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Title: Efficient expression and isolation of recombinant human interleukin-11 (rhIL-11) in pichia pastoris
Authors: Yu, KM 
YiuNam, Lau, J
Fok, M
Yeung, YK
Fok, SP
Shek, F
Wong, WT 
Choo, QL
Keywords: IL-11
Soluble aggregate
Issue Date: 2018
Publisher: Academic Press
Source: Protein expression and purification, 2018, v. 146, p. 69-77 How to cite?
Journal: Protein expression and purification 
Abstract: Current source of recombinant human interleukin-11 (rhIL-11) is isolated from a fusion protein expressed by E. coli that requires additional enterokinase to remove linked protein, resulting in product heterogeneity of N-terminal sequence. Due to lack of glycosylation, rhIL-11 is suitable to be expressed by yeast cells. However, the only available yeast-derived rhIL-11 presents an obstacle in low production yield, as well as an unamiable process, such as the use of reverse-phase chromatography employing plenty of toxic organic solvents. Our findings showed that the low yield was due to self-aggregation of rhIL-11. A novel process recovering bioactive rhIL-11 from the yeast secretory medium therefore has been developed and demonstrated, involving fermentation from Pichia pastoris, followed by a two-phase extraction to precipitate rhIL-11. After renaturing, the protein of interest was purified by a two-column step, comprising a cation-exchanger, and a hydrophobic interaction chromatography in tandem at high sample loads that was facile and cost-effective in future scale-up. Identity and quality assessments confirmed the expected amino acid sequence without N-terminal heterogeneity, as well as high quality in potency and purity. Such a process provides an alternative and adequate supply of the starting material for the PEGylated rhIL-11.
ISSN: 1046-5928
EISSN: 1096-0279
DOI: 10.1016/j.pep.2018.01.012
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