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Evaluation of the alternating magnetic field (AMF) influence in catalytic activities of enzymes immobilized into magnetic graphene oxide: A new approach

dc.contributor.authorCardoso Pinto, Gabriel [UNESP]
dc.contributor.authorLucena, Guilherme Nunes [UNESP]
dc.contributor.authorDebone Piazza, Rodolfo [UNESP]
dc.contributor.authorLopes Costa, João Miguel
dc.contributor.authorCoimbra e Silva, Eduardo Torres Couto
dc.contributor.authorGu, Yuanyu
dc.contributor.authorde Paula, Ariela Veloso [UNESP]
dc.contributor.authorSilva, Nuno João Oliveira
dc.contributor.authorCosta Marques, Rodrigo Fernando [UNESP]
dc.contributor.institutionCICECO - Aveiro Institute of Materials
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)
dc.date.accessioned2025-04-29T18:41:02Z
dc.date.issued2023-08-01
dc.description.abstractThe conventional methods of production of biofuels generate hazardous by-products, one way to reduce them, by using reusable enzymatic process that requires insoluble enzyme carriers. This investigation allowed the obtention of magnetic graphene oxide (MGO) carrier containing aminosilane functional groups with and without the crosslinker glutaraldehyde. Thus, it was possible to immobilize cellulases and lipases enzymes and evaluate its enzymatic activity in normal conditions, as well as the novelty that was under alternating magnetic field (AMF) conditions. Through enzymatic essays it was determined the optimal working activities for both enzymes using these two magnetic carriers, being pH 4 and 60ºC for cellulases and pH 5 and 50ºC for lipase. Different frequencies were used during AMF test (20, 30, 50 and 70 kHz) and it was confirmed for both groups that with the increase in frequency during the reaction, the less pronounced will be the activity decrease at pH values different from the optimal condition. Due to magnetic properties from the carrier and the medium reaction used the recycle test was satisfactory for the two immobilized groups of the cellulase enzyme, being recycled 9 times without losses greater than 50 % of relative activity. As for the two groups of immobilized lipases, drastic decreases in activity were observed, possibly caused by the strong enzyme/substrate interaction. For both groups of immobilized enzymes, an inhibitory behavior of the glutaraldehyde reagent, widely used as an enzyme/carrier cross-linker, was also observed. Nevertheless, the immobilization of cellulase and lipases enzymes into MGO derivates shows a promising and suitable strategy for the conversion of cellulose and long-chain acyl esters into value-added inputs.en
dc.description.affiliationUniversity of Aveiro CICECO - Aveiro Institute of Materials
dc.description.affiliationSão Paulo State University (Unesp) Laboratory of Magnetic Materials and Colloids (LaMMC) Physical Chemistry Department Institute of Chemistry
dc.description.affiliationSão Paulo State University (Unesp) School of Pharmaceutical Science
dc.description.affiliationSão Paulo State University (Unesp) Institute of Chemistry Araraquara Brazil. Monitoring and Research Center for the Quality of Fuels Biofuels Petroleum and Derivatives (CEMPEQC/IQ-Unesp)
dc.description.affiliationUnespSão Paulo State University (Unesp) Laboratory of Magnetic Materials and Colloids (LaMMC) Physical Chemistry Department Institute of Chemistry
dc.description.affiliationUnespSão Paulo State University (Unesp) School of Pharmaceutical Science
dc.description.affiliationUnespSão Paulo State University (Unesp) Institute of Chemistry Araraquara Brazil. Monitoring and Research Center for the Quality of Fuels Biofuels Petroleum and Derivatives (CEMPEQC/IQ-Unesp)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipFinanciadora de Estudos e Projetos
dc.identifierhttp://dx.doi.org/10.1016/j.mtcomm.2023.106441
dc.identifier.citationMaterials Today Communications, v. 36.
dc.identifier.doi10.1016/j.mtcomm.2023.106441
dc.identifier.issn2352-4928
dc.identifier.scopus2-s2.0-85162203616
dc.identifier.urihttps://hdl.handle.net/11449/298978
dc.language.isoeng
dc.relation.ispartofMaterials Today Communications
dc.sourceScopus
dc.subjectAlternating magnetic field
dc.subjectEnzyme immobilization
dc.subjectMagnetic graphene oxide
dc.titleEvaluation of the alternating magnetic field (AMF) influence in catalytic activities of enzymes immobilized into magnetic graphene oxide: A new approachen
dc.typeArtigopt
dspace.entity.typePublication
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relation.isOrgUnitOfPublicationbc74a1ce-4c4c-4dad-8378-83962d76c4fd
relation.isOrgUnitOfPublication.latestForDiscovery95697b0b-8977-4af6-88d5-c29c80b5ee92
unesp.campusUniversidade Estadual Paulista (UNESP), Instituto de Química, Araraquarapt
unesp.campusUniversidade Estadual Paulista (UNESP), Faculdade de Ciências Farmacêuticas, Araraquarapt

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