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Titolo:
Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19
Autore:
Atrih, A; Rekhif, N; Moir, AJG; Lebrihi, A; Lefebvre, G;
Indirizzi:
INPT, ENSAT, Lab Chem Engn Fermentat & Bioreactors, F-31326 Auzeville Tolosane, France INPT Auzeville Tolosane France F-31326 -31326 Auzeville Tolosane, France Univ Sheffield, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield Sheffield S Yorkshire England S10 2TN S Yorkshire, England Nestec Ltd, Nestle Res Ctr, CH-1000 Lausanne, Switzerland Nestec Ltd Lausanne Switzerland CH-1000 r, CH-1000 Lausanne, Switzerland
Titolo Testata:
INTERNATIONAL JOURNAL OF FOOD MICROBIOLOGY
fascicolo: 1-2, volume: 68, anno: 2001,
pagine: 93 - 104
SICI:
0168-1605(20010815)68:1-2<93:MOAPAA>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTIBACTERIAL SUBSTANCE; 2-PEPTIDE BACTERIOCINS; STRAINS; EF; JK;
Keywords:
Lactobacillus plantarum; plantaricin C19; purification; amino acid sequence; mode of action;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Lebrihi, A INPT, ENSAT, Lab Chem Engn Fermentat & Bioreactors, 1 Ave Agrobiopole,BP107, F-31326 Auzeville Tolosane, France INPT 1 Ave Agrobiopole,BP107 Auzeville Tolosane France F-31326
Citazione:
A. Atrih et al., "Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19", INT J F MIC, 68(1-2), 2001, pp. 93-104

Abstract

Plantaricin C19, an anti-Listeria bacteriocin, was successfully purified by adsorption to and release from producing cells at low pH combined with reverse phase high-performance liquid chromatography (HPLC). The purificationresulted in a 900-fold increase in specific activity with a yield of 15% of the original activity. Mass spectrometry analysis gave a molecular weightof 3845.3. Protein microsequencing identified 36 amino acids. Plantaricin C19 is rich in both hydrophobic and basic amino acids in good accordance with its basic and hydrophobic character. Comparison of the amino acid sequence of plantaricin C19, with the sequence of some other anti-Listeria bacteriocins produced with lactic acid bacteria, revealed that plantaricin C19 has in its N-terminal region the consensus sequence-YYGNGL-(uniquely with Valine instead of Leucine as found in all other bacteriocins), identifying plantaricin C 19 as a pediocin-like bacteriocin. Plantaricin C 19 exerted a bacteriostatic action on sensitive cells of Listeria grayi IP 6818 in BHT broth. No loss of intracellular K+, Mg2+ or UV-absorbing materials was observed. Adsorption of plantaricin C19 on L. grayi CIP 6818 decreased in the presence of salts. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 12:20:13