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| Content Provider | Springer Nature Link |
|---|---|
| Author | Khasa, Yogender Pal Khushoo, Amardeep Tapryal, Suman Mukherjee, K. J. |
| Copyright Year | 2011 |
| Abstract | The toxicity of the recombinant protein towards the expression host remains a significant deterrent for bioprocess development. In this study, the expression of human granulocyte macrophage-colony stimulating factor (hGM-CSF), which is known to be toxic to its host, was enhanced many folds using a combination of genetic and bioprocess strategies in Escherichia coli. The N terminus attachment of endoxylanase and asparaginase signal sequences from Bacillus subtilis and E. coli, respectively, in combination with and without His-tag, considerably improved expression levels. Induction and media optimization studies in shake flask cultures resulted in a maximal hGM-CSF concentration of 365 mg/L in the form of inclusion bodies (IBs) with a specific product yield (Y $_{P/X}$) of 120 mg/g dry cell weight in case of the asparaginase signal. Culturing the cells in nutrient rich Terrific broth maintained the specific product yields (Y $_{P/X}$) while a 6.6-fold higher volumetric concentration of both product and biomass was obtained. The purification and refolding steps were optimized resulting in a 95% pure protein with a fairly high refolding yield of 45%. The biological activity of the refolded protein was confirmed by a cell proliferation assay on hGM-CSF dependent human erythroleukemia TF-1 cells. This study demonstrated that this indeed is a viable route for the efficient production of hGM-CSF. |
| Starting Page | 523 |
| Ending Page | 537 |
| Page Count | 15 |
| File Format | |
| ISSN | 02732289 |
| Journal | Applied Biochemistry and Biotechnology |
| Volume Number | 165 |
| Issue Number | 2 |
| e-ISSN | 15590291 |
| Language | English |
| Publisher | Humana Press Inc |
| Publisher Date | 2011-05-12 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | hGM-CSF Asparaginase Endoxylanase Signal sequence Recombinant protein E. coli Biotechnology Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology |
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