Production and stability of lignin peroxidases of Phanerochaete chrysosporium cultivated on glycerol in the presence of solid manganese(IV)oxide

Summary Lignin peroxidase production by Phanerochaete chrysosporium, under shaking conditions in an N-limited glycerol medium supplied with solid manganese(IV)oxide, increased to a high level. It was shown that the high enzymatic level was due to a higher specific enzymatic activity compared to corresponding –MnO₂ cultures when measurements were based upon the haem component (A₄₀₉). The superiority of cultivation in the presence of MnO₂ was reflected by the longevity of the enzymes produced in the culture fluid. By tracing enzymatic activities (toward veratryl alcohol and phenol red) as a function of time of incubation, a higher specific activity of single peroxidases from +MnO₂ cultures was determined compared to corresponding –MnO₂ cultures. Different patterns of peroxidases were found in glucose and glycerol cultures and the problems of classifying peroxidases are discussed. The effect of veratryl alcohol on peroxidases was compared with that of MmO₂. Even at higher levels of enzymatic activity an additional influence of MnO₂ on the stabilization of the enzymes was observed. By applying homoveratryl amine instead of veratryl alcohol the activity of the peroxidases in agitated +MnO₂ cultures exceeded 2000 units/l.