作者: Robin Kastilan , Alexander Boes , Holger Spiegel , Nadja Voepel , Ivana Chudobová
DOI: 10.1038/S41598-017-11819-4
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摘要: Pichia pastoris is a simple and powerful expression platform that has the ability to produce wide variety of recombinant proteins, ranging from peptides complex membrane proteins. A well-established fermentation strategy available comprising three main phases: batch phase, followed by glycerol fed-batch phase increases cell density, finally an induction for product using methanol as inducer. We previously used this three-phase at 15-L scale express different AMA1-DiCo-based malaria vaccine candidates develop cocktail. For two candidates, we switched two-phase lacking intermediate phase. The new not only provided more convenient process flow but also achieved 1.5-fold 2.5-fold higher space-time yields respectively, simultaneously reduced final mass factor 1.3, thus simplifying solid–liquid separation. This quantity host proteins remained be separated (by 34% 13%, respectively), reducing effort required in subsequent purification steps. Taken together, our increased overall performance production candidates.