Effective removal of sulfur dyes from water by biosorption and subsequent immobilized laccase degradation on crosslinked chitosan beads

Nguyen, Thai Anh; Fu, Chun‐Chieh; Juang, Ruey‐Shin

doi:10.1016/j.cej.2016.06.102

Cited by 105 publications

(36 citation statements)

References 43 publications

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“…Following the early attempts to produce stable systems, the applications of immobilized enzymes are continuously increasing [1]. One of the smartest uses of immobilized enzymes is their application in the treatment of wastes, including waste waters [2][3][4][5][6] where both the specific activity and possibility of recycle are combined for maximum performance [7].…”

Section: Introductionmentioning

confidence: 99%

Enhanced biocatalytic sustainability of laccase by immobilization on functionalized carbon nanotubes/polysulfone membranes

Costa

Lima

Sampaio

et al. 2019

Chemical Engineering Journal

139

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Chemically functionalized multi-walled carbon nanotubes (CNTs) are used as carriers for laccase immobilization. In this work, CNTs were modified using different approaches with a combination of methods involving hydrothermal oxidation with nitric acid, treatment with 3-aminopropyltriethoxysilane, glutaraldehyde, N-ethyl-N-(3-(dimethylamino)-propyl) carbodiimide hydrochloride and N-hydroxysuccinimide. The enzyme immobilization efficiency and recovered activity were evaluated towards-azino-bis(3-ethylbenzathiazoline-6-sulfonic acid) biocatalytic oxidation. The best compromise between immobilization efficiency and recovered activity was obtained using the CNTs functionalized with 0.3 M HNO 3 , treated with N-ethyl-N-(3-(dimethylamino)propyl) carbodiimide hydrochloride and N-hydroxysuccinimide. This catalyst also showed the best thermal stability (at 50 and 60 ºC). The bioconjugate based on this material was characterized by vibrational spectroscopies (FTIR and Raman) and by N 2 adsorption. The results from reutilization tests showed that laccase activity was kept above 65% of its initial value after five consecutive cycles of reuse. The biocatalytic performance of the immobilized enzyme was evaluated for the degradation of a mixture of phenolic compounds in water containing phenol, resorcinol, 4-methoxyphenol and 4-chlorophenol. As means of cost efficient to enzyme reutilization, laccase was immobilized over polysulfone membranes blended with the functionalized CNTs and studied in the degradation of 4-methoxyphenol.

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Section: Introductionmentioning

confidence: 99%

Enhanced biocatalytic sustainability of laccase by immobilization on functionalized carbon nanotubes/polysulfone membranes

Costa

Lima

Sampaio

et al. 2019

Chemical Engineering Journal

139

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“…Dye wastewater can be treated by conventional physical and chemical methods including adsorption, coagulation, and oxidation [ 21 , 22 , 23 ]. Among them, dye decolorization using enzymes such as laccase has gained great attention due to its processing efficiency [ 24 , 25 ].…”

Section: Introductionmentioning

confidence: 99%

Enhanced Performance of Magnetic Graphene Oxide-Immobilized Laccase and Its Application for the Decolorization of Dyes

et al. 2017

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In this study, magnetic graphene oxide (MGO) nanomaterials were synthesized based on covalent binding of amino Fe3O4 nanoparticles onto the graphene oxide (GO), and the prepared MGO was successfully applied as support for the immobilization of laccase. The MGO-laccase was characterized by transmission electron microscopy (TEM) and a vibrating sample magnetometer (VSM). Compared with free laccase, the MGO-laccase exhibited better pH and thermal stabilities. The optimum pH and temperature were confirmed as pH 3.0 and 35 °C. Moreover, the MGO-laccase exhibited sufficient magnetic response and satisfied reusability after being retained by magnetic separation. The MGO-laccase maintained 59.8% activity after ten uses. MGO-laccase were finally utilized in the decolorization of dye solutions and the decolorization rate of crystal violet (CV), malachite green (MG), and brilliant green (BG) reached 94.7% of CV, 95.6% of MG, and 91.4% of BG respectively. The experimental results indicated the MGO-laccase nanomaterials had a good catalysis ability to decolorize dyes in aqueous solution. Compared with the free enzyme, the employment of MGO as enzyme immobilization support could efficiently enhance the availability and facilitate the application of laccase.

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“…Laccase (p-diphenol: dioxygen oxidoreductases, EC 1.10.3.2) a multi-copper polyphenol oxidase, has a wide substrate range and has attracted great interest in recent years for catalyzing phenols, chlorinated phenols, dyes and some inorganic compounds. [1][2][3] However, free laccase is not widely used in practical applications because of its poor stability and non-reusability. 4 Immobilization of laccase can reduce these deficiencies by increasing operational and storage stability and realizing reusability.…”

Section: Introductionmentioning

confidence: 99%

Improving catalytic activity of laccase immobilized on the branched polymer chains of magnetic nanoparticles under alternating magnetic field

Xia

Wan

Liu

et al. 2017

J of Chemical Tech & Biotech

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Effective removal of sulfur dyes from water by biosorption and subsequent immobilized laccase degradation on crosslinked chitosan beads

Cited by 105 publications

References 43 publications

Enhanced biocatalytic sustainability of laccase by immobilization on functionalized carbon nanotubes/polysulfone membranes

Enhanced biocatalytic sustainability of laccase by immobilization on functionalized carbon nanotubes/polysulfone membranes

Enhanced Performance of Magnetic Graphene Oxide-Immobilized Laccase and Its Application for the Decolorization of Dyes

Improving catalytic activity of laccase immobilized on the branched polymer chains of magnetic nanoparticles under alternating magnetic field

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