2026-10-16T16:02:04Zhttps://riubu.ubu.es/oai/request

oai:riubu.ubu.es:10259/53482022-04-08T10:34:38Zcom_10259_4376com_10259_5086com_10259_2604col_10259_4377

00925njm 22002777a 4500 dc Cunha Silva, Hugo author Pires, Filipa Velez author Cabral, A. Cristina Dias author Arcos Martínez, Julia author 2019-12 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. 0927-7765 http://hdl.handle.net/10259/5348 10.1016/j.colsurfb.2019.110490 Lactate oxidase inhibition Amperometric biosensor Lactic acid Fluorescence spectrometry Dynamic light scattering Inhibited enzymatic reaction of crosslinked lactate oxidase through a pH-dependent mechanism