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

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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 10-5 mol l-1 and a V(max) value of 4.43 x 10-3 s-1 were measured at pH 8.6. Trace amount of hydrogen peroxide (2 x 10-7 1.0 x 10-5 mol-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.

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Zhu, M., Huang, X., Liu, L., & Shen, H. (1997). Spectrophotometric determination of hydrogen peroxide by using the cleavage of Eriochrome black T in the presence of peroxidase. Talanta, 44(8), 1407–1412. https://doi.org/10.1016/S0039-9140(97)00012-X

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