[Oxidation of luminol with peroxidase from royal palm leaves].
We optimized the conditions for luminol oxidation by hydrogen peroxide in the presence of peroxidase (EC 1.11.1.7) from royal palm leaves (Roystonea regia). The pH range (8.3-8.6) corresponding to maximum chemiluminescence was similar for palm tree peroxidase and horseradish peroxidase. Variations in the concentration of the Tris buffer were accompanied by changes in chemiluminescence. Note that maximum chemiluminescence was observed in the 30 mM solution. The detection limit of the enzyme assay during luminol oxidation by hydrogen peroxide was 1 pM. The specific feature of palm tree peroxidase was the generation of a long-term chemiluminescent signal. In combination with the data on the high stability of palm tree peroxidase, our results indicate that this enzyme is promising for its use in analytical studies.
Alpeeva
I S
IS
Sakharov
I Iu
IIu
D028023:Arecaceae / Q000201:enzymology*; D006735:Horseradish Peroxidase / Q000737:chemistry; D006861:Hydrogen Peroxide / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D049449:Luminescence; D008165:Luminol / Q000737:chemistry*; D009195:Peroxidase / Q000737:chemistry*; D018515:Plant Leaves / Q000201:enzymology*; D010940:Plant Proteins / Q000737:chemistry*
D010940:Plant Proteins; D008165:Luminol; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; D009195:Peroxidase