Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
71307 | Journal of Molecular Catalysis B: Enzymatic | 2006 | 8 Pages |
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 (j1) 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 (j3 and K3) 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 j3 values.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Catalysis
Authors
Paolo Toti, Antonella Petri, Tiziana Gambicorti, Ahmed M. Osman, Carlo Bauer,