An amperometric glucose biosensor based on the immobilization of glucose oxidase on the ZnO nanotubes

Kong, Tao; Chen, Yang; Ye, Yiping; Zhang, Kun; Wang, Zhenxing; Wang, Xiaoping

doi:10.1016/j.snb.2009.01.002

Cited by 306 publications

(170 citation statements)

References 45 publications

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“…The current produced was increasing as the pH value was increased until it reached pH 7.0-7.3 before it started to decrease at pH 8.0 [7,14]. Therefore optimum pH for GOx biosensor is 7.0-7.3 [7,12,14].…”

Section: Applied Mechanics and Materials Vols 773-774mentioning

confidence: 91%

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Review on Immobilization of Nanoparticles for Fabrication of Glucose Biosensor

Anuar

Misran

Manap

et al. 2015

AMM

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Glucose biosensor has been improvised from time to time in order to provide fast and accurate detection of glucose concentration especially for diabetic patients. Recently, nanoparticles have rising attention engaging with biosensor application. Nanoparticles serve as the carrier of enzyme immobilization whereas; enzyme is a biological catalyst that reacts with specific substrate in metabolic reaction. Glucose oxidase (GOx) in particular, is the most common enzyme used for fabrication of biosensor. Glucose measurement was done by using amperometric measurement that converted corresponding biochemical reaction between glucose and GOx into electrical output. Response behavior studies were conducted in order to compare the successfulness of GOx immobilization onto GOx-biosensor. Immobilization of glucose oxidase onto nanoparticles can lead towards tremendous impacts especially in new, high sensitivity biosensor.

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Section: Applied Mechanics and Materials Vols 773-774mentioning

confidence: 91%

“…Therefore optimum pH for GOx biosensor is 7.0-7.3 [7,12,14]. Temperature effect experiment towards response of GOx biosensor was also conducted between 20°C (293.15K) and 65°C (338.15K).…”

Section: Applied Mechanics and Materials Vols 773-774mentioning

confidence: 99%

Review on Immobilization of Nanoparticles for Fabrication of Glucose Biosensor

Anuar

Misran

Manap

et al. 2015

AMM

View full text Add to dashboard Cite

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“…The repeatability of the system was tested by doing CA on a single electrode twice on the next day, which showed reproducible results. Common interfering species such as ascorbic acid, cholesterol, urea & cysteine require a high oxidation potential for detection [43]. It may be inferred that GOx immobilized electrodes does not have interference from the fact that its operation condition is negative potential.…”

Section: Calibration Curve and Michaelis Menton Contant (Km)mentioning

confidence: 99%

Mediator-free interaction of glucose oxidase, as model enzyme for immobilization, with Al-doped and undoped ZnO thin films laser-deposited on polycarbonate supports

V.T.K.P.

Inguva

Krishnamurthy

et al. 2017

Enzyme and Microbial Technology

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Research Highlights: Electrochemical interaction of ZnO and AZO thin films with the enzyme glucose oxidase was studied.  Nature of interaction of GOx with AZO was explored using XPS.  Mechanism of the electron transfer between GOx and AZO/ZnO was studied using EIS.  The results show that AZO is preferable to ZnO for GOx immobilization and glucose sensor development. Abstract:Al doped and undoped ZnO thin films were deposited by pulsed-laser deposition on polycarbonate sheets. The films were characterized by optical transmission, Hall effect measurement, XRD and SEM. Optical transmission and surface reflectometry studies showed good transparency with thicknesses ~100 nm and surface roughness of 10 nm. Hall effect measurements showed that the sheet carrier concentration was -1.44 x 10 15 cm -2 for AZO and -6 x 10 14 cm -2 for ZnO. The films were then modified by drop-casting glucose oxidase (GOx) without the use of any mediators. Higher protein concentration was observed on ZnO as compared to AZO with higher specific activity for ZnO (0.042 U mg -1 ) compared to AZO (0.032 U mg -1 ), and was in agreement with cyclic voltemmetry (CV). X-ray photoelectron spectroscopy (XPS) suggested that the protein was bound by dipole interactions between AZO lattice oxygen and the amino group of the enzyme. Chronoamperometry showed sensitivity of 5.5 µA mM -1 cm -2 towards glucose for GOx/AZO and 2.2 µA mM -1 cm -2 for GOx/ZnO. The limit of detection (LoD) was 167 µM of glucose for GOx/AZO, as compared to 360 µM for GOx/ZnO. The linearity was 0.28-28 mM for GOx/AZO whereas it was 0.6-28 mM for GOx/ZnO with a response time of 10s. Possibly due to higher enzyme loading, the decrease of impedance in presence of glucose was larger for GOx/ZnO as compared to GOx/AZO in electrochemical impedance spectroscopy (EIS). Analyses with clinical blood serum samples showed that the systems had good reproducibility and accuracy. The characteristics of novel ZnO and AZO thin films with GOx as a model enzyme, should prove useful for the future fabrication of inexpensive, highly sensitive, disposable electrochemical biosensors for high throughput diagnostics.

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“…The effect of the coupling agents, (3-aminopropyl) trimethoxysilane, (3-aminopropyl) triethoxysilane, and (3-aminopropyl) methyldiethoxysilane (APS), on the covalent immobilization of GOx on ZnO nanorods was studied [36]. The APS-treated glucose sensor exhibited the highest sensitivity and lowest K M app , which was attributed to the APS-treated ZnO nanowires containing the largest number of C-N Immobilizing GOx on more complex ZnO nanostructures as working electrodes to detect glucose has also been investigated [12,[37][38][39][40][41][42][43]. Yang et al [37] prepared a highly oriented single-crystal ZnO nanotube array (Fig.…”

Section: Science China Materialsmentioning

confidence: 99%

ZnO nanostructures in enzyme biosensors

et al. 2015

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Biosensing has developed tremendously since it was demonstrated by Leland C. Clark Jr. in 1962. ZnO nanomaterials are attractive candidates for fabricating biosensors, because of their diverse range of nanostructures, high electron mobility, chemical stability, electrochemical activity, high isoelectric points which promote enzyme adsorption, biocompatibility, and piezoelectric properties. This review covers ZnO nanostructures applied in enzyme biosensors, in the light of electrochemical transduction and field effect transduction. Different assembly processes and immobilization methods have been used to load enzymes into various ZnO nanostructures, providing enzymes with favorable micro-environments and enhancing their sensing performance. We briefly describe recent trends in ZnO syntheses, and the analytical performance of the fabricated biosensors, summarize the advantages of using ZnO nanostructures in biosensors, and conclude with future challenges and prospects.

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An amperometric glucose biosensor based on the immobilization of glucose oxidase on the ZnO nanotubes

Cited by 306 publications

References 45 publications

Review on Immobilization of Nanoparticles for Fabrication of Glucose Biosensor

Review on Immobilization of Nanoparticles for Fabrication of Glucose Biosensor

Mediator-free interaction of glucose oxidase, as model enzyme for immobilization, with Al-doped and undoped ZnO thin films laser-deposited on polycarbonate supports

ZnO nanostructures in enzyme biosensors

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