2005
DOI: 10.1016/j.bios.2004.08.051
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Electrochemical study of a new methylene blue/silicon oxide nanocomposition mediator and its application for stable biosensor of hydrogen peroxide

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Cited by 128 publications
(48 citation statements)
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“…It is clear that a rapid and sensitive response to H 2 O 2 was achieved. When the H 2 O 2 was added, the biosensor responded rapidly to the substrate increase and achieved 95% of steady-current in 12 s. It is faster than the reported results of HRP that immobilized on a b-type zeolite modified glassy carbon electrode (30 s) [6], and a SiO 2 -MB/gelatine modified glassy carbon electrode(20 s) [36]. This may result from The apparent Michaelis -Menten constant (K m ), which gives an indication of the enzyme-substrate kinetics for the biosensor, can be calculated from the electrochemical version of the Lineweaver -Burk equation [37], 1/i ss ¼ 1/i max þ K m /i max C, where i ss is the steady state current after the addition of substrate, C is the bulk concentration of the substrate, and i max is the maximum current measured under saturated substrate condition.…”
Section: Electrochemical Impedance Spectroscopy Characterizationcontrasting
confidence: 45%
“…It is clear that a rapid and sensitive response to H 2 O 2 was achieved. When the H 2 O 2 was added, the biosensor responded rapidly to the substrate increase and achieved 95% of steady-current in 12 s. It is faster than the reported results of HRP that immobilized on a b-type zeolite modified glassy carbon electrode (30 s) [6], and a SiO 2 -MB/gelatine modified glassy carbon electrode(20 s) [36]. This may result from The apparent Michaelis -Menten constant (K m ), which gives an indication of the enzyme-substrate kinetics for the biosensor, can be calculated from the electrochemical version of the Lineweaver -Burk equation [37], 1/i ss ¼ 1/i max þ K m /i max C, where i ss is the steady state current after the addition of substrate, C is the bulk concentration of the substrate, and i max is the maximum current measured under saturated substrate condition.…”
Section: Electrochemical Impedance Spectroscopy Characterizationcontrasting
confidence: 45%
“…The simplest biosensor format consists of a thin layer of protein (such as enzyme, antibody, DNA), which can be used for direct measurement [3]. However, immobilization of enzymes directly on electrode surfaces shows a slow rate of electron transfer and can hardly get efficient response because the electroactive centers are buried deeply in the protein structure, and an unfavorable orientation of protein molecules on the electrode surface can block electron transfer.…”
Section: Introductionmentioning
confidence: 99%
“…The peak at about 1260 cm −1 can be attributed to vibration of the CH 2 of HMT [31][32][33]. The peak at 1595 cm −1 corresponds to the vibration of the aromatic ring of MB [34]. The 795, 893, and 1400 cm −1 peaks of MAC overlap with other peaks, and only 623 cm −1 peak appears in the composite without overlapping.…”
Section: Mb Adsorption Experimentsmentioning
confidence: 93%