[Physicochemical and enzymatic properties of Aspergillus oryzae aminopeptidase]

The paper deals with properties of Aspergillus oryzae (strain KC) purified aminopeptidase. The enzyme is homogeneous in electrophoresis in polyacrylamide gel and enzyme-electrophoresis with the synthetic substrate leucyl-beta-naphthylamide applied. The molecular mass is 60000-61000 Daltons. The amino acidic composition of the enzyme is characterized by a high content of dicarboxylic acids. The substrate specificity is studied. Leucyl-glycyl-glycin and leucinamide are most intensive in splitting. Peptides with a blocked amino group are not hydrolyzed.