dc.contributor.authorChen, Yu.
dc.date.accessioned2011-05-18T04:18:44Z
dc.date.available2011-05-18T04:18:44Z
dc.date.copyright2011en_US
dc.date.issued2011
dc.identifier.citationChen, Y. (2011). Chromatography refolding of recombinant alpha-fetoprotein for high refolding productivity and intensified bioprocessing. Doctoral thesis, Nanyang Technological University, Singapore.
dc.identifier.urihttp://hdl.handle.net/10356/43987
dc.description.abstractAlpha-fetoprotein (AFP) is a commercially valuable biopharmaceutical candidate for autoimmune indications. Transgenically-derived recombinant AFP has recently successfully completed a Phase Two clinical trial study for rheumatoid arthritis indications at Merrimack Pharmaceuticals (Cambridge, MA, USA). The launch of this protein on market shelves in the future will subsequently demand cheaper second-generation product when product patent expires, thus necessitating new processes that can reduce product cost. The production of AFP as inclusion bodies (IBs) in Escherichia coli (E. coli) is advantageous for process-scale commercial manufacture due to speed, simplicity and cost reasons but conversion of the inactive protein aggregate into biologically active protein requires an efficient refolding step. The use of dilution refolding in previously reported recombinant human AFP (rhAFP) laboratory processes has resulted in low refolding yields, which negatively impacts the overall process yield and productivity. A superior refolding and bioprocessing route is clearly needed to facilitate efficient and rapid product delivery to market, if a commercial process for rhAFP is to be possible. In this thesis, chromatography refolding was researched to address the poor refolding performance or rhAFP in previous ‘dilution refolding’-based rhAFP processes.en_US
dc.format.extent185 p.en_US
dc.language.isoenen_US
dc.subjectDRNTU::Engineering::Chemical engineering::Biotechnological productionen_US
dc.titleChromatography refolding of recombinant alpha-fetoprotein for high refolding productivity and intensified bioprocessing.en_US
dc.typeThesis
dc.contributor.supervisorSusanna Leong Su Janen_US
dc.contributor.schoolSchool of Chemical and Biomedical Engineeringen_US
dc.description.degreeDOCTOR OF PHILOSOPHY (SCBE)en_US


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