The basidiomycete Phanerochaete chrysosporium produces several isoforms
of lignin peroxidase, which catalyzes the oxidative depolymerization of
lignin To date, ion-exchange chromatography and preparative isoelectric
focusing (IEF) have been commonly used for isolation of lignin
peroxidase isoenzymes. In this work we have purified major lignin
peroxidases to high purity by a one-step chromatographic method,
chromatofocusing. The purified isoenzymes were identified by analytical
IEF using isoenzymes purified by preparative IEF as standards. The
specific activities and spectral properties of the isoenzymes were
comparable with the previously published data. The predominant isoenzyme
under the growth conditions used was LiP 4.65. Almost 50% of the lignin
peroxidase activity applied into the column was recovered in the LiP
4.65 fraction. The total recovery of the lignin peroxidase activity was
over 80%.