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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/54453
Ver los metadatos del registro completo
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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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1844613082397016064 |
score |
13.070432 |