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dc.contributor.authorCunha Silva, Hugo 
dc.contributor.authorPires, Filipa Velez
dc.contributor.authorCabral, A. Cristina Dias
dc.contributor.authorArcos Martínez, Julia 
dc.date.accessioned2020-06-18T08:42:57Z
dc.date.available2020-06-18T08:42:57Z
dc.date.issued2019-12
dc.identifier.issn0927-7765
dc.identifier.urihttp://hdl.handle.net/10259/5348
dc.description.abstractLactate oxidase (LOx), recognized to selectively catalyze the lactate oxidation in complex matrices, has been highlighted as preferable biorecognition element for the development of lactate biosensors. In a previous work, we have demonstrated that LOx crosslinking on a modified screen-printed electrode results in a dual range lactate biosensor, with one of the analysis linear range (4 to 50 mM) compatible with lactate sweat levels. It was advanced that such behavior results from an atypical substrate inhibition process. To understand such inhibition phenomena, this work relies in the study of LOx structure when submitted to increased substrate concentrations. The results found by fluorescence spectroscopy and dynamic light scattering of LOx solutions, evidenced conformational changes of the enzyme, occurring in presence of inhibitory substrate concentrations. Therefore, the inhibition behavior found at the biosensor, is an outcome of LOx structural alterations as result of a pH-dependent mechanism promoted at high substrate concentrations.es
dc.description.sponsorshipSpanish Ministry of Science and Innovation (MICINN), Ministry of Economy and Competitiveness (MINECO) and the European Regional Development Fund (FEDER) (TEC20013-40561-P and MUSSEL RTC-2015-4077-2). Hugo Cunha-Silva would like to acknowledge funding from the Spanish Ministry of Economy (BES-2014-068214)es
dc.format.mimetypeapplication/pdf
dc.language.isoenges
dc.publisherElsevieres
dc.relation.ispartofColloids and Surfaces B: Biointerfaces. 2019, V. 184, 110490es
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectLactate oxidase inhibitiones
dc.subjectAmperometric biosensores
dc.subjectLactic acides
dc.subjectFluorescence spectrometryes
dc.subjectDynamic light scatteringes
dc.titleInhibited enzymatic reaction of crosslinked lactate oxidase through a pH-dependent mechanismes
dc.typeinfo:eu-repo/semantics/articlees
dc.rights.accessRightsinfo:eu-repo/semantics/embargoedAccesses
dc.relation.publisherversionhttps://doi.org/10.1016/j.colsurfb.2019.110490es
dc.identifier.doi10.1016/j.colsurfb.2019.110490
dc.journal.titleColloids and Surfaces B: Biointerfaceses
dc.volume.number184es
dc.page.initial110490es
dc.type.hasVersioninfo:eu-repo/semantics/acceptedVersiones


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