OXIDATIVE-DEGRADATION OF HIGH-MOLECULAR-WEIGHT CHLOROLIGNIN BY MANGANESE PEROXIDASE OF PHANEROCHAETE-CHRYSOSPORIUM

Phanerochaete chrysosporium was able to degrade high molecular weight chlorolignins (Mr > 30,000) from bleach plant effluents, although a direct contact between ligninolytic enzymes and chlorolignin was prevented by a dialysis tubing. In the absence of the enzymes, Mn3+ depolymerized chlorolignin when complexed with lactate causing the color, chemical oxygen demand (COD) and dry weight to decrease by 80%, 60% and 40%, respectively. Manganese peroxidase effectively catalyzed the depolymerization of chlorolignin in the presence of Mn2+ and H2O2. It can be concluded from these results that manganese peroxidase plays the major role in the initial breakdown and decolorization of high mofecular weight chlorolignin in bleach plant effluents by P. chrysosporium in vivo. © 1991.