Please use this identifier to cite or link to this item:
Title: Solubility studies of a viral proteins
Authors: Singh, Parvinder.
Keywords: DRNTU::Engineering::Chemical engineering::Biotechnology
Issue Date: 2010
Abstract: Hepatitis B virus (HBV) infects many people world-wide. An X protein (HBx) is produced during the virus replication and in order to study its role in the progression of the virus, a regular continuous supply of pure bioactive HBx proteins is required. Presently, when HBx is produced recombinantly, they form inclusion bodies and this leads to very poor yields of bioactive HBx proteins. The current strategy to produce sufficient amounts of HBx proteins for characterization studies is to solubilize and refold the inclusion body-derived HBx proteins. However, the yield of the refolded HBx protein is currently low because of a kinetic competition between aggregation and refolding. The objective in this project was to conduct a literature review investigation into dilution and on-column refolding techniques base on published HBx refolding studies. An investigation on the kinetic competition between aggregation and refolding was carried as well. The results of the investigations showed that there was little correlation between the yield of refolded HBx proteins and the refolding method used. Despite the lack of reliable kinetic data on HBx refolding, the model was able to predict generally a high yield of refolded proteins at low concentrations of denatured proteins. As a result, improvements to the current methods of refolding are required to scale-up the refolding process to provide a regular continuous supply of pure bioactive HBx proteins.
Rights: Nanyang Technological University
Fulltext Permission: restricted
Fulltext Availability: With Fulltext
Appears in Collections:SCBE Student Reports (FYP/IA/PA/PI)

Files in This Item:
File Description SizeFormat 
  Restricted Access
453.18 kBAdobe PDFView/Open

Page view(s)

Updated on Jan 24, 2021


Updated on Jan 24, 2021

Google ScholarTM


Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.