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dc.contributor.author
Benavidez, Tomás Enrique  
dc.contributor.author
Torrente, Daniel  
dc.contributor.author
Marucho, Marcelo  
dc.contributor.author
Garcia, Carlos D.  
dc.date.available
2018-08-07T18:14:33Z  
dc.date.issued
2014-12  
dc.identifier.citation
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  
dc.identifier.issn
0021-9797  
dc.identifier.uri
http://hdl.handle.net/11336/54453  
dc.description.abstract
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.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Academic Press Inc Elsevier Science  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/  
dc.subject
Adsorption  
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Carbon Electrode  
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Electrochemical  
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Ellipsometry  
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Glucose Oxidase  
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Otras Ciencias Químicas  
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Ciencias Químicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Adsorption and catalytic activity of glucose oxidase accumulated on OTCE upon the application of external potential  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2018-07-30T15:24:08Z  
dc.journal.volume
435  
dc.journal.pagination
164-170  
dc.journal.pais
Estados Unidos  
dc.description.fil
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  
dc.description.fil
Fil: Torrente, Daniel. University of Texas; Estados Unidos  
dc.description.fil
Fil: Marucho, Marcelo. University of Texas; Estados Unidos  
dc.description.fil
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  
dc.journal.title
Journal of Colloid and Interface Science  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.jcis.2014.08.012  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4198490/  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0021979714005694