| dc.description.abstract | The production of protein-based drugs rely on a basic protein purification method to extract and purify the desired protein from host cells. This research seeks to optimize the protein purification process to isolate Taq polymerase from E. coli host cells, which is used to model the purification of protein-based drugs such as insulin. This research identifies a purification process and subsequently explores the impact of: 1) changing the incubation time and temperature of the initial cell culture, 2) inducing protein expression with different concentrations of IPTG, and 3) changing the flow rate during ion-exchange column chromatography. These changes may introduce more time-efficient steps and/or yield a larger volume of pure, active protein than the traditional purification method. Both of these results would improve the drug industry’s efficiency by allowing companies to produce a large amount of active product in a short amount of time at a low cost. | en_US |
