Enhanced expression of soluble antibody fragments by low-temperature and overdosing with a nitrogen source

Enzyme Microb Technol. 2018 Aug:115:9-15. doi: 10.1016/j.enzmictec.2018.04.002. Epub 2018 Apr 4.

Abstract

Escherichia coli has been a primary host for the prokaryotic production of antibody fragments (Fabs) and has contributed to several successes in the pharmaceutical industry. Nevertheless, the requirement of disulfide bonds often results in low-yield fermentation and a lack of cost-effectiveness. Despite the improved production of functional Fabs by fermentation below 30 °C, the limited cellular growth needs further work. To address these issues, we investigated the effect of nitrogen supply on the cellular growth and the Fab productivity. We used the anti-human VEGF-A Fab as a model that exhibited poor expression at 37 °C regardless of the amount of nitrogen supplied during fermentation. In stark contrast, the expression yield of soluble Fab with a gross nitrogen supply of 6.91 g/L of broth throughout the fermentation at 25 °C was 332 mg/L. Furthermore, and increased nitrogen supply of 10.9 g/L significantly improved the yield of active form by 59.7% and the cellular growth rate by 39.3%. These results indicate that overdosing of a nitrogen source at low temperature is critical to Fab productivity in E. coli.

Keywords: Antibody fragment; Fed-batch fermentation; Low-temperature; Nitrogen effect; Soluble Fab.

MeSH terms

  • Cold Temperature
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Escherichia coli / immunology
  • Escherichia coli / metabolism*
  • Fermentation*
  • Humans
  • Immunoglobulin Fragments / genetics
  • Immunoglobulin Fragments / immunology*
  • Nitrogen / metabolism*
  • Vascular Endothelial Growth Factor A / immunology

Substances

  • Immunoglobulin Fragments
  • VEGFA protein, human
  • Vascular Endothelial Growth Factor A
  • Nitrogen