An unmediated hydrogen peroxide biosensor based on hemoglobin incorporated in a montmorillonite membrane
Abstract
Hemoglobin was incorporated in a montmorillonite membrane. Electrochemical and spectroscopic studies revealed that the electron transfer reactivity and peroxidase activity of the protein were both enhanced. Nevertheless, its structure was still maintained native-like in the membrane. An unmediated hydrogen peroxide biosensor was accordingly prepared. The calibration plot of this H2O2 sensor was linear in the range of 1.0 × 10−6–6.0 × 10−4 mol L−1. The relative standard deviation was 3.1% for six successive determinations at a concentration of 1.0 × 10−4 mol L−1. The detection limit was 6.0 × 10−7 mol L−1. Possible interferences in real sample analyses are discussed.