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Applied Microbiology and Biotechnology

, Volume 70, Issue 5, pp 541–547 | Cite as

Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica

  • Jiro Arima
  • Yoshiko Uesugi
  • Masaki Iwabuchi
  • Tadashi HatanakaEmail author
Biotechnologically Relevant Enzymes and Proteins

Abstract

We developed a spectrophotometric assay for peptide hydrolysis by aminopeptidases (APs). The assay enables the measurement of free amino acids liberated by AP-catalyzed peptide hydrolysis using 4-aminoantipyrine, phenol, peroxidase, and l-amino acid oxidase. We investigated the specificity of bacterial APs [enzymes from Streptomyces griseus (SGAP), Streptomyces septatus (SSAP), and Aeromonas proteolytica (AAP)] toward peptide substrates using this assay method. Although these enzymes most efficiently cleave leucyl derivatives among 20 aminoacyl derivatives, in peptide hydrolysis, the catalytic efficiencies of Phe-Phe hydrolysis by SGAP and SSAP exceed that of Leu-Phe hydrolysis. Furthermore, all enzymes showed the maximum catalytic efficiencies for Phe-Phe-Phe hydrolysis. These results indicate that the hydrolytic activities of bacterial APs are affected by the nature of the penultimate residue or flanking moiety and the length of the peptide substrate.

Keywords

Streptomyces Peptide Substrate Streptomyces Griseus Peptide Hydrolysis Bulky Side Chain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag 2005

Authors and Affiliations

  • Jiro Arima
    • 1
  • Yoshiko Uesugi
    • 1
  • Masaki Iwabuchi
    • 1
  • Tadashi Hatanaka
    • 1
    Email author
  1. 1.Research Institute for Biological Sciences (RIBS)OkayamaJapan

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