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Optimization of Cho Cell Recombinant Protein Expression

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DOI: 10.23977/ICETMR2022.016


Hong Yunchao, Chen Yuanjing, Yu Jiaping

Corresponding Author

Yu Jiaping


Chinese hamster ovary cells are the most widely used cells to produce therapeutic proteins in the biopharmaceutical field. They proliferate very quickly in large-scale culture systems and can express a variety of recombinant proteins at a high level. This paper studied the optimization of CHO cell culture technology. Objective: To explore a method to improve the purity of recombinant protein in CHO cells. Methods: Different cooling time (the 5th and 6th day), temperature (33 ℃ and 31 ℃) and pH control strategy (7.00 ± 0.30 and 7.10 ± 0.10) were set to observe the changes of cell viability, protein yield and protein purity. Results: The process of cooling to 31.0 ℃ on the sixth day of culture, and pH control at 7.00 ± 0.30 after cooling, could further improve the purity of the product, and had no significant impact on cell growth, metabolism and recombinant protein yield. Conclusion: The experiment determined the appropriate protein optimization strategy, which laid the foundation for the subsequent scale-up production.


Cho cells, Process optimization, Cell culture

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