title: Spectrophotometric determination of hydrogen peroxide by using the cleavage of Eriochrome black T in the presence of peroxidase.
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 1.72x10(-5) mol l(-1) and a V(max) value of 4.43x10(-3) s(-1) were measured at pH 8.6. Trace amount of hydrogen peroxide (2x10(-7)-1.0x10(-5) mol l(-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.
authors.affiliation: Department of Chemistry, Nankai University, Tianjin, 30 0071, People's Republic of China.
authors.forename: M
authors.initials: M
authors.lastname: Zhu
authors.forename: X
authors.initials: X
authors.lastname: Huang
authors.forename: L
authors.initials: L
authors.lastname: Liu
authors.forename: H
authors.initials: H
authors.lastname: Shen