Adsorption Property and Chromatographic Affinity of Dye-Like Poly (Styrene Sodium Sulfonate) Sorbent toward Human Serum Albumin

Abstract

Adsorption of proteins on various polymer surfaces plays an important role in different fields particularly in immobilization of enzymes and chromatographic processes for purification of biologically active compounds. On the basis of interactions of albumin with a multitude of endogenous and exogenous substances such as dyes, insoluble cross-linked polystyrene gel beads functionalized by sulfonate groups, the major chemical group of dyes was synthesized and its adsorption property and chromatographic affinity toward human serum albumin (HSA) was investigated in batch and by column respectively. The adsorption rate at interface was significantly high and the affinity constant evaluated by Langmuir model was in the order of 7.78 Â 10 5 M À1 . The affinity of HSA onto this adsorbent achieved in two pH ranges demonstrates that almost full albumin was adsorbed. The elution accomplished by using a continuous pH gradient allows substantially recovery in the range of 70-80% of the initial content.