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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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Published in: | Analytical and bioanalytical chemistry 2007-09, Vol.389 (2), p.527-532 |
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container_title | Analytical and bioanalytical chemistry |
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creator | Guo, Cunlan Song, Yonghai Wei, Hui Li, Peicai Wang, Li Sun, Lanlan Sun, Yujing Li, Zhuang |
description | 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] |
doi_str_mv | 10.1007/s00216-007-1478-6 |
format | article |
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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]</description><identifier>ISSN: 1618-2642</identifier><identifier>EISSN: 1618-2650</identifier><identifier>DOI: 10.1007/s00216-007-1478-6</identifier><identifier>PMID: 17643230</identifier><language>eng</language><publisher>Germany: Berlin/Heidelberg : Springer-Verlag</publisher><subject>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</subject><ispartof>Analytical and bioanalytical chemistry, 2007-09, Vol.389 (2), p.527-532</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c420t-3cf2798b1b23a18faf081c00d181466e33c399cadf68570aa96fc44eaac6a3ab3</citedby><cites>FETCH-LOGICAL-c420t-3cf2798b1b23a18faf081c00d181466e33c399cadf68570aa96fc44eaac6a3ab3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17643230$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Guo, Cunlan</creatorcontrib><creatorcontrib>Song, Yonghai</creatorcontrib><creatorcontrib>Wei, Hui</creatorcontrib><creatorcontrib>Li, Peicai</creatorcontrib><creatorcontrib>Wang, Li</creatorcontrib><creatorcontrib>Sun, Lanlan</creatorcontrib><creatorcontrib>Sun, Yujing</creatorcontrib><creatorcontrib>Li, Zhuang</creatorcontrib><title>Room temperature ionic liquid doped DNA network immobilized horseradish peroxidase biosensor for amperometric determination of hydrogen peroxide</title><title>Analytical and bioanalytical chemistry</title><addtitle>Anal Bioanal Chem</addtitle><description>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]</description><subject>Biosensing Techniques</subject><subject>Biosensor</subject><subject>Calibration</subject><subject>DNA</subject><subject>DNA - chemistry</subject><subject>Electrochemistry - methods</subject><subject>Enzymes, Immobilized - chemistry</subject><subject>Horseradish peroxidase</subject><subject>Horseradish Peroxidase - chemistry</subject><subject>hydrogen peroxide</subject><subject>Hydrogen Peroxide - chemistry</subject><subject>Ions</subject><subject>Reproducibility of Results</subject><subject>Room temperature ionic liquid</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Temperature</subject><issn>1618-2642</issn><issn>1618-2650</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><recordid>eNqFkcFu1DAURS0EoqXwAWzAK3ah79kZx7OsWgpIVZGAri3Hfu4YknhqJ4LyFf1kPJoBliwsX1nnXC8uYy8R3iJAd1oABKqmxgbbTjfqETtGhboRagWP_-ZWHLFnpXwDwJVG9ZQdYadaKSQcs4fPKY18pnFL2c5LJh7TFB0f4t0SPfdpS55fXJ_xieYfKX_ncRxTH4f4q75vUi5V87FsePXTz-htId7HVGgqKfNQj91Vp5HmXGs9zZTHONm5fsNT4Jt7n9MtTX98es6eBDsUenG4T9jN5buv5x-aq0_vP56fXTWuFTA30gXRrXWPvZAWdbABNDoAjxpbpUhKJ9drZ31QetWBtWsVXNuStU5ZaXt5wt7se7c53S1UZjPG4mgY7ERpKUZpAVK08r-gBBRaaV1B3IMup1IyBbPNcbT53iCY3V5mv5fZxd1eRlXn1aF86Ufy_4zDQBV4vQeCTcbe5ljMzRcBKAE0gKzUb6Jqnh8</recordid><startdate>20070901</startdate><enddate>20070901</enddate><creator>Guo, Cunlan</creator><creator>Song, Yonghai</creator><creator>Wei, Hui</creator><creator>Li, Peicai</creator><creator>Wang, Li</creator><creator>Sun, Lanlan</creator><creator>Sun, Yujing</creator><creator>Li, Zhuang</creator><general>Berlin/Heidelberg : Springer-Verlag</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>20070901</creationdate><title>Room temperature ionic liquid doped DNA network immobilized horseradish peroxidase biosensor for amperometric determination of hydrogen peroxide</title><author>Guo, Cunlan ; 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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. 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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 |
title | Room temperature ionic liquid doped DNA network immobilized horseradish peroxidase biosensor for amperometric determination of hydrogen peroxide |
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