Glucose Sensor Based on Glucose Oxidase Immobilized by Zirconium Phosphate

Park, Se Jin; Chung, Taek Dong; Kang, Sun Kil; Jeong, Ran-A; Boo, Hankil; Kim, Hee Chan

doi:10.2116/analsci.20.1635

Cited by 12 publications

(6 citation statements)

References 17 publications

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“…One of the materials that has been used for protein immobilization are the layered zirconium phosphates (ZrP) [14,16,26,27]. Zirconium phosphates are acidic inorganic ion exchangers with layered structures [28 -30].…”

Section: Introductionmentioning

confidence: 99%

Effect of Enzyme and Cofactor Immobilization on the Response of Ethanol Oxidation in Zirconium Phosphate Modified Biosensors

et al. 2010

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Two different self-contained ethanol amperometric biosensors incorporating layered [Ru(phend) 2 bpy] 2þ -intercalated zirconium phosphate (ZrP) as the mediator as well as yeast-alcohol dehydrogenase (y-ADH) and its cofactor nicotinamide adenine dinucleotide (NAD þ ) were constructed to improve upon a design previously reported where only this mediator was immobilized in the surface of a modified electrode. In the first biosensor, a [Ru(phend) 2 bpy] 2þ -intercalated ZrP modified carbon paste electrode (CPE) was improved by immobilizing in its surface both y-ADH and NAD þ using quaternized Nafion membrane. In the second biosensor, a glassy carbon electrode was modified with [Ru(phend) 2 bpy] 2þ -intercalated ZrP, y-ADH, and NAD þ using Nafion as the holding matrix. Calibration plots for ethanol sensing were constructed in the presence and absence of ZrP. In the absence of ZrP in the surface of the modified glassy carbon electrode, leaching of ADH was observed as detected by UV-vis spectrophotometry. Ethanol sensing was also tested in the presence and absence of ascorbate to measure the selectivity of the sensor for ethanol. These two ethanol biosensors were compared to a previously reported one where the y-ADH and the NAD þ were in solution, not immobilized.

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Section: Introductionmentioning

confidence: 99%

Effect of Enzyme and Cofactor Immobilization on the Response of Ethanol Oxidation in Zirconium Phosphate Modified Biosensors

et al. 2010

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“…These materials show great promise as chemical/biochemical sensors, separation media, or catalysts for laboratory and/or industrial transformations. Successful enzyme-containing biocomposites have been prepared using silica glasses derived through sol−gel processing , clays , and other inorganic host materials . A promising class of host materials for this application are layered double hydroxides (LDHs), which are readily prepared from inexpensive starting materials, provide large, two-dimensional surfaces for the adsorption of enzymes, and are considered more biocompatible and nontoxic than other inorganic materials .…”

Section: Introductionmentioning

confidence: 99%

Immobilization of the Aminopeptidase from Aeromonas proteolytica on Mg²⁺/Al³⁺ Layered Double Hydroxide Particles

Frey

Guilmet

Egan

et al. 2010

ACS Appl. Mater. Interfaces

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A novel biomaterial formed by the immobilization of the Aminopeptidase from Aeromonas Proteolytica (AAP) on synthetic Mg 2+ and Al 3+ ion-containing layered double hydroxide (LDH) particles was prepared. Immobilization of AAP on the LDH particles in a buffered, aqueous mixture is rapid such that the maximum loading capacity, 1 × 10 -9 moles of AAP/mg LDH, is achieved in a few minutes. X-ray powder diffraction of LDH samples before and after treatment with AAP indicates that the enzyme does not intercalate between the layers of LDH, but instead binds to the surface. Treatment of AAP/LDH with various amounts of salt in a buffered mixture demonstrates that between 15 and 20% of AAP can be removed from the LDH by washing the composite material in 0.2 M NaCl. However, the residual AAP remains bound to the LDH even at 1 M salt concentrations. A suspension of the AAP/LDH biomaterial in 10 mM Tricine buffered, aqueous solution (pH 8.0 and 25 ° C) catalyzes the hydrolysis of L-leucine-p-nitroanilide demonstrating that immobilized AAP remains available to substrate and retains its catalytic activity. Recycling experiments reveal that the AAP/LDH particles can be recovered and reused multiple times without appreciable loss of activity. This work provides the foundation for the development of materials that will function in the degradation or detection of peptide hormones or neurotoxins.

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“…There are numerous reports on the electrochemical glucose detection. − ,− Unfortunately, the performance data in those reports are presented in widely different ways, making direct comparison with our data almost impossible. Nevertheless, it seems reasonable to say that the sensitivity of a glassy carbon electrode modified by Pt nanoparticles and, then, by GOx represents a medium value, 4.1 μA mM –1 .…”

Section: Resultsmentioning

confidence: 86%

Mesoporous Zirconia Thin Films with Three-Dimensional Pore Structures and Their Application to Electrochemical Glucose Detection

Kwon

2013

ACS Appl. Mater. Interfaces

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Mesoporous zirconia thin films (MZFs) were synthesized using zirconium hydroxide sol particles and a structure directing agent, Pluronic F127 (PEO106PPO70PEO106, EO = ethylene oxide, PO = propylene oxide). By controlling the F127/Zr ratio, we obtained two distinct MZFs with one in the Fmmm structure and the other in the P63/mmc structure. The pore structures of these films were characterized by low-angle X-ray diffraction, grazing incidence small-angle X-ray scattering, electron microscopy, and N2 sorption measurement. The Fmmm structure has interconnected pores and the P63/mmc structure has less accessible pores. The MZFs were functionalized with glucose oxidase (GOx) and were studied for their potentials as an electrochemical sensor for glucose. The GOx-functionalized MZF electrodes show high sensitivity to glucose in a broad range of glucose concentration of 0.025 - 6.8 mM, which can be attributed to their biocompatibility providing a favorable microenvironment for GOx immobilization and to their 3D pore structures with good accessibility of pores.

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Glucose Sensor Based on Glucose Oxidase Immobilized by Zirconium Phosphate

Cited by 12 publications

References 17 publications

Effect of Enzyme and Cofactor Immobilization on the Response of Ethanol Oxidation in Zirconium Phosphate Modified Biosensors

Effect of Enzyme and Cofactor Immobilization on the Response of Ethanol Oxidation in Zirconium Phosphate Modified Biosensors

Immobilization of the Aminopeptidase from Aeromonas proteolytica on Mg²⁺/Al³⁺ Layered Double Hydroxide Particles

Mesoporous Zirconia Thin Films with Three-Dimensional Pore Structures and Their Application to Electrochemical Glucose Detection

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Glucose Sensor Based on Glucose Oxidase Immobilized by Zirconium Phosphate

Cited by 12 publications

References 17 publications

Effect of Enzyme and Cofactor Immobilization on the Response of Ethanol Oxidation in Zirconium Phosphate Modified Biosensors

Effect of Enzyme and Cofactor Immobilization on the Response of Ethanol Oxidation in Zirconium Phosphate Modified Biosensors

Immobilization of the Aminopeptidase from Aeromonas proteolytica on Mg2+/Al3+ Layered Double Hydroxide Particles

Mesoporous Zirconia Thin Films with Three-Dimensional Pore Structures and Their Application to Electrochemical Glucose Detection

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Immobilization of the Aminopeptidase from Aeromonas proteolytica on Mg²⁺/Al³⁺ Layered Double Hydroxide Particles