Proteomic Profile of Recombinant Escherichia coli Producing a Biopharmaceutical in a High Cell Density Fermentation

摘要

Using two-dimensional polyacrylamide gel electrophoresis (2D PAGE), we conducted a proteomic analysis over the course of a 10-L high cell density (HCD), industrial, E. coli fermentation. This process produces a recombinant, humanized antibody fragment that is secreted and assembled in the periplasm. Physiological changes associated with high cell density culture were distinguished from product-related changes associated with heterologous protein expression.