Purification and Properties of Peroxidase from Phanerochaete chrysosporium

The wood-destroying fungus Phanerochaete chrysosporium secretes extracellular enzymes known as lignin peroxidases that are involved in the biodegradation of lignin and a number of environmental pollutants.Several lignin peroxidases are produced in liquid cultures of this fungus.Here two lignin degradation enzymes,lignin peroxidase(LiP) and manganese peroxidase(MnP) were purified and characterized from Phanerochaete chrysosporium culture.The molecular weight of LiP and MnP are 37 KD and 40 KD respectively.Both of them have the same optimized activity temperature of 37 ℃.The temperature for losing half of the activity(t1/2) within 2 h is 40 ℃ for LiP and 45 ℃ for MnP.The optimum pH of MnP and LiP are 4.6 and 2.8 respectively.MnP is relatively stable in pH 4.0~7.0 and LiP in 2.2~5.2.Fe2+ promotes the activity of both LiP and MnP,Na+、K+、Ca2+、Mg2+、Zn2+、Fe3+、Ag+、Co2+、NH promote the activity of LiP but inhibit that of MnP.Cu2+ shows strong inhibition only to MnP but has no effect on LiP.