Monday, August 11, 2008
P62

Optimization of Recombinant Protein Secretion in Pfenex Expression Technology™

Russell Coleman1, Lawrence Chew2, Stacey Lee1, and Diane Retallack1. (1) Biopharma, The Dow Chemical Company, 5501 Oberlin Dr, San Diego, CA 92121, (2) Fermentation, Pfçnex Inc, 5501 Oberlin Dr, San Diego, CA 92121

The ability to export recombinant proteins to the periplasmic space enables the formation of a precise N-terminus and formation of disulfide bonds. Moreover, export to the periplasm can simplify downstream processing for protein recovery.  Multiple P. fluorescens secretion signal peptides have been evaluated for the ability to direct heterologous proteins to the periplasm. A high throughput screening method was developed to evaluate protein secretion in various P. fluorescens host strains. Several secretion signal peptides were shown to effectively enable secretion of recombinant proteins with precise N-terminal processing at the expected amino acid. Secretion signal peptides and host strains were identified that exhibited improved yield, solubility and advantaged recovery for model proteins.

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