Isolation and characterization of aminopeptidase from Capnocytophaga granulosa ATCC 51502

K. Ohishi, T. Yamamoto, T. Tomofuji, N. Tamaki, Tatsuo Watanabe

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


There is evidence that enzymes from the genus Capnocytophaga play a role in dental calculus formation. Although most of the species in the genus produce aminopeptidases, there is a paucity of data on the purification and characterization of the enzyme, except in the case of Capnocytophaga gingivalis. The aim of this study was to purify aminopeptidase from culture supernatant of Capnocytophaga granulosa ATCC 51502, a new species of the genus. Purification was performed using ammonium sulfate fractionation and two chromatographic steps. The aminopeptidase was purified 158,433-fold with a yield of 12.0%. The enzyme appeared to be a trimer with a molecular mass of 270 kDa. The optimal pH of the aminopeptidase was 6.5 and its activity was completely inhibited by incubation at 50°C for 10 min. The enzyme showed maximum specificity for basic amino acids (Arg and Lys) and also hydrolyzed noncharged amino acids (Met, Leu and Ala). Ca2+, Zn2+ and Fe3+ activated the enzyme, while EDTA, Ag+, Hg+ and Cu2+ inhibited it. These results suggest that aminopeptidase of C. granulosa is different from that of C. gingivalis but similar to aminopeptidase B.

Original languageEnglish
Pages (from-to)67-72
Number of pages6
JournalOral microbiology and immunology
Issue number2
Publication statusPublished - Apr 2005


  • Aminopeptidase
  • Arginine
  • Capnocytophaga granulosa
  • Dental calculus

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Dentistry(all)
  • Microbiology (medical)


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