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Humic acid aggregates with laccase and decreases the performance of the enzyme catalytic systems through various mechanisms

2025-09Journal article Open access
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datacite.subject.fosCiências Naturais::Ciências Biológicas
datacite.subject.fosEngenharia e Tecnologia
datacite.subject.fosCiências Naturais::Ciências Químicas
datacite.subject.sdg03:Saúde de Qualidade
datacite.subject.sdg17:Parcerias para a Implementação dos Objetivos
dc.contributor.authorLopes, João
dc.contributor.authorMarques-da-Silva, Dorinda
dc.contributor.authorPeralta, Cláudia
dc.contributor.authorRodrigues, Joaquim Rui
dc.contributor.authorVaz, Daniela
dc.contributor.authorLagoa, Ricardo
dc.date.accessioned2025-09-09T13:54:57Z
dc.date.available2025-09-09T13:54:57Z
dc.date.issued2025-09
dc.descriptionArticle number - 146405
dc.description.abstractLaccases are among the best-rated enzymes for industrial and environmental applications, yet their use in bioremediation is limited by interference from environmental components like humic acid (HA). This study evaluated HA impact on the oxidation of 2,2 ′-azino-bis-(3-ethylbenzothiazoline-6-sulphonate (ABTS) and two model pollutants — anthracene and methyl orange — by laccase( mediator) systems. HA consistently diminished conversion rates, with EC50 values between 5 and 51 mg/L suggesting diverse inhibitory mechanisms. We investigated potential mechanisms including substrate sequestration, radical quenching, and chelation of laccase coppers by HA. Incubations with free and immobilized HA showed that adsorption can impede anthracene degradation, at least at high concentrations, but not methyl orange. Using chemically generated ABTS radical and azide-blocked enzyme, it was demonstrated that HA scavenges free radicals produced by laccase, though this alone did not fully explain the observed interference with catalysis. Further assays with metal chelator and added copper or calcium ruled out HA binding to the laccase metal centers. Instead, data from molecular docking, f luorescence, light scattering, and microscopy revealed that HA forms micrometer-scale aggregates with laccase that encapsulate the enzyme. This newly identified mechanism likely applies broadly to laccase-based systems and must be considered in applications involving aqueous media containing humic substances.eng
dc.description.sponsorshipThis research was funded by Fundação para a Ciência e Tecnologia (FCT—Portugal) through the project PTDC/BIA-MIB/31864/2017 and the PhD scholarship reference 2023.04204.BD awarded to J.L.. It was also supported by national funds through FCT/MCTES (PIDDAC) to the research units: LSRE-LCM, UIDB/50020/2020 (DOI: 10.54499/UIDB/50020/2020) and UIDP/50020/2020 (DOI: 10.54499/UIDP/50020/2020); ALiCE, LA/P/0045/2020 (DOI: 10.54499/LA/P/0045/2020); and CQC, UIDB/00313/2020 (DOI: 10.54499/UIDB/00313/2020).
dc.identifier.citationLopes J, Marques-da-Silva D, Peralta C, Rodrigues JR, Vaz D, Lagoa R. Humic acid aggregates with laccase and decreases the performance of the enzyme catalytic systems through various mechanisms. Int J Biol Macromol. 2025 Aug 6;322(Pt 3):146405. doi: 10.1016/j.ijbiomac.2025.146405.
dc.identifier.doi10.1016/j.ijbiomac.2025.146405
dc.identifier.issn01418130
dc.identifier.urihttp://hdl.handle.net/10400.8/14021
dc.language.isoeng
dc.peerreviewedyes
dc.publisherElsevier
dc.relationMultifunctional biomolecular systems for new methods of decontamination, protection and toxicological assessment
dc.relationLaboratory of Separation and Reaction Engineering - Laboratory of Catalysis and Materials
dc.relationALICE - Associate Laboratory in Chemical Engineering
dc.relationCoimbra Chemistry Center
dc.relation.hasversionhttps://www.sciencedirect.com/science/article/pii/S0141813025069624
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectBiocatalysis
dc.subjectCopper oxidases
dc.subjectPolycyclic aromatic hydrocarbons
dc.titleHumic acid aggregates with laccase and decreases the performance of the enzyme catalytic systems through various mechanismseng
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleMultifunctional biomolecular systems for new methods of decontamination, protection and toxicological assessment
oaire.awardTitleLaboratory of Separation and Reaction Engineering - Laboratory of Catalysis and Materials
oaire.awardTitleALICE - Associate Laboratory in Chemical Engineering
oaire.awardTitleCoimbra Chemistry Center
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBIA-MIB%2F31864%2F2017/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F50020%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/LA%2FP%2F0045%2F2020/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDB%2F00313%2F2020/PT
oaire.citation.issuePart 3
oaire.citation.titleInternational Journal of Biological Macromolecules
oaire.citation.volume322
oaire.fundingStream3599-PPCDT
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.fundingStream6817 - DCRRNI ID
oaire.versionhttp://purl.org/coar/version/c_970fb48d4fbd8a85
person.familyNameMarques da Silva
person.familyNameRodrigues
person.familyNameBarroso de Moura Cipreste Vaz
person.familyNameLagoa
person.givenNameDorinda
person.givenNameJoaquim Rui
person.givenNameDaniela
person.givenNameRicardo
person.identifier124357
person.identifier.ciencia-id9018-0B83-E2C6
person.identifier.ciencia-id801A-7761-328C
person.identifier.ciencia-id5C18-A29A-44AB
person.identifier.orcid0000-0003-0460-5421
person.identifier.orcid0000-0002-9756-1124
person.identifier.orcid0000-0001-7562-4676
person.identifier.orcid0000-0003-2375-6612
person.identifier.ridL-4137-2014
person.identifier.ridR-5243-2017
person.identifier.scopus-author-id10242931100
person.identifier.scopus-author-id6602838931
person.identifier.scopus-author-id23051352300
project.funder.identifierhttp://doi.org/10.13039/501100001871
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project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
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