Quaternized chitosan as support for the assembly of gold nanoparticles and glucose oxidase: Physicochemical characterization of the platform and evaluation of its biocatalytic activity

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...

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Bibliographic Details
Published in:Electrochimica acta 2011, Vol.56 (3), p.1316-1322
Main Authors: Bracamonte, Maria V., Bollo, Soledad, Labbé, Pierre, Rivas, Gustavo A., Ferreyra, Nancy F.
Format: Article
Language:English
Subjects:
Accumulation
Adsorption
Biological and medical sciences
Biosensors
Biotechnology
Chemical Sciences
Chitosan
Fundamental and applied biological sciences. Psychology
Glucose oxidase
Gold
Gold nanoparticles
Immobilization
Methods. Procedures. Technologies
Nanoparticles
Platforms
Quaternized chitosan
Scanning electrochemical microscopy
Surface chemistry
Surface plasmon resonance
Various methods and equipments
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Summary: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.
ISSN:0013-4686
1873-3859
DOI:10.1016/j.electacta.2010.10.022