Immobilization of HRP Enzyme on Layered Double Hydroxides for Biosensor Application | Zendy

Z. M. Baccar | Zendy; I. Hafaiedh | Zendy

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Immobilization of HRP Enzyme on Layered Double Hydroxides for Biosensor Application

Author(s) -

Z. M. Baccar,

I. Hafaiedh

Publication year - 2011

Publication title -

international journal of electrochemistry

Language(s) - English

Resource type - Journals

eISSN - 2090-3537

pISSN - 2090-3529

DOI - 10.4061/2011/934893

Subject(s) - biosensor , layered double hydroxides , chronoamperometry , detection limit , coprecipitation , horseradish peroxidase , chemistry , hydrogen peroxide , adsorption , hydrotalcite , chromatography , immobilized enzyme , cyclic voltammetry , nuclear chemistry , inorganic chemistry , organic chemistry , electrode , enzyme , electrochemistry , catalysis , biochemistry

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 H2O2 was obtained with a good reproducibility. We investigate the sensitivity of our developed biosensor for H2O2 detection in raw milk

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