Bioprocessing of Therapeutic Proteins from the Inclusion Bodies of Escherichia coli

High Yield Production of Heterologous Proteins with Escherichia coli

“…E. coli is genetically well characterised and efficient expression of recombinant product to more than 50 percent of total cell mass has been reported 40 . The selection and design of the expression plasmids influence synthesis rates, plasmid copy number, the segregational plasmid stability and therefore productivity and regulatory issues.…”

“…High cell density culture systems also suffer from several drawbacks, including limited availability of dissolved oxygen, carbon dioxide levels which can decrease growth rates and stimulate acetate formation, reduction in the mixing efficiency of the fermentor, and heat generation [16][17]40,44 . A major challenge in the production of recombinant protein at high cell density is the accumulation of acetate, a lipophilic agent that is detrimental to cell growth.…”

“…For example, optical density of about 124 resulted for high cell density culture for production of recombinant ovine growth harmone in E. coli 40 . It is also essential that cell growth be achieved in optimal time period to improve the overall production of the recombinant protein.…”

“…Dense culture requires large amounts of O 2 to support good growth and thus necessitates unconventional aeration strategy to maintain dissolved O 2 concentration at a suitable level throughout the growth period. In most of the cases of E. coli being used as a host for recombinant protein, the production phase start after induction with suitable inducer 8,40 . Thus in principle, growth phase and production phase can be delineated in the same vessel for the high volumetric yield of the recombinant protein.…”

Strategies for the production of difficult-to-express full-length eukaryotic proteins using microbial cell factories: production of human alpha-galactosidase A

“…As expression system, E. coli offers many advantages over eukaryotic 355 systems referring to rapidity, simplicity and expenditure (Demain and Vaishnav, 2009). However it has some 356 disadvantages which in some cases are difficult to override as the lack of many posttranslational 357 modifications and high tendency to form aggregated species (Panda, 2003). In the present study, a human full-358 length protein, GLA, which has been purified from eukaryotic expression systems (Chen et production of an active hGLA in E. coli (Hantzopoulos and Calhoun, 1987).…”