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Enzyme-catalyzed reaction of voltammetric enzyme-linked immunoassay system based on OAP as substrate

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Abstract

Theo-aminophenol (OAP)-H2O2-horseradish peroxidase (HRP) voltammetric enzyme-linked immunoassay new system has extremely high sensitivity. HRP can be measured with a detection limit of 6.0×1010 g/L and a linear range of 1.0×10-9-4.0×10-6 g/L. The pure product of H2O2 oxidizing OAP catalyzed by HRP was prepared with chemical method. The enzyme-catalyzed reaction has been investigated with electroanalytical chemistry, UV/Vis spectrum, IR spectrum,13C NMR,1H NMR, mass spectrum, elemental analysis, etc. Under the selected enzyme-catalyzed reaction conditions, the oxidation product of OAP with H2O2 catalyzed by HRP is 2-aminophenoxazine-3-one. The processes of the enzyme-catalyzed reaction and the electroreduction of the product of the enzymecatalyzed reaction have been described.

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Authors and Affiliations

  1. Department of Chemistry, Nanjing University, 210093, Nanjing, China

    Shusheng Zhang & Hongyuan Chen

  2. Department of Applied Chemistry, Qingdao Institute of Chemical Technology, 266042, Qingdao, China

    Kui Jiao

Authors
  1. Shusheng Zhang
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  2. Hongyuan Chen
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  3. Kui Jiao
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Project supported by the National Natural Science Foundation of China (Grant No. 29775012).

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Zhang, S., Chen, H. & Jiao, K. Enzyme-catalyzed reaction of voltammetric enzyme-linked immunoassay system based on OAP as substrate. Sc. China Ser. B-Chem. 42, 195–203 (1999). https://doi.org/10.1007/BF02875517

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  • DOI: https://doi.org/10.1007/BF02875517

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