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Determination of lactose in milk products: a comparison of three-enzyme amperometric biosensor and gas chromatography/tandem mass spectrometry

Identifikátory výsledku

  • Kód výsledku v IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F17%3A73583927" target="_blank" >RIV/61989592:15310/17:73583927 - isvavai.cz</a>

  • Výsledek na webu

    <a href="https://link.springer.com/article/10.1007%2Fs00706-016-1903-7" target="_blank" >https://link.springer.com/article/10.1007%2Fs00706-016-1903-7</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1007/s00706-016-1903-7" target="_blank" >10.1007/s00706-016-1903-7</a>

Alternativní jazyky

  • Jazyk výsledku

    angličtina

  • Název v původním jazyce

    Determination of lactose in milk products: a comparison of three-enzyme amperometric biosensor and gas chromatography/tandem mass spectrometry

  • Popis výsledku v původním jazyce

    Two completely different analytical methods for lactose determination are presented. Three-enzyme biosensor involving b-galactosidase, glucose oxidase, and horseradish peroxidase was constructed with successive steps of optimization. Primary experiments were carried out with horseradish peroxidase biosensor in solution of hydrogen peroxide. Addition of poly(ethylene glycol) diglycidyl ether was examined and the best constant potential for chronoamperometric experiments was selected at -0.05 V using cyclic voltammetry. Ferrocene was chosen as the best from three tested mediators and optimum concentration of ferrocene was found out at 2 g dm(-3). Two electrode materials were compared. Spectroscopic graphite electrode proved better electrochemical response for its twice larger electro-active surface than screen-printed carbon electrode. Phosphate buffer solution of pH 7.5, at which the three-enzyme system provided the highest current signal, was used for lactose determination in milk, milk powder, curd cheese, and yogurt. Gas chromatography with tandem mass spectrometric detection was used for determination of lactose, glucose, and galactose in the real samples with internal standard salicine using single ion monitoring mode. Determined content of lactose in the milk products was compared with declared values. Gas chromatography with tandem mass spectrometric detection offers higher sensitivity and orthogonal selectivity in comparison to enzyme biosensor.

  • Název v anglickém jazyce

    Determination of lactose in milk products: a comparison of three-enzyme amperometric biosensor and gas chromatography/tandem mass spectrometry

  • Popis výsledku anglicky

    Two completely different analytical methods for lactose determination are presented. Three-enzyme biosensor involving b-galactosidase, glucose oxidase, and horseradish peroxidase was constructed with successive steps of optimization. Primary experiments were carried out with horseradish peroxidase biosensor in solution of hydrogen peroxide. Addition of poly(ethylene glycol) diglycidyl ether was examined and the best constant potential for chronoamperometric experiments was selected at -0.05 V using cyclic voltammetry. Ferrocene was chosen as the best from three tested mediators and optimum concentration of ferrocene was found out at 2 g dm(-3). Two electrode materials were compared. Spectroscopic graphite electrode proved better electrochemical response for its twice larger electro-active surface than screen-printed carbon electrode. Phosphate buffer solution of pH 7.5, at which the three-enzyme system provided the highest current signal, was used for lactose determination in milk, milk powder, curd cheese, and yogurt. Gas chromatography with tandem mass spectrometric detection was used for determination of lactose, glucose, and galactose in the real samples with internal standard salicine using single ion monitoring mode. Determined content of lactose in the milk products was compared with declared values. Gas chromatography with tandem mass spectrometric detection offers higher sensitivity and orthogonal selectivity in comparison to enzyme biosensor.

Klasifikace

  • Druh

    J<sub>imp</sub> - Článek v periodiku v databázi Web of Science

  • CEP obor

  • OECD FORD obor

    10406 - Analytical chemistry

Návaznosti výsledku

  • Projekt

    Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

  • Návaznosti

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Ostatní

  • Rok uplatnění

    2017

  • Kód důvěrnosti údajů

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

Údaje specifické pro druh výsledku

  • Název periodika

    Monatshefte für Chemie

  • ISSN

    0026-9247

  • e-ISSN

  • Svazek periodika

    148

  • Číslo periodika v rámci svazku

    3

  • Stát vydavatele periodika

    AT - Rakouská republika

  • Počet stran výsledku

    8

  • Strana od-do

    517-524

  • Kód UT WoS článku

    000396528600017

  • EID výsledku v databázi Scopus