Kinetics of phenol oxidation by peroxidase |
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Authors: | Palligarnai T Vasudevan Luting Olivia Li |
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Institution: | (1) Department of Chemical Engineering, Kingsbury Hall, University of New Hampshire, 03824 Durham, NH |
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Abstract: | Studies of the kinetic behavior of horseradish peroxidase (HRP) at pH 8 and at room temperature indicate that the reaction
of phenol with H2O2 catalyzed by HRP exhibits normal Michaelis-Menten saturation kinetics. An irreversible reaction mechanism for the steady-state
kinetics of HRP, which is consistent with the experimental data, is considered. The second-order rate constants for the reactions
of HRP with H2O2 and compound II with phenol are 4.14 × 105 M-1s-1 and 5.54 × 104M-1s-1, respectively. |
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Keywords: | Horseradish peroxidase phenol hydrogen peroxide |
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