Abstract
The catalytic reaction of catalase was investigated, by means of a Clark oxygen sensor, in the presence of various concentrations of acetylsalicylic acid. Michaelis-Menten kinetic parameters were determined from Lineweaver-Burk plots, obtained in the absence and in the presence of the inhibitor. The inhibition pattern, suggested by the Lineweave-Burk plots, corresponds to a fully mixed inhibition mechanism. A kinetic method, based on the indicator reaction: \({\text{H}}_{{\text{2}}} {\text{O}}_{{\text{2}}} \xrightarrow{{{\text{catalase, acetylsalicylic acid}}}}{\text{H}}_{{\text{2}}} {\text{O}} + 0.5{\text{O}}_{{\text{2}}} \), was developed for the quantitative determination of acetylsalicylic acid. Calibration graphs of the reciprocal value of first-order rate constant versus acetylsalicylic concentration covered the concentration range (2.99–19.98)×10−4 mol/L, while the detection limit was 4.12×10−4 mol/L acetylsalicylic acid with a standard deviation of 2.1×10−5 mol/L.
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Mureşanu, C., Copolovici, L. Kinetic method for acetylsalicylic acid determination based on its inhibitory effect upon the catalytic decomposition of H2O2 . Anal Bioanal Chem 378, 1868–1872 (2004). https://doi.org/10.1007/s00216-003-2470-4
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DOI: https://doi.org/10.1007/s00216-003-2470-4