High-level secretory production of human granulocyte-colony stimulating factor by fed-batch culture of recombinant Escherichia coli

2001 ◽  
Vol 24 (4) ◽  
pp. 249-254 ◽  
Author(s):  
Yim S. ◽  
Jeong K. ◽  
Chang H. ◽  
Lee S.
Keyword(s):  
Escherichia Coli ◽  
Batch Culture ◽  
Recombinant Escherichia Coli ◽  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
Fed Batch ◽  
Secretory Production ◽  
Fed Batch Culture ◽  
High Level ◽  
Stimulating Factor

High level production of human proapo A-I by fed-batch culture of recombinant Escherichia coli

1993 ◽  
Vol 75 (2) ◽  
pp. 155-157 ◽  
Author(s):  
Kunihiko Ohta ◽  
Tatsuro Shibui ◽  
Yuuki Morimoto ◽  
Shinji Iijima ◽  
Takeshi Kobayashi
Keyword(s):  
Escherichia Coli ◽  
Batch Culture ◽  
Recombinant Escherichia Coli ◽  
Fed Batch ◽  
Fed Batch Culture ◽  
High Level ◽  
Level Production

Suitable Signal Peptides for Secretory Production of Recombinant Granulocyte Colony Stimulating Factor in Escherichia coli

2020 ◽  
Vol 14 (4) ◽  
pp. 269-282
Author(s):  
Sadra S. Tehrani ◽  
Golnaz Goodarzi ◽  
Mohsen Naghizadeh ◽  
Seyyed H. Khatami ◽  
Ahmad Movahedpour ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Signal Peptide ◽  
Fusion Proteins ◽  
Inclusion Bodies ◽  
Clinical Aspects ◽  
Granulocyte Colony Stimulating Factor ◽  
Colony Stimulating Factor ◽  
E Coli ◽  
Secretory Production ◽  
Stimulating Factor

Background: Granulocyte colony-stimulating factor (G-CSF) expressed in engineered Escherichia coli (E. coli) as a recombinant protein is utilized as an adjunct to chemotherapy for improving neutropenia. Recombinant proteins overexpression may lead to the creation of inclusion bodies whose recovery is a tedious and costly process. To overcome the problem of inclusion bodies, secretory production might be used. To achieve a mature secretory protein product, suitable signal peptide (SP) selection is a vital step. Objective: In the present study, we aimed at in silico evaluation of proper SPs for secretory production of recombinant G-CSF in E. coli. Methods: Signal peptide website and UniProt were used to collect the SPs and G-CSF sequences. Then, SignalP were utilized in order to predict the SPs and location of their cleavage site. Physicochemical features and solubility were investigated by ProtParam and Protein-sol tools. Fusion proteins sub-cellular localization was predicted by ProtCompB. Results: LPP, ELBP, TSH, HST3, ELBH, AIDA and PET were excluded according to SignalP. The highest aliphatic index belonged to OMPC, TORT and THIB and PPA. Also, the highest GRAVY belonged to OMPC, ELAP, TORT, BLAT, THIB, and PSPE. Furthermore, G-CSF fused with all SPs were predicted as soluble fusion proteins except three SPs. Finally, we found OMPT, OMPF, PHOE, LAMB, SAT, and OMPP can translocate G-CSF into extracellular space. Conclusion: Six SPs were suitable for translocating G-CSF into the extracellular media. Although growing data indicate that the bioinformatics approaches can improve the precision and accuracy of studies, further experimental investigations and recent patents explaining several inventions associated to the clinical aspects of SPs for secretory production of recombinant GCSF in E. coli are required for final validation.

scholarly journals Kinetics of High Cell Density Fed-batch Culture of Recombinant Escherichia coli Producing Human-like Collagen

2006 ◽  
Vol 14 (2) ◽  
pp. 242-247 ◽  
Author(s):  
Xiufu HUA ◽  
Daidi FAN ◽  
Yan'e LUO ◽  
Xi ZHANG ◽  
Huijuan SHI ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Density ◽  
Batch Culture ◽  
High Cell Density ◽  
Recombinant Escherichia Coli ◽  
High Cell ◽  
Fed Batch ◽  
Fed Batch Culture ◽  
Kinetics Of

Model-based optimization of viral capsid protein production in fed-batch culture of recombinant Escherichia coli

2003 ◽  
Vol 25 (4) ◽  
pp. 255-262 ◽  
Author(s):  
D. Levisauskas ◽  
V. Galvanauskas ◽  
S. Henrich ◽  
K. Wilhelm ◽  
N. Volk ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Capsid Protein ◽  
Batch Culture ◽  
Protein Production ◽  
Recombinant Escherichia Coli ◽  
Viral Capsid ◽  
Fed Batch ◽  
Viral Capsid Protein ◽  
Model Based ◽  
Fed Batch Culture

Production of thermophilic protease by glucose-controlled fed-batch culture of recombinant Escherichia coli

1994 ◽  
Vol 78 (4) ◽  
pp. 304-309 ◽  
Author(s):  
Shinji Sakamoto ◽  
Masaharu Iijima ◽  
Hiroshi Matsuzawa ◽  
Takahisa Ohta
Keyword(s):  
Escherichia Coli ◽  
Batch Culture ◽  
Recombinant Escherichia Coli ◽  
Fed Batch ◽  
Fed Batch Culture

Refolding and Purification of Zymomonas mobilis Levansucrase Produced as Inclusion Bodies in Fed-Batch Culture of Recombinant Escherichia coli

2000 ◽  
Vol 18 (3) ◽  
pp. 388-393 ◽  
Author(s):  
Kandula Sunitha ◽  
Bong Hyun Chung ◽  
Ki-Hyo Jang ◽  
Ki-Bang Song ◽  
Chul Ho Kim ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Batch Culture ◽  
Zymomonas Mobilis ◽  
Inclusion Bodies ◽  
Recombinant Escherichia Coli ◽  
Fed Batch ◽  
Fed Batch Culture
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