Purification and characterization of oxalate decarboxylase from<i>Coriolus versicolor</i>

Abstract

Oxalate decarboxylase was detected both intra- and extracellularly in liquid cultures of Coriolus versicolor. Induction of the enzyme by addition of oxalic acid to the medium on day 6 of growth resulted in a 50-fold increase in specific activity in the mycelia and a 30-fold increase in the extracellular specific activity in the media. The protein was isolated and purified from mycelia, and characterised by polyacrylamide gel electrophoresis and Western blotting against a polyclonal antibody raised to oxalate decarboxylase from Collybia velutipes (Basidiomycete). A major protein band of Mr 59000 cross-reacted with the antibody. Immunogold-cytochemical labelling of ultra-thin sections of beechwood infected with C. versicolor showed that the enzyme was localised close to the plasma membrane and in intracellular vesicles.