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Natural Occurence of Enzymes Linked to Inorganic Supports

Venice Lagoon and Internal City Canals
  • N. Sabil
  • Y. Aissouni
  • B. Pavoni
  • D. Tagliapietra
  • M.-A. Coletti-Previero

Abstract

Powerful enzyme activities were found in the sediments of the Venice lagoon and internal city canals. No detectable enzyme activity was present in the aqueous phase even after centrifugation. These insolubilized enzymes showed remarkable heat stability and an increased resistance to severe environmental conditions. They were probably of bacterial origin, mostly immobilized on the inorganic component of the sediment, so that they could survive the organisms from which they were generated, since their lifespan is prolonged by insolubilisation. As a consequence they resist to conditions where the same enzyme under soluble form would be rapidly inactivated. They are useful diagnostic factors of the ecosystem, since their presence is related to the waste products. A study on the linkage between enzymes and clays suggested that a spontaneous and specific affinity between them, previously unsuspected, allowed the formation of “activated” sediments, the leading force in the first step of organic matter degradation in ecosystems.

Keywords

Cellulase Activity Septic Tank Sediment Composition Phosphate Anion Venice Lagoon 
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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References

  1. 1.
    Maunoir, S., Sabil, N., Rambaud, A., and Coletti-Previero, M-A. (1991) Env. Technol. 12: 313–323.CrossRefGoogle Scholar
  2. 2.
    Haddane, M., Baudinat, C., Rambaud, A. and Coletti-Previero M-A. (1986) J. Fra. Hydr. 17: 253–262.Google Scholar
  3. 3.
    Sabil, N., Tagliapietra, D. and Coletti-Previero, M-A. (1993) Env. Technol. 14: 1089–1095.CrossRefGoogle Scholar
  4. 4.
    Sabil, N., Chergui, A., Tagliapietra, D. and Coletti-Previero, M-A. (1994) Wat. Res. 28: 1, 77–84.CrossRefGoogle Scholar
  5. 5.
    Sabil, N., Chergui, A., Tagliapietra, D. and Coletti-Previero, M-A. (1994) Wat. Res. 28: 1, 77–84.CrossRefGoogle Scholar
  6. 6.
    Sabil, N., Chergui, A., Tagliapietra, D. and Coletti-Previero, M-A. (1994) Wat. Res. 28: 1, 77–84.CrossRefGoogle Scholar
  7. 7.
    Sabil, N., Chergui, A., Tagliapietra, D. and Coletti-Previero, M-A. (1994) Wat. Res. 28: 1, 77–84.CrossRefGoogle Scholar
  8. 8.
    Froelich, P.N. (1980) Limnol. Oceanogr. 25: 564–572.CrossRefGoogle Scholar
  9. 9.
    Agemian, H. and Chau, A.S.Y. (1976) Analyst. 101: 91–95.PubMedCrossRefGoogle Scholar
  10. 10.
    Brunk, C.F., Jones, K.C. and James, T.W. (1979) Anal. Biochem. 92: 497–500.PubMedCrossRefGoogle Scholar
  11. 11.
    Coletti-Previero, M-A. and Previero, A. (1989) Anal. Biochem. 180: 1–10.PubMedCrossRefGoogle Scholar
  12. 12.
    Coletti-Previero, M-A., Pugnière, M., Favel, A.and Previero, A. (1988) In: Protein Structure-Function Relationhip, ( Zaidi, Z.H. ed. ), pp. 39–58.Google Scholar
  13. 13.
    Pavoni, B., Donazzolo, R., Marcomini, A., Degobbis, D. and Orio, A.A. (1987) Mar. Poll. Bull. 18: 18–24.CrossRefGoogle Scholar
  14. 14.
    Donazzolo, R., Orio, A.A., Pavoni, B. and Perin, G. (1984) Oceanol. Acta. 7: 25–32.Google Scholar
  15. 15.
    Shaw, E. and Green, G.D.J. (1981) In: Methods in Enzymology, 80: pp. 820–826, Acad. Press, New York.Google Scholar

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • N. Sabil
    • 1
  • Y. Aissouni
    • 1
  • B. Pavoni
    • 2
  • D. Tagliapietra
    • 2
  • M.-A. Coletti-Previero
    • 1
  1. 1.Centre de RechercheINSERMMontpellierFrance
  2. 2.Dipartimento di ScienzeAmbientali dell’ UniversitàVeneziaItaly

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