Purification and properties of two forms of glucoamylase from Penicillium oxalicum.

Penicillium oxalicum produced two forms (isoenzymes) of glucoamylase which could be separated from each other by gel electrofocusing, and they were designated as glucoamylase I and glucoamylase II. Glucoamylases I and II were homogeneous on polyacrylamide gel electrophoresis, gel electrofocusing and ultracentrifugation, respectively. The sedimentation constant (s020, w) and molecular weight of glucoamylase I were 4.42 S and 84, 000, and those of glucoamylase II were 4.53 S and 86, 000, respectively. Certain properties of these enzymes were also investigated.