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

Plantaricin S, one of the two bacteriocins produced by Lactobacillus plantarum LPCO10, which was isolated from a green-olive fermentation (R. Jimenez-Diaz, R.M. Rios-Sanchez, M. Desmazeaud, J.L. Ruiz-Barba, and J.-C. Piard, Appl. Environ. Microbiol. 59:1416-1424, 1993), has been purified to homogene...

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Bibliographic Details
Published in:	Applied and Environmental Microbiology Vol. 61; no. 12; pp. 4459 - 4463
Main Authors:	Jimenez-Diaz, R. (Consejo Superior de Investigaciones Cientificas, Seville, Spain.), Ruiz-Barba, J.L, Cathcart, D.P, Holo, H, Nes, I.F, Sletten, K.H, Warner, P.J
Format:	Journal Article
Language:	English
Published:	Washington, DC American Society for Microbiology 01-12-1995
Subjects:	ACEITUNA AGENT DE CONSERVATION Amino Acid Sequence Amino acids Bacteria Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification BACTERIOCINAS BACTERIOCINE Bacteriocins - chemistry Bacteriocins - isolation & purification Bacteriocins - metabolism Bacteriology Biological and medical sciences COMPOSICION QUIMICA COMPOSITION CHIMIQUE FERMENTACION FERMENTATION Food industries Food microbiology Fundamental and applied biological sciences. Psychology Lactobacillus - metabolism LACTOBACILLUS PLANTARUM Microbiology Molecular Sequence Data OLIVE Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains PEPTIDE Peptide Fragments - chemistry Peptides PEPTIDOS PRESERVADORES PROPIEDADES ANTIMICROBIANAS PROPRIETE ANTIMICROBIENNE PURIFICACION PURIFICATION Lactobacillus plantarum Purification Peptides Bacteriocin Bacteria Lactobacillaceae Homology Biological activity Antimicrobial agent Aminoacid sequence
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Summary:	Plantaricin S, one of the two bacteriocins produced by Lactobacillus plantarum LPCO10, which was isolated from a green-olive fermentation (R. Jimenez-Diaz, R.M. Rios-Sanchez, M. Desmazeaud, J.L. Ruiz-Barba, and J.-C. Piard, Appl. Environ. Microbiol. 59:1416-1424, 1993), has been purified to homogeneity by ammonium sulfate precipitation, by binding to SP-Sepharose fast-flow, phenyl-Sepharose CL-4B, and C2/C18 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 alpha and beta, which were separated by C2/C18 reverse-phase chromatography. Although beta alone appeared to retain a trace of inhibitory activity, the complementary action of both the alpha and beta 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 alpha and beta, 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 alpha and beta show no apparent homology to each other or to other bacteriocins purified from lactic acid bacteria
Bibliography:	9600646 Q02 Q05 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0099-2240 1098-5336
DOI:	10.1128/aem.61.12.4459-4463.1995