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- Publisher
- Springer Journals
- Copyright
- Copyright © 2010 by Pleiades Publishing, Ltd.
- Subject
- Life Sciences; Medical Microbiology ; Microbiology ; Biochemistry, general
- ISSN
- 0003-6838
- eISSN
- 1608-3024
- DOI
- 10.1134/S0003683810010114
- Publisher site
- See Article on Publisher Site
Abstract
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. Detection limit of the enzyme 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.
Journal
Applied Biochemistry and Microbiology – Springer Journals
Published: Jan 6, 2010