Purification and properties of oxalate oxidase from barley seedlings.

Abstract

Oxalate oxidase from barley seedlings (Hordeum vulgare L. var. distichon ALEFELD) was purified to homogeneity as determined by disc gel electrophoresis. The enzyme hydrolyzed oxalate, but no other related acids. The optimum pH was around pH 3.5, and this enzyme was stable at acidic pHs. The enzyme appears to consist of two identical subunits. Various other properties were investigated.