Effects of Dissolved Oxygen on the Production and Glycosylation of Albumin-Erythropoietin in CHO cells

초록

Human albumin erythropoietin (Alb-EPO), a fusion protein, with higher stability, was produced from recombinant Chinese hamster ovary (rCHO) cells. Batch cultures of the cells were performed in controlled bioreactors in which the set-points for dissolved oxygen (DO) varied at 20%, 40%, and 60%, respectively. However, there were no significant differences in growth rate and specific recombinant protein production at both 20% and 60% DO levels compared to control cultures run under a normoxic condition (40%). DO levels were monitored continuously throughout the cell culture process and have shown to affect protein glycosylation. Typically 10~100% DO level supported consistent glycosylation. Effects of process changes on the specific production or the quality of a recombinant protein are difficult to predict and it is important to study the effects of those parameters on the glycosylation of the glycoprotein under the specific production conditions. In this study, we showed the effects of DO concentration on CHO cell growth, Alb-EPO production, and glycosylation.