Abstract
We present a new biosensor for hydrogen peroxide (H2O2) detection. The biosensor was based on the immobilization of horseradish peroxidase (HRP) enzyme on layered double hydroxides- (LDH-) modified gold surface. The hydrotalcite LDH (Mg2Al) was prepared by coprecipitation in constant pH and in ambient temperature. The immobilization of the peroxidase on layered hybrid materials was realized via electrostatic adsorption autoassembly process. The detection of hydrogen peroxide was successfully observed in PBS buffer with cyclic voltammetry and the chronoamperometry techniques. A limit detection of 9 μM of H2O2was obtained with a good reproducibility. We investigate the sensitivity of our developed biosensor for H2O2detection in raw milk.
Highlights
Horseradish peroxidase (HRP) is a glycoprotein with four lysine residues for conjugation to a labeled molecule
We present a new biosensor for hydrogen peroxide (H2O2) detection based on layered double hydroxides (LDH) layer
The biosensor was developed by the immobilization of horseradish peroxidase (HRP) enzyme on layered double hydroxides- (LDH-)modified gold electrode
Summary
Horseradish peroxidase (HRP) is a glycoprotein with four lysine residues for conjugation to a labeled molecule. It was established that cationic clays and especially anionic ones or layered double hydroxides were considered as a new class of materials with a high trapping potential of molecules of different sizes and that they form hybrid materials. These materials present very attractive advantages such as a low cost of purification or synthesis and their biocompatibility. The detection of hydrogen peroxide was successfully observed in PBS buffer with cyclic voltammetry and the chronoamperometry techniques
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