Voltammetric study of a detergent-stable Actinomadura keratinilytica lipase CPT29-cross-linked GA/BSA platinum biosensor
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Abstract
This study describes the immobilization of a native lipase (LCPT29) from Actinomadura keratinilytica strain CPT29 isolated from poultry compost in north-east of Algeria in order to detect ester pollutants in an aqueous environment. For this purpose this detergent-stable lipase was immobilized with glutaraldehyde as a cross-linker, in the presence of bovine serum albumin (BSA) onto a platinum (Pt) electrode. The prepared enzyme membrane was characterized by FT-IR spectroscopy, confirming its formation network, and its coating the Pt-electrode by evaluating electrochemical changes using cyclic voltammetry. The effectiveness of the cross-linked enzyme membrane-coated working electrode was evaluated electrochemically by detecting propyl 4-hydroxybenzoate (PHB) as a model analyte. Under optimal conditions and at an applied potential of -250 mV, the LCPT29-based biosensor showed a linear response over the concentration range from10-14 to 10-8 mol L-1 (r = 0.991), with a detection limit of 10-14 mol L-1. The biosensor exhibited high sensitivity (0.0327 mA L mol-1), good stability (RSD = 0.37 %) and significant selectivity as well as the ability to analyze trace amounts of PHB in real water samples, demonstrating its potential for electrochemical biosensing applications.
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