| dc.contributor.author |
Karalemas, ID |
en |
| dc.contributor.author |
Georgiou, CA |
en |
| dc.contributor.author |
Papastathopoulos, DS |
en |
| dc.date.accessioned |
2014-06-06T06:44:15Z |
|
| dc.date.available |
2014-06-06T06:44:15Z |
|
| dc.date.issued |
2000 |
en |
| dc.identifier.issn |
00399140 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/S0039-9140(00)00506-3 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/1765 |
|
| dc.subject |
Electropolymerization |
en |
| dc.subject |
Lysine biosensor |
en |
| dc.subject |
Lysine oxidase immobilization |
en |
| dc.subject |
o-Phenylenediamine |
en |
| dc.subject.other |
Electrochemical electrodes |
en |
| dc.subject.other |
Electropolymerization |
en |
| dc.subject.other |
Enzyme immobilization |
en |
| dc.subject.other |
Polymeric membranes |
en |
| dc.subject.other |
Lysine oxidase |
en |
| dc.subject.other |
Biosensors |
en |
| dc.subject.other |
arginine |
en |
| dc.subject.other |
cystine |
en |
| dc.subject.other |
gold complex |
en |
| dc.subject.other |
histidine |
en |
| dc.subject.other |
lysine |
en |
| dc.subject.other |
lysine oxidase |
en |
| dc.subject.other |
metal complex |
en |
| dc.subject.other |
ornithine |
en |
| dc.subject.other |
phenylalanine |
en |
| dc.subject.other |
poly(2 phenylenediamine)gold |
en |
| dc.subject.other |
silicon |
en |
| dc.subject.other |
tyrosine |
en |
| dc.subject.other |
unclassified drug |
en |
| dc.subject.other |
amperometry |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
biosensor |
en |
| dc.subject.other |
calculation |
en |
| dc.subject.other |
electrode |
en |
| dc.subject.other |
enzyme immobilization |
en |
| dc.subject.other |
polymerization |
en |
| dc.title |
Construction of a L-lysine biosensor by immobilizing lysine oxidase on a gold-poly(o-phenylenediamine) electrode |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/S0039-9140(00)00506-3 |
en |
| heal.publicationDate |
2000 |
en |
| heal.abstract |
The construction of a L-lysine biosensor on a Si-gold strip electrode (SGSE) is described in this study. The construction comprises (a) the formation of poly(o-phenylenediamine, o-PD) membrane on the electrode surface via electropolymerization and (b) the immobilization of lysine oxidase on the gold/poly(o-PD) electrode with glutaraldehyde. The behavior of the gold/poly(o-PD) electrode against H2O2 and lysine, as well as the repeatability of the electropolymerization and the time stability of the polymer were studied. The study showed that the electropolymerization procedure is repeatable, and that the polymer is quite stable for at least 40 days. The biosensor showed a linear calibration curve in the range 0.01-1 x 10-5 M (0.1-10 μM) lysine. The interfering effect of other aminoacids on the biosensor performance was also studied and amperometric selectivity coefficients were calculated. The biosensor responded mainly against tyrosine and cysteine, while the response to phenylalanine, arginine, histidine and ornithine was very low. By changing the electropolymerization conditions, the effect of interferents was further reduced. (C) 2000 Elsevier Science B.V.The construction of a L-lysine biosensor on a Si-gold strip electrode (SGSE) is described in this study. The construction comprises (a) the formation of poly(o-phenylenediamine, o-PD) membrane on the electrode surface via electropolymerization and (b) the immobilization of lysine oxidase on the gold/poly(o-PD) electrode with glutaraldehyde. The behavior of the gold/poly(o-PD) electrode against H2O2 and lysine, as well as the repeatability of the electropolymerization and the time stability of the polymer were studied. The study showed that the electropolymerization procedure is repeatable, and that the polymer is quite stable for at least 40 days. The biosensor showed a linear calibration curve in the range 0.01-1×10-5 M (0.1-10 μM) lysine. The interfering effect of other amino acids on the biosensor performance was also studied and amperometric selectivity coefficients were calculated. The biosensor responded mainly against tyrosine and cysteine, while the response to phenylalanine, arginine, histidine and ornithine was very low. By changing the electropolymerization conditions, the effect of interferents was further reduced. |
en |
| heal.publisher |
Elsevier Science Publ Co Inc, New York, NY, United States |
en |
| heal.journalName |
Talanta |
en |
| dc.identifier.issue |
2 |
en |
| dc.identifier.volume |
53 |
en |
| dc.identifier.doi |
10.1016/S0039-9140(00)00506-3 |
en |
| dc.identifier.spage |
391 |
en |
| dc.identifier.epage |
402 |
en |