Ali, Muhamad and HARYANTI, RAMDHANI and DEPAMEDE, SULAIMAN N GST Fusion Assisted Overexpression and Purification of Recombinant Parasite Lactate Dehydrogenase Enzyme in Escherichia coli. -.
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Abstract
Escherichia coli is one of the well-established and most popular organisms for the production of recombinant proteins. However, expression levels and solubility may be issue, since some proteins are generated in low amount and aggregate in inclusion body. Fusion proteins have become essential for the overexpression and solubility improvement of recombinant proteins in E. coli. In this study, parasite Lactate dehydrogenase-encoding gene was fused in the C-terminal of glutathione-s-transferase gene and subsequently expressed in E. coli BL21. Expression levels and purification results of the fused protein were determined by SDS-PAGE. The SDS-PAGE result shows that the 58 kDa band corresponding to the GST-pLDH protein was successfully overexpressed and purified using GSTrap column. Our results are not only useful for robust production of parasite Lactate dehydrogenase, but also helpful for the enzyme purification.
| Item Type: | Article |
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| Keywords (Kata Kunci): | parasite Lactate Dehydrogenase (pLDH), Glutathione-s-Transferase (GST), Fusion Protein, Escherichia coli, GSTrap column |
| Subjects: | Q Science > Q Science (General) |
| Divisions: | Fakultas Peternakan |
| Depositing User: | . Zulkarnain Zulkarnain |
| Date Deposited: | 30 Sep 2021 02:30 |
| Last Modified: | 30 Sep 2021 02:30 |
| URI: | http://eprints.unram.ac.id/id/eprint/24746 |
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