Applied Biochemistry and Biotechnology

, Volume 31, Issue 1, pp 53–58 | Cite as

Immobilization of protein on ferromagnetic Dacron

  • A. M. A. Carneiro LeÃo
  • E. A. Oliveira
  • L. B. Carvalho


Ferromagnetic Dacron (polyethyleneterephthalate) is proposed as a matrix to immobilize proteins covalently. Dacron in powder was magnetized by reacting ferrous (Fe+2) and ferric (Fe+3) ions with its hydrazide form at pH 8.3. Ferromagnetic hydrazide Dacron was converted to ferromagnetic azide Dacron and amyloglucosidase (E.C. was covalently bound through the latter group. The catalytic property of the enzyme was preserved (8% of the specific activity estimated for the soluble enzyme) and all the magnetic amyloglucosidase Dacron derivative was recovered by using a magnetic field. No activity was detected in the supernatant.


Apply Biochemistry Hydrazide Hydrazine Hydrate Soluble Starch Polyethyleneterephthalate 
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.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Weetall, H. H. (1970),J. Biomed. Mater. Res. 4, 597–599.CrossRefGoogle Scholar
  2. 2.
    Goldstein, L., Freeman, A., Blassberger, D., Granot, R., and Sokolovsky. (1977),Biotechnological Applications of Proteins and Enzymes, Bohak, Z. and Sharon, N., eds., New York, pp. 156-159.Google Scholar
  3. 3.
    Melo, E. H. M. (1984), MS thesis, submitted to the Department of Biochemistry of Universidade Federal de Pernambnco, Brazil.Google Scholar
  4. 4.
    Carvalho, L. B., Jr., Melo, E. H. M., Vasconcelos, A. R. A., and Lira, R. R. (1986),Arquivos de Biologia e Tecnologia 29, 525–531.Google Scholar
  5. 5.
    Carvalho, L. B., Jr., Silva, M. P. C., and Melo, E. H. M. (1987),Brazilian J. Med. Biol. Res. 20, 521–526.Google Scholar
  6. 6.
    Oliveira, E. A., Silva, M. P. C., Figueiredo, Z. M. B., and Carvalho, L. B., Jr. (1989),Appl. Biochem. Biotechnol.22, 109–114.CrossRefGoogle Scholar
  7. 7.
    Tamaura, Y., Takahashi, K., Kodera, Y., Saito, Y., and Inada, Y. (1986),Biotechnol. Lett. 8, 877–880.CrossRefGoogle Scholar
  8. 8.
    Takahashi, K., Tamaura, Y., Kodera, Y., Mihama, T., Saito, Y., and Inada, Y. (1987),Biochem. Biophys. Res. Commun.142, 291–296.CrossRefGoogle Scholar
  9. 9.
    Yoshimoto, T., Takeshi, M., Takahashi, K., Saito, Y., Tamaura, Y., and Inada, Y. (1987),Biochem. Biophys. Res. Commun.145, 908–914.CrossRefGoogle Scholar
  10. 10.
    Inada, Y., Ohwada, K., Yoshimoto, T., Kojima, S., Takahashi, K., Kodera, Y., Matsushima, A., and Saito, Y. (1987),Biochem. Biopliys. Res. Commun.148, 392–396.CrossRefGoogle Scholar
  11. 11.
    Inada, Y., Takahashi, K., Yoshimoto, T., Kodera, Y., Matsushima, A., and Saito, Y. (1988),TIBTECH 6, 131–134.Google Scholar
  12. 12.
    Bernfeld, P. (1955),Methods in Enzymology, Colowich, S. P. and Kaplan, N. O., eds., Academic, New York, pp. 149-150.Google Scholar
  13. 13.
    Eggstein, H. and Kreutz, F. H. (1955),Klin. Wochschr.33, 879–884.CrossRefGoogle Scholar

Copyright information

© Humana Press Inc. 1991

Authors and Affiliations

  • A. M. A. Carneiro LeÃo
    • 1
  • E. A. Oliveira
    • 1
  • L. B. Carvalho
    • 1
  1. 1.Laboratório de Enzimologia do Departamento de Bioquímica & Laboratório de ImunopatologiaKeizo Asami da Universidade Federal de PernambucoRecifeBrazil

Personalised recommendations