Oxalate oxidase activity was detected in the cell wall fraction isolated from maize roots (Zea mays L.). The enzyme was active at acidic pH with optimal activity at pH 3.2. It was thermally extremely stable and resistant to high salt concentration, SDS and pepsin. The enzyme activity was inhibited by sulphydryl reagents 2-mercaptoethanol (2-ME), N-ethyl maleimide (NEM) and dithiotreitol (DTT), but was insensitive to EDTA, KCN and metal ions. Measurements of enzyme activity were performed using colorimetric assay of H(2)O(2), as well as polarographic detection of O(2) consumption. Maximal activity was obtained with 5 mM oxalic acid for the colorimetric method, and 10 mM oxalic acid for the polarographic method. Both methods were applicable in oxalate oxidase characterization, the polarographic method being more suitable under conditions of H(2)O(2) interaction with some of the analyzed substances.