Laccase as an efficacious approach to remove anticancer drugs: A study of doxorubicin degradation, kinetic parameters, and toxicity assessment

Kelbert, Maikon; Pereira, Cláudia Maria; Daronch, Naionara Ariete; Cesca, Karina; Michels, Camila; Oliveira, Débora de; Soares, Hugo Moreira

doi:10.1016/j.jhazmat.2020.124520

Cited by 50 publications

(31 citation statements)

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“…strong affinity and reaction velocity of this enzyme toward the substrate (Rivera-Hoyos et al, 2013;Yang et al, 2020). This kinetic behavior may be dependent on genetic diversity of the different laccase producing sources as well as the nature and structure of the enzyme (Rivera-Hoyos et al, 2013;Kelbert et al, 2021).…”

Section: Kinetic Parameters Of Thlacc-smentioning

confidence: 99%

Introducing a Thermo-Alkali-Stable, Metallic Ion-Tolerant Laccase Purified From White Rot Fungus Trametes hirsuta

Cao

et al. 2021

Front. Microbiol.

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This study introduces a valuable laccase, designated ThLacc-S, purified from white rot fungus Trametes hirsuta. ThLacc-S is a monomeric protein in nature with a molecular weight of 57.0 kDa and can efficiently metabolize endocrine disrupting chemicals. The enzyme was successfully purified to homogeneity via three consecutive steps consisting of salt precipitation and column chromatography, resulting in a 20.76-fold increase in purity and 46.79% yield, with specific activity of 22.111 U/mg protein. ThLacc-S was deciphered as a novel member of the laccase family and is a rare metalloenzyme that contains cysteine, serine, histidine, and tyrosine residues in its catalytic site, and follows Michaelis-Menten kinetic behavior with a Km and a kcat/Km of 87.466 μM and 1.479 s–1μM–1, respectively. ThLacc-S exerted excellent thermo-alkali stability, since it was markedly active after a 2-h incubation at temperatures ranging from 20 to 70°C and retained more than 50% of its activity after incubation for 72 h in a broad pH range of 5.0–10.0. Enzymatic activities of ThLacc-S were enhanced and preserved when exposed to metallic ions, surfactants, and organic solvents, rendering this novel enzyme of interest as a green catalyst for versatile biotechnological and industrial applications that require these singularities of laccases, particularly biodegradation and bioremediation of environmental pollutants.

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Section: Kinetic Parameters Of Thlacc-smentioning

confidence: 99%

Introducing a Thermo-Alkali-Stable, Metallic Ion-Tolerant Laccase Purified From White Rot Fungus Trametes hirsuta

Cao

et al. 2021

Front. Microbiol.

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“…Another study regarding the removal of anticancer drugs using laccase was made by Kelbert M. et al, in 2021 [170]. The researchers evaluated the efficiency of laccase from Trametes versicolor on doxorubicin degradation for various operating conditions, meaning enzyme concentrations, pH, and temperature.…”

Section: Degradation Of Pharmaceutical Productsmentioning

confidence: 99%

Laccases—Versatile Enzymes Used to Reduce Environmental Pollution

et al. 2022

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The accumulation of waste and toxic compounds has become increasingly harmful to the environment and human health. In this context, the use of laccases has become a focus of interest, due to the properties of these versatile enzymes: low substrate specificity, and water formation as a non-toxic end product. Thus, we begin our study with a general overview of the importance of laccase for the environment and industry, starting with the sources of laccases (plant, bacterial and fungal laccases), the structure and mechanism of laccases, microbial biosynthesis, and the immobilization of laccases. Then, we continue with an overview of agro-waste treatment by laccases wherein we observe the importance of laccases for the biodisponibilization of substrates and the biodegradation of agro-industrial byproducts; we then show some aspects regarding the degradation of xenobiotic compounds, dyes, and pharmaceutical products. The objective of this research is to emphasize and fully investigate the effects of laccase action on the decomposition of lignocellulosic materials and on the removal of harmful compounds from soil and water, in order to provide a sustainable solution to reducing environmental pollution.

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“…Biological processes do not achieve high removal efficiencies for these compounds, since many of them are poorly biodegradable and have a high metabolic activity (Ferre-Aracil et al 2016). However, some studies indicate that the removal of anticancer drugs can be better with enzymatic degradation and ozonation (Castellet-Rovira et al 2018;Kelbert et al 2020;Ferre-Aracil et al 2016). A study by Somensi et al (2012) demonstrated that O 3 oxidation of doxorubicin was a pH-dependent process with a second-order rate constant at neutral pH of 0.3373/min.…”

Section: Efficiency Of Pharmaceuticals Compounds Removalmentioning

confidence: 99%

Pharmaceutical compound removal efficiency by a small constructed wetland located in south Brazil

Vargas

Bastos

Badany

et al. 2021

Environ Sci Pollut Res

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HAL is a multi-disciplinary open access archive for the deposit and dissemination of scientific research documents, whether they are published or not. The documents may come from teaching and research institutions in France or abroad, or from public or private research centers. L'archive ouverte pluridisciplinaire HAL, est destinée au dépôt et à la diffusion de documents scientifiques de niveau recherche, publiés ou non, émanant des établissements d'enseignement et de recherche français ou étrangers, des laboratoires publics ou privés.

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Laccase as an efficacious approach to remove anticancer drugs: A study of doxorubicin degradation, kinetic parameters, and toxicity assessment

Cited by 50 publications

References 50 publications

Introducing a Thermo-Alkali-Stable, Metallic Ion-Tolerant Laccase Purified From White Rot Fungus Trametes hirsuta

Introducing a Thermo-Alkali-Stable, Metallic Ion-Tolerant Laccase Purified From White Rot Fungus Trametes hirsuta

Laccases—Versatile Enzymes Used to Reduce Environmental Pollution

Pharmaceutical compound removal efficiency by a small constructed wetland located in south Brazil

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