Realization of an ultra-sensitive hydrogen peroxide sensor with conductance change of horseradish peroxidase-immobilized polyaniline and investigation of the sensing mechanism

Fang, Kuan-Chung; Hsu, Chen-Pin; Kang, Yen-Wen; Fang, Jung-Ying; Huang, Chih-Cheng; Hsu, Charles Ching–Hsiang; Huang, Yu‐Fen; ChihChen, Chen; Li, Sheng-Shian; Yeh, J. Andrew; Yao, Da‐Jeng; Wang, Yulin

doi:10.1016/j.bios.2013.12.029

Cited by 32 publications

(9 citation statements)

References 27 publications

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“…Therefore, PANI is frequently used as a support for enzymes that operate at neutral pH values. , The electrodeposited PANI films were successfully used for HRP immobilization. − Typical detection limit values of the electrodeposited PANI-HRP amperometric sensors fall within the micromolar range with a linear range up to a few millimoles. An excellent detection limit, which is equal to 0.7 nM, has been reported for the HRP-PANI disposable sensor based on a conductivity measurement . The sensing ability was limited to H 2 O 2 concentrations less than 1 μM.…”

Section: Introductionmentioning

confidence: 88%

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Enhancement of Direct Electrocatalytic Activity of Horseradish Peroxidase on Polyaniline Nanotubes

2015

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The advantages of nanotubes over compact conducting polymer films include the large surface area available for enzyme immobilization, facile diffusion of analyte molecules and enhanced conductivity. Heat treatment of PANI induces the formation of phenazine cross-links between PANI chains, which influences the electrocatalytic response of the immobilized enzymes. In this study, both polyaniline (PANI) bulk films and nanotubes were studied as a support for horseradish peroxidase (HRP). Two types of nanotubes, with diameters of 100 and 400 nm, were investigated. HRP was immobilized by physical adsorption or covalent bonding via the carbodiimide reaction. The influence of the heat treatment of PANI prior to enzyme immobilization on the electrochemical responses of the PANI/HRP electrodes was studied. The electrocatalytic current due to hydrogen peroxide (H 2 O 2 ) reduction was observed in all of the studied samples. However, the current values observed for HRP immobilized on PANI nanotubes with diameters of 100 nm (PANI/100 nm) were an order of magnitude higher than that of the bulk film. The electrocatalytic currents for the PANI/ 400 nm nanotubes had intermediate values between PANI/100 nm and the PANI bulk film. Linear responses to H 2 O 2 were observed over a wide concentration range for all of the HRP/PANI systems. The formation of phenazine cross-links due to the thermal treatment of PANI was confirmed from the Raman spectra. The cross-linking contributes to the enhanced mechanical stability of the PANI nanotubes. However, this cross-linking does not enhance significantly the electrocatalytic activity of the immobilized enzyme.

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Section: Introductionmentioning

confidence: 88%

“…Biosensors employing enzymes specific to H 2 O 2 exhibit better sensitivity and selectivity. Among the enzymes used for H 2 O 2 detection, horseradish peroxidase (HRP) is interesting due to its high sensitivity and short analytical response time. − …”

Section: Introductionmentioning

confidence: 99%

Enhancement of Direct Electrocatalytic Activity of Horseradish Peroxidase on Polyaniline Nanotubes

2015

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“…HRP is used as a reagent for organic synthesis, biotransformation, as well, as in coupled enzyme assays, chemiluminescent assays, immunoassays and the treatment of waste waters. And it is also widely used in medical diagnostic, biosensing, bioremediation and biotechnological applications [3][4][5][6] . In recent years, HRP is widely used in the field of biochemistry, enzyme-linked immunosorbent detection [7,8] .…”

Section: Introductionmentioning

confidence: 99%

Enzyme properties and thermal stability of horseradish peroxidase (HRP-DL)

Wang¹,

Tian²,

Li³

et al. 2016

Proceedings of the 2016 International Conference on Engineering and Technology Innovations

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Horseradish peroxidase (HRP) is widely used in biological engineering, wastewater treatment, enzyme-linked immunosorbent assay and other fields. It is great significance to study its enzyme properties, stress resistance and protective agent. In order to provide good quality HRP, and protection method of HRP thermal stability, horseradish peroxidase (HRP-DL) was extracted and purified from horseradish which was collected from Dalian, China in this paper. It was investigated that the enzyme characterization, thermal stability, thermal protection from thermal stability protection agents of HRP-DL. The optimum temperature of HRP-DL was 30°C, the optimum pH of HRP-DL was 5.5. HRP-DL enzyme activity was inhibited significantly by NaCl. HRP-DL was activated by Ca 2+ , Mn 2+ , Zn 2+ , Pb 2+ , Mg 2+ , Go 2+ , Fe 3+ , and inhibited by K + , Cu 2+ , Hg 2+ , Ag + , Fe 2+ in different degree. When HRP-DL was processed at the temperature greater than or equal to 35°C, the residual enzyme activity was reduced. The HRP-DL residual enzyme activity increase 49.3% when added 1 mmol/L Ectoine and heat treatment at 60°C for 15 min. The study of HRP-DL enzyme characterization provided the basis for its practical application. Ectoine as HRP-DL thermally stable protective agent has advantages such as the use of less, the effect is significant.

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“…Electronic mail: ylwang@mx.nthu.edu.tw 0003-6951/2014/105(11)/113304/5/$30.00 V C 2014 AIP Publishing LLC 105, 113304-1 microsensor using horseradish peroxidase (HRP)-immobilized polyaniline (PANI) to detect H 2 O 2 previously. 13 Hydrogen peroxide can oxidize HRP, and then the oxidized HRP can be reduced by oxidizing the highly conductive PANI thin film again. PANI provides an efficient surface for the direct electrochemical reduction of HRP.…”

mentioning

confidence: 99%

Cost-effective and highly sensitive cholesterol microsensors with fast response based on the enzyme-induced conductivity change of polyaniline

Fang

Chu²,

Hsu

et al. 2014

Applied Physics Letters

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In this study, a cost-effective and highly sensitive cholesterol microsensor, which is consisted of cholesterol oxidase (ChOx), horseradish peroxidase (HRP), and polyaniline (PANI), was developed based on the enzyme-induced conductivity change of PANI with fast response. Hydrogen peroxide is produced via the reaction between cholesterol and ChOx, which was immobilized in a dialysis membrane. The produced hydrogen peroxide can oxidize HRP, which can be reduced by oxidizing PANI, thus resulting in decreased conductivity of the polyaniline thin film. The reduced HRP can be oxidized again by hydrogen peroxide and the cycle of the oxidation/reduction continues until all hydrogen peroxide are reacted, leading to the high sensitivity of the sensor due to the signal contributed from all hydrogen peroxide molecules. Cholesterol was detected near the physiological concentrations ranging from 100 mg/dl to 400 mg/dl with the cholesterol microsensors. The results show linear relation between cholesterol concentration and the conductivity change of the PANI. The microsensor showed no response to cholesterol when the PANI was standalone without cholesterol oxidase immobilized, indicating that the enzymatic reaction is required for cholesterol detection. The simple process of the sensor fabrication allows the sensor to be cost-effective and disposable usage. This electronic cholesterol microsensor is promising for point-of-care health monitoring in cholesterol level with low cost and fast response.

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Realization of an ultra-sensitive hydrogen peroxide sensor with conductance change of horseradish peroxidase-immobilized polyaniline and investigation of the sensing mechanism

Cited by 32 publications

References 27 publications

Enhancement of Direct Electrocatalytic Activity of Horseradish Peroxidase on Polyaniline Nanotubes

Enhancement of Direct Electrocatalytic Activity of Horseradish Peroxidase on Polyaniline Nanotubes

Enzyme properties and thermal stability of horseradish peroxidase (HRP-DL)

Cost-effective and highly sensitive cholesterol microsensors with fast response based on the enzyme-induced conductivity change of polyaniline

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