Amperometric biosensor for polyphenol based on horseradish peroxidase immobilized on gold electrodes

Shinichiro Imabayashi, Young Tae Kong, Masayoshi Watanabe

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

Horseradish peroxidase (HRP) is covalently immobilized on a self-assembled monolayer of mercaptopropionic acid on vapor-deposited gold electrode. The electrode allows the polyphenol detection down to 2 μM with a linear relationship up to 25 μM. The reduction current of oxidized polyphenols, formed during the enzymatic oxidation of polyphenolic compounds in the presence of H2O2, is proportional to their concentration. The sensitivity of the detection of various polyphenols by the present method depends on both the electron-donating properties of polyphenols and the electron-accepting properties of oxidized polyphenols. The total amounts of polyphenols in several wine and tea samples detected by the present method are well correlated with those determined by the Folin-Ciocalteu method. In addition, this method has several advantages over the Folin-Ciocalteu method: shorter detection time, smaller sample volume, and more torelant to interference substances.

Original languageEnglish
Pages (from-to)408-412
Number of pages5
JournalElectroanalysis
Volume13
Issue number5
DOIs
Publication statusPublished - 2001 Apr
Externally publishedYes

Fingerprint

Polyphenols
Horseradish Peroxidase
Biosensors
Gold
Electrodes
Polyphenolic compounds
Wine
Electrons
Self assembled monolayers
Vapors
Oxidation
Acids

Keywords

  • 3-Mercaptopropionic acid
  • Biosensors
  • Horseradish peroxidase
  • Polyphenol
  • Self-assembled monolayer
  • Tea
  • Wine

ASJC Scopus subject areas

  • Analytical Chemistry

Cite this

Amperometric biosensor for polyphenol based on horseradish peroxidase immobilized on gold electrodes. / Imabayashi, Shinichiro; Kong, Young Tae; Watanabe, Masayoshi.

In: Electroanalysis, Vol. 13, No. 5, 04.2001, p. 408-412.

Research output: Contribution to journalArticle

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N2 - Horseradish peroxidase (HRP) is covalently immobilized on a self-assembled monolayer of mercaptopropionic acid on vapor-deposited gold electrode. The electrode allows the polyphenol detection down to 2 μM with a linear relationship up to 25 μM. The reduction current of oxidized polyphenols, formed during the enzymatic oxidation of polyphenolic compounds in the presence of H2O2, is proportional to their concentration. The sensitivity of the detection of various polyphenols by the present method depends on both the electron-donating properties of polyphenols and the electron-accepting properties of oxidized polyphenols. The total amounts of polyphenols in several wine and tea samples detected by the present method are well correlated with those determined by the Folin-Ciocalteu method. In addition, this method has several advantages over the Folin-Ciocalteu method: shorter detection time, smaller sample volume, and more torelant to interference substances.

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