1998
DOI: 10.1271/bbb.62.2098
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A Novel Catechol Oxidase Enzyme Electrode for the Specific Determination of Catechol

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Cited by 7 publications
(5 citation statements)
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“…5). Chemical immobilization of uricase in gelatine support [3,11] or in sepharose beads [27] revealed poorer robustness since activity decreases of 17% and 30% were respectively obtained in shorter time (25 days). The evaluation of the extent of interferences was carried out for different chemical species normally present in human serum by injection of 50 mmol dm À3 of uric acid solutions to which interferents were added in concentrations similar or above those found in human serum samples.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…5). Chemical immobilization of uricase in gelatine support [3,11] or in sepharose beads [27] revealed poorer robustness since activity decreases of 17% and 30% were respectively obtained in shorter time (25 days). The evaluation of the extent of interferences was carried out for different chemical species normally present in human serum by injection of 50 mmol dm À3 of uric acid solutions to which interferents were added in concentrations similar or above those found in human serum samples.…”
Section: Resultsmentioning
confidence: 99%
“…In the first approach the O 2 consumption or the H 2 O 2 formed is usually monitored while in the second the peroxidase consumption of H 2 O 2 produced in the enzymatic oxidation of uric acid is determined. However, the construction procedures described usually requires time consuming enzyme immobilization procedures [3,7,8], are of relative complex preparation or exhibit lack of robustness [4 -7, 9 -11], and are applied to real sample analysis in a manual batch fashion. Moreover the analytical benefits of the above-mentioned preparations is questionable since some of these electrodes are still capable to oxidize another analytes present in serum samples, or exhibit slow responses [3,4] and short useful lifetime [3,7,11].…”
Section: Introductionmentioning
confidence: 99%
“…The catalytic properties of laccase and tyrosinase, which have been used in biosensors to assess the TPI in FRSs, are discussed below. Catechol oxidase (EC 1.10.3.1) is rarely used in biosensors [ 74 , 75 ] due to the ortho-phenol specificity of this enzyme [ 76 ]. However, the recent study [ 77 ] argued that Taraxacum officinale catechol oxidase unexpectedly exhibited tyrosinase activity, i.e., it was able not only to oxidize ortho-diphenols (catecholase activity), but also to ortho-oxygenate monophenols (cresolase activity).…”
Section: Phenol Oxidasesmentioning
confidence: 99%
“…Catechol oxidases (o-diphenol oxidases) oxidize odiphenols into the respective o-quinones in oxygen dependent reactions (Figure 2) [40,41]. A pair of coupled cupric ions is present in active site of catechol oxidase rendering them a status as type-3 copper proteins.…”
Section: Characteristics Of Catechol Oxidasementioning
confidence: 99%