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


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Article Info

DATE

1986-03

AUTHORS

Lj. Vitale, M. Renko, B. Lenarčič, V. Turk, M. Pokorny

ABSTRACT

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. More... »

PAGES

449-455

References to SciGraph publications

  • 1981-09. Streptomyces rimosus extracellular proteases in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • 1979-03. Streptomyces rimosus extracellular proteases in APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1007/bf02346059

    DOI

    http://dx.doi.org/10.1007/bf02346059

    DIMENSIONS

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