Purification of Recombinant Monoclonal Antibodies from Transgenic Chicken Eggs and Removal of Egg-White Proteins.

Abstract

The high cost and limited scalability of monoclonal antibody (mAb) production necessitate the development of alternative systems. Transgenic chickens offer a promising platform for recombinant mAb production; however, efficient purification methods remain underexplored. This study investigated the initial purification of recombinant mAbs from transgenic chicken egg whites. We utilized Protein A chromatography, followed by ammonium sulfate precipitation and cation-exchange chromatography, to improve the purification efficiency. Although Protein A chromatography was able to purify mAbs, there was substantial egg-white contamination. Ammonium sulfate precipitation and cation-exchange chromatography successfully removed 84.6 and 93.8% of egg-white proteins, respectively, enhancing mAb purification efficiency. Overall, this study proposes an efficient method for initial mAb purification from transgenic chicken egg whites, providing a basis to develop a scalable, cost-effective biopharmaceutical production approach.