Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic acti...
- Autores
- Bracamonte, Maria Victoria; Bollo, Soledad; Labbé, Pierre; Rivas, Gustavo Adolfo; Ferreyra, Nancy Fabiana
- Año de publicación
- 2011
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- We report for the first time the use of quaternized chitosan (QCHI) for the immobilization of gold nanoparticles (NP) and glucose oxidase (GOD), the characterization of the resulting platform and its biocatalytic activity using glucose as substrate. The chemical substitution of chitosan has allowed us to work at physiologic pH to build up self-assembled layers of QCHI-NP as platform for the enzyme immobilization. The adsorption of GOD was analyzed by surface plasmon resonance (SPR) to compare the surface coverage of GOD in absence and presence of the QCHI-NP platform. The results obtained with cyclic voltammetry and scanning electrochemical microscopy (SECM) revealed that the adsorption of NP improves the conductivity of the structure and its electrochemical reactivity, facilitating the oxidation of the hydrogen peroxide produced by GOD. The electrodes modified with NP present higher amperometric response demonstrating the efficient transduction of the enzymatic activity in this structure. © 2010 Elsevier Ltd. All rights reserved.
Fil: Bracamonte, Maria Victoria. 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
Fil: Bollo, Soledad. Universidad de Chile; Chile
Fil: Labbé, Pierre. Universite Joseph Fourier; Francia
Fil: Rivas, Gustavo Adolfo. 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
Fil: Ferreyra, Nancy Fabiana. 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 - Materia
-
Glucose Oxidase
Gold Nanoparticles
Quaternized Chitosan
Scanning Electrochemical Microscopy
Surface Plasmon Resonance - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/61612
Ver los metadatos del registro completo
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Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activityBracamonte, Maria VictoriaBollo, SoledadLabbé, PierreRivas, Gustavo AdolfoFerreyra, Nancy FabianaGlucose OxidaseGold NanoparticlesQuaternized ChitosanScanning Electrochemical MicroscopySurface Plasmon Resonancehttps://purl.org/becyt/ford/1.4https://purl.org/becyt/ford/1We report for the first time the use of quaternized chitosan (QCHI) for the immobilization of gold nanoparticles (NP) and glucose oxidase (GOD), the characterization of the resulting platform and its biocatalytic activity using glucose as substrate. The chemical substitution of chitosan has allowed us to work at physiologic pH to build up self-assembled layers of QCHI-NP as platform for the enzyme immobilization. The adsorption of GOD was analyzed by surface plasmon resonance (SPR) to compare the surface coverage of GOD in absence and presence of the QCHI-NP platform. The results obtained with cyclic voltammetry and scanning electrochemical microscopy (SECM) revealed that the adsorption of NP improves the conductivity of the structure and its electrochemical reactivity, facilitating the oxidation of the hydrogen peroxide produced by GOD. The electrodes modified with NP present higher amperometric response demonstrating the efficient transduction of the enzymatic activity in this structure. © 2010 Elsevier Ltd. All rights reserved.Fil: Bracamonte, Maria Victoria. 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; ArgentinaFil: Bollo, Soledad. Universidad de Chile; ChileFil: Labbé, Pierre. Universite Joseph Fourier; FranciaFil: Rivas, Gustavo Adolfo. 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; ArgentinaFil: Ferreyra, Nancy Fabiana. 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; ArgentinaPergamon-Elsevier Science Ltd2011-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/61612Bracamonte, Maria Victoria; Bollo, Soledad; Labbé, Pierre; Rivas, Gustavo Adolfo; Ferreyra, Nancy Fabiana; Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity; Pergamon-Elsevier Science Ltd; Electrochimica Acta; 56; 3; 1-2011; 1316-13220013-4686CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.electacta.2010.10.022info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0013468610013885info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:45:49Zoai:ri.conicet.gov.ar:11336/61612instacron: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:34982025-10-15 14:45:49.556CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity |
title |
Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity |
spellingShingle |
Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity Bracamonte, Maria Victoria Glucose Oxidase Gold Nanoparticles Quaternized Chitosan Scanning Electrochemical Microscopy Surface Plasmon Resonance |
title_short |
Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity |
title_full |
Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity |
title_fullStr |
Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity |
title_full_unstemmed |
Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity |
title_sort |
Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity |
dc.creator.none.fl_str_mv |
Bracamonte, Maria Victoria Bollo, Soledad Labbé, Pierre Rivas, Gustavo Adolfo Ferreyra, Nancy Fabiana |
author |
Bracamonte, Maria Victoria |
author_facet |
Bracamonte, Maria Victoria Bollo, Soledad Labbé, Pierre Rivas, Gustavo Adolfo Ferreyra, Nancy Fabiana |
author_role |
author |
author2 |
Bollo, Soledad Labbé, Pierre Rivas, Gustavo Adolfo Ferreyra, Nancy Fabiana |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
Glucose Oxidase Gold Nanoparticles Quaternized Chitosan Scanning Electrochemical Microscopy Surface Plasmon Resonance |
topic |
Glucose Oxidase Gold Nanoparticles Quaternized Chitosan Scanning Electrochemical Microscopy Surface Plasmon Resonance |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
We report for the first time the use of quaternized chitosan (QCHI) for the immobilization of gold nanoparticles (NP) and glucose oxidase (GOD), the characterization of the resulting platform and its biocatalytic activity using glucose as substrate. The chemical substitution of chitosan has allowed us to work at physiologic pH to build up self-assembled layers of QCHI-NP as platform for the enzyme immobilization. The adsorption of GOD was analyzed by surface plasmon resonance (SPR) to compare the surface coverage of GOD in absence and presence of the QCHI-NP platform. The results obtained with cyclic voltammetry and scanning electrochemical microscopy (SECM) revealed that the adsorption of NP improves the conductivity of the structure and its electrochemical reactivity, facilitating the oxidation of the hydrogen peroxide produced by GOD. The electrodes modified with NP present higher amperometric response demonstrating the efficient transduction of the enzymatic activity in this structure. © 2010 Elsevier Ltd. All rights reserved. Fil: Bracamonte, Maria Victoria. 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 Fil: Bollo, Soledad. Universidad de Chile; Chile Fil: Labbé, Pierre. Universite Joseph Fourier; Francia Fil: Rivas, Gustavo Adolfo. 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 Fil: Ferreyra, Nancy Fabiana. 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 |
description |
We report for the first time the use of quaternized chitosan (QCHI) for the immobilization of gold nanoparticles (NP) and glucose oxidase (GOD), the characterization of the resulting platform and its biocatalytic activity using glucose as substrate. The chemical substitution of chitosan has allowed us to work at physiologic pH to build up self-assembled layers of QCHI-NP as platform for the enzyme immobilization. The adsorption of GOD was analyzed by surface plasmon resonance (SPR) to compare the surface coverage of GOD in absence and presence of the QCHI-NP platform. The results obtained with cyclic voltammetry and scanning electrochemical microscopy (SECM) revealed that the adsorption of NP improves the conductivity of the structure and its electrochemical reactivity, facilitating the oxidation of the hydrogen peroxide produced by GOD. The electrodes modified with NP present higher amperometric response demonstrating the efficient transduction of the enzymatic activity in this structure. © 2010 Elsevier Ltd. All rights reserved. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-01 |
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/11336/61612 Bracamonte, Maria Victoria; Bollo, Soledad; Labbé, Pierre; Rivas, Gustavo Adolfo; Ferreyra, Nancy Fabiana; Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity; Pergamon-Elsevier Science Ltd; Electrochimica Acta; 56; 3; 1-2011; 1316-1322 0013-4686 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/61612 |
identifier_str_mv |
Bracamonte, Maria Victoria; Bollo, Soledad; Labbé, Pierre; Rivas, Gustavo Adolfo; Ferreyra, Nancy Fabiana; Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity; Pergamon-Elsevier Science Ltd; Electrochimica Acta; 56; 3; 1-2011; 1316-1322 0013-4686 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.electacta.2010.10.022 info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0013468610013885 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Pergamon-Elsevier Science Ltd |
publisher.none.fl_str_mv |
Pergamon-Elsevier Science Ltd |
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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13.22299 |