Production and Characterization of Ovalbumin and Ovotransferrin from Chicken Egg White

Abstract

An efficient and easily scaled up method to separate ovalbumin and ovotransferrin simultaneously from chicken egg white using ultrafiltration is proposed. The purities of ovalbumin and ovotransferrin obtained were 94% and 89%, with the yields of 82% and 76%, respectively. The resulting ovalbumin and ovotransferrin products was then characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, isoelectric focusing, dynamic light scattering, circular dichroism, and amino acid analysis to confirm their molecular weights, isoelectric points, aggregate sizes, molecular secondary structures, and amino acid compositions. The iron-binding capacity of the purified ovotransferrin was also evaluated.