Covalent immobilization of chloroperoxidase on silica gel and properties of the immobilized biocatalyst

Immobilization of chloroperoxidase (CPO) isolated from the mold Caldariomyces fumago on silica gel was performed. The support was derivatized with 3-glycidoxypropyltrimethoxysilane by using a reported method and the enzyme was covalently bound via reaction with epoxide groups under mild conditions. The enzyme was still active after the immobilization process. No leaching of the enzyme from the support was detectable after repeated washings. The halogenation reaction catalysed by the immobilized enzyme in buffer was compared to that catalysed by the free enzyme. The immobilization of CPO enhanced the stability of the enzyme with respect to the effect of pH and oxidizing agent concentration.