A H(2)O(2) Biosensor Based on Immobilization of Horseradish Peroxidase in a Gelatine Network Matrix

A simple and promising H(2)O(2) biosensor has been developed by successful entrapment of horseradish peroxidase (HRP) in a gelatine matrix which was cross-linked with formaldehyde. The large microscopic surface area and porous morphology of the gelatine matrix lead to high enzyme loading and the enzyme entrapped in this matrix can retain its bioactivity. This biosensor exhibited a fast amperometric response to hydrogen peroxide (H(2)O(2)). The linear range for H(2)O(2) determination was from 2.5×10(-5) to 2.5×10(-3) M, with a detection limit of 2.0×10(-6) M based on S / N = 3. This biosensor possessed very good reproducibility.