Amperometrický průtočný biosensor pro stanovení fenolických sloučenin s imobilisovanou lakasou, peroxidasou a tyrosinasou

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F05%3A00014346" target="_blank" >RIV/00216224:14310/05:00014346 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Amperometric flow-injection determination of phenolic compounds using a biosensor with immobilised laccase, peroxidase and tyrosinase

Popis výsledku v původním jazyce

A screen-printed four-electrode sensor based on immobilization of laccase (Coriolus hirsutus), peroxidase (horseradish) and tyrosinase (mushroom) in the same array was developed for monitoring of phenols. The enzymes were immobilized onto a self-assembled monolayer (4-mercapto-1-butanol) modified gold surface via covalent attachment by epichlorohydrin coupling. The experimental conditions for simultaneous operation of the three enzymes were optimized based on catechol determination. The sensors were further applied for the amperometric detection of several substituted phenolic compounds, carried out using a single line flow-injection system. Hydrogen peroxide served as co-substrate for peroxidase. The limits of detection for phenols in aqueous solutions were in the micromolar range, one assay was completed in less than 5 min. The preliminary studies showed that the compatibility of the above mentioned enzyme array enabled the multielectrode biosensor to be applied to real samples inclu

Název v anglickém jazyce

Amperometric flow-injection determination of phenolic compounds using a biosensor with immobilised laccase, peroxidase and tyrosinase

Popis výsledku anglicky

A screen-printed four-electrode sensor based on immobilization of laccase (Coriolus hirsutus), peroxidase (horseradish) and tyrosinase (mushroom) in the same array was developed for monitoring of phenols. The enzymes were immobilized onto a self-assembled monolayer (4-mercapto-1-butanol) modified gold surface via covalent attachment by epichlorohydrin coupling. The experimental conditions for simultaneous operation of the three enzymes were optimized based on catechol determination. The sensors were further applied for the amperometric detection of several substituted phenolic compounds, carried out using a single line flow-injection system. Hydrogen peroxide served as co-substrate for peroxidase. The limits of detection for phenols in aqueous solutions were in the micromolar range, one assay was completed in less than 5 min. The preliminary studies showed that the compatibility of the above mentioned enzyme array enabled the multielectrode biosensor to be applied to real samples inclu

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

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Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2005

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Electroanalysis

ISSN

1040-0397

e-ISSN

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Svazek periodika

17

Číslo periodika v rámci svazku

23

Stát vydavatele periodika

CZ - Česká republika

Počet stran výsledku

10

Strana od-do

2137-2146

Kód UT WoS článku

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EID výsledku v databázi Scopus

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