1982
DOI: 10.1016/s0003-2670(01)95307-3
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Direct electron transfer in immobilized flavoenzyme chemically modified graphite electrodes

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1983
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Cited by 21 publications
(3 citation statements)
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“…For this purpose, the bioelectrode prepared by incubation in chitosan solution was submitted to a treatment with concentrated KCl solutions to assess the enzyme denaturation process. It has been reported that treatment with concentrated salt solutions can strip FAD from flavoenzymes, but the same treatment is ineffective in removing adsorbed FAD from graphite surfaces [41][42][43]. Thus, if the specie adsorbed on the graphite surface is the whole GOx enzyme with its protein embedding structure, basic treatment will strip it from the electrode surface and the corresponding redox peaks will disappear from the cyclic voltammogram.…”
Section: Bioelectrode Modification With Glucose Oxidasementioning
confidence: 99%
“…For this purpose, the bioelectrode prepared by incubation in chitosan solution was submitted to a treatment with concentrated KCl solutions to assess the enzyme denaturation process. It has been reported that treatment with concentrated salt solutions can strip FAD from flavoenzymes, but the same treatment is ineffective in removing adsorbed FAD from graphite surfaces [41][42][43]. Thus, if the specie adsorbed on the graphite surface is the whole GOx enzyme with its protein embedding structure, basic treatment will strip it from the electrode surface and the corresponding redox peaks will disappear from the cyclic voltammogram.…”
Section: Bioelectrode Modification With Glucose Oxidasementioning
confidence: 99%
“…A series of articles has appeared on amperometric biosensors for amino acids based on a variety of detection principles, e.g., for L-amino acids with hydrogen peroxide detection [26][27][28], with oxygen detection [29][30][31], with ferrocene derivatives [321 as artificial electron acceptor facilitating the electron transfer between the enzyme and the electrode at a less positive .UOD and a less negative potential than the electrochemical reactions for hydrogen peroxide and molecular oxygen, respectively, at tetrathiafulvalene-tetracyanoquinodimethane (TTF TCNQ) conducting salt electrodes [33], direct electron transfer between enzyme and electrode [34], and as mentioned earlier on coimmobilizing HRP with L-MOD [20,21] and for D-amino acids with hydrogen peroxide detection [28], TTF TCNQ electrodes [33], and using an electrode with coimmobilized D-AAOD with HRP and using dimethylferrocene or "TF as a mediator between electrode and HRP [21]. Here we report on reagentless sensors for L-and D-amino acids based on L-or D-MOD coimmobilized with HRP in CPs.…”
Section: Introductionmentioning
confidence: 99%
“…In recent years increasing attention has been paid l -- 15 ) to the electron transfer between an electrode and the active center (or cofactor) of oxidoreductase immobilized on electrode surface. By behaving as a substitute for a chemical elecron acceptor (e.g.…”
mentioning
confidence: 99%