Journal of Chemical Technology and Biotechnology, Vol.87, No.11, 1600-1606, 2012
Oxalate decarboxylase of Trametes versicolor: biochemical characterization and performance in bleaching filtrates from the pulp and paper industry
BACKGROUND: Oxalate decarboxylase (ODC) from acid-induced cultures of the white-rot fungus Trametes versicolor was purified and characterized with respect to its biochemical properties and the possibility to utilize the enzyme for treatment of process water with the intention to prevent problems with calcium-oxalate scaling in the pulp and paper industry. RESULTS: Purified T. versicolor ODC was identified by tandem mass spectrometry. As estimated by using SDS-PAGE, the molecular mass was 69 kDa, and 60 kDa after deglycosylation with N-glycosidase F. The pH optimum was 2.5 and the temperature optimum was 4045 degrees C. The effects of ten potential inhibitors in industrial filtrates were examined. The enzyme was sensitive to low concentrations (0.1 mmol L-1) of chlorite and sulfite. T. versicolor ODC exhibited activity in 16 filtrates collected from mechanical pulping and kraft pulping. It had higher activity than ODC from Aspergillus niger in all of the filtrates and higher activity than oxalate oxidase from barley in all filtrates except two. CONCLUSIONS: The investigation shows basic biochemical properties of T. versicolor ODC and indicates that the enzyme may be useful for treatment of industrial filtrates under acidic conditions. Copyright (c) 2012 Society of Chemical Industry