Soybean peroxidase-catalyzed oxidation of luminol by hydrogen peroxide.
Anionic soybean peroxidase Glycine max (SbP) is shown to efficiently catalyze luminol oxidation by hydrogen peroxide. Contrary to horseradish peroxidase, the presence of p-iodophenol in the reaction medium affects slightly the efficiency of SbP catalysis. A maximal intensity of chemiluminescence, produced through this enzymatic reaction, was detected at pH 8.4-8.6. Contrary to anionic palm tree peroxidase, in the presence of SbP, chemiluminescence intensity increases with the reaction buffer concentration. The detection limit of SbP in the reaction of luminol oxidation is 0.3 x 10(-12) M. Therefore, high sensitivity in combination with the long-term chemiluminescent signal is indicative of good prospects for application of this enzyme in enzyme immunoassay with chemiluminescent detection.
Chemical Enzymology Department, Faculty of Chemistry, The M. V. Lomonosov Moscow State University, Moscow 119992, Russia.
Inna S
IS
Alpeeva
Ivan Yu
IY
Sakharov
D002384:Catalysis; D006861:Hydrogen Peroxide / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007124:Immunoenzyme Techniques; D008163:Luminescent Measurements; D008165:Luminol / Q000378:metabolism*; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000378:metabolism*; D013025:Glycine max / Q000201:enzymology*
D008165:Luminol; D006861:Hydrogen Peroxide; D009195:Peroxidase