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Volume 139, Issue 3

Purification and Properties of an Extracellular Aminopeptidase from 1326 Free

Abstract

was investigated for extracellular proteinases. The major extracellular proteinase activity detected under all conditions tested was -leucine aminopeptidase activity. Slight extracellular -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 -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 -leucine--nitroanilide of 300 μ and a of 4·2 μmol min mg. The pure enzyme did not exhibit proteolytic activity on azocasein or -proline--nitroanilide, substrates for other proteinase activities observed in crude extracts of .

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© Society for General Microbiology 1993
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1993-03-01
2022-07-02
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Purification and Properties of an Extracellular Aminopeptidase from Streptomyces Lividans 1326
Microbiology 139, 417 (1993); https://doi.org/10.1099/00221287-139-3-417
/content/journal/micro/10.1099/00221287-139-3-417
/content/journal/micro/10.1099/00221287-139-3-417
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