Kinetic and stability studies on the chloroperoxidase complexes in presence of tert-butyl hydroperoxide
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Updated: Aug 20, 2026

Fast and Specific Assessment of the Halogenating Peroxidase Activity in Leukocyte-enriched Blood Samples
Published on: July 28, 2016
Paolo Toti1, Antonella Petri, Tiziana Gambicorti
1Unità di Biochimica, Dipartimento di Fisiologia e Biochimica, Università di Pisa, via S. Zeno 51, 56027 Pisa, Italy.
Abstract:
The inactivation of native chloroperoxidase (CPO) from Caldariomyces fumago in the presence of tert-butyl hydroperoxide (tert-BuOOH) was investigated. A kinetic analysis was made and the inactivation constants (V(3) and K(3)) were evaluated. In prolonged times, uni-exponential equation describes the enzyme time course inactivation. A method based on the rate of inactivation of the enzyme in the presence of the inactivating molecule tert-BuOOH was also performed. A second group of inactivation constants (j(3) and K) was obtained, which is sufficiently close to the first two, thus verifying that the decreasing of enzyme absorbance corresponds to the decay of activity.
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