Effects of temperature shifts and oscillations on recombinant protein production expressed in Escherichia coli

Jazini, M ; Sharif University of Technology | 2013

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  1. Type of Document: Article
  2. DOI: 10.1007/s00449-013-0927-1
  3. Publisher: 2013
  4. Abstract:
  5. Escherichia coli is widely used host for the intracellular expression of many proteins. However, in some cases also secretion of protein from periplasm was observed. Improvement of both intracellular and extracellular production of recombinant protein in E. coli is an attractive goal in order to reduce production cost and increase process efficiency and economics. Since heat shock proteins in E. coli were reported to be helpful for protein refolding and hindering aggregation, in this work different types of single and periodic heat shocks were tested on lab scale to enhance intracellular and extracellular protein production. A single heat shock prior to induction and different oscillatory temperature variations during the induction phase were executed. The results showed that these variations influence protein production negatively. In other words, 45 and 50 % reduction in extracellular protein production were observed for the single heat shock and oscillated temperature between 35 and 40°C, respectively. However, the oscillatory temperature approach introduced in this study is recommended as a tool to quantitatively analyze the effects of inhomoge-neous temperature on cell physiology and productivity in large-scale bioreactors
  6. Keywords:
  7. Intracellular protein ; Protein release ; Temperature oscillation ; Effects of temperature ; Extracellular proteins ; Heat-shock ; Intracellular proteins ; Recombinant protein productions ; Temperature oscillations ; Temperature variation ; Cytology ; Enzyme activity ; Escherichia coli ; Physiology ; Temperature ; Alkaline phosphatase ; Cell protein ; Heat shock protein ; Recombinant protein ; Rhamnose ; Bioreactor ; Cell function ; Cytoplasm ; Gene expression system ; Heat shock ; Nonhuman ; Oscillation ; Priority journal ; Protein expression ; Protein refolding ; Protein secretion ; Quantitative analysis ; Temperature sensitivity ; Escherichia coli ; Hot Temperature ; Recombinant Proteins
  8. Source: Bioprocess and Biosystems Engineering ; Volume 36, Issue 11 , 2013 , Pages 1571-1577 ; 16157591 (ISSN)
  9. URL: http://link.springer.com/article/10.1007%2Fs00449-013-0927-1