Biotechnology and Bioprocess Engineering

, Volume 18, Issue 3, pp 538–545

Chymotrypsin — Eudragit® complex formation

Authors

  • Valeria Boeris
    • Laboratorio de Fisicoquímica Aplicada a Bioseparación, Departamento de Química-Física, Facultad de Ciencias Bioquímicas y FarmacéuticasUniversidad Nacional de Rosario
  • Laura Verónica Cappella
    • Laboratorio de Fisicoquímica Aplicada a Bioseparación, Departamento de Química-Física, Facultad de Ciencias Bioquímicas y FarmacéuticasUniversidad Nacional de Rosario
  • Gisele Peres
    • Instituto de QuímicaUniversidade Federal do Rio Grande do Sul
  • Inés Burgos
    • Departamento de Química Biológica, Centro de Investigaciones en Química Biológica Facultad de Ciencias QuímicasUniversidad Nacional de Coìrdoba
  • Nádya Pesce da Silveira
    • Instituto de QuímicaUniversidade Federal do Rio Grande do Sul
  • Gerardo Fidelio
    • Departamento de Química Biológica, Centro de Investigaciones en Química Biológica Facultad de Ciencias QuímicasUniversidad Nacional de Coìrdoba
    • Laboratorio de Fisicoquímica Aplicada a Bioseparación, Departamento de Química-Física, Facultad de Ciencias Bioquímicas y FarmacéuticasUniversidad Nacional de Rosario
Research Paper

DOI: 10.1007/s12257-012-0553-9

Cite this article as:
Boeris, V., Cappella, L.V., Peres, G. et al. Biotechnol Bioproc E (2013) 18: 538. doi:10.1007/s12257-012-0553-9

Abstract

Eudragit® L100 (EuL) and Eudragit® S100 (EuS) are synthetic polyanions differing on their electric charge density. They interact with chymotrypsin (ChTRP), a basic protein forming soluble and non-soluble complexes. The complex formation was studied by dynamic light scattering, isothermal titration calorimetry, native fluorescence emission, circular dichroism and thermodynamical thermal stability of the enzyme. EuS was able to bind 33 ChTRP molecules while EuL, 60. The binding of ChTRP to both Eu was slightly endothermic and the entropic factor was responsible for the soluble complexes formation. The ChTRP-Eu size increases with pH and the binding of ChTRP to Eu modifies the Eu hydrodynamic radium. The interaction of ChTRP with Eu did not modify its secondary or tertiary structure. The thermal stability of ChTRP was increased when it interacted with both Eu.

Keywords

eudragit chymotrypsin polyelectrolytes calorimetry

Copyright information

© The Korean Society for Biotechnology and Bioengineering and Springer-Verlag Berlin Heidelberg 2013