An Aminopeptidase of Aspergilius sojae

Abstract

An aminopeptidase was purified from Aspergillus sojae X-816. The molecular weight of the enzyme was estimated to be 220, 000. The isoelectric point was at pH 5.3. The optimum pH for L-leucylglycylglyeine was 7.5. The enzyme was stable up to 37°C against temperature treatment for 15min. Some chelating agents inhibited the enzyme activity. The Km value for L-leucylglycylglycine at pH 7.5 and 37°C was 45mM. The Km value for L-leucyl-β-naphthylamide at pH 7.0 and 37°C was 2.2mM.