Improvement in ligninolytic activity of Phanerochaete chrysosporium cultures by glucose oxidase

The effects of glucose oxidase (GOx) addition on enzymatic activity of manganese peroxidase (MnP) and lignin peroxidase (LiP) and protein production of Phanerochaete chrysosporium cultures were studied for the first time. In cultures supplemented daily with 300 U/L GOx after beginning of ligninolysis, MnP activity was increased 4-fold (6144 U/L) on day 15, LiP activity was induced (maximum activity was 220 U/L.) and protein content of culture filtrates was increased significantly as compared to the control culture (i.e., no GOx-glucose was added.). In addition, remarkable increase in stability of MnP productivity by fungi, in cultures supplemented daily with GOx-glucose (more than 32 days), as compared with control cultures (22 days) was observed. Neither H2O2 nor gluconic acid produced by GOx was responsible for improvement of peroxidase activity in nitrogen-limited cultures. The new findings could be useful for improving the yield of peroxidase enzymes for degradation of a broad range of man-made aromatic compounds.