Bacteriocins are ribosomally produced antimicrobial peptides that are synthesized by various types of bacteria.  These peptides hold promise as potential food preservatives to prevent the growth of pathogens and spoilage bacteria.  Additionally, naturally produced bacteriocins generated by lactic acid bacteria (LAB) are of special interest due to their generally regarded as safe (GRAS) status in food production.  Analysis of the novel bacteriocin thermophilin 110 from Streptococcus thermophilus indicated that this peptide requires glycosylation for activity.  Elucidation of the primary sequence of this peptide is in progress.  We present here additional information on the properties of this bacteriocin, including an optimized purification protocol and isolation of active material from bacterial culture supernatant by cation exchange chromatography followed by reverse phase high performance liquid chromatography (RP-HPLC) of fully glycosylated material as well as deglycosylated peptide.  A comparison of the masses of glycosylated and deglycosylated material will aid in the elucidation of the overall amino acid sequence as well as determination of glycosylation sites in the bacteriocin.