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Peroxidase‐glucose oxidase‐poly(amphiphilic pyrrole) bioelectrode for selectively mediated amperometric detection of glucose
Author(s) -
Popescu Ionel C.,
Cosnier Serge,
Labbé Pierre
Publication year - 1997
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.1140091306
Subject(s) - amperometry , biosensor , chemistry , glucose oxidase , cyclic voltammetry , horseradish peroxidase , monolayer , electrode , glassy carbon , nuclear chemistry , chromatography , electrochemistry , organic chemistry , biochemistry , enzyme
Monoenzyme (HRP) and bilyer/monolayer bienzyme (HRP‐GOX) bioelectrodes were realized by the oxidative electropolymerization of amphiphilic pyrrole monomer 1 enzyme(s) mixtures, previously adsorbed on the surface of a glassy carbon electrode. Cyclic voltammetry measurements, carried out on poly 1‐HRP modified electrodes showed that the electrocatalytical reduction of H 2 O 2 , in the presence of K 4 Fe(CN) 6 as mediator, occurs at applied potentials well placed in the optimal potential range for amperometric detection. An optimization study concerning the mediator concentration, the amount of the immobilized enzyme(s), the electrode material and the matrix structure (mono‐ or bilayer) was performed in order to obtain the glucose biosensor. At an applied potential of −0.1 V (vs. SCE), batch amperometric response to H 2 O 2 for the HRP modified electrodes gave a sensitivity of ca. 280 mA M −1 cm −2 (up to 0.65 mM). For monolayer biosensor the sensitivity to glucose was ca. 170 mA M −1 cm −2 (up to 1.9 mM). The interference of ascorbate, urate and acetaminophen was found almost negligible.