Soybean Peroxidase-Catalyzed Oxidation of Luminol by Hydrogen Peroxide

Inna S. Alpeeva† and Ivan Yu. Sakharov*†§
Chemical Enzymology Department, Faculty of Chemistry, The M. V. Lomonosov Moscow State University, Moscow 119992, Russia, and Division of Chemistry, G. V. Plekhanov Russian Economic Academy, Stremyanny per. 28, 113054 Moscow, Russia
J. Agric. Food Chem., 2005, 53 (14), pp 5784–5788
DOI: 10.1021/jf0506075
Publication Date (Web): June 11, 2005
Copyright © 2005 American Chemical Society
†

 The M. V. Lomonosov Moscow State University.

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*

 Address correspondence to this author at the Chemical Enzymology Department, Faculty of Chemistry, The M. V. Lomonosov Moscow State University, Moscow 119992, Russia [fax (095) 9392742; e-mail sakharov@ enz.chem.msu.ru].

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§

 G. V. Plekhanov Russian Economic Academy.

Abstract

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 × 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.

Keywords: Peroxidase; soy; chemiluminescence; luminol; hydrogen peroxide; enhancement

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History

  • Published In Issue July 13, 2005
  • Received for review March 17, 2005. Revised manuscript received May 10, 2005. Accepted May 17, 2005. We thank INTAS (Grant 03-55-2428) and the program “Universities of Russia” (Contract UR.07.01.247) for support of this work.

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