Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/241963
Type: Artigo de periódico
Title: Multifunctional Catalytic Platform For Peroxidase Mimicking, Enzyme Immobilization And Biosensing
Author: Maroneze
Camila Marchetti; dos Santos
Glauco P.; de Moraes
Vitoria B.; da Costa
Luiz P.; Kubota
Lauro Tatsuo
Abstract: A hybrid platform based on ionic liquid-based alkoxysilane functionalized mesoporous silica was applied for the synthesis of supported Pt nanoparticles with peroxidase-like catalytic activity. The positively charged groups (imidazolium) chemically bonded to the surface provide dual-functionality as ion-exchangers to the hybrid material, firstly used for the in situ synthesis of the highly dispersed Pt nanostructures and, secondly, for the immobilization of biological species aiming biosensing purposes. The peroxidase-like catalytic activity of the SiO2/Imi/Pt material was evaluated towards the H2O2-mediated oxidation of a chromogenic peroxidase substrate (TMB), allowing the colorimetric detection of H2O2. Finally, to further explore the practical application of this nanomaterial-based artificial system, glucose oxidase (GOx) was immobilized on the catalytic porous platform and a bioassay for the colorimetric determination of glucose was successfully conducted as a model system. The enzyme-like catalytic properties of the SiO2/Imi/Pt as well as its ability to immobilize and keep active biological entities on the porous structure indicate that this hybrid porous platform is potentially useful for the development of biosensing devices. (C) 2015 Elsevier B.V. All rights reserved.
Subject: Artificial Enzymes
Glucose Detection
Colorimetric Immunoassay
Gold Nanoparticles
Hydrogen-peroxide
Visual Detection
Graphene Oxide
Mimetics
Cells
Nanomaterials
Country: OXFORD
Editor: ELSEVIER ADVANCED TECHNOLOGY
Citation: Multifunctional Catalytic Platform For Peroxidase Mimicking, Enzyme Immobilization And Biosensing. Elsevier Advanced Technology, v. 77, p. 746-751 Mar-2016.
Rights: embargo
Identifier DOI: 10.1016/j.bios.2015.10.042
Address: http://www.sciencedirect.com/science/article/pii/S0956566315305078
Date Issue: 2016
Appears in Collections:Unicamp - Artigos e Outros Documentos

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