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The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68

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2009
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Аутори
Dimitrijević, Rajna
Stojanović, Marijana
Živković, Irena
Petersen, Arnd
Jankov, Ratko
Dimitrijević, Ljiljana
Gavrović-Jankulović, Marija
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Апстракт
Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C,... 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.

Кључне речи:
bacteriocin / class II / isolation / Lactobacillus rhamnosus / rhamnosin A
Извор:
Journal of Applied Microbiology, 2009, 107, 6, 2108-2115
Издавач:
  • Wiley, Hoboken
Финансирање / пројекти:
  • Испитивање структуре и функције биолошки важних макромолекула у физиолошким и патолошким стањима (RS-142020)

DOI: 10.1111/j.1365-2672.2009.04539.x

ISSN: 1364-5072

PubMed: 19796123

WoS: 000271785400037

Scopus: 2-s2.0-72849108588
[ Google Scholar ]
24
21
URI
http://intor.torlakinstitut.com/handle/123456789/275
Колекције
  • Radovi istraživača / Researchers’ publications
Институција/група
Torlak
TY  - JOUR
AU  - Dimitrijević, Rajna
AU  - Stojanović, Marijana
AU  - Živković, Irena
AU  - Petersen, Arnd
AU  - Jankov, Ratko
AU  - Dimitrijević, Ljiljana
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://intor.torlakinstitut.com/handle/123456789/275
AB  - Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.
PB  - Wiley, Hoboken
T2  - Journal of Applied Microbiology
T1  - The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68
EP  - 2115
IS  - 6
SP  - 2108
VL  - 107
DO  - 10.1111/j.1365-2672.2009.04539.x
UR  - conv_244
ER  - 
@article{
author = "Dimitrijević, Rajna and Stojanović, Marijana and Živković, Irena and Petersen, Arnd and Jankov, Ratko and Dimitrijević, Ljiljana and Gavrović-Jankulović, Marija",
year = "2009",
abstract = "Aims: This study focuses on the isolation and characterization of a peptide with bacteriocin-like properties isolated from Lactobacillus rhamnosus strain 68, previously identified by 16S rRNA gene sequencing and originating from human gastrointestinal flora. Methods and Results: The peptide was isolated from a supernatant of bacteria maintained under restrictive conditions by a combination of ethanol precipitation and reversed-phase chromatography. The molecular mass of the peptide as assessed by mass spectrometry was 6433 center dot 8 Da. An isoelectric point of 9 center dot 8 was determined by 2D-PAGE. The peptide designated rhamnosin A inhibited Micrococcus lysodeikticus ATCC 4698 but did not inhibit Lactobacillus plantarum 8014 or Lact. plantarum 39268. Inhibitory activity against M. lysodeikticus at concentrations used in this study was shown to be bacteriostatic rather than bacteriolytic or bactericidal. Rhamnosin A retained biological activity after heat treatment (95 degrees C, 30 min) but was sensitive to proteolytic activity of pepsin and trypsin. Conclusions: The N-terminal sequence of rhamnosin A, as determined by Edman degradation and in more detail by blast analysis, did not show identity with any currently available Lact. rhamnosus HN001-translated protein sequences, nor any significant similarity with other sequences in the nonredundant protein sequence database. Being a small, heat-stable, nonlanthionine-containing peptide, rhamnosin A should be categorized as a class II bacteriocin. Significance and Impact of the Study: This study describes a partial bacteriocin sequence isolated from Lact. rhamnosus 68 and broadens our understanding of bacteriocins.",
publisher = "Wiley, Hoboken",
journal = "Journal of Applied Microbiology",
title = "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68",
pages = "2115-2108",
number = "6",
volume = "107",
doi = "10.1111/j.1365-2672.2009.04539.x",
url = "conv_244"
}
Dimitrijević, R., Stojanović, M., Živković, I., Petersen, A., Jankov, R., Dimitrijević, L.,& Gavrović-Jankulović, M.. (2009). The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. in Journal of Applied Microbiology
Wiley, Hoboken., 107(6), 2108-2115.
https://doi.org/10.1111/j.1365-2672.2009.04539.x
conv_244
Dimitrijević R, Stojanović M, Živković I, Petersen A, Jankov R, Dimitrijević L, Gavrović-Jankulović M. The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. in Journal of Applied Microbiology. 2009;107(6):2108-2115.
doi:10.1111/j.1365-2672.2009.04539.x
conv_244 .
Dimitrijević, Rajna, Stojanović, Marijana, Živković, Irena, Petersen, Arnd, Jankov, Ratko, Dimitrijević, Ljiljana, Gavrović-Jankulović, Marija, "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68" in Journal of Applied Microbiology, 107, no. 6 (2009):2108-2115,
https://doi.org/10.1111/j.1365-2672.2009.04539.x .,
conv_244 .

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