Abstract
Expression of human epidermal growth factor using Ssp DnaB mini-intein as fusion partner in Escherichia coli BL21(DE3)
Highlights
Human epidermal growth factor is a protein with 53 amino acid residues with 6.2 kDa of molecular weight
The inclusion bodies were solubilized in 8 M urea, the solubilized CBD-Ssp DnaB-human epidermal growth factor (hEGF) was reformed by dialysis, and hEGF was spliced by shifting the pH from 8.5 to 6.0 to yield a concentration of 0.163 mg/ml
We concluded that hEGF was obtained from the solubilized CBD-Ssp DnaB-hEGF from inclusion bodies produced by E. coli BL21(DE3)
Summary
Human epidermal growth factor (hEGF) is a protein with 53 amino acid residues with 6.2 kDa of molecular weight This polypeptide has three intramolecular disulfide bonds and heat resistance properties (Eissazadeh et al, 2017; Sriwidodo et al, 2019; Tang et al, 2016). E. coli was one of the most widely used hosts for recombinant protein expression (Hayat et al, 2018) It has a Intracellular protein expression in E. coli especially small protein such as hEGF mostly did not work well because the small protein was degraded by proteases from the host cell. This causes a significant loss in yields and made it difficult in the purification process.
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