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Streptomyces rimosus extracellular proteases 3. Isolation and characterization of leucine aminopeptidase

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Summary

A leucine aminopeptidase was purified to homogeneity fromStreptomyces rimosus culture filtrates, which are waste broth of oxytetracycline bioproduction process. Purification procedure includes ultrafiltration and chromatography on CM-Sephadex, AH-Sepharose and FPLC Mono S column.

The enzyme is a monomer with molecular weight of 27,500 Daltons and pI of 7.3, stable in broad pH range and up to 70°C. It is a metallo enzyme dependent on Ca2+ ions for its full activity. By its specificity it is a true aminopeptidase active on amino acid amide, arylamide, peptide and ester bonds. The hydrolysing activity shows preference for leucine at the N-terminal position of substrates, also acts on aromatic acids and methionine, but does not release glycine, proline, acidic amino acids orD-amino acid residues.

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Authors and Affiliations

  1. Ruđer Boškovic Institute, 41001, Zagreb, Yugoslavia

    Lj. Vitale

  2. Jožef Stefan Institute, 61000, Ljubljana, Yugoslavia

    M. Renko, B. Lenarčič & V. Turk

  3. Research and Development Institute, Krka Pharmaceutical and Chemical Works, 68 000, Novo mesto, Yugoslavia

    M. Pokorny

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  1. Lj. Vitale
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  2. M. Renko
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  3. B. Lenarčič
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  4. V. Turk
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  5. M. Pokorny
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Vitale, L., Renko, M., Lenarčič, B. et al. Streptomyces rimosus extracellular proteases 3. Isolation and characterization of leucine aminopeptidase. Appl Microbiol Biotechnol 23, 449–455 (1986). https://doi.org/10.1007/BF02346059

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  • DOI: https://doi.org/10.1007/BF02346059

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