Abstract
This article attempts to review the techniques typically used to purify recombinant protein, intended for industrial usage. The initial part of this review briefly describes the choices of expression systems available to produce recombinant protein and based on the choices made, techniques used for sample harvesting is deliberated. The method to prepare samples prior to the purification step is also discussed which includes clarification and retaining the stability of protein of interest. The detection and quantitation of the protein methods are also pondered upon, since these two steps are essential for the success of any purification steps. This is followed by several purification strategies, emphasizing on the purification of tagged recombinant protein. Two additional methods of purification are also suggested, and they are, conventional column chromatography and Aqueous Two-Phase Systems (ATPS), which can be applied to both, tagged or untagged protein. ATPS comes with several advantages, including scale-up potential and continuous operation, which are useful at the industrial scale purification. The common problems faced in purification of recombinant proteins at higher or industrial scales are also highlighted. Finally, this article suggests that before any industrial scale protein purification can be exploited, some issues have to be clarified and resolved which includes its economic viability, adherence to regulatory requirements and environmental friendliness.
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Yusof, F. (2015). Purification of Recombinant Protein for Industrial Use. In: Amid, A. (eds) Recombinant Enzymes - From Basic Science to Commercialization. Springer, Cham. https://doi.org/10.1007/978-3-319-12397-4_5
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DOI: https://doi.org/10.1007/978-3-319-12397-4_5
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