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Utilizing Aspergillus niger Fumonisin Amine Oxidase for the Electrochemical Detection of Fumonisin

  • Fumonisins are a class of toxic secondary metabolites produced by various Fusarium species. The two most important producers of fumonisins are F. verticillioides and F. proliferatum but also Aspergillus niger is known to produce fumonisins. Most frequently they occur on maize, but also other grains can be contaminated with this group of mycotoxins. Exposure to fumonisins by dietary intake can have serious health effects on farm animals and also within humans. Thus, the European Commission sets legal limits for fumonisins in feed and foodstuffs. The detection of fumonisins is frequently performed in laboratories by chromatographic methods, which are costly and require trained personnel. Simplifying the analysis is therefore a major goal using portable detection systems. Electrochemical enzymatic biosensors offer great promise to meet this demand. Here we report for the first time an enzymatic fumonisin sensing approach with amperometric detection. For this purpose, an Aspergillus nigerFumonisins are a class of toxic secondary metabolites produced by various Fusarium species. The two most important producers of fumonisins are F. verticillioides and F. proliferatum but also Aspergillus niger is known to produce fumonisins. Most frequently they occur on maize, but also other grains can be contaminated with this group of mycotoxins. Exposure to fumonisins by dietary intake can have serious health effects on farm animals and also within humans. Thus, the European Commission sets legal limits for fumonisins in feed and foodstuffs. The detection of fumonisins is frequently performed in laboratories by chromatographic methods, which are costly and require trained personnel. Simplifying the analysis is therefore a major goal using portable detection systems. Electrochemical enzymatic biosensors offer great promise to meet this demand. Here we report for the first time an enzymatic fumonisin sensing approach with amperometric detection. For this purpose, an Aspergillus niger fumonisin amine oxidase (AnFAO) catalyzing the oxidative deamination of fumonisins, producing hydrogen peroxide, was recombinantly produced in E. coli. It was found that the specific activity of AnFAO using 20 μM Fumonisin B1 as substrate is higher than for 20 μM Fumonisin B2 with 0.122 U mg-1 and 0.058 U mg-1, respectively. It was possible to show a dependence of enzyme activity with enzyme – and substrate-concentration. For fumonisin B1 detection, the enzyme was coupled covalently to magnetic particles and the enzymatically produced H2O2 was detected amperometrically in a flow injection system using Prussian blue carbon electrodes. The developed method allows to quantify fumonisin B1 concentrations down to 1.5 µM and demonstrates that the recombinantly produced AnFAO was able to deaminate different concentrations of fumonisin even in immobilized form. Thus, this enzyme is well suited to develop an enzyme based electrochemical biosensor for fumonisin contaminated food and feed.zeige mehrzeige weniger

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Metadaten
Autor*innen:Zoltán KonthurORCiD
Koautor*innen:Soraya Riedel, Rabia Bayram, Sarah Döring, Rudolf Schneider
Dokumenttyp:Vortrag
Veröffentlichungsform:Präsentation
Sprache:Englisch
Jahr der Erstveröffentlichung:2023
Organisationseinheit der BAM:1 Analytische Chemie; Referenzmaterialien
1 Analytische Chemie; Referenzmaterialien / 1.8 Umweltanalytik
DDC-Klassifikation:Naturwissenschaften und Mathematik / Chemie / Analytische Chemie
Freie Schlagwörter:Amperometry; Biosensor; Food analysis; Mycotoxin
Themenfelder/Aktivitätsfelder der BAM:Chemie und Prozesstechnik
Chemie und Prozesstechnik / Chemische Charakterisierung und Spurenanalytik
Veranstaltung:Affinity 2023 - the 25th meeting of the International Society for Molecular Recognition
Veranstaltungsort:Lisbon, Portugal
Beginndatum der Veranstaltung:05.06.2023
Enddatum der Veranstaltung:07.06.2023
Bemerkung:
Geburtsname von Riedel, Soraya: Höfs, S. -  Birth name of Riedel, Soraya: Höfs, S.
Verfügbarkeit des Dokuments:Datei im Netzwerk der BAM verfügbar ("Closed Access")
Datum der Freischaltung:20.06.2023
Referierte Publikation:Nein
Eingeladener Vortrag:Nein
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