Pichia pastoris (Komagataella phaffii) is an established, FDA approved, safe (GRAS) and highly competitive expression host with strong secretory capacities while secreting only low amounts of endogenous proteins. Today, a large number of recombinant protein products on the market (pharma and non-pharma applications) are produced in Pichia pastoris.

The yeast P. pastoris combines the advantages of prokaryotes, such as easy genetic manipulation and fast growth on inexpensive & chemically defined media with eukaryotic features such as a subcellular protein processing machinery needed for post-translational modification.

Yet another advantageous feature is Pichia´s ability to actively and effectively secrete recombinant target proteins into the culture supernatant with an exceptionally low amount of extracellular endogenous proteins furnishing a raw product with high purity. Thus, Pichia not only enables cultivation processes with high volumetric productivity but also simplifies downstream processes rendering manufacturing of recombinant proteins even more economically viable.

As compared to e.g. E. coli, no cell lysis and tedious isolation from a usually very crude lysate or refolding from inclusion bodies is required to obtain the target protein. At the same time the probability of unwanted enzymatic side activities is minimized.