Summary: was investigated for extracellular proteinases. The major extracellular proteinase activity detected under all conditions tested was L-leucine aminopeptidase activity. Slight extracellular L-proline aminopeptidase activity was also detected. No clear evidence for the presence of serine proteinases in culture broths was found using several different methods. The major extracellular proteinase of , i.e. the L-leucine aminopeptidase, was purified 33-fold to homogeneity. The purified enzyme was found by SDS-PAGE to have an of 34000. The purified enzyme had a final specific activity of 3·6 units mg, a for L-leucine--nitroanilide of 300 μM and a of 4·2 μmol min mg. The pure enzyme did not exhibit proteolytic activity on azocasein or L-proline--nitroanilide, substrates for other proteinase activities observed in crude extracts of .


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