详细信息
High purity recombinant human growth hormone (rhGH) expression in Escherichia coli under phoA promoter ( SCI-EXPANDED收录)
文献类型:期刊文献
英文题名:High purity recombinant human growth hormone (rhGH) expression in Escherichia coli under phoA promoter
作者:Song, Hao[1];Jiang, Jingxin[1];Wang, Xuedong[1];Zhang, Jianguo[2]
机构:[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China;[2]Univ Shanghai Sci & Technol, Inst Food Sci & Engn, Shanghai, Peoples R China
年份:2017
卷号:8
期号:2
起止页码:147
外文期刊名:BIOENGINEERED
收录:;WOS:【SCI-EXPANDED(收录号:WOS:000399530000012)】;
基金:The work was supported by National Major Science and Technology Projects (863) of China (No. 2012ZX09304009) and National Basic Research Program (973) of China (Program No. 2012CB721103).
语种:英文
外文关键词:alkaline phosphatase; Escherichia coli; fed-batch; fermentation strategy; rhGH; variant
摘要:Recombinant human Growth Hormone (rhGH) is an important protein for human growth and is in high demand in clinics. Hence, it is necessary to develop an efficient fermentation process to produce highly pure rhGH. In this study, rhGH was expressed in Escherichia coli under alkaline phosphatase (phoA) promoter. The cultivation conditions for high expression level and purity of rhGH were investigated. The best initial phosphate concentration for rhGH expression, out of the 4 levels of initial phosphate concentration tests performed, was 12.6mmol/L. Subsequently, 2 fed-batch cultivations under low dissolved oxygen (DO) (0% - 10%) and high DO (20% - 30%) conditions were carried out. High purity rhGH (92%) was obtained from 20% - 30% DO-stat cultivation, although the biomass did not show any significant difference. In summary, this research provided an efficient fermentation process for high purity rhGH production from E. coli under phoA promoter, which can lower the production and purification costs for large-scale production of rhGH.
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