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Paper Information

Journal:   IRANIAN JOURNAL OF PUBLIC HEALTH   AUGUST 2014 , Volume 43 , Number SUPPLEMENT 2; Page(s) 28 To 28.
 
Paper: 

OVER-PRODUCTION OF EPIDERMAL GROWTH FACTOR (EGF) IN E. COLI

 
 
Author(s):  NAMVARAN MOHAMMAD MEHDI*, BABAEIPOUR VALIOLLAH, VAHIDI HOSSEIN, EBRAHIMI FIROUZ, ABARGHOOYI FATEMEH
 
* DEPARTMENT OF BIOTECHNOLOGY, SCHOOL OF PHARMACY AND PHARMACEUTICAL SCIENCE, SHAHID BEHESHTI UNIVERSITY OF MEDICAL SCIENCES, TEHRAN, IRAN
 
Abstract: 

Background: Epidermal Growth Factor (EGF) is a monomer polypeptide, which is produce from different tissue in human. It has many applications in medicine and Pharmaceutical Science. The main source of EGF is Parotid gland. Production of EGF from animal’s source has many disadvantages and it is not suitable for human applications. The best way for production of this protein is recombinant DNA technology, batch fermentation and High cell density culture for E. coli. In this study, we report the heterologous over-expression of EGF in E. coli BL21 (DE3).
Methods: Escherichia coli is the most widely used host for producing recombinant proteins. Using BL21 derived strain can reduce proteolyses of heterologous protein. In this study we increased several times recombinant human EGF production in E. coli BL21 (DE3) by optimization media and temperature in induction duration. For this reason the transformed BL21 (DE3) with pET28a including synthetic gene kinetic cell growth and rhEGF production investigated at three different medium like LB, TB and 32Y with different temperatures such as 24, 28, 32 and 37oC. The results of experiments were analyzed by SDS-PAGE, and cell growth and recombinant protein production kinetics.
Results: The optimal expression of EGF in E. coli can be easily achieved when the growth conditions are properly controlled. Media components, induction time, growth temperature, and IPTG concentration have profound effects on the way in which recombinant protein is produced. In this study the maximum expression was obtained from TB medium at 28oC with IPTG concentration of 0.1mM. The last OD600 and dry cell weight at this condition was 12.2 and 5.61 g/L respectively. The final yield was 32% of total soluble proteins, which has an important value for EGF production in Escherichia coli.
Conclusion: Using rich medium like TB and decrease temperatures can improve the amount of protein considerably.

 
Keyword(s): ESCHERICHIA COLI, EPIDERMAL GROWTH FACTOR (EGF), OVER-EXPRESSION
 
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