Pichia pastoris is widely used as a host for recombinant protein production and shows great promise for use in biotherapeutics. More than 500 proteins have been expressed in the organism at a variety of cultivation scales, from small shake flasks to large bioreactors. Large-scale fermentation strategies typically employ chemically-defined growth media because of its greater batch-to-batch consistency and in many cases, lower cost compared to complex media. For biopharmaceuticals, defined growth media may also simplify downstream purification and regulatory documentation. Standard formulations of defined media for Pichia are minimal ones that lack the metabolic intermediates provided by complex components such as peptone and yeast extract. As a result, growth rates and per-cell productivities are significantly lower than in complex media. In this talk, we describe our approach to developing a general media for Pichia pastoris based on metabolic profiling, transcriptomics, and high-throughput screening in microtiter plates. We also demonstrate the use of this media for expression of multiple heterologous proteins. This general media has the potential to accelerate process development for new molecules and to improve productivity of Pichia pastoris fermentations.

Development of a general defined media for Pichia pastoris protein expression

253rd National Meeting (2017)

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