Isolation and characterization of a novel lignin peroxidase from the white-rot basidiomycete Trametes cervina

Abstract

To isolate lignin peroxidase (LiP), extracellular activity of this type of enzyme was assayed against several white-rot basidiomycetes. Trametes cervina was found to show relatively higher lignin peroxidase (LiP) activity in extracellular culture medium. LiP from T. cervina (TcLiP) was purified using several Chromatographic techniques. The molecular weight and pI value of TcLiP were found to be 37 kDa by SDS-PAGE and 3.55 by the isoelectric focusing, respectively. TcLiP activity against veratryl alcohol was higher at lower pH. A one-electron oxidation mechanism of TcLiP was spectroscopically confirmed using 1, 4-dimethoxylbenzene as a reducing substrate. Furthermore, TcLiP effectively oxidize a polymeric substrate, ferrocytochrome c to ferricytochrome c. These results strongly suggested that TcLiP meets criterion for lignin peroxidase established by the study on LiP from Phanerochaete chrysosporium. Production of LiP by T. cervina is reported for the first time.