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A New Enzyme-catalytic Resonance Scattering Assay for Glucose in Serum Using Cationic Surfactant

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Abstract

In acetic acid buffer solution, glucose oxidase (GOD) catalyzed the dissolved oxygen oxidation of glucose to form H2O2. In succession, horseradish peroxidase (HRP) catalyzed the H2O2 oxidizing excess I− to form I3−. The I3− combined with a cationic surfactant (CS) such as tetradecyl dimethyl benzyl ammonium chloride (TDMBA) to produce TDMBA-I3 association particles that exhibited the strongest resonance scattering (RS) peak at 460 nm. The enhanced RS intensity at 460 nm was linear with glucose concentration in the range of 2.0 × 10−8 − 2.0 × 10−6 mol/L, with a detection limit of 8.5 × 10−9 mol/L. The glucose in serum samples were assayed by the enzyme catalytic RS assay and by spectrophotometry. The results of both assays showed a close correlation. This assay has simplicity, sensitivity and good specificity for quantitative determination of glucose.

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Authors and Affiliations

  1. School of Chemistry and Chemical Engineering, Guangxi University, Nanning, 530004, China

    Xiaoling Wei

  2. School of Environment and Resource, Guangxi Normal University, Guilin, 541004, China

    Ji Ma & Zhiliang Jiang

  3. Key Laboratory of New Processing Technology for Nonferrous Metals and Materials of the Education Ministry, Guilin University of Technology, Guilin, 541004, China

    Aihui Liang

Authors
  1. Xiaoling Wei
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  2. Ji Ma
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  3. Aihui Liang
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  4. Zhiliang Jiang
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Correspondence to Zhiliang Jiang.

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Wei, X., Ma, J., Liang, A. et al. A New Enzyme-catalytic Resonance Scattering Assay for Glucose in Serum Using Cationic Surfactant. ANAL. SCI. 25, 887–890 (2009). https://doi.org/10.2116/analsci.25.887

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  • DOI: https://doi.org/10.2116/analsci.25.887

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