Title |
Functional recombinant protein is present in the pre-induction phases of Pichia pastoris cultures when grown in bioreactors, but not shake-flasks
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Published in |
Microbial Cell Factories, September 2014
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DOI | 10.1186/s12934-014-0127-y |
Pubmed ID | |
Authors |
Zharain Bawa, Sarah J Routledge, Mohammed Jamshad, Michelle Clare, Debasmita Sarkar, Ian Dickerson, Markus Ganzlin, David R Poyner, Roslyn M Bill |
Abstract |
Pichia pastoris is a widely-used host for recombinant protein production; expression is typically driven by methanol-inducible alcohol oxidase (AOX) promoters. Recently this system has become an important source of recombinant G protein-coupled receptors (GPCRs) for structural biology and drug discovery. The influence of diverse culture parameters (such as pH, dissolved oxygen concentration, medium composition, antifoam concentration and culture temperature) on productivity has been investigated for a wide range of recombinant proteins in P. pastoris. In contrast, the impact of the pre-induction phases on yield has not been as closely studied. In this study, we examined the pre-induction phases of P. pastoris bioreactor cultivations producing three different recombinant proteins: the GPCR, human A(2a) adenosine receptor (hA(2a)R), green fluorescent protein (GFP) and human calcitonin gene-related peptide receptor component protein (as a GFP fusion protein; hCGRP-RCP-GFP). |
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