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Activity of an enzyme immobilized on polyelectrolyte multilayers

  • Biopolymers
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Abstract

The immobilization of α-chymotrypsin on the surface of boron silicate glass microspheres is conducted via the technique of multilayer adsorption of polyelectrolytes. It is shown that the enzyme is adsorbed on both positively and negatively charged surfaces and its activity is partially preserved relative to that in solution. The activity of the enzyme depends on the number of polyectrolyte layers preliminarily adsorbed on glass microspheres and on the charge of the surface. The activity of α-chymotrypsin adsorbed on the negatively charged surface is four times higher than the activity of this enzyme adsorbed on a positively charged surface.

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Authors and Affiliations

  1. Faculty of Chemistry, Moscow State University, Moscow, 119991, Russia

    A. S. Malinin, A. A. Rakhnyanskaya, A. V. Bacheva & A. A. Yaroslavov

Authors
  1. A. S. Malinin
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  2. A. A. Rakhnyanskaya
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  3. A. V. Bacheva
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  4. A. A. Yaroslavov
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Corresponding author

Correspondence to A. S. Malinin.

Additional information

Original Russian Text © A.S. Malinin, A.A. Rakhnyanskaya, A.V. Bacheva, A.A. Yaroslavov, 2011, published in Vysokomolekulyarnye Soedineniya, Ser. A, 2011, Vol. 53, No. 1, pp. 54–59.

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Malinin, A.S., Rakhnyanskaya, A.A., Bacheva, A.V. et al. Activity of an enzyme immobilized on polyelectrolyte multilayers. Polym. Sci. Ser. A 53, 52–56 (2011). https://doi.org/10.1134/S0965545X10121041

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  • DOI: https://doi.org/10.1134/S0965545X10121041

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