Anti-Candida Peptide Production Using a Recombinant Expression Platform

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.