RT info:eu-repo/semantics/article
T1 Inhibited enzymatic reaction of crosslinked lactate oxidase through a pH-dependent mechanism
A1 Cunha Silva, Hugo
A1 Pires, Filipa Velez
A1 Cabral, A. Cristina Dias
A1 Arcos Martínez, Julia
K1 Lactate oxidase inhibition
K1 Amperometric biosensor
K1 Lactic acid
K1 Fluorescence spectrometry
K1 Dynamic light scattering
K1 Química analítica
K1 Chemistry, Analytic
AB 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.
PB Elsevier
SN 0927-7765
YR 2019
FD 2019-12
LK http://hdl.handle.net/10259/5348
UL http://hdl.handle.net/10259/5348
LA eng
NO 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)
DS Repositorio Institucional de la Universidad de Burgos
RD 20-abr-2024