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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/61612

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spelling 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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