Influence of Surface Hydrophobic Groups on the Adsorption of Proteins onto Nonporous Polymeric Particles with Immobilized Metal Ions.

Iminodiacetic acid (IDA) and octyl moieties were covalently bound on nonporous particles, which were prepared from dispersion polymerization of methyl methacrylate and glycidyl methacrylate. After being charged with copper ions, the IDA-bound particles could specifically adsorb deoxyribonuclease I (DNase I) through the affinity interaction between protein and immobilized metal ion. A mixed-ligand (metal-chelate and octyl-bound) support was obtained after hydrophobic (octyl) groups were also introduced to the particle surface. The affinity adsorption of DNase I on the copper-IDA chelate was influenced by interaction between the protein and the bound octyl group. Both the affinity and the hydrophobic interactions could be well described by the Langmuir isotherms. The equilibrium adsorption constants were estimated separately to be 0.96 and 0.50 liter g(-1) for affinity and hydrophobic bindings, respectively. For binding on mixed-ligand support, the adsorption constant was 0.45 liter g(-1). It was evident that both affinity and hydrophobic interactions are involved in the adsorption of proteins onto mixed-ligand particles. Desorption of the inactive proteins from the support was possible by increasing the hydrophobicity of the solution. Copyright 2001 Academic Press.