Macromolecular Research

The Polymer Society of Korea (한국고분자학회)
권호 표지

Salt-Induced Protein Precipitation in Aqueous Solution: Single and Binary Protein Systems

  • Kim, Sang-Gon (Division of Chemical Engineering and molecular Thermodynamics Lab., Hanyang University) ;
  • Bae, Young-Chan (Division of Chemical Engineering and molecular Thermodynamics Lab., Hanyang University)
  • Published : 2003.02.01
Download PDF
⟨ Previous Next ⟩

Abstract

A molecular-thermodynamic model is developed for the salt-induced protein precipitation. The protein molecules interact through four intermolecular potentials. An equation of state is derived based on the statistical mechanical perturbation theory with the modified Chiew's equation for the fluid phase, Young's equation for the solid phase as the reference system and a perturbation based on the protein-protein effective two body potential. The equation of state provides an expression for the chemical potential of the protein. In a single protein system, the phase separation is represented by fluid-fluid equilibria. The precipitation behaviors are simulated with the partition coefficient at various salt concentrations and degree of pre-aggregation effect for the protein particles. In a binary protein system, we regard the system as a fluid-solid phase equilibrium. At equilibrium, we compute the reduced osmotic pressure-composition diagram in the diverse protein size difference and salt concentrations.

Keywords

References

  1. Biochem. Biophys. Acta v.317 P. R. Foster;P. Dunhill;M. D. Lilly
  2. Biopolymers v.23 R. N. Haire;W. A. Tisel;J. C. White;A. Rosenberg https://doi.org/10.1002/bip.360231206
  3. Biotech. Bioeng. v.40 Y. C. Shih;H. W. Blanch;J. M. Prausnitz https://doi.org/10.1002/bit.260401004
  4. Adv. Biochem. Eng. Technol. v.47 M. Q. Niederauer;C. E. Glatz https://doi.org/10.1007/BFb0046200
  5. Protein Precipitation Process Engineering F. Rothstein;R. G. Harrion(ed.)
  6. AIChE J. v.41 C. J. Coen;H. W. Blanch;J. M. Prausnitz https://doi.org/10.1002/aic.690410102
  7. Theory of Stability of Lyophobic Colloids E. Verwey;J. Overbeek
  8. J. Polym. Sci. v.33 S. Askura;F. Oosawa https://doi.org/10.1002/pol.1958.1203312618
  9. Pure & Appl. Chem. v.48 A. Vrij https://doi.org/10.1351/pac197648040471
  10. J. Polym. Sci., Polym. Phys. Ed. v.17 J. F. Joanny;L. Leibler;P. G. de Gennes https://doi.org/10.1002/pol.1979.180170615
  11. J. Colloid Interf. Sci. v.41 H. De Hek;A. Vrij
  12. J. Farad. Discuss. Chem. Soc. v.76 A. P. Gast;C. K. Hall;W. G. Russel https://doi.org/10.1039/dc9837600189
  13. J. Chem. Soc. Farad. Trans. v.79 no.2 M. J. Grimson https://doi.org/10.1039/f29837900817
  14. J. Phys. Lett. v.45 J. M. Victor;J. P. Hansen
  15. AIChE J. v.36 H. Mahadevan;C. K. Hall https://doi.org/10.1002/aic.690361007
  16. AIChE J. v.38 H. Mahadevan;C. K. Hall https://doi.org/10.1002/aic.690380411
  17. J. Phys. Chem. v.96 V. Vlachy;J. M. Prausnitz https://doi.org/10.1021/j100194a066
  18. AIChE J. v.39 V. Vlachy;H. W. Blanch;J. M. Prausnitz https://doi.org/10.1002/aic.690390204
  19. Molec. Phys. v.70 Y. C. Chiew https://doi.org/10.1080/00268979000100891
  20. Fluid Phase Equilibria v.116 D. Kuehner;H. W. Blanch;J. M. Prausnitz https://doi.org/10.1016/0378-3812(95)02882-X
  21. J. Chem. Phys. v.22 S. Asakura;F. Oosawa
  22. J. Colloid Interf. Sci. v.96 A. P. Gast;C. K. Hall;W. G. Russel https://doi.org/10.1016/0021-9797(83)90027-9
  23. Molecular Thermodynamics of Fluid Phase Equilibria J. M. Prausnitz;R. N. Lichtenthaler;E. G. D. Azevedo
  24. J. Chem. Phys. v.98 D. A. Young https://doi.org/10.1063/1.464360
  25. Ind. Eng. Chem. Res. v.33 Y. Song;S. M. Lambert;J. M. Prausnitz
  26. J. Chem. Phys. v.51 N. F. Carnahan;K. E. Starling https://doi.org/10.1063/1.1672048
  27. Biophysical J. v.73 D. Kuehner;C. Heyer;C. Ramsch;U. M. Fornefeld;H. W. Blanch;J. M. Prausnitz https://doi.org/10.1016/S0006-3495(97)78346-2
  28. Partition of Cell Particles and Macromolecules P. A. Albertsson
  29. Physica Ⅳ v.10 H. C. Hamaker
  30. Korean J. Chem. Eng. v.17 no.6 S. G. Kim;Y. C. Bae https://doi.org/10.1007/BF02699110
  31. Biophysical Chemistry v.98 R. A. Curtis;C. Steinbrecher;M. Heinemann;H. W. Blanch;J. M. Prausnitz https://doi.org/10.1016/S0301-4622(02)00071-6