PURIFICATION AND CHARACTERIZATION OF OXALATE DECARBOXYLASE FROM CORIOLUS-VERSICOLOR

Oxalate decarboxylase was detected both intra- and extracellularly in liquid cultures of Coriolus versicolor. Induction of the enzyme by add ition 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 incre ase in the extracellular specific activity in the media. The protein w as isolated and purified from mycelia, and characterised by polyacryla mide gel electrophoresis and Western blotting against a polyclonal ant ibody raised to oxalate decarboxylase from Collybia velutipes (Basidio mycete). A major protein band of M(r) 59000 cross-reacted with the ant ibody. Immunogold-cytochemical labelling of ultra-thin sections of bee chwood infected with C. versicolor showed that the enzyme was localise d close to the plasma membrane and in intracellular vesicles.