Optimization of an extracellular zinc-metalloprotease (SVP2) expression in Escherichia coli BL21 (DE3) using response surface methodology

A comparison of statistical approaches used for the optimization of soluble protein expression in Escherichia coli

“…It has been demonstrated by our work ( [15,16] and this article), and the work of others [14,29,30] that besides the expression host, the most important factors affecting soluble protein expression are the post-induction temperature and the duration of induction, especially since these two variables often interact [14]. (Table 8, run 10) and it was approximately 3 times higher than the lowest expression level (5.6 mg/L) obtained using the combination BL21(DE3)/30 o C/20 h (Table 8, [16].…”

Recombinant Expression of a Novel Fungal Immunomodulatory Protein with Human Tumor Cell Antiproliferative Activity from Nectria haematococca

“…However, improving the production rate and simplifying the purification procedure are important. The E. coli expression system is a widely used expression platform because of its advantages of short growth cycle, low cost and high yield [23]. In this study, bioactive FIP-nha production in E. coli reached 42.7 mg/L, which was two times higher than the result of Bastiaan-Net et al in 2013 [22].…”

High-Yield Production in Escherichia coli of Fungal Immunomodulatory Protein Isolated from Flammulina velutipes and Its Bioactivity Assay in Vivo

“…Compared with other expression platforms, the E. coli expression system is a useful benchmark because of its advantages, such as short growth cycle and low cost [25]. Although there are some disadvantages using E. coli as the expression host for production of recombinant protein for research and clinical applicaton, e.g., post-translational modifications, lipopolysaccharide (LPS) contamination, yet because FIP-fve is a pure protein with a molecular weight of 12.7 kDa and without carbohydrate [2], it could be produced in E. coli.…”

“…Due to the complicated technology and high cost, the yield of natural FIP-fve was very low (87.5–165 mg/kg) [2,24], thus, selecting a suitable expression system is the premise of the application of FIP-fve. While the FIP-fve expressed in insect cells can also induce the expression of IL-2 of mouse spleen cells [24], yet it’s yield was low (6 mg/L) [25]. Meanwhile, recombinant GST- FIP-fve from E. coli with the yield (5 mg/L) only has 50% activity of natural FIP-fve [2,11], whereas we get 29.1 mg recombinant FIP-fve from 1L culture of E. coli Transetta (DE3), and the obtained His-FIP-fve increased the secretion of IL-2 and IFN-γ at suitable concentrations, which correlated with the findings of Wang P.H.…”