Spectrophotometric determination of hydrogen peroxide by using the cleavage of Eriochrome black T in the presence of peroxidase

  • Zhu M
  • Huang X
  • Liu L
 et al. 
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Abstract

A new hydrogen donor for peroxidase, Eriochrome black T, was reported for the first time. Steady-state catalytic velocity depends upon enzyme and substrate concentrations, and a Michaelis Menten K(m) value of 1.72 x 10-5mol l-1and a V(max) value of 4.43 x 10-3s-1were measured at pH 8.6. Trace amount of hydrogen peroxide (2 x 10-71.0 x 10-5mol-1) was determined in aqueous solution by using the cleavage of Eriochrome black T catalyzed by peroxidase. The method is simple and practical, with high sensitivity and enzymatic activity.

Author-supplied keywords

  • Catalytic cleavage
  • Eriochrome black T
  • Peroxidase
  • Spectrophotometric determination of H2O2

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Authors

  • Min Zhu

  • Xuemei Huang

  • Liuzhan Liu

  • Hanxi Shen

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