Purification and characterization of a peptide from Bacillus licheniformis showing dual antimicrobial and emulsifying activities

Bacillus licheniformis strain P40 produces a bacteriocin-like substance (BLS) that inhibits important pathogenic and food spoilage bacteria such as Listeria monocytogenes, Streptococcus spp., Bacillus cereus, and Erwinia carotovora. The antimicrobial peptide produced by B. licheniformis P40 was purified by ammonium sulfate precipitation, gel filtration chromatography on Sephadex G-100 and reversed phase chromatography on Source-RPC. The purification was about 100-fold with a yield of 0.3%. The molecular mass of the purified BLS about 800 Da, as determined by mass spectroscopy. The BLS was resistant for up to 100 °C and pH ranging 3–10, but lost its activity when treated with proteases and trichloroacetic acid. Reaction with ninhydrin produced the yellowish color instead the characteristic purple. Data from infrared spectroscopy also indicate the peptide is cyclic, resembling the lipopeptides surfactin and lichenisin. The BLS also showed emulsifying properties with several hydrophobic compounds, and dual antimicrobial and emulsifying activity in a meat model system. This antimicrobial peptide presents potential for use in as a food biopreservative or biodetergent.