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dc.contributor.author | Cunha Silva, Hugo | |
dc.contributor.author | Pires, Filipa Velez | |
dc.contributor.author | Cabral, A. Cristina Dias | |
dc.contributor.author | Arcos Martínez, Julia | |
dc.date.accessioned | 2020-06-18T08:42:57Z | |
dc.date.available | 2020-06-18T08:42:57Z | |
dc.date.issued | 2019-12 | |
dc.identifier.issn | 0927-7765 | |
dc.identifier.uri | http://hdl.handle.net/10259/5348 | |
dc.description.abstract | Lactate 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. | en |
dc.description.sponsorship | Spanish 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.mimetype | application/pdf | |
dc.language.iso | eng | es |
dc.publisher | Elsevier | es |
dc.relation.ispartof | Colloids and Surfaces B: Biointerfaces. 2019, V. 184, 110490 | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.subject | Lactate oxidase inhibition | en |
dc.subject | Amperometric biosensor | en |
dc.subject | Lactic acid | en |
dc.subject | Fluorescence spectrometry | en |
dc.subject | Dynamic light scattering | en |
dc.subject.other | Química analítica | es |
dc.subject.other | Chemistry, Analytic | en |
dc.title | Inhibited enzymatic reaction of crosslinked lactate oxidase through a pH-dependent mechanism | en |
dc.type | info:eu-repo/semantics/article | |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | |
dc.relation.publisherversion | https://doi.org/10.1016/j.colsurfb.2019.110490 | |
dc.identifier.doi | 10.1016/j.colsurfb.2019.110490 | |
dc.relation.projectID | info:eu-repo/grantAgreement/MINECO/MUSSEL RTC-2015-4077-2 | |
dc.relation.projectID | info:eu-repo/grantAgreement/MICINN/TEC20013-40561-P | |
dc.journal.title | Colloids and Surfaces B: Biointerfaces | es |
dc.volume.number | 184 | es |
dc.page.initial | 110490 | es |
dc.type.hasVersion | info:eu-repo/semantics/acceptedVersion |