Supramolecular immobilization of redox enzymes on cyclodextrin-coated magnetic nanoparticles for biosensing applications

[Display omitted] ► Novel cyclodextrin-coated superparamagnetic Fe3O4 nanoparticles were prepared. ► They were used to immobilize adamantane-modified redox enzymes via host–guest association. ► Biosensors toward xanthine and cathecol were designed with these supramolecular nanocomplexes. Mono-6-form...

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Bibliographic Details
Published in:Journal of colloid and interface science 2012-11, Vol.386 (1), p.181-188
Main Authors: Díez, Paula, Villalonga, Reynaldo, Villalonga, María L., Pingarrón, José M.
Format: Article
Language:English
Subjects:
alkylation
beta-Cyclodextrins - chemistry
Biosensing Techniques
biosensors
carbon
Chemistry
Colloidal state and disperse state
Cyclodextrin
detection limit
electrodes
Enzyme biosensor
Enzymes, Immobilized - chemistry
Exact sciences and technology
General and physical chemistry
iron oxides
Magnetic nanoparticles
Magnetics
Metal Nanoparticles - chemistry
nanoparticles
Oxidation-Reduction
Physical and chemical studies. Granulometry. Electrokinetic phenomena
Supramolecular interactions
xanthine
xanthine oxidase
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Summary:[Display omitted] ► Novel cyclodextrin-coated superparamagnetic Fe3O4 nanoparticles were prepared. ► They were used to immobilize adamantane-modified redox enzymes via host–guest association. ► Biosensors toward xanthine and cathecol were designed with these supramolecular nanocomplexes. Mono-6-formyl-β-cyclodextrin moieties were attached to (3-aminopropyl)triethoxysilane-coated superparamagnetic Fe3O4 nanoparticles by reductive alkylation with NaBH3CN. The oligosaccharide-capped core–shell nanoparticles were employed as support for the supramolecular immobilization of two different adamantane-modified enzymes, tyrosinase and xanthine oxidase, through host–guest interactions. The enzyme-modified nanomaterial was further used to magnetically modify carbon paste electrodes for constructing amperometric biosensors toward cathecol and xanthine. The tyrosinase and xanthine oxidase based biosensors showed excellent electroanalytical behaviours, with linear ranges of 100nM–12μM cathecol and 5.0–120μM xanthine, sensitivities of 12mA/M and 130mA/M, and low detection limits of 22nM and 2.0μM, respectively. The supramolecular nature of the immobilization approach was confirmed by electroanalytical methods.
ISSN:0021-9797
1095-7103
DOI:10.1016/j.jcis.2012.07.050