Springer Nature is making SARS-CoV-2 and COVID-19 research free. View research | View latest news | Sign up for updates

Immobilization of proteolytic enzymes in carboxymethylchitin films and sponges (review)

  • 36 Accesses

  • 4 Citations

Abstract

The possibility of immobilization of the proteolytic enzymes collagenase and terrilytin in chitin carboxymethyl ester films and sponges was demonstrated and some characteristics of this process were investigated. It was found that the optimum pH for immobilization of collagenase and terrilytin lies in the range of 6.5–7.5, which approximately corresponds to the optimum pH of the effect of native enzymes. According to the data from in vitro experiments, the activity of the immobilized enzymes at the optimum pH of immobilization is 75–50% for collagenase and 80–90% for terrilytin. An increase in the molecular weight of carboxymethylchitin in the range of 60–600 kilodaltons significantly strengthens the films and simultaneously decreases the activity of the immobilized enzymes, probably due to the stronger binding of the molecules of the enzyme in the matrix of higher molecular weight. In immobilization of enzymes in sponges, the molecular weight of the polymer matrix has no effect on the activity of the immobilized enzymes. Changing the degree of substitution of carboxymethylchitin in the 0.7–1.3 range has almost no effect on the activity of the enzymes immobilized in the films and sponges.

This is a preview of subscription content, log in to check access.

References

  1. 1.

    Z. A. Rogovin and L. S. Gal'braikh, Chemical Transformations and Modification of Cellulose [in Russian], Khimiya, Moscow (1979); Z. A. Rogovin and L. S. Galbraich, Die chemische Behandlung und Modifizierung der Zellulose, Georg Thieme Verlag, Stuttgart - New York (1983).

  2. 2.

    A. D. Virnik, N. R. Kil'deeva, et al., Fabrication of Fibre Materials Containing Immobilized Enzymes [in Russian], Chemical Fibre Industry Data Sheets, NIITEKhim, Moscow (1985).

  3. 3.

    W. L. Stanley, G. G. Watters, et al., Biotechnol. Bioeng., 18, 430 (1976).

  4. 4.

    W. L. Stanley, G. G. Watters, et al., Biotechnol. Bioeng., 17, 315 (1975).

  5. 5.

    S. I. Nishimura, N. Nishi, and S. Tokura, Carbohydr. Res., 146, 251 (1986).

  6. 6.

    RF Patent No. 1,666,459.

  7. 7.

    G. A. Vikhoreva, D. Yu. Gladyshev, et al., Cell. Chem. Technol., 26, No. 6, 663 (1992).

  8. 8.

    I. Yu. Sakharov, F. E. Litvin, et al., Biokhimiya, 53, No. 11, 1844 (1988).

  9. 9.

    E. D. Kaverzneva, Prikl. Biokhim. Mikrobiol., 7, No. 2, 225 (1971).

  10. 10.

    W. Brawn and D. Henly, Makromol. Chem., 79, 68 (1964).

Download references

Additional information

Translated from Khimicheskie Volokna, No. 5, pp. 34–37, September–October, 1995.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Vikhoreva, G.A., Khomyakov, K.P., Sakharov, I.Y. et al. Immobilization of proteolytic enzymes in carboxymethylchitin films and sponges (review). Fibre Chem 27, 337–342 (1996). https://doi.org/10.1007/BF00551148

Download citation

Keywords

  • Enzyme
  • Polymer
  • Ester
  • Molecular Weight
  • Immobilization