Novel enzyme biosensor for hydrogen peroxide via supramolecular associations

Camacho, Conrado; Chico, Belkis; Cao, Roberto; Matías, Juan C.; Hernández, Javier; Palchetti, Ilaria; Simpson, Benjamin K.; Mascini, Marco; Villalonga, Reynaldo

doi:10.1016/j.bios.2008.10.008

Cited by 30 publications

(22 citation statements)

References 36 publications

(31 reference statements)

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“…In fact, it was previously reported that adamantane-modified proteins could be easily immobilized on bCD-coated metal electrodes through the formation of supramolecular complexes [23]. Such approach was further employed to construct stable enzyme biosensors with supramolecular design [24][25][26].…”

Section: Introductionmentioning

confidence: 97%

Immobilization of Xanthine Oxidase on Carbon Nanotubes Through Double Supramolecular Junctions for Biosensor Construction

et al. 2011

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A novel approach for the noncovalent functionalization of single-walled carbon nanotubes with enzymes, using a bcyclodextrin-modified pyrene derivative, mono-6-ethylenediamino-(2-pyrene carboxamido)-6-deoxy-b-cyclodextrin (Pyr-bCD), as a molecular bridge for the construction of a supramolecular assembly between the nanotube surface and an adamantane-modified enzyme, is reported. The Pyr-bCD derivative was synthesized and its stacking to SWNT through p-p interactions accomplished. The functionalized nanotubes showed low capacity for the nonspecific adsorption of proteins, but were able to immobilize adamantane-modified xanthine oxidase via host-guest associations. This double supramolecular junctions-based approach was employed to modify a glassy carbon electrode with the enzyme/nanotubes complex for designing a biosensor device toward xanthine. The biosensor showed fast electroanalytical response (10 s), high sensitivity (5.9 mA/M cm 2 ) low detection limit (2 mM) and high stability.

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Section: Introductionmentioning

confidence: 97%

Immobilization of Xanthine Oxidase on Carbon Nanotubes Through Double Supramolecular Junctions for Biosensor Construction

et al. 2011

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“…Biosensors based on horseradish peroxidase (HRP) have emerged as the most convenient tools for hydrogen peroxide determination [1][2][3][4]. It is well-known that immobilizing a biomolecule on the sensing electrode surface, and maintaining the enzyme activity is a crucial step in enzyme biosensor design [4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

Enzyme biosensor based on the immobilization of HRP on SiO2/BSA/Au composite nanoparticles

Yuan

Zhuo

et al. 2010

Appl Biochem Biotechnol

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In this work, an enzyme biosensor based on the immobilization of horseradish peroxidase (HRP) on SiO₂/BSA/Au/thionine/nafion-modified gold electrode was fabricated successfully. Firstly, nafion was dropped on the surface of the gold electrode to form a nafion film followed by chemisorption of thionine (Thi) as an electron mediator via the ion-exchange interaction between the Thi and nafion. Subsequently, the SiO₂/BSA/Au composite nanoparticles were assembled onto Thi film through the covalent bounding with the amino groups of Thi. Finally, HRP was immobilized on the SiO₂/BSA/Au composite nanoparticles due to the covalent conjugation to construct an enzyme biosensor. The surface topographies of the SiO₂/BSA/Au composite nanoparticles were investigated by using scanning electronic microscopy. The stepwise self-assemble procedure of the biosensor was further characterized by means of cyclic voltammetry and chronoamperometry. The enzyme biosensor showed high sensitivity, good stability and selectivity, a wide linear response to hydrogen peroxide (H₂O₂) in the range of 8.0 x 10⁻⁶ ~3.72 x 10⁻³ mol/L, with a detection limit of 2.0 x 10⁻⁶ mol/L. The Michaelies-Menten constant K(app)(M) value was estimated to be 2.3 mM.

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“…5B However, these sensors are very difficult to compare due to differences in sensor performance, especially with respect to applied potential and the use of supporting electrolytes. Compared to the commonly used glassy carbon and gold electrodes, the detection limit of the AgPs-SWCNT sensor was three-fold higher than those of enzyme-based biosensors [36,37] and was comparable to those of most non-enzyme-based H 2 O 2 sensors [38,39] under equivalent operating conditions. We attribute the high sensitivity of the AgPs-SWCNT sensor to the high electrocatalytic activity of the silver particles and the good conductivity of the SWCNT film, which provides many transport channels on the nanoscale, thereby enhancing electron-transfer reactions on the SWCNT film electrode.…”

Section: Resultsmentioning

confidence: 66%

Electrocatalytic reduction of hydrogen peroxide by silver particles patterned on single-walled carbon nanotubes

Bui

Pham

Han

et al. 2010

Sensors and Actuators B: Chemical

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Novel enzyme biosensor for hydrogen peroxide via supramolecular associations

Cited by 30 publications

References 36 publications

Immobilization of Xanthine Oxidase on Carbon Nanotubes Through Double Supramolecular Junctions for Biosensor Construction

Immobilization of Xanthine Oxidase on Carbon Nanotubes Through Double Supramolecular Junctions for Biosensor Construction

Enzyme biosensor based on the immobilization of HRP on SiO2/BSA/Au composite nanoparticles

Electrocatalytic reduction of hydrogen peroxide by silver particles patterned on single-walled carbon nanotubes

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