Advertisement

Experientia

, Volume 43, Issue 10, pp 1110–1111 | Cite as

A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese Natto; a typical and popular soybean food in the Japanese diet

  • H. Sumi
  • H. Hamada
  • H. Tsushima
  • H. Mihara
  • H. Muraki
Short Communications

Summary

A strong fibrinolytic activity was demonstrated in the vegetable cheese Natto, which is a typical soybean food eaten in Japan. The average activity was calculated at about 40 CU (plasmin units)/g wet weight. This novel fibrinolytic enzyme, named nattokinase, was easily extracted with saline. The mol. wt and pI were about 20,000 and 8.6, respectively. Nattokinase not only digested fibrin but also the plasmin substrate H-D-Val-Leu-Lys-pNA (S-2251), which was more sensitive to the enzyme than other substrates tried. Diisopropyl fluorophosphate and 2,2,2-trichloro-1-hydroxyethyl-o,o-dimethylphosphate strongly inhibited this fibrinolytic enzyme.

Key words

Natto soybean food fibrinolytic enzyme serine protease 

References

  1. 1.
    Yabe, K., Bull. Coll. Agr. Tokyo Univ.2 (1894) 2.Google Scholar
  2. 2.
    National Federation of Cooperatives on Natto, in: A Historical Record of Natto, p. 19. Ed. Food Pionia, Natto Research Center, Tokyo 1977.Google Scholar
  3. 3.
    Hayashi, W., Natto Kagakukenkyu Kaishi (in Japanese)1 (1977) 85.Google Scholar
  4. 4.
    Kameda, S., Chem. pharm. Bull.16 (1968) 189.Google Scholar
  5. 5.
    Miyake, S., and Shimizu, J., Bull. Hyogo Agr. Coll. (in Japanese)1 (1953) 11.Google Scholar
  6. 6.
    Miyake, S., Watanabe, K., Yoshikawa, M., and Nonoguchi, Y., Seikagaku (in Japanese)28 (1956) 527.Google Scholar
  7. 7.
    Claeson, G., Friberger, P., Knos, M., and Eriksson, E., Haemostasis7 (1978) 76.PubMedGoogle Scholar
  8. 8.
    Milstone, H., J. Immun.42 (1941) 109.Google Scholar
  9. 9.
    Astrup, T., and Müllertz, S., Archs Biochem. Biophys.40 (1952) 346.Google Scholar
  10. 10.
    Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J., J. biol. Chem.193 (1951) 265.PubMedGoogle Scholar
  11. 11.
    Vesterberg, O., and Svensson, H., Acta chem. scand.20 (1966) 820.PubMedGoogle Scholar
  12. 12.
    Okamoto, S., Sato, S., Takada, Y., and Okamoto, U., Keio J. Med.13 (1964) 177.PubMedGoogle Scholar
  13. 13.
    Okamoto, S., and Hijikata, A., Drug Design6 (1975) 143.Google Scholar
  14. 14.
    Sumi, H., Sasaki, K., Toki, N., and Robbins, K. C., Thromb. Res.20 (1980) 711.PubMedGoogle Scholar
  15. 15.
    Toki, N., Sumi, H., Sasaki, K., Boreisha, I., and Robbins, K. C., J. clin. Invest.75 (1985) 1212.PubMedGoogle Scholar
  16. 16.
    Mihara, H., Sumi, H., Akazawa, K., Yoneta, T., and Mizumoto, H., Thromb. Haemost.50 (1983) 258.Google Scholar

Copyright information

© Birkhäuser Verlag 1987

Authors and Affiliations

  • H. Sumi
    • 1
  • H. Hamada
    • 2
  • H. Tsushima
    • 1
  • H. Mihara
    • 1
  • H. Muraki
    • 3
  1. 1.Department of PhysiologyMiyazaki Medical CollegeMiyazaki(Japan)
  2. 2.Department of Fundamental Natural ScienceOkayama University of ScienceOkayama(Japan)
  3. 3.Department of Fermentation Technology, Faculty of EngineeringYamanashi UniversityKofu(Japan)

Personalised recommendations