Effect of redox mediators in pharmaceuticals degradation by laccase: A comparative study

Guardado, Ana Luisa Parra; Belleville, Marie‐Pierre; Alanis, Magdalena de Jesús Rostro; Saldivar, Roberto Parra; Sánchez-Marcano, José

doi:10.1016/j.procbio.2018.12.032

Cited by 74 publications

(34 citation statements)

References 56 publications

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“…the micropollutant solution. After 48h, no significant bio-oxidation was observed for any pharmaceutical confirming the recalcitrance of these micropollutants to laccase degradation, as already reported with free enzymes by Parra Guardado et al (2019). These authors attributed the low removal to the complex chemical structure of the compounds.…”

Section: Oxidation Of Pharmaceuticals By Immobilized Laccasesupporting

confidence: 76%

“…Nevertheless, the depletion of recalcitrant micropollutants needs the addition of redox mediators. When they react with laccase, these mediators lead to highly reactive and stable radical species, thus reacting with micropollutants (Parra Guardado et al 2019). Despite all advantages of enzymatic treatment of wastewaters, the use of laccases in environmental applications presents some drawbacks related to their limited stability in solution, difficult recovery, and reusability, resulting in high operational costs.…”

Section: Introductionmentioning

confidence: 99%

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A novel process for the covalent immobilization of laccases on silica gel and its application for the elimination of pharmaceutical micropollutants

Guardado

Druon‐Bocquet

Belleville

et al. 2021

Environ Sci Pollut Res

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In the present work, pharmaceutical micropollutants degradation by laccase immobilized on silica through an innovative process is proposed. The influence of different parameters on the immobilization conditions was evaluated by a 2 3 full factorial design, and parameters leading to the highest activity were identified.Under these conditions, laccase activity reached 14 ± 2 U g -1 of silica with a protein immobilization yield of 35%. The biocatalyst characterization did not show any change in pH and thermal stabilities but enhanced the long-term storage of laccases. Immobilized T. versicolor laccases were then tested to remove four pharmaceutical micropollutants (amoxicillin, ciprofloxacin, carbamazepine and sulfamethoxazole) in the presence of redox mediators (syringaldehyde, p-coumaric acid, and ABTS). High removal yields (50-100% according to the pollutant) were obtained within 4 h of treatment due to the synergistic effect of laccasemediator biotransformation and adsorption on the support. Overall, the pharmaceuticals' removal efficiency was highly influenced by their physicochemical properties; however, the presence of redox mediators impacted not only the oxidation mechanism but also the interactions between the biocatalyst and micropollutants. Finally, the reusability of the biocatalyst was proved during 7 degradation cycles.

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Section: Oxidation Of Pharmaceuticals By Immobilized Laccasesupporting

confidence: 76%

Section: Introductionmentioning

confidence: 99%

A novel process for the covalent immobilization of laccases on silica gel and its application for the elimination of pharmaceutical micropollutants

Guardado

Druon‐Bocquet

Belleville

et al. 2021

Environ Sci Pollut Res

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“…Anti‐inflammatory drugs, antiepileptic and antidepressants are present in high concentration in wastewater and are challenging to be removed completely due to their physicochemical properties and resistance towards biological attack . Laccase enzymes can catalyze oxidation–reduction reactions to efficiently biodegrade some of these contaminants in a very efficient way and have been widely studied to improve the biodegradation of pharmaceutical contaminants (Table ) . The structure of the toxic compound will determine its toxicity degree and the appropriated laccase to be used for its degradation.…”

Section: Laccases As Versatile Enzymes: Traditional and New Industriamentioning

confidence: 99%

Laccases as versatile enzymes: from industrial uses to novel applications

Moreno

Ibarra²,

Eugenio³

et al. 2019

J of Chemical Tech & Biotech

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The application of enzymes offers an enormous potential in the improvement of existing industrial procedures and in the establishment of new processes for obtaining high-added value products. Enzymes provide cleaner and more efficient industrial processes and contribute to the sustainability concept. In this sense, laccases are very versatile biocatalysts currently used in food, textile and pulp and paper sectors among others. During the last years, scientific efforts have been diverted to the exploitation of such interesting enzymes in novel fields like lignocellulosic biorefineries, biosensors or enzymatic biofuel cells. This review provides a general vision of the use of laccase enzymes describing their main characteristics and mode of action. Furthermore, their current uses in industrial processes are summarized and the most novel potential application of laccases are revealed. The increasing interest on laccases is also demonstrated by the research efforts on enzyme engineering as it is detailed in this review. wileyonlinelibrary.com/jctb www.soci.org AD Moreno et al. J Chem Technol Biotechnol 2020; 95: 481-494

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“…This system has great potential to be used as an alternative for PAHs treatment [12]. Specifically, laccase (EC: 1.10.3.2), the simplest copper-containing (T1, T2 and binuclear T3 copper atom) polyphenol oxidase, which could oxidize a wide range of aromatic and nonaromatic compounds via continuous single-electron oxidation processes stimulated by the unique redox ability of copper ions [13]. However, there are two main problems in the catalytic processes of laccase: the first one is the low redox potential of the T1 copper atom as a direct electron acceptor, which limits its catalytic activities for many refractory organic compounds [14]; the other one is the reusability of laccase, which leads to large amount of reagents waste [10].…”

Section: Introductionmentioning

confidence: 99%

Enhanced biocatalysis of phenanthrene in aqueous phase by novel CA-Ca-SBE-laccase biocatalyst: Performance and mechanism

Xin-han

Xie

et al. 2021

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Enzymes-mediated biocatalysis is believed to be a promising strategy for the degradation of polycyclic aromatic hydrocarbon (e.g., phenanthrene) in aqueous phase, due to its high efficiency and environmental harmfulness. However, the reusability of enzymes-mediated biocatalysis and its requirement for redox mediators limited its application. In this paper, enhanced phenanthrene removal was achieved by using a novel biocatalyst which coencapsulating laccase and natural redox mediator soybean meal extract on calcium modified chitosan-alginate (CA-Ca-SBE-laccase) beads with a network pore structure. High degradation efficiency of 94.4 % was achieved after treating aqueous solutions of 0.5 ppm phenanthrene for 20 min with the CA-Ca-SBE-laccase beads, which was 20-30 % higher than that of free laccase and ordinary immobilized laccase beads. Both the radical pathway of oxygen-containing stable free radicals and the nonradical laccase-SBE combined substrates with higher redox potential generated in CA-Ca-SBE-laccase beads contributed to the degradation of phenanthrene, and achieved the maximum double synergy of mediator and laccase. Benefiting from redox-mediating encapsulated SBE and from Ca modification of chitosan, the biocatalyst maintained fairly stable catalytic activities over a wide range of pH values, and considerable repeatability and storage stability were obtained. This study put forward an efficient laccase, redox mediator and immobilized support cofunctionalization technology, and would provide a new perspective for the increasing application scope of enzymes-mediated biocatalysis.

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Effect of redox mediators in pharmaceuticals degradation by laccase: A comparative study

Cited by 74 publications

References 56 publications

A novel process for the covalent immobilization of laccases on silica gel and its application for the elimination of pharmaceutical micropollutants

A novel process for the covalent immobilization of laccases on silica gel and its application for the elimination of pharmaceutical micropollutants

Laccases as versatile enzymes: from industrial uses to novel applications

Enhanced biocatalysis of phenanthrene in aqueous phase by novel CA-Ca-SBE-laccase biocatalyst: Performance and mechanism

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