Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential

Autores
Benavidez, Tomás Enrique; Torrente, Daniel; Marucho, Marcelo; Garcia, Carlos D.
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
This article describes the adsorption of glucose oxidase (GOx) onto optically transparent carbon electrodes (OTCE) under the effect of applied potential and the analysis of the enzymatic activity of the resulting GOx/OTCE substrates. In order to avoid electrochemical interferences with the enzyme redox center, control electrochemical experiments were performed using flavin adenine dinucleotide (FAD) and GOx/OTCE substrates. Then, the enzyme adsorption experiments were carried out as a function of the potential applied (ranged from the open circuit potential to +950. mV), the pH solution, the concentration of enzyme, and the ionic strength on the environment. The experimental results demonstrated that an increase in the adsorbed amount of GOx on the OTCE can be achieved when the potential was applied. Although the increase in the adsorbed amount was examined as a function of the potential, a maximum enzymatic activity was observed in the GOx/OTCE substrate achieved at +800. mV. These experiments suggest that although an increase in the amount of enzyme adsorbed can be obtained by the application of an external potential to the electrode, the magnitude of such potential can produce detrimental effects in the conformation of the adsorbed protein and should be carefully considered. As such, the article describes a simple and rational approach to increase the amount of enzyme adsorbed on a surface and can be applied to improve the sensitivity of a variety of biosensors.
Fil: Benavidez, Tomás Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina. University of Texas; Estados Unidos
Fil: Torrente, Daniel. University of Texas; Estados Unidos
Fil: Marucho, Marcelo. University of Texas; Estados Unidos
Fil: Garcia, Carlos D.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina. University of Texas; Estados Unidos
Materia
ADSORPTION
CARBON ELECTRODE
ELECTROCHEMICAL
ELLIPSOMETRY
GLUCOSE OXIDASE
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/54453

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network_name_str CONICET Digital (CONICET)
spelling Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potentialBenavidez, Tomás EnriqueTorrente, DanielMarucho, MarceloGarcia, Carlos D.ADSORPTIONCARBON ELECTRODEELECTROCHEMICALELLIPSOMETRYGLUCOSE OXIDASEhttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1This article describes the adsorption of glucose oxidase (GOx) onto optically transparent carbon electrodes (OTCE) under the effect of applied potential and the analysis of the enzymatic activity of the resulting GOx/OTCE substrates. In order to avoid electrochemical interferences with the enzyme redox center, control electrochemical experiments were performed using flavin adenine dinucleotide (FAD) and GOx/OTCE substrates. Then, the enzyme adsorption experiments were carried out as a function of the potential applied (ranged from the open circuit potential to +950. mV), the pH solution, the concentration of enzyme, and the ionic strength on the environment. The experimental results demonstrated that an increase in the adsorbed amount of GOx on the OTCE can be achieved when the potential was applied. Although the increase in the adsorbed amount was examined as a function of the potential, a maximum enzymatic activity was observed in the GOx/OTCE substrate achieved at +800. mV. These experiments suggest that although an increase in the amount of enzyme adsorbed can be obtained by the application of an external potential to the electrode, the magnitude of such potential can produce detrimental effects in the conformation of the adsorbed protein and should be carefully considered. As such, the article describes a simple and rational approach to increase the amount of enzyme adsorbed on a surface and can be applied to improve the sensitivity of a variety of biosensors.Fil: Benavidez, Tomás Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina. University of Texas; Estados UnidosFil: Torrente, Daniel. University of Texas; Estados UnidosFil: Marucho, Marcelo. University of Texas; Estados UnidosFil: Garcia, Carlos D.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina. University of Texas; Estados UnidosAcademic Press Inc Elsevier Science2014-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/54453Benavidez, Tomás Enrique; Torrente, Daniel; Marucho, Marcelo; Garcia, Carlos D.; Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential; Academic Press Inc Elsevier Science; Journal of Colloid and Interface Science; 435; 12-2014; 164-1700021-9797CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jcis.2014.08.012info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4198490/info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0021979714005694info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:52Zoai:ri.conicet.gov.ar:11336/54453instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:34:52.964CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
title Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
spellingShingle Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
Benavidez, Tomás Enrique
ADSORPTION
CARBON ELECTRODE
ELECTROCHEMICAL
ELLIPSOMETRY
GLUCOSE OXIDASE
title_short Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
title_full Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
title_fullStr Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
title_full_unstemmed Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
title_sort Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential
dc.creator.none.fl_str_mv Benavidez, Tomás Enrique
Torrente, Daniel
Marucho, Marcelo
Garcia, Carlos D.
author Benavidez, Tomás Enrique
author_facet Benavidez, Tomás Enrique
Torrente, Daniel
Marucho, Marcelo
Garcia, Carlos D.
author_role author
author2 Torrente, Daniel
Marucho, Marcelo
Garcia, Carlos D.
author2_role author
author
author
dc.subject.none.fl_str_mv ADSORPTION
CARBON ELECTRODE
ELECTROCHEMICAL
ELLIPSOMETRY
GLUCOSE OXIDASE
topic ADSORPTION
CARBON ELECTRODE
ELECTROCHEMICAL
ELLIPSOMETRY
GLUCOSE OXIDASE
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.4
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv This article describes the adsorption of glucose oxidase (GOx) onto optically transparent carbon electrodes (OTCE) under the effect of applied potential and the analysis of the enzymatic activity of the resulting GOx/OTCE substrates. In order to avoid electrochemical interferences with the enzyme redox center, control electrochemical experiments were performed using flavin adenine dinucleotide (FAD) and GOx/OTCE substrates. Then, the enzyme adsorption experiments were carried out as a function of the potential applied (ranged from the open circuit potential to +950. mV), the pH solution, the concentration of enzyme, and the ionic strength on the environment. The experimental results demonstrated that an increase in the adsorbed amount of GOx on the OTCE can be achieved when the potential was applied. Although the increase in the adsorbed amount was examined as a function of the potential, a maximum enzymatic activity was observed in the GOx/OTCE substrate achieved at +800. mV. These experiments suggest that although an increase in the amount of enzyme adsorbed can be obtained by the application of an external potential to the electrode, the magnitude of such potential can produce detrimental effects in the conformation of the adsorbed protein and should be carefully considered. As such, the article describes a simple and rational approach to increase the amount of enzyme adsorbed on a surface and can be applied to improve the sensitivity of a variety of biosensors.
Fil: Benavidez, Tomás Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina. University of Texas; Estados Unidos
Fil: Torrente, Daniel. University of Texas; Estados Unidos
Fil: Marucho, Marcelo. University of Texas; Estados Unidos
Fil: Garcia, Carlos D.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones en Físico-química de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Instituto de Investigaciones en Físico-química de Córdoba; Argentina. University of Texas; Estados Unidos
description This article describes the adsorption of glucose oxidase (GOx) onto optically transparent carbon electrodes (OTCE) under the effect of applied potential and the analysis of the enzymatic activity of the resulting GOx/OTCE substrates. In order to avoid electrochemical interferences with the enzyme redox center, control electrochemical experiments were performed using flavin adenine dinucleotide (FAD) and GOx/OTCE substrates. Then, the enzyme adsorption experiments were carried out as a function of the potential applied (ranged from the open circuit potential to +950. mV), the pH solution, the concentration of enzyme, and the ionic strength on the environment. The experimental results demonstrated that an increase in the adsorbed amount of GOx on the OTCE can be achieved when the potential was applied. Although the increase in the adsorbed amount was examined as a function of the potential, a maximum enzymatic activity was observed in the GOx/OTCE substrate achieved at +800. mV. These experiments suggest that although an increase in the amount of enzyme adsorbed can be obtained by the application of an external potential to the electrode, the magnitude of such potential can produce detrimental effects in the conformation of the adsorbed protein and should be carefully considered. As such, the article describes a simple and rational approach to increase the amount of enzyme adsorbed on a surface and can be applied to improve the sensitivity of a variety of biosensors.
publishDate 2014
dc.date.none.fl_str_mv 2014-12
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/54453
Benavidez, Tomás Enrique; Torrente, Daniel; Marucho, Marcelo; Garcia, Carlos D.; Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential; Academic Press Inc Elsevier Science; Journal of Colloid and Interface Science; 435; 12-2014; 164-170
0021-9797
CONICET Digital
CONICET
url http://hdl.handle.net/11336/54453
identifier_str_mv Benavidez, Tomás Enrique; Torrente, Daniel; Marucho, Marcelo; Garcia, Carlos D.; Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential; Academic Press Inc Elsevier Science; Journal of Colloid and Interface Science; 435; 12-2014; 164-170
0021-9797
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jcis.2014.08.012
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4198490/
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0021979714005694
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Academic Press Inc Elsevier Science
publisher.none.fl_str_mv Academic Press Inc Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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