Room temperature ionic liquid doped DNA network immobilized horseradish peroxidase biosensor for amperometric determination of hydrogen peroxide

A novel electrochemical H₂O₂ biosensor was constructed by embedding horseradish peroxide (HRP) in a 1-butyl-3-methylimidazolium tetrafluoroborate doped DNA network casting on a gold electrode. The HRP entrapped in the composite system displayed good electrocatalytic response to the reduction of H₂O₂...

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Bibliographic Details
Published in:Analytical and bioanalytical chemistry 2007-09, Vol.389 (2), p.527-532
Main Authors: Guo, Cunlan, Song, Yonghai, Wei, Hui, Li, Peicai, Wang, Li, Sun, Lanlan, Sun, Yujing, Li, Zhuang
Format: Article
Language:English
Subjects:
Biosensing Techniques
Biosensor
Calibration
DNA
DNA - chemistry
Electrochemistry - methods
Enzymes, Immobilized - chemistry
Horseradish peroxidase
Horseradish Peroxidase - chemistry
hydrogen peroxide
Hydrogen Peroxide - chemistry
Ions
Reproducibility of Results
Room temperature ionic liquid
Spectrophotometry, Ultraviolet
Temperature
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Summary:A novel electrochemical H₂O₂ biosensor was constructed by embedding horseradish peroxide (HRP) in a 1-butyl-3-methylimidazolium tetrafluoroborate doped DNA network casting on a gold electrode. The HRP entrapped in the composite system displayed good electrocatalytic response to the reduction of H₂O₂. The composite system could provide both a biocompatible microenvironment for enzymes to keep their good bioactivity and an effective pathway of electron transfer between the redox center of enzymes, H₂O₂ and the electrode surface. Voltammetric and time-based amperometric techniques were applied to characterize the properties of the biosensor. The effects of pH and potential on the amperometric response to H₂O₂ were studied. The biosensor can achieve 95% of the steady-state current within 2 s response to H₂O₂. The detection limit of the biosensor was 3.5 μM, and linear range was from 0.01 to 7.4 mM. Moreover, the biosensor exhibited good sensitivity and stability. The film can also be readily used as an immobilization matrix to entrap other enzymes to prepare other similar biosensors. [graphic removed]
ISSN:1618-2642
1618-2650
DOI:10.1007/s00216-007-1478-6