Advertisement

Bioprocess Engineering

, Volume 17, Issue 5, pp 301–305 | Cite as

Adsorption-desorption of BSA to highly substituted dye-ligand adsorbent: quantitative study of the effect of ionic strength

  • L.-Z. He
  • Y.-R. Gan
  • Y. Sun
Article

Abstract

Cibacron Blue 3GA was immobilized on Sepharose CL-6B to obtain a highly substituted dye-ligand adsorbent which dye concentration was 17.4 μmol dye per gram wet gel. This adsorbent had a highly binding capacity for bovine serum albumin (BSA). The effects of ionic strength on the adsorption and desorption of BSA to the adsorbent were studied. Adsorption isotherms were expressed by the Langmuir model. The quantitative relationships between the model parameters and the ionic strength were obtained. The desorptions were performed by adding salt to the BSA solutions in which adsorption equilibria had been reached. Adding salt to the solution resulted in the desorption of the bound protein. It was found that the isotherm obtained from the desorption experiments agreed well to the isotherm obtained from the adsorption experiments at the same ionic strength. The result demonstrated that the adsorption of BSA to the highly substituted adsorbent was reversible.

Keywords

Albumin Bovine Serum Bovine Serum Albumin Serum Albumin Ionic Strength 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Copyright information

© Springer-Verlag Berlin Heidelberg 1997

Authors and Affiliations

  • L.-Z. He
    • 1
  • Y.-R. Gan
    • 1
  • Y. Sun
    • 1
  1. 1.Department of Chemical Engineering and Research Center for Biotechnology, Tianjin University, Tianjin 300072, P. R. ChinaCN

Personalised recommendations