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Comparison of Laccases and Hemeproteins Systems in Bioremediation of Organic Pollutants

2022-06Artigo científico Acesso aberto
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datacite.subject.fosEngenharia e Tecnologia::Engenharia Química
datacite.subject.sdg15:Proteger a Vida Terrestre
datacite.subject.sdg11:Cidades e Comunidades Sustentáveis
dc.contributor.authorLopes, João M.
dc.contributor.authorMarques-da-Silva, Dorinda
dc.contributor.authorVideira, Paula Q.
dc.contributor.authorLagoa, Ricardo L.
dc.date.accessioned2026-03-16T12:04:38Z
dc.date.available2026-03-16T12:04:38Z
dc.date.issued2022-06
dc.description.abstractAim: Laccases and peroxidases have attracted great interest for industrial and environmental applications. These enzymes have a broad substrate range and a robust oxidizing ability. Moreover, using mediators or co-oxidants makes it possible to increase their catalytic activity and extend their substrate scope to more resistant chemical structures. Background: Fungal laccases and ligninolytic peroxidases, mainly lignin and manganese peroxidases, are the privileged oxidoreductases for bioremediation processes. Nonetheless, an increasing diversity of laccases and peroxidase-type enzymes has been proposed for environmental technologies. Objective: This article aims to provide an overview of these enzymes and compare their applicability in the degradation of organic pollutants. Methods: Fundamental properties of the proteins are covered and applications towards polycyclic aromatic hydrocarbons (PAHs) and pesticides are specially focused. Results: Laccases are multicopper oxidases initially studied for applications in the pulp and paper in-dustry but able to oxidize a variety of environmentally concerning compounds. Relying on O2, laccases do not require peroxides nor auxiliary agents, like Mn2+, although suitable redox mediators are needed to attack the more recalcitrant pollutants (e.g., PAHs). True and pseudo-peroxidases use a stronger oxi-dant (H2O2) and the redox chemistry at the heme site generates high potential species that allow the oxidation of dyes and some pesticides. Conclusion: Lately, research efforts have been directed to enzyme discovery, testing with micropollu-tants, and improving biocatalysts’ stability by immobilization and protein engineering. Further under-standing of the effects of natural media components and solvents on the enzymes might lead to compet-itive enzymatic treatments of highly toxic media.eng
dc.description.sponsorshipThis work was funded by “Fundação para a Ciência e Tecnologia” (FCT - Portugal) through the research project PTDC/BIA-MIB/31864/2017.
dc.identifier.citationLopes JM, Marques-da-Silva D, Videira PQ, Lagoa RL. Comparison of Laccases and Hemeproteins Systems in Bioremediation of Organic Pollutants. Curr Protein Pept Sci. 2022;23(6):402-423. doi: 10.2174/1389203723666220704090416. PMID: 35794739.
dc.identifier.doi10.2174/1389203723666220704090416
dc.identifier.eissn1875-5550
dc.identifier.issn1389-2037
dc.identifier.urihttp://hdl.handle.net/10400.8/15876
dc.language.isoeng
dc.peerreviewedyes
dc.publisherBentham Science Publishers
dc.relationMultifunctional biomolecular systems for new methods of decontamination, protection and toxicological assessment
dc.relation.hasversionhttps://www.benthamdirect.com/content/journals/cpps/10.2174/1389203723666220704090416
dc.relation.ispartofCurrent Protein & Peptide Science
dc.rights.uriN/A
dc.subjectdye-decolorizing peroxidases
dc.subjecten-zyme-mediator system
dc.subjecthalogenated pesticides
dc.subjectHemoglobin
dc.subjecthorseradish peroxidase
dc.subjectlignin peroxidases
dc.subjectorganophosphorus toxicants
dc.subjectversatile peroxidases
dc.titleComparison of Laccases and Hemeproteins Systems in Bioremediation of Organic Pollutantseng
dc.typejournal article
dspace.entity.typePublication
oaire.awardNumberPTDC/BIA-MIB/31864/2017
oaire.awardTitleMultifunctional biomolecular systems for new methods of decontamination, protection and toxicological assessment
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-MIB%2F31864%2F2017/PT
oaire.citation.endPage423
oaire.citation.issue6
oaire.citation.startPage402
oaire.citation.titleCurrent Protein & Peptide Science
oaire.citation.volume23
oaire.fundingStream3599-PPCDT
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85
person.familyNameLopes
person.familyNameMarques da Silva
person.familyNameLagoa
person.givenNameJoão
person.givenNameDorinda
person.givenNameRicardo
person.identifier124357
person.identifier.ciencia-id5C18-A29A-44AB
person.identifier.orcid0000-0003-4374-6577
person.identifier.orcid0000-0003-0460-5421
person.identifier.orcid0000-0003-2375-6612
person.identifier.scopus-author-id23051352300
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
relation.isAuthorOfPublication805ee98c-108a-4816-b0c1-9027cfc803e4
relation.isAuthorOfPublication475787c4-cf46-4b3b-96ec-a5278d5cc6f5
relation.isAuthorOfPublication8a139213-9a89-4bd3-93ee-1e332519f96b
relation.isAuthorOfPublication.latestForDiscovery805ee98c-108a-4816-b0c1-9027cfc803e4
relation.isProjectOfPublication2097cd8a-31ac-4da8-9326-1493f8925358
relation.isProjectOfPublication.latestForDiscovery2097cd8a-31ac-4da8-9326-1493f8925358

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