Chloroperoxidase from Caldariomyces fumago

A useful alternative to lactoperoxidase for ¹³¹I ion labeling studies, for bromination of proteins, and for ³⁶Cl labeling of macromolecules in long-term isolation procedures.

Chloroperoxidase from Caldariomyces fumagois is useful alternative to lactoperoxidase for ¹³¹I ion labeling studies, for bromination of proteins, and for ³⁶Cl labeling of macromolecules in long-term isolation procedures. It has been used to study biocatalytic oxidation in polymersome nanoreactors .

It has been used to study biocatalytic oxidation in polymersome nanoreactors.

Chloroperoxidase (CPO) is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme and it also catalyzes peroxidase, catalase and cytochrome P450-type reactions of dehydrogenation, hydrogenperoxide (H₂O₂) decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs). PAHs are considered to be a potential health risk because of their possible carcinogenic and mutagenic activities and are widely dispersed in the environment.

Chloroperoxidase is a heme containing glycoprotein that is secreted from fungus. Chloroperoxidase (CPO) is a extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group.

One unit will catalyze the conversion of 1.0 μmole of monochlorodimedon to dichlorodimedon per min at pH 2.75 at 25 °C in the presence of potassium chloride and H₂O₂.

Crude suspension in 0.1 M sodium phosphate, pH ~4.5