dc.contributorUniv Padua Agripolis
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniv Padua
dc.contributorPalacky Univ Olomouc
dc.date.accessioned2020-12-10T19:58:02Z
dc.date.accessioned2022-12-19T20:21:54Z
dc.date.available2020-12-10T19:58:02Z
dc.date.available2022-12-19T20:21:54Z
dc.date.created2020-12-10T19:58:02Z
dc.date.issued2020-04-01
dc.identifierMaterials. Basel: Mdpi, v. 13, n. 7, 10 p., 2020.
dc.identifierhttp://hdl.handle.net/11449/196846
dc.identifier10.3390/ma13071776
dc.identifierWOS:000529875600294
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/5377483
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.
dc.languageeng
dc.publisherMdpi
dc.relationMaterials
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 Xanthine
dc.typeArtículos de revistas


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