[Luminol oxidation by hydrogen peroxide with chemiluminescent signal formation catalyzed by peroxygenase from the fungus Agrocybe aegerita V.Brig].
Conditions of luminol oxidation by hydrogen peroxide in the presence of peroxygenase from the mushroom Agrocybe aegerita V.Brig have been optimized. The pH value (8.8) at which fungal peroxygenase produces a maximum chemiluminescent signal has been shown to be similar to the pH optimum value of horseradish peroxidase. Luminescence intensity changed when the concentration of Tris buffer was varied; maximum intensity of chemiluminescence was observed in 40 mM solution. It has been shown that enhancer (p-iodophenol) addition to the substrate mixture containing A. aegerita peroxygenase exerted almost no influence on the intensity of the chemiluminescent signal, similarly to soybean, palm, and sweet potato peroxidases. Enzyme detection limit in the reaction of luminol oxidation by hydrogen peroxide was 0.8 pM. High stability combined with high sensitivity make this enzyme a promising analytical reagent.
Vdovenko
M M
MM
Ulrich
R
R
Hofrichter
M
M
Sakharov
I Iu
IIu
D055362:Agrocybe / Q000201:enzymology*; D031215:Armoracia / Q000201:enzymology; D005656:Fungal Proteins / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism*; D008163:Luminescent Measurements; D008165:Luminol / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010084:Oxidation-Reduction
D005656:Fungal Proteins; D008165:Luminol; D006861:Hydrogen Peroxide; D006899:Mixed Function Oxygenases; C022333:peroxygenase