Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/38897
Title: Solubilization and purification studies of GST-HBx-6His
Authors: Goh, Kester Zhi Hao.
Keywords: DRNTU::Engineering::Chemical engineering::Biotechnological production
Issue Date: 2010
Abstract: The Hepatitis B Virus X (HBx) protein is a protein expressed within an organism’s body infected with the Hepatitis B Virus (HBV). Its characterization in depth could develop an improved treatment for both acute and chronic Hepatitis B patients. However expression of HBx in Escherichia coli (E. coli) resulted in inclusion body formation, creating a hurdle in its purification and production as a bioactive protein. As such, the overall aim of this Final Year Project is to improve bioprocessing of ‘inclusion body’-derived HBx protein for higher process yield via a simpler bioprocess flow sheet. The HBx model protein used in this work is expressed as a Glutathione S-Transferase (GST) fusion protein. The use of detergents (i.e. N-Lauroylsarcosine sodium salt) was found to improve solubility of the fusion protein during the cell lysis step. Two methods to simultaneously purify and cleave the GST tag from the GST-HBx-6His protein were also developed and studied. Both methods showed potential in producing the HBx-6His protein. Fusion protein recovery and cleavage produced HBx-6His protein in purer forms from the bioprocess utilizing Glutathione Agarose beads as compared to the bioprocess utilizing Nickel NitriloTriacetic Acid beads.
URI: http://hdl.handle.net/10356/38897
Rights: Nanyang Technological University
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SCBE Student Reports (FYP/IA/PA/PI)

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