2026-10-12T10:41:47Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/53482022-04-08T10:34:38Zcom_10259_4376com_10259_5086com_10259_2604col_10259_4377
Repositorio Institucional de la Universidad de Burgos
author
Cunha Silva, Hugo
author
Pires, Filipa Velez
author
Cabral, A. Cristina Dias
author
Arcos Martínez, Julia
2020-06-18T08:42:57Z
2020-06-18T08:42:57Z
2019-12
0927-7765
http://hdl.handle.net/10259/5348
10.1016/j.colsurfb.2019.110490
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.
eng
Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Lactate oxidase inhibition
Amperometric biosensor
Lactic acid
Fluorescence spectrometry
Dynamic light scattering
Inhibited enzymatic reaction of crosslinked lactate oxidase through a pH-dependent mechanism
info:eu-repo/semantics/article
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