Determination of the most effective procedure for the immobilization of enzymes and amperometric biosensor for bonded glucose
2007
Mojica, E.R.E., Philippines Univ. Los Banos, College, Laguna (Philippines). Inst. of Chemistry | Kalcher, K., Karl Franzens Univ., A-8010 Graz (Austria). Inst. for Analytical Chemistry
Amperometric biosensors for bonded glucose were fabricated using screen printed carbon elecrode bulk modified with manganese dioxide onto which glucosidase and glucose oxidase were immobilized by Nafion film entrapment. Three methods of enzyme immobilization were performed (layering, mixing and sequencing of enzyme solutions). The analytical performance of the biosensor prepared by different enzyme immobilization methods was assessed in a flow injection mode using three sugar standards: sucrose, cellobiose and (-)-4-nitro-phenyl-beta-D-glucopyranoside at a potential of 480 mV (vs Ag/AgCl), pH 7.0 carrier solution (0.1 M phosphate buffer solution) and at a flow rate of 0.1 mL/min. Peak heights of the current response were used to evaluate the results. Based on the results, the mixing of enzyme solutions was the most effective immobilization method because it produced the highest signal, followed by layering as the second most effective and sequencing of enzyme solutions as the third most effective method.
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