• KSBB Journal
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• v.23 no.4
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• pp.340-344
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• 2008

Coprinus cinereus peroxidase (CiP) was often used as a catalyst for oxidative polymerization of a variety of phenol derivatives to produce a new class of polyphenols. Economical point of view, to know the mechanism of enzyme deactivation is significantly important because cost of enzyme is critically high. Hydrogen peroxide being used as oxidizing agent induced deactivation of peroxidase by destruction of heme structure. In the presence of hydrogen peroxide the stability of peroxidase was unexpectedly improved by adding organic solvent. Especially 2-propanol significantly improved enzyme stability among tested solvents. Radical scavenging by organic solvents may play a major role in protecting peroxidase from the oxidation of oxidizing radicals.