A novel amperometric biosensor based on a co-crosslinked l-lysine-α-oxidase/overoxidized polypyrrole bilayer for the highly selective determination of l-lysine

•We report a novel, highly selective, l-lysine amperometric biosensor.•Kinetic control of l-lysine-α-oxidase increased enzyme specificity.•Overoxidized polypyrrole membrane allowed interferent rejection.•The biosensor proved successfully for preliminary lysine analysis of pharmaceutical and food samples.

An amperometric biosensor for the determination of l-lysine based on l-lysine-α-oxidase immobilized by co-crosslinking on a platinum electrode previously modified by an overoxidized polypyrrole film is described. The optimization of experimental parameters, such as pH and flow rate, permitted to minimize significantly substrate interferences even using a low specific, commercial enzyme. The relevant biases introduced in the measurement of lysine were just about 1% for l-arginine, l-histidine and l-ornithine, roughly 4% for l-phenylalanine and l-tyrosine. The developed approach allowed linear lysine responses from 0.02 mM up to 2 mM with a sensitivity of 41 nA/(mM × mm2) and a detection limit of 4 μM (S/N = 3). No appreciable loss in lysine sensitivity was observed up to about 40 days. Allowing polypyrrole layer to remove interference from electroactive compounds, the present method revealed suitable to detect l-lysine in a pharmaceutical and cheese sample, showing a good agreement with the expected values.

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