Enzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthine

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dc.contributor.authorMagro, Massimiliano
dc.contributor.authorBaratella, Davide
dc.contributor.authorVenerando, Andrea
dc.contributor.authorNalotto, Giulia
dc.contributor.authorBasso, Caroline R. [UNESP]
dc.contributor.authorMolinari, Simone
dc.contributor.authorSalviulo, Gabriella
dc.contributor.authorUgolotti, Juri
dc.contributor.authorPedrosa, Valber A. [UNESP]
dc.contributor.authorVianello, Fabio
dc.contributor.institutionUniv Padua Agripolis
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionUniv Padua
dc.contributor.institutionPalacky Univ Olomouc
dc.date.accessioned2020-12-10T19:58:02Z
dc.date.available2020-12-10T19:58:02Z
dc.date.issued2020-04-01
dc.description.abstractGenerally, enzyme immobilization on nanoparticles leads to nano-conjugates presenting partially preserved, or even absent, biological properties. Notwithstanding, recent research demonstrated that the coupling to nanomaterials can improve the activity of immobilized enzymes. Herein, xanthine oxidase (XO) was immobilized by self-assembly on peculiar naked iron oxide nanoparticles (surface active maghemite nanoparticles, SAMNs). The catalytic activity of the nanostructured conjugate (SAMN@XO) was assessed by optical spectroscopy and compared to the parent enzyme. SAMN@XO revealed improved catalytic features with respect to the parent enzyme and was applied for the electrochemical studies of xanthine. The present example supports the nascent knowledge concerning protein conjugation to nanoparticle as a means for the modulation of biological activity.en
dc.description.affiliationUniv Padua Agripolis, Dept Comparat Biomed & Food Sci, Viale Univ 16, Legnaro 35020, PD, Italy
dc.description.affiliationUniv Estadual Paulista, Dept Chem & Biochem, Inst Biosci, BR-18618000 Botucatu, SP, Brazil
dc.description.affiliationUniv Padua, Dept Geosci, Via G Gradenigo 6, Padua 35131, Italy
dc.description.affiliationPalacky Univ Olomouc, Reg Ctr Adv Technol & Mat, Slechtitelu 27, Olomouc 78371, Czech Republic
dc.description.affiliationUnespUniv Estadual Paulista, Dept Chem & Biochem, Inst Biosci, BR-18618000 Botucatu, SP, Brazil
dc.description.sponsorshipItalian Ministry of Education, University and Research (MIUR) Centro di Eccellenza per la Salute degli Animali Acquatici -ECCE AQUA
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipIdCNPq: 157877/2018-3
dc.description.sponsorshipIdCAPES: 8888.1135363/2016-01
dc.description.sponsorshipIdFAPESP: 2019/13411-5
dc.description.sponsorshipIdFAPESP: 2019/20573-1
dc.format.extent10
dc.identifierhttp://dx.doi.org/10.3390/ma13071776
dc.identifier.citationMaterials. Basel: Mdpi, v. 13, n. 7, 10 p., 2020.
dc.identifier.doi10.3390/ma13071776
dc.identifier.urihttp://hdl.handle.net/11449/196846
dc.identifier.wosWOS:000529875600294
dc.language.isoeng
dc.publisherMdpi
dc.relation.ispartofMaterials
dc.sourceWeb of Science
dc.subjectxanthine oxidases
dc.subjectenzyme immobilization
dc.subjectcatalytic properties
dc.subjectmetal nanoparticles
dc.titleEnzyme Immobilization on Maghemite Nanoparticles with Improved Catalytic Activity: An Electrochemical Study for Xanthineen
dc.typeArtigo
dcterms.rightsHolderMdpi
unesp.author.orcid0000-0001-7454-5423[2]
unesp.author.orcid0000-0001-8198-6913[6]
unesp.author.orcid0000-0002-4874-7205[10]

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Artigos - Química e Bioquímica - IBB