2024-03-29T10:40:58Zhttps://riubu.ubu.es/oai/requestoai:riubu.ubu.es:10259/53482022-04-08T10:34:38Zcom_10259_4376com_10259_5086com_10259_2604col_10259_4377
Inhibited enzymatic reaction of crosslinked lactate oxidase through a pH-dependent mechanism
Cunha Silva, Hugo
Pires, Filipa Velez
Cabral, A. Cristina Dias
Arcos Martínez, Julia
Lactate oxidase inhibition
Amperometric biosensor
Lactic acid
Fluorescence spectrometry
Dynamic light scattering
Química analítica
Chemistry, Analytic
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.
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)
2020-06-18T08:42:57Z
2020-06-18T08:42:57Z
2019-12
info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
0927-7765
http://hdl.handle.net/10259/5348
10.1016/j.colsurfb.2019.110490
eng
Colloids and Surfaces B: Biointerfaces. 2019, V. 184, 110490
https://doi.org/10.1016/j.colsurfb.2019.110490
info:eu-repo/grantAgreement/MINECO/MUSSEL RTC-2015-4077-2
info:eu-repo/grantAgreement/MICINN/TEC20013-40561-P
Attribution-NonCommercial-NoDerivatives 4.0 Internacional
http://creativecommons.org/licenses/by-nc-nd/4.0/
info:eu-repo/semantics/openAccess
application/pdf
Elsevier
https://riubu.ubu.es/bitstream/10259/5348/4/Cunha-csbb_2019.pdf.jpg
Hispana
TEXT
http://creativecommons.org/licenses/by-nc-nd/4.0/
RIUBU. Repositorio Institucional de la Universidad de Burgos
http://hdl.handle.net/10259/5348