Purification, characterization, and coal depolymerizing activity of lignin peroxidase from Gloeophyllum sepiarium MTCC-1170

Biochemistry (Mosc). 2009 Oct;74(10):1125-31. doi: 10.1134/s0006297909100083.


Lignin peroxidase from the liquid culture filtrate of Gloeophyllum sepiarium MTCC-1170 has been purified to homogeneity. The molecular weight of the purified enzyme was 42 kDa as determined by SDS-PAGE. The K(m) values were 54 and 76 microM for veratryl alcohol and H2O2, respectively. The pH and temperature optima were 2.5 and 25 degrees C, respectively. Depolymerization of coal by the fungal strain has been demonstrated using humic acid as a model of coal. Depolymerization of humic acid by the purified lignin peroxidase has been shown by the decrease in absorbance at 450 nm and increase in absorbance at 360 nm in presence of H2O2. Depolymerization of humic acid by the purified enzyme has also been demonstrated by the decrease in the viscosity with time of the reaction solution containing humic acid, H2O2, and the purified lignin peroxidase. The influence of NaCl and NaN3 and inhibitory effects of various metal chelating agents on the lignin peroxidase activity were studied.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agaricales / chemistry
  • Agaricales / enzymology*
  • Agaricales / isolation & purification
  • Benzyl Alcohols / pharmacology
  • Catalysis
  • Coal / statistics & numerical data*
  • Electrophoresis, Polyacrylamide Gel
  • Molecular Sequence Data
  • Peroxidases / chemistry
  • Peroxidases / isolation & purification*
  • Peroxidases / metabolism


  • Benzyl Alcohols
  • Coal
  • Peroxidases
  • lignin peroxidase
  • veratryl alcohol