Interest in peptides as diagnostic and therapeutic materials require their manufacture via either a recombinant or synthetic route. This study examined the former, where a recombinant fusion consisting of an antifungal peptide was expressed and isolated from Escherichia coli. Fed batch fermentation with E. coli harboring an arabinose-inducible plasmid produced the 12 residue anti-Candida peptide fused to the N-terminal of Green Fluorescent Protein (GFP(UV)). The purification of the fusion protein, using ion-exchange chromatography, was monitored by using the intrinsic fluorescence of GFP(UV). The recombinant antifungal peptide was successfully released by cyanogen bromide-induced cleavage of the fusion protein. The recombinant peptide showed the expected antifungal activity. (c) 2016 American Institute of Chemical Engineers Biotechnol. Prog., 32:865-871, 2016