Protein adsorption behavior and immunoglobulin separation with a mixed‐mode resin based on p ‐aminohippuric acid

p ‐Aminohippuric acid is a newly developed ligand for mixed‐mode chromatography with a commercial resin name of N uvia c P rime. In this study, bovine immunoglobulin G and bovine serum albumin were used as two model proteins, and the adsorption isotherms with N uvia c P rime were investigated under different pH and salt concentrations. The results showed that pH had a strong but different influence on the adsorption of these two proteins. The adsorption capacity for bovine immunoglobulin G and BSA was 170.4 and 28.1 mg/g at pH 6.0, respectively. Different salts also showed varying effects on the protein adsorption. Moreover, the adsorption and elution behaviors of the two proteins in a column were determined under varying pH and salt concentrations. An optimized process showed that feedstock loaded under pH 6.0 with 0.8 M (NH 4 ) 2 SO 4 and eluted under pH 8.0 with 1.0 M NaCl could effectively purify bovine immunoglobulin G from feedstock containing BSA . The purity of bovine immunoglobulin G could reach 99.8% and the recovery was 92.7%. The results demonstrated that the control of pH and salt addition during the loading and elution processes were two key factors in improving separation efficiency with N uvia c P rime resin.