Recent Achievements in Dyes Removal Focused on Advanced Oxidation Processes Integrated with Biological Methods

Ledakowicz, S.; Paździor, Katarzyna

doi:10.3390/molecules26040870

Cited by 168 publications

(68 citation statements)

References 248 publications

(386 reference statements)

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“…Synthetic dyes are widely used in the paper and textile industry causing large amounts of contaminated wastewater. Efficient wastewater treatment is thus of great importance to remove these harmful compounds being toxic to humans and aquatic organisms (Ledakowicz and Pazdzior 2021 ). Besides physical and chemical treatments, biological methods relying on fungi, bacteria, or isolated enzymes are of high importance.…”

Section: Biotechnological Applicationmentioning

confidence: 99%

Pecularities and applications of aryl-alcohol oxidases from fungi

Urlacher

Koschorreck

2021

Appl Microbiol Biotechnol

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Aryl-alcohol oxidases (AAOs) are FAD-containing enzymes that oxidize a broad range of aromatic as well as aliphatic allylic alcohols to aldehydes. Their broad substrate spectrum accompanied by the only need for molecular oxygen as cosubstrate and production of hydrogen peroxide as sole by-product makes these enzymes very promising biocatalysts. AAOs were used in the synthesis of flavors, fragrances, and other high-value-added compounds and building blocks as well as in dye decolorization and pulp biobleaching. Furthermore, AAOs offer a huge potential as efficient suppliers of hydrogen peroxide for peroxidase- and peroxygenase-catalyzed reactions. A prerequisite for application as biocatalysts at larger scale is the production of AAOs in sufficient amounts. Heterologous expression of these predominantly fungal enzymes is, however, quite challenging. This review summarizes different approaches aiming at enhancing heterologous expression of AAOs and gives an update on substrates accepted by these promising enzymes as well as potential fields of their application. Key points • Aryl-alcohol oxidases (AAOs) supply ligninolytic peroxidases with H2O2. • AAOs accept a broad spectrum of aromatic and aliphatic allylic alcohols. • AAOs are potential biocatalysts for the production of high-value-added bio-based chemicals.

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Section: Biotechnological Applicationmentioning

confidence: 99%

Pecularities and applications of aryl-alcohol oxidases from fungi

Urlacher

Koschorreck

2021

Appl Microbiol Biotechnol

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“…The removal efficiencies of the AR dye were 100%, 100%, 94%, and 91% at dye concentrations of 1, 5, 10 and 20 mg/L, respectively, while they were 78%, 81%, 65% and 55% for the RB dye at the same range of concentrations, respectively. The decreased efficiency of the Fe 3 O 4 -NH 2 @MIL-101(Cr)-laccase system as a result of increasing the dye concentration, especially in case of the RB dye, was attributed to the inadequate amount of laccase over the MOF surface, as well as the dyes' complicated structures opposite these inadequate amounts of laccase that inhibit the total removal of these contaminants at higher concentrations [42].…”

Section: Dye Concentration Effect On Removal Efficienciesmentioning

confidence: 99%

Magnetic Metal Organic Framework Immobilized Laccase for Wastewater Decolorization

et al. 2021

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The laccase enzyme was successfully immobilized over a magnetic amino-functionalized metal–organic framework Fe3O4-NH2@MIL-101(Cr). Different techniques were used for the characterization of the synthesized materials. The Fe3O4-NH2@MIL-101(Cr) laccase showed excellent resistance to high temperatures and low pH levels with a high immobilization capacity and large activity recovery, due to the combination of covalent binding and adsorption advantages. The long-term storage of immobilized laccase for 28 days indicated a retention of 88% of its initial activity, due to the high stability of the immobilized system. Furthermore, a residual activity of 49% was observed at 85 °C. The immobilized laccase was effectively used for the biodegradation of Reactive Black 5 (RB) and Alizarin Red S (AR) dyes in water. The factors affecting the RB and AR degradation using the immobilized laccase (dye concentration, temperature and pH) were investigated to determine the optimum treatment conditions. The optimum conditions for dye removal were a 5 mg/L dye concentration, temperature of 25 °C, and a pH of 4. At the optimum conditions, the biodegradation and sorption-synergistic mechanism of the Fe3O4-NH2@MIL-101(Cr) laccase system caused the total removal of AR and 81% of the RB. Interestingly, the reusability study of this immobilized enzyme up to five cycles indicated the ability to reuse it several times for water treatment.

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“…Globally, at least 10% of the total textile dye produced (approximately 280,000 tons) is discharged in industrial effluent every year [1,2], with the colored wastewater produced by the textile industry rated as the most polluted wastewater of all industrial sectors. It has been estimated that over 10,000 different textile dyes and pigments are in common use, while total world organic colorant production is estimated at more than 100,000 tons per year [3,4]. Synthetic textile dyes are one of the most dangerous pollutants [5].…”

Section: Introductionmentioning

confidence: 99%

Isolation of Fungi from a Textile Industry Effluent and the Screening of Their Potential to Degrade Industrial Dyes

Juárez-Hernández

Castillo-Hernández

Pérez-Parada

et al. 2021

JoF

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Six fungal strains were isolated from the textile industry effluent in which they naturally occur. Subsequently, the fungal strains were identified and characterized in order to establish their potential decolorizing effect on textile industry effluents. The strains of interest were selected based on their capacity to decolorize azo, indigo, and anthraquinone dyes. Three of the strains were identified as Emmia latemarginata (MAP03, MAP04, and MAP05) and the other three as Mucor circinelloides (MAP01, MAP02, and MAP06), while the efficiency of their decolorization of the dyes was determined on agar plate and in liquid fermentation. All the strains co-metabolized the dyes of interest, generating different levels of dye decolorization. Plate screening for lignin-degrading enzymes showed that the MAP03, MAP04, and MAP05 strains were positive for laccase and the MAP01, MAP02, and MAP06 strains for tyrosinase, while all strains were positive for peroxidase. Based on its decolorization capacity, the Emmia latemarginata (MAP03) strain was selected for the further characterization of its growth kinetics and ligninolytic enzyme production in submerged fermentation under both enzyme induction conditions, involving the addition of Acetyl yellow G (AYG) dye or wheat straw extract, and no-induction condition. The induction conditions promoted a clear inductive effect in all of the ligninolytic enzymes analyzed. The highest level of induced enzyme production was observed with the AYG dye fermentation, corresponding to versatile peroxidase (VP), manganese peroxidase (MnP), and lignin peroxidase (LiP). The present study can be considered the first analysis of the ligninolytic enzyme system of Emmia latemarginata in submerged fermentation under different conditions. Depending on the results of further research, the fungal strains analyzed in the present research may be candidates for further biotechnological research on the decontamination of industrial effluents.

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Recent Achievements in Dyes Removal Focused on Advanced Oxidation Processes Integrated with Biological Methods

Cited by 168 publications

References 248 publications

Pecularities and applications of aryl-alcohol oxidases from fungi

Pecularities and applications of aryl-alcohol oxidases from fungi

Magnetic Metal Organic Framework Immobilized Laccase for Wastewater Decolorization

Isolation of Fungi from a Textile Industry Effluent and the Screening of Their Potential to Degrade Industrial Dyes

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