No abstract

In order to substitute for the marketed horseradish peroxidase, a hydrogen peroxide sensor embedded with tobacco leaf in carbon pastes was constructed and its sensing ability was electrochemically evaluated. Ten and more electrode parameters obtained implied that the enzyme electrode exerts its remarkable specificity quantitatively in the experimental range of potential. Especially the small symmetry factor (α, 0.21) showed that the electrode kinetics is very sensitive to the change of electrode potential. The experimental facts above suggested that our enzyme electrode functions as a hydrogen peroxide sensor normally and tobacco peroxidase can be used in the place of the marketed one as an alternative to marketed ones.

No abstract

A biosensor including the homogenized tissue of mugwort embedded in carbon paste, which senses hydrogen peroxide, was constructed and its electrochemical properties were validated using voltammetry. The good linearity of Hanes-Woolf plot implied that the reduction reaction of substrate was catalyzed by mugwort peroxidase at the electrode surface. Also the small value of symmetry factor, 0.28, indicated that electrochemical kinetics of the sensor is very sensitive to the change of electrode potential. Many experimental results collected above proved that the dissociation of hydrogen peroxide is dependent on the catalytic power of mugwort peroxidase qualitatively and quantitatively at the surface of the mugwort electrode. It is our firm belief that the marketed HRP can be replaced with mugwort tissue.