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Amperometric Determination of Histamine using Immobilized Enzyme Reactors with Different Carriers  

Ji, Jung-Youn (Dept. of Food Science and Nutrition, Kyungpook National University)
Jeon, Yeon-Hee (Dept. of Food Science and Nutrition, Kyungpook National University)
Kim, Mee-Ra (Dept. of Food Science and Nutrition, Center for Beautiful Aging, Kyungpook National University)
Publication Information
Journal of the East Asian Society of Dietary Life / v.22, no.1, 2012 , pp. 88-94 More about this Journal
Abstract
Histamine is a kind of primary biogenic amine arising from the decarboxylation of the amino acid L-histidine. The toxicology of histamine and its occurrence and formation in foods are especially emphasized in fermented foods. In this study, the biosensor for detection of histamine with functionalized multi-walled carbon nanotubes (MWCNT) was developed. We also searched for an appropriate insoluble substrate to immobilize the enzyme. The developed biosensor showed a detection limit of $0.1{\mu}M$ hydrogen peroxide. The enzyme reactor was prepared with diamine oxidase immobilized on insoluble carriers including CNBr-activated sepharose 4B, calcium alginate, and controlled pore size glass beads. The coupling efficiency of CNBr-activated sepharose 4B, calcium alginate, and controlled pore size glass beads were 48.5%, 40.3%, and 51.0%, respectively. In addition, the response currents on histamine with each immobilized enzyme reactor prepared with CNBr-activated sepharose 4B, calcium alginate, and controlled pore size glass beads were 120 nA, 110 nA, and 140 nA at $100{\mu}M$ of histamine concentration, respectively. Therefore, it is suggested that controlled pore size glass beads are the best carriers for immobilizing diamine oxidase to detect histamine in this biosensor.
Keywords
Biosensor; MWCNT; histamine; carrier;
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Times Cited By KSCI : 2  (Citation Analysis)
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