Advertisement

Applied Biochemistry and Biotechnology

, Volume 76, Issue 3, pp 229–236 | Cite as

Partial purification and properties of putrescine oxidase from Candida guilliermondii

  • Muthukumaran GunasekaranEmail author
  • Uma Gunasekaran
Article

Abstract

Putrescine oxidase ([PO]; E.C. 1.4.3.4), which catalyzes the oxidative deamination of putrescine into γ-aminobutyraldehyde, has been partially purified from Candida guilliermondii. Among the substrates tested, putrescine has the highest reaction rate, followed by spermidine and cadaverine. The K IN values for putrescine, spermidine, and cadaverine were 20, 200, and 1.1 mM, respectively. The optimum pH and the temperature for PO were 8.0 and 37°C, respectively. Growth of Candida species on putrescine as the solenitrogen source induced the synthesis of PO that converts putrescine into Δ1-pyrroline and γ-aminobutyric acid. These two products were detected and identified from the culture medium. The enzyme was not activated by divalent cations. Among the species of Candida tested, the highest enzyme activity was found in cell-free extracts of C. guilliermondii. The pathway of putrescine degradation was identified by substrate analysis to be along the nonacetylated pathway in C. guilliermondii.

Index Entries

Candida sp. enzyme purification spermidine polyamines 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Tabor, C. W. and Tabor, H. (1976), Annu. Rev. Biochem. 45, 285–306.CrossRefGoogle Scholar
  2. 2.
    Haywood, G. W. and Large, P. J. (1984), J. Gen. Microbiol. 130, 1123–1136.Google Scholar
  3. 3.
    Haywood, G. W. and Large, P. J. (1985), Eur. J. Biochem. 148, 277–283.CrossRefGoogle Scholar
  4. 4.
    Tabor, C. W. and Tabor, H. (1985), Microbiol. Rev. 49, 81–99.Google Scholar
  5. 5.
    Large, P. J. (1992), FEMS Microbiol. Rev. 88, 249–262.CrossRefGoogle Scholar
  6. 6.
    Bradford, M. M. (1976), Anal. Biochem. 72, 248–254.CrossRefGoogle Scholar
  7. 7.
    Shimizu, E., Tabata, Y., Hayakawa, R., and Yorifuji, T. (1988), Agric. Biol. Chem. 52, 2865–2871.Google Scholar
  8. 8.
    Yamada, H. (1971), Methods Enzymol. 17B, 726–730.CrossRefGoogle Scholar
  9. 9.
    De Sa, R. J. (1972), J. Biol. Chem. 247, 5527–5534.Google Scholar
  10. 10.
    Tabor, C. W. and Tabor, H. (1984), Annu. Rev. Biochem. 53, 749–790.CrossRefGoogle Scholar
  11. 11.
    Haywood, G. W. and Large, P. J. (1986), J. Gen. Microbiol. 132, 7–14.Google Scholar
  12. 12.
    Yamada, H., Isobe, K., and Tani, Y. (1980), Agric. Biol. Chem. 44, 2469–2476.Google Scholar
  13. 13.
    Ishizuka, H., Horinouchi, S., and Beppu, T. (1993), J. Gen. Microbiol. 139, 425–432.Google Scholar

Copyright information

© Humana Press Inc 1999

Authors and Affiliations

  1. 1.Department of BiologyFisk UniversityNashville

Personalised recommendations