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Two cationic antimicrobial peptides, salvicin K (sal K) and antimicrobial-like bacteriocin (alb ) from Lactobacillus salivarius K4 were isolated from chicken intestine. In the active form, each peptide contains 47 amino acids with 2 cysteine residues. The antimicrobial activity showed that sal K could inhibit the food pathogens Enterococcus faecalis JCM 5803, Lb. plantarum ATCC 14917, and Streptococcus sp. TISTR 1030. The alb showed activity against E. faecalis JCM 5803, Leuconostoc mesenteroides subsp. mesenteroides JCM 6124, Lb. sakei TISTR 890, Lb. plantarum ATCC 14917, and Streptococcus sp. TISTR 1030. A high concentration of these bacteriocins was found to cause hemolysis in rat erythrocytes. Each peptide was predicted to have a mixed secondary structure of -helix, -sheet, and random coil structure with one disulphide bond. Two antimicrobial peptides were found to be unstructured in Tris-Cl pH 9. These two peptides adopted an -helix conformation in 10% SDS micelles (to simulate the bacterial cell wall). In zwitterionic dodecylphosphocholine micelles and liposome, these two peptides adopted a -sheet structure. The results suggest that the -helix is an important conformation for these peptides to express their antimicrobial activity.

Antimicrobial peptides of Lactobacillus salivarius K4 isolated from chicken intestine