Fungal laccases as tools for biodegradation of industrial dyes

Zucca, Paolo; Cocco, Gianmarco; Sollai, Francesca; Sanjust, Enrico

doi:10.1515/boca-2015-0007

Cited by 51 publications

(37 citation statements)

References 97 publications

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“…LC catalyzes the oxidation of phenols, aromatic amines, and other non-phenolic compounds, while reducing molecular oxygen to water; LC activity can be further extended to non-phenolic substrates by the use of synthetic or natural redox mediators [ 8 ]. The mediators, after being oxidized by LC, diffuse out of the active site and oxidize recalcitrant compounds which possess high redox potential or high molecular weight.…”

Section: Introductionmentioning

confidence: 99%

Aflatoxin B1 and M1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators

Loi

Fanelli

Zucca

et al. 2016

Toxins

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106

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Laccases (LCs) are multicopper oxidases that find application as versatile biocatalysts for the green bioremediation of environmental pollutants and xenobiotics. In this study we elucidate the degrading activity of Lac2 pure enzyme form Pleurotus pulmonarius towards aflatoxin B1 (AFB1) and M1 (AFM1). LC enzyme was purified using three chromatographic steps and identified as Lac2 through zymogram and LC-MS/MS. The degradation assays were performed in vitro at 25 °C for 72 h in buffer solution. AFB1 degradation by Lac2 direct oxidation was 23%. Toxin degradation was also investigated in the presence of three redox mediators, (2,2′-azino-bis-[3-ethylbenzothiazoline-6-sulfonic acid]) (ABTS) and two naturally-occurring phenols, acetosyringone (AS) and syringaldehyde (SA). The direct effect of the enzyme and the mediated action of Lac2 with redox mediators univocally proved the correlation between Lac2 activity and aflatoxins degradation. The degradation of AFB1 was enhanced by the addition of all mediators at 10 mM, with AS being the most effective (90% of degradation). AFM1 was completely degraded by Lac2 with all mediators at 10 mM. The novelty of this study relies on the identification of a pure enzyme as capable of degrading AFB1 and, for the first time, AFM1, and on the evidence that the mechanism of an effective degradation occurs via the mediation of natural phenolic compounds. These results opened new perspective for Lac2 application in the food and feed supply chains as a biotransforming agent of AFB1 and AFM1.

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Section: Introductionmentioning

confidence: 99%

Aflatoxin B1 and M1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators

Loi

Fanelli

Zucca

et al. 2016

Toxins

Self Cite

106

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“…Laccase (Lac) has shown many applications in biomedical, biotechnological, and environmental areas such as organic synthesis, wine cork making, teeth whitening, immunoassay analyte labeling, biofuel cells, and biosensors [4][5][6]. Moreover, Lac can also play a major role in bioremediation processes such as dye removal from wastewater [7,8].…”

Section: Introductionmentioning

confidence: 99%

Laccase Immobilization on Poly(p-Phenylenediamine)/Fe3O4 Nanocomposite for Reactive Blue 19 Dye Removal

et al. 2016

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Magnetic poly(p-phenylenediamine) (PpPD) nanocomposite was synthesized via mixing p-phenylenediamine solution and Fe 3 O 4 nanoparticles and used as a carrier for immobilized enzymes. Successful synthesis of PpPD/Fe 3 O 4 nanofiber was confirmed by transmission electron microscopy and Fourier transform infrared spectroscopy. Laccase (Lac) was immobilized on the surface of PpPD/Fe 3 O 4 nanofiber through covalent bonding for reactive blue 19 dye removal. The immobilized Lac-nanofiber conjugates could be recovered from the reaction solution using a magnet. The optimum reaction pH and temperature for the immobilized Lac were 3.5 and 65 • C, respectively. The storage, operational stability, and thermal stability of the immobilized Lac were higher than those of its free counterpart. The dye removal efficiency of immobilized Lac was about 80% in the first 1 h of incubation, while that of free Lac was about 20%. It was found that the unique electronic properties of PpPD might underlie the high dye removal efficiency of immobilized Lac. Over a period of repeated operation, the dye removal efficiency was above 90% during the first two cycles and remained at about 43% after eight cycles. Immobilized Lac on PpPD/Fe 3 O 4 nanofiber showed high stability, easy recovery, reuse capabilities, and a high removal efficiency for reactive blue 19 dye; therefore, it provides an optional tool for dye removal from wastewater.

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“…Biocatalysts are a very powerful tool for solving environmental safety problems, reducing economic costs . Such enzymes as laccases show high ability to remove hazardous dyes from wastewater …”

Section: Introductionmentioning

confidence: 99%

Comparison of N‐Hydroxy Compounds as Mediators in Laccase‐Catalysed Decolorization of Indigo Carmine

et al. 2019

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A comparative study of N-hydroxy compounds -violuric acid, 1-hydroxybenzotriazole and N-hydroxyphthalimide as the redox mediators during laccase-catalyzed Indigo Carmine decolorization has been carried out. It is shown that the enzymatic oxidation of N-hydroxy-mediators to radicals > N-O * , which act as a real oxidizing agent for indigo carmine, is a rate-limiting stage. The effectiveness of N-hydroxy compounds as the mediators in the Indigo Carmine decolorization in the presence of laccase Trametes versicolor increases in the following order: N-hydroxyphthalimide < 1-hydroxybenzotriazole < violuric acid. The main reason for the low activity of N-hydroxyphthalimide is the low rate of generation of phthalimide-N-oxyl radicals in the process of oxidation by laccase of N-hydroxyphthalimide, which is confirmed by inhibition of the studied process by ascorbic acid. The initiation rate corresponds to the total process rate and is equal to 4.20 × 10 À 8 , 2.82 × 10 À 8 , 2.90 × 10 À 9 M s À 1 with the participation of violuric acid, 1-hydroxybenzotriazole and N-hydroxyphthalimide, respectively.

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Fungal laccases as tools for biodegradation of industrial dyes

Cited by 51 publications

References 97 publications

Aflatoxin B1 and M1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators

Aflatoxin B1 and M1 Degradation by Lac2 from Pleurotus pulmonarius and Redox Mediators

Laccase Immobilization on Poly(p-Phenylenediamine)/Fe3O4 Nanocomposite for Reactive Blue 19 Dye Removal

Comparison of N‐Hydroxy Compounds as Mediators in Laccase‐Catalysed Decolorization of Indigo Carmine

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