Project description:These research areas concentrate on stress induced proteases in recombinant Escherichia coli, glycosylation heterogeneity due to bioprocess conditions produced in mammalian cells, and metabolic engineering of E. coli. The hypothesis of this project is that recombinant protein glycosylation is inefficient under normal bioreactor conditions since the additional glycosylation reactions necessary for the recombinant protein exceed the metabolic capacity of the cells. Normal bioreactor conditions have been optimized for cell growth, and sometimes for protein productivity. Only recently has it been accepted that optimal glycosylation may not occur under optimal growth or protein productivity conditions. Specific Aim: Determine the relationship between bioreactor conditions and glycosylation gene expression in NS0 cells.
Project description:PluriTest score for iPSCs cultured for 7 days in a small bioreactor received a pluripotency score of 36.87 ± 0.12. n = 3. PluriTest score for iPSCs cultured in a standard bioreactor for 6 or 7 days was 41.28 ± 0.32. n = 3. KaryoStat assays revealed no chromosomal or genetic mutations occurred in the iPSCs cultured in the small and standard bioreactors. n = 3.
