期刊
BIOTECHNOLOGY JOURNAL
卷 9, 期 4, 页码 526-537出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/biot.201300305
关键词
CHO cells; Fed batch; Protein secretion; Recombinant protein production; Volumetric productivity
资金
- Federal Ministry of Economy, Family and Youth (BMWFJ)
- Federal Ministry of Traffic, Innovation and Technology (bmvit)
- Styrian Business Promotion Agency SFG
- Standortagentur Tirol
- PhD program BioToP - Biomolecular Technology of Proteins (Austrian Science Fund, FWF Project) [W1224]
- ZIT - Technology Agency of the City of Vienna through the COMET-Funding Program
Chinese hamster ovary (CHO) cells are currently the workhorse of the biopharmaceutical industry. However, yeasts such as Pichia pastoris are about to enter this field. To compare their capability for recombinant protein secretion, P. pastoris strains and CHO cell lines producing human serum albumin (HSA) and the 3D6 single chain Fv-Fc anti-HIV-1 antibody (3D6scFv-Fc) were cultivated in comparable fed batch processes. In P. pastoris, the mean biomass-specific secretion rate (q(p)) was 40-fold lower for 3D6scFv-Fc compared to HSA. On the contrary, q(p) was similar for both proteins in CHO cells. When comparing both organisms, the mean q(p) of the CHO cell lines was 1011-fold higher for 3D6scFv-Fc and 26-fold higher for HSA. Due to the low q(p) of the 3D6scFv-Fc producing strain, the space-time yield (STY) was 9.6-fold lower for P. pastoris. In contrast, the STY of the HSA producer was 9.2-fold higher compared to CHO cells because of the shorter process time and higher biomass density. The results indicate that the protein secretion machinery of P. pastoris is much less efficient and the secretion rate strongly depends on the complexity of the recombinant protein. However, process efficiency of the yeast system allows higher STYs for less complex proteins.
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