GST Fusion Assisted Overexpression and Purification of Recombinant Parasite Lactate Dehydrogenase Enzyme in Escherichia coli

Ali, Muhamad and Depemade, Sulaiman N and Ramdhani, Haryanti GST Fusion Assisted Overexpression and Purification of Recombinant Parasite Lactate Dehydrogenase Enzyme in Escherichia coli. In: The 3rd Animal Production International seminar, The 3rd ASEAN REgional Conference On Animal Production, 3rd APIS & 3rd ARCAP-2016 "Enchancing Synergistic Roles of Stakeholders for Development of Sustainable Livestock Production.

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Abstract

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.

Item Type: Conference or Workshop Item (Paper)
Keywords (Kata Kunci): parasite Lactate Dehydrogenase (pLDH), Glutathione-s-Transferase (GST), Fusion Protein,Escherichia coli, GSTrap column
Subjects: Q Science > Q Science (General)
S Agriculture > SF Animal culture
Divisions: Fakultas Peternakan
Depositing User: . Zulkarnain Zulkarnain
Date Deposited: 02 Nov 2020 07:18
Last Modified: 02 Nov 2020 07:18
URI: http://eprints.unram.ac.id/id/eprint/18113

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