Abstract
Laccase enzyme, a commonly used enzyme for the construction of biosensors for phenolic compounds was used for the first time to develop a new biosensor for the determination of the azo-dye tartrazine. The electrochemical biosensor was based on the immobilization of laccase on functionalized methacrylate-acrylate microspheres. The biosensor membrane is a composite of the laccase conjugated microspheres and gold nanoparticles (AuNPs) coated on a carbon-paste screen-printed electrode. The reaction involving tartrazine can be catalyzed by laccase enzyme, where the current change was measured by differential pulse voltammetry (DPV) at 1.1 V. The anodic peak current was linear within the tartrazine concentration range of 0.2 to 14 μM (R2 = 0.979) and the detection limit was 0.04 μM. Common food ingredients or additives such as glucose, sucrose, ascorbic acid, phenol and sunset yellow did not interfere with the biosensor response. Furthermore, the biosensor response was stable up to 30 days of storage period at 4 °C. Foods and beverage were used as real samples for the biosensor validation. The biosensor response to tartrazine showed no significant difference with a standard HPLC method for tartrazine analysis.
Highlights
Laccase is a well-known enzyme for the oxidization of a wide range of compounds such as polyphenols, methoxy-substituted phenols and diamines
Statistical analysis was performed to determine whether the developed method biosensor are correlated or not. These results showed that the biosensor method has a good correlation with the high performance liquid chromatography (HPLC) method with slopes of 0.9958 and 1.0577 respectively for candy coated with chocolate and commercial mango juice
A new electrochemical enzymatic biosensor based on laccase enzyme for tartrazine analysis was successfully developed
Summary
Laccase (polyphenoloxidase; EC 1.10.3.2) is a well-known enzyme for the oxidization of a wide range of compounds such as polyphenols, methoxy-substituted phenols and diamines This enzyme, which belongs to the blue multi-copper-oxidase family undergoes typical reactions where a phenolic group is often oxidised via one electron transfer to form a phenoxyl free radical. Laccase based voltammetric/amperometric biosensors have been developed for food and beverages analyses These biosensors have found wide applications in the analysis of phenol, polyphenol, guaiacol, gallic acid, caffeic acid, catechin, catechol, hydroquinone and resorcinol to name a few in various food and beverage products [2,3,4]. The enzyme laccase immobilisation methods for the construction of biosensors reported for food analysis were based on several procedures involving laccase adsorptions (e.g., in carbon/graphite materials, nafion nanocomposite and screen-printed gold); enzyme entrapments (e.g., in polyazetidine prepolymer, chitosan, MWCNTs, PVA photopolymer and sonogel), enzyme
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