P55: Screening of Yeast derived products for protein expression in Escherichia coli

Following the outstanding progress of recombinant DNA technology, the expression of heterologous genes in diverse hosts allows for bioproduction of a wide range of recombinant proteins. Several organisms are currently used for recombinant protein production. One of the most critical choices in bioprocess design is the selection of a suitable host relying on: i) cultivation facility, ii) easy genetic manipulation and availability of molecular tools, iii) ability of post-translational modifications e.g. glycosylation and iv) protein secretion and downstream purification. Among them, the easily genetically modifiable Escherichia coli is the most used bacteria as it has the advantage to grow rapidly on versatile substrates such as yeast hydrolysates and to yield high protein titer.

As the global leader in yeast extracts and yeast peptones manufacturing, Bio Springer provides high performance, animal free nutrients for biopharmaceuticals and bio-ingredients fermentation. In response to the rising demand for high quality and consistent protein hydrolysates, the Bio Springer Biotech Applications Lab has developed a bioperformance assay to investigate yeast-derived products contribution for recombinant protein production in E. coli and others microorganisms.

Many yeast-derived products were assessed separately or in combination for E. coli BL21 growth and GFP (expression marker) production. Our experimental strategy allows reaching high cell densities and GFP yields while reducing acetate formation. The results indicate that selecting the optimal yeast extract and yeast peptone is critical for high protein productivity. In addition, these findings provide further insights in our process of developing a new product line dedicated for recombinant protein production.