Abstract
An enzymatic biosensor has been developed for detection of hydrogen peroxide with immobilized Horseradish peroxidase (HRP). HRP was immobilized by using glutaraldehyde (GA) that cross linked with modified polyaniline (PANI) as mediator to improve electron transfer. Modified carbon paste electrodes (MCPE) PANI was more effective during electron transfer compared to carbon paste electrodes (CPE). Cyclic voltammetry method (VC) was used to determine the electrochemical properties of the modified electrode substrate to produce redox reactions. The effect of pH and temperature were analyzed by cyclic voltammetry. The optimum performance of HRP/GA/PANI was at pH 7 and 50°C. Kinetics parameters HRP enzyme were determined in optimum condition. The Michaelis-Menten constant (Km) value and current maximum (Imax) have been obtained as 1.71 mM and 0.29 mA.
Highlights
Hydrogen peroxide is one of the molecules involved in reactive oxygen species
Horseradish peroxidase (HRP) is one of enzyme that used in electrochemistry as biosensor [7] and biofuel cell [8], as decolorization agent [10], immunoassay [11], biodegradation [12] and synthesis of polyaniline [13]
The modified carbon paste electrodes (MCPE) PANI were prepared with 0.15 gr mixed carbon and 100 mL of paraffin with 2 mg PANI in mortal (Figure 1)
Summary
Hydrogen peroxide are produced by catalysis of glucose oxidase, cholesterol oxidase, xanthine oxidase, alcohol oxidase, and uricase reaction. These enzymes were applied for monitoring levels of glucose, cholesterol, xanthine, alcohol, and gout. Horseradish peroxidase (HRP) is one of enzyme that used in electrochemistry as biosensor [7] and biofuel cell [8], as decolorization agent [10], immunoassay [11], biodegradation [12] and synthesis of polyaniline [13]. One of the critical point should be considered to make biosensor is electron transfer. Other compound that can be used for electron transfer is polyaniline. Polyaniline has unique properties was called doping dedoping or protonation deprotonation [14]
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