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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2000-1-10
pubmed:databankReference
pubmed:abstractText
The strongly hydrophobic bacteriocin amylovorin L471 from Lactobacillus amylovorus DCE 471 was isolated and purified to homogeneity from complex culture broth by a novel, rapid and simple three-step protocol including (i) ammonium sulphate precipitation, (ii) chloroform/methanol extraction/precipitation and (iii) reversed-phase HPLC, the only chromatographic step involved. The molecular mass of the peptide was determined to be 4876.9 Da by electrospray mass spectrometric analysis. N-terminal amino acid sequencing identified 35 amino acid residues as being identical to the N-terminal sequence of lactobin A, a bacteriocin from another L. amylovorus strain. These non-identical strains produce bacteriocins that display small differences in molecular mass and inhibitory spectrum. The amino acid sequence of amylovorin L471 shared significant homology with lactacin X, one of the two bactericidal peptides produced by Lactobacillus johnsonii VPI11088. A purified amylovorin L471 preparation permitted confirmation of the inhibitory spectrum previously established with a crude extract. It displayed a bactericidal mode of action on lactobacilli after an extremely rapid adsorption to the target cells. Two Listeria spp. were only weakly sensitive. Amylovorin L471 appears to be produced constitutively. Ethanol not only stimulated specific bacteriocin production but also prevented adsorption of the bacteriocin molecules to the producer cells upon prolonged fermentation. The latter result supports the hypothesis that the apparent inactivation of bacteriocin observed during the stationary phase of batch fermentations is due to adsorption.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1350-0872
pubmed:author
pubmed:issnType
Print
pubmed:volume
145 ( Pt 9)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2559-68
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Characterization and production of amylovorin L471, a bacteriocin purified from Lactobacillus amylovorus DCE 471 by a novel three-step method.
pubmed:affiliation
Research Group of Industrial Microbiology, Fermentation Technology and Downstream Processing, Department of Applied Biological Sciences, Vrije Universiteit Brussel, Brussels, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't