Selective Synthesis of Lignin Peroxidase and Manganese Peroxidases by Phanerochaete chrysosporium
黄孢原毛平革菌选择性合成木质素过氧化物酶和锰过氧化物酶

Selective synthesis of lignin peroxidase (LiP) and manganese peroxidase (MnP) by Phanerochaete chrysosporium in N-limited submerged cultures was studied under different physiological conditions. Whereas lignin peroxidase was detectable only in a narrow range of nitrogen source concentration (0.8~1.8 mmol/L), manganese peroxidase reached considerable levels over a broad range (0.4~2.0 mmol/L). In the absence of Mn2+, only lignin peroxidase was detectable, which was also found when the concentration of Mn2+ was in the range of 0.06~0.84 mmol/L. High level of manganese peroxidase was obtained at very low concentration of Mn2+, and almost kept constant with the increment of Mn2+, but was repressed obviously when the concentration of Mn2+ was beyond 3.36 mmol/L. Pure oxygen increased the activity of lignin peroxidase by 50%, but had no obvious effect on manganese peroxidase.