An improved procedure for production of human epidermal growth factor from recombinant E. coli

2001 ◽  
Vol 57 (5-6) ◽  
pp. 674-679 ◽  
Author(s):  
W.-Y. Tong ◽  
S.-J. Yao ◽  
Z.-Q. Zhu ◽  
J. Yu
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
E Coli ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth

scholarly journals COMPARISON OF EXTRACELLULAR SECRETION OF RECOMBINANT HUMAN EPIDERMAL GROWTH FACTOR USING TORA AND PELB SIGNAL PEPTIDES IN ESCHERICHIA COLI BL21 (DE3)

2019 ◽  
pp. 81-84 ◽  
Author(s):  
RIMA MELATI ◽  
ANNISA INDRIYANI ◽  
SHABARNI GAFFAR ◽  
SRIWIDODO ◽  
IMAN PERMANA MAKSUM
Keyword(s):  
Escherichia Coli ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Signal Peptides ◽  
Extracellular Expression ◽  
E Coli ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth

Objective: The objective of this study was to evaluate two signal peptides (TorA and PelB), representing the most common secretion pathways in Escherichia coli, for their ability to secrete recombinant human epidermal growth factor (rhEGF) protein in the extracellular expression. Methods: E. coli BL21 (DE3) as the host cell to be transformed using recombinant plasmid pD881-TorA the consensus already containing hEGF gene and the signal peptide TorA or PelB, then expressed by L-rhamnose induction. rhEGF purified by heat treatment and ion-exchange chromatography. The hEGF protein was characterized using sodium dodecyl sulfate-polyacrylamide gel electrophoresis and ELISA. Results: The result showed that PelB was secreting more hEGF protein compared to TorA with protein expression results of 48.2 μg/L and purification results of 0.360 μg/L, with a purity level of 83%. Conclusion: The results of this study explain in extracellular expression of hEGF protein in E. coli, PelB helps hEGF protein secretion to culture media better than TorA.

scholarly journals Expression, Microencapsulation of Recombinant Human Epidermal Growth Factor, and Release Study in Gastric Ulcer Representing Condition

2021 ◽  
pp. 493-502
Author(s):  
Riyona Desvy Pratiwi
Keyword(s):  
Gastric Ulcer ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Expression Systems ◽  
E Coli ◽  
Human Epidermal Growth Factor ◽  
Chitosan Microparticles ◽  
Proliferation Activity ◽  
Epidermal Growth ◽  
External Wound

Recombinant human epidermal growth factor (rhEGF) has been studied and expressed in various expression systems. It has been also commercialized and clinically used, yet limited to topical diseases. However, being naturally expressed in different tissues, the rhEGF is potential to be applied not only for external wound and skin disorders, but also to regenerates internal damaged epidermal cells such found in gastric ulcer. In the recent study, chitosan microparticles were developed to facilitate delivery of the rhEGF and to overcome gastric degradation that majorly interfere protein, particularly rhEGF oral administration. The rhEGF was expressed in E. coli BL21(DE3) and purified using Ni-NTA chromatography. The refolded rhEGF showed proliferation activity on MC7 cells. rhEGF loaded chitosan microparticles were stable in the gastric and specifically released the loaded rhEGF in the high oxidative environment in acidic pH representing gastric ulcer condition.    

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