes versicolorlaccase on magnetic chitosan–clay composite beads for phenol removal

Aydemir

Güler

2015

Artificial Cells, Nanomedicine, and Biotechnology

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Laccase from Trametes versicolor was immobilized on magnetic chitosan-clay composite beads by glutaraldehyde crosslinking. The physical, chemical, and biochemical properties of the immobilized laccase and its application in phenol removal were comprehensively investigated. The structure and morphology of the composite beads were characterized by SEM, TGA, and FTIR analyses. The immobilized laccase showed better storage stability and higher tolerance to the changes in pH and temperature compared with free laccase. Moreover, the immobilized laccase retained more than 75% of its original activity after 10 cycles. The efficiency of phenol removal by immobilized laccase was about 80% under the optimum conditions after 4 h.

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Triclosan removal by laccase immobilized on mesoporous nanofibers: Strong adsorption and efficient degradation

Cited by 84 publications

References 41 publications

A comparison between the oxidation with laccase and horseradish peroxidase for triclosan conversion

A comparison between the oxidation with laccase and horseradish peroxidase for triclosan conversion

Optimization of the enzymatic elimination of flumequine by laccase-mediated system using response surface methodology

Characterization and immobilization ofTrametes versicolorlaccase on magnetic chitosan–clay composite beads for phenol removal

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