dc.contributor.author |
Georgalaki, M |
en |
dc.contributor.author |
Papadelli, M |
en |
dc.contributor.author |
Chassioti, E |
en |
dc.contributor.author |
Anastasiou, R |
en |
dc.contributor.author |
Aktypis, A |
en |
dc.contributor.author |
De Vuyst, L |
en |
dc.contributor.author |
Van Driessche, G |
en |
dc.contributor.author |
Devreese, B |
en |
dc.contributor.author |
Tsakalidou, E |
en |
dc.date.accessioned |
2014-06-06T06:50:34Z |
|
dc.date.available |
2014-06-06T06:50:34Z |
|
dc.date.issued |
2010 |
en |
dc.identifier.issn |
00992240 |
en |
dc.identifier.uri |
http://dx.doi.org/10.1128/AEM.00151-09 |
en |
dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/5071 |
|
dc.subject.other |
Active fraction |
en |
dc.subject.other |
Autoinduction |
en |
dc.subject.other |
Bacteriocins |
en |
dc.subject.other |
Coculture |
en |
dc.subject.other |
Culture medium |
en |
dc.subject.other |
Heat-stable proteins |
en |
dc.subject.other |
Induction factors |
en |
dc.subject.other |
Lactoglobulin |
en |
dc.subject.other |
Lantibiotics |
en |
dc.subject.other |
Low molecular mass |
en |
dc.subject.other |
Milk protein |
en |
dc.subject.other |
Partial purification |
en |
dc.subject.other |
PCR approach |
en |
dc.subject.other |
Resistant strains |
en |
dc.subject.other |
Reverse transcription |
en |
dc.subject.other |
Tandem mass spectrometric |
en |
dc.subject.other |
Adhesive joints |
en |
dc.subject.other |
Biosynthesis |
en |
dc.subject.other |
Casein |
en |
dc.subject.other |
Chromatographic analysis |
en |
dc.subject.other |
Mass spectrometers |
en |
dc.subject.other |
Spectrometry |
en |
dc.subject.other |
Strain |
en |
dc.subject.other |
Sugars |
en |
dc.subject.other |
Biochemistry |
en |
dc.subject.other |
bacterial DNA |
en |
dc.subject.other |
bacteriocin |
en |
dc.subject.other |
casein |
en |
dc.subject.other |
human epithelial antigen 125 |
en |
dc.subject.other |
human epithelial antigen-125 |
en |
dc.subject.other |
lactoglobulin |
en |
dc.subject.other |
macedocin, Streptococcus macedonicus |
en |
dc.subject.other |
milk protein |
en |
dc.subject.other |
peptide fragment |
en |
dc.subject.other |
peptide hydrolase |
en |
dc.subject.other |
primer DNA |
en |
dc.subject.other |
tumor marker |
en |
dc.subject.other |
bacterium |
en |
dc.subject.other |
mass spectrometry |
en |
dc.subject.other |
milk |
en |
dc.subject.other |
polymerase chain reaction |
en |
dc.subject.other |
protein |
en |
dc.subject.other |
amino acid sequence |
en |
dc.subject.other |
animal |
en |
dc.subject.other |
article |
en |
dc.subject.other |
bacterial gene |
en |
dc.subject.other |
biosynthesis |
en |
dc.subject.other |
chemistry |
en |
dc.subject.other |
culture medium |
en |
dc.subject.other |
drug effect |
en |
dc.subject.other |
food control |
en |
dc.subject.other |
genetics |
en |
dc.subject.other |
growth, development and aging |
en |
dc.subject.other |
in vitro study |
en |
dc.subject.other |
metabolism |
en |
dc.subject.other |
molecular genetics |
en |
dc.subject.other |
nucleotide sequence |
en |
dc.subject.other |
Streptococcus |
en |
dc.subject.other |
tandem mass spectrometry |
en |
dc.subject.other |
Amino Acid Sequence |
en |
dc.subject.other |
Animals |
en |
dc.subject.other |
Bacteriocins |
en |
dc.subject.other |
Base Sequence |
en |
dc.subject.other |
Caseins |
en |
dc.subject.other |
Culture Media |
en |
dc.subject.other |
DNA Primers |
en |
dc.subject.other |
DNA, Bacterial |
en |
dc.subject.other |
Food Microbiology |
en |
dc.subject.other |
Genes, Bacterial |
en |
dc.subject.other |
Lactoglobulins |
en |
dc.subject.other |
Milk Proteins |
en |
dc.subject.other |
Molecular Sequence Data |
en |
dc.subject.other |
Peptide Fragments |
en |
dc.subject.other |
Peptide Hydrolases |
en |
dc.subject.other |
Streptococcus |
en |
dc.subject.other |
Tandem Mass Spectrometry |
en |
dc.subject.other |
Tumor Markers, Biological |
en |
dc.subject.other |
Streptococcus macedonicus |
en |
dc.title |
Milk protein fragments induce the biosynthesis of macedocin, the lantibiotic produced by Streptococcus macedonicus ACA-DC 198 |
en |
heal.type |
journalArticle |
en |
heal.identifier.primary |
10.1128/AEM.00151-09 |
en |
heal.publicationDate |
2010 |
en |
heal.abstract |
The aim of the present work was to study the mode of the induction of the biosynthesis of macedocin, the lantibiotic produced by Streptococcus macedonicus ACA-DC 198. Macedocin was produced when the strain was grown in milk but not in MRS or M17 broth. No autoinduction mechanism was observed. Production did not depend on the presence of lactose or galactose in the culture medium or on a coculture of the producer strain with macedocin-sensitive or macedocin-resistant strains. Induction seemed to depend on the presence of one or more heat-stable protein components produced when 5. macedonicus ACA-DC 198 was grown in milk. The partial purification of the induction factor was performed by a combination of chromatography methods, and its activity was confirmed by a reverse transcription-PCR approach (RT-PCR). Mass spectrometric (MS) and tandem mass spectrometric (MS/MS) analyses of an induction-active fraction showed the presence of several peptides of low molecular mass corresponding to fragments of αs1- and β-casein as well as β-lactoglobulin. The chemically synthesized βs1-casein fragment 37-55 (2,253.65 Da) was proven to be able to induce macedocin biosynthesis. This is the first time that milk protein degradation fragments are reported to exhibit a bacteriocin induction activity. Copyright © 2010, American Society for Microbiology. All Rights Reserved. |
en |
heal.journalName |
Applied and Environmental Microbiology |
en |
dc.identifier.issue |
4 |
en |
dc.identifier.volume |
76 |
en |
dc.identifier.doi |
10.1128/AEM.00151-09 |
en |
dc.identifier.spage |
1143 |
en |
dc.identifier.epage |
1151 |
en |