Purification and partial amino acid sequence of plantaricin S, a bacteriocin produced by Lactobacillus plantarum LPCO10, the activity of which depends on the complementary action of two peptides

Abstract

been purified to homogeneity by ammonium sulfate precipitation, by binding to SP-Sepharose fast-flow, phenyl-Sepharose CL-4B, and C 2 /C 18 reverse-phase chromatographies. The purification resulted in a final yield of 91.6% and a 352,617-fold increase in the specific activity. The bacteriocin activity was associated with two distinct peptides, termed ␣ and ␤, which were separated by C 2 /C 18 reverse-phase chromatography. Although ␤ alone appeared to retain a trace of inhibitory activity, the complementary action of both the ␣ and ␤ peptides was required for full bacteriocin activity, as judged by both the agar well diffusion and the microtiter plate assays. From the N-terminal end, 26 and 24 amino acids residues of ␣ and ␤, respectively, were sequenced. Further attempts at sequencing revealed no additional amino acids residues, suggesting that either modifications in the next amino acid residue blocked the sequencing region or that the C-terminal end had been reached. The amino acid sequences of ␣ and ␤ show no apparent homology to each other or to other bacteriocins purified from lactic acid bacteria.

Isolation, purification and partial characterization of plantaricin 423, a bacteriocin produced by Lactobacillus plantarum

“…This also conforms to the classification of Klaenhammer (1993). Plantaricins that have been completely © 1998 The Society for Applied Microbiology, Journal of Applied Microbiology 84, [1131][1132][1133][1134][1135][1136][1137] characterized are all smaller than 10 kDa (Nissen-Meyer et al 1993 ;González et al 1994 ;Kato et al 1994 ;Jiménez-Díaz et al 1995).…”

“…(Atrih et al 1993 ;Garriga et al 1993), but their relatedness to the class IIa bacteriocins has, to the authors' knowledge, not been established. Plantaricins A, S, C and 149 have been completely characterized (Jiménez-Díaz et al 1995), but none of these are classified as Listeria-active peptides and they do not show DNA homology with any of the pediocins described.…”

Thein vitroeffect of hydrogen peroxide on vaginal microbial communities

“…peptide bacteriocins are more effective in the later phase of the Lactobacillus-Candida interactions (Jimenez-Diaz et al, 1995;Graz et al, 1999;Ström et al, 2002).…”

Lantibiotics: structure, biosynthesis and mode of action

“…the FNLDV box, and have a net negative or slightly positive charge. This group also possesses a conserved Ser 63 and Pro 23 . When mutations were created in the 318 to 315 region (i.e., the FNLD consensus of the nisin leader) the secretion or intracellular accumulation of nisin was undetectable, indicating that even conservative changes in this highly conserved region leads to a block in nisin production [101].…”