2016 AIChE Annual Meeting

(336b) Anti-Candida Peptide Production Using a Recombinant Expression Platform

Authors

Rudra Palash Mukherjee - Presenter, University of Arkansas
Rita Tejada Vaprio, University of Arkansas
Ellen M. Brune, University of Arkansas
McKinzie Fruchtl, University of Arkansas
Bob Beitle, University of Arkansas
A smart design for recombinant peptide expression of various lengths is possible with the knowledge of target product, cell line, fermentation strategy, and downstream recovery options. Using a novel anti-Candida peptide as an illustrative example, we show that the combination of a cell line engineered with a reduced host cell proteome (Lotus®), and a mutant version of Green Fluorescent Protein that is chemically resistant confers several advantages for bioprocessing. Specifically, the use of this newEscherichia coli strain permitted a 37% increase in column capacity for the primary capture step (ion exchange) and purification from a CNBr-digested mixture was greatly simplified as the number of peptides were reduced. In all, the blending of judicious mutations provide an argument for the recombinant approach to peptide manufacturing, especially as the length of the product increases.