GST Fusion Assisted Overexpression and Purification of Recombinant Parasite Lactate Dehydrogenase Enzyme in Escherichia coli
| Main Authors: | Ali, Muhamad, Depemade, Sulaiman N, Ramdhani, Haryanti |
|---|---|
| Format: | Proceeding PeerReviewed Book |
| Bahasa: | eng |
| Subjects: | |
| Online Access: |
http://eprints.unram.ac.id/18113/1/18.%20SINP-06%20APIS%202016-2.pdf http://eprints.unram.ac.id/18113/ |
Daftar Isi:
- Recently, Escheria coliu is one of the well-estabilished and most popular organisms for the production of recombinant proteins. However, expressiom leve;s and solubility issuem, 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 result are not only useful for robust production of parasite Lactate dehydrogenase, but also helful for the enzyme purification.