Abstract
A pH stability analysis was made, in the presence of
tert-butyl hydroperoxide, of both immobilized and native chloroperoxidase obtained from
Caldariomyces fumago and the inactivation constants (
j
1) evaluated. The native enzyme displays a uni-exponential decay, whereas for the immobilized enzyme a three exponential equation describes the time dependent enzyme inactivation.
For immobilized enzyme, three-exponential equation describes the enzyme time-course inactivation. The obtained inactivation constants (
j
3 and
K
3) showed an increase in the stability of a fraction of the immobilized enzyme. This is probably due to a decrease of the affinity of the enzyme for the oxidant and not to a decrease in
j
3 values.