LAUSR

Abstract The importance of immunoglobulin Y (IgY) as a specific antibody equivalent to mammalian immunoglobulin G (IgG) is well recognized. However, production of highly purified IgY is still difficult due to the lack of specific purification methods. In this study, adsorption behaviors of IgY on four mixed-mode resins with functional ligands of 4-mercatoethyl-pyridine (MEP), 2-mercapto-1-methyli-midazole (MMI), 5-aminobenzi-midazole (ABI) and tryptophan-5-aminobenzi-midazole (W-ABI) were evaluated. The results showed that high adsorption ratio were found at pH 6.0–7.0 with little adsorption under acidic conditions. The resin with ABI ligand was then used to separate IgY from immunized chicken serum. An efficient process with IgY purity of 95% and recovery of 90% was developed after optimization of loading and elution pH and injection volume. The biological activity of the purified IgY was fully maintained. These results indicated that mixed-mode chromatography with specially-designed ligands has great potential for the separation of IgY from crude feedstock.