Faculty of Chemistry Repository - Cherry
University of Belgrade - Faculty of Chemistry
    • English
    • Српски
    • Српски (Serbia)
  • English 
    • English
    • Serbian (Cyrilic)
    • Serbian (Latin)
  • Login
View Item 
  •   Faculty of Chemistry Repository - Cherry
  • Hemijski fakultet
  • Publikacije
  • View Item
  •   Faculty of Chemistry Repository - Cherry
  • Hemijski fakultet
  • Publikacije
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

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

Authorized Users Only
2009
Authors
Dimitrijevic, R.
Stojanovic, M.
Zivkovic, I.
Petersen, A.
Jankov, Ratko M.
Dimitrijevic, L.
Gavrović-Jankulović, Marija
Article (Published version)
Metadata
Show full item record
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.

Keywords:
bacteriocin / class II / isolation / Lactobacillus rhamnosus / rhamnosin A
Source:
Journal of Applied Microbiology, 2009, 107, 6, 2108-2115
Publisher:
  • Wiley-Blackwell, Hoboken
Projects:
  • Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima (RS-142020)
Note:
  • Free full text: https://doi.org/10.1111/j.1365-2672.2009.04539.x

DOI: 10.1111/j.1365-2672.2009.04539.x

ISSN: 1364-5072

PubMed: 19796123

WoS: 000271785400037

Scopus: 2-s2.0-72849108588
[ Google Scholar ]
19
17
URI
http://cherry.chem.bg.ac.rs/handle/123456789/1028
Collections
  • Publikacije
Institution
Hemijski fakultet
TY  - JOUR
AU  - Dimitrijevic, R.
AU  - Stojanovic, M.
AU  - Zivkovic, I.
AU  - Petersen, A.
AU  - Jankov, Ratko M.
AU  - Dimitrijevic, L.
AU  - Gavrović-Jankulović, Marija
PY  - 2009
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1028
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-Blackwell, Hoboken
T2  - Journal of Applied Microbiology
T1  - The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68
VL  - 107
IS  - 6
SP  - 2108
EP  - 2115
DO  - 10.1111/j.1365-2672.2009.04539.x
ER  - 
@article{
author = "Dimitrijevic, R. and Stojanovic, M. and Zivkovic, I. and Petersen, A. and Jankov, Ratko M. and Dimitrijevic, L. and Gavrović-Jankulović, Marija",
year = "2009",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1028",
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-Blackwell, Hoboken",
journal = "Journal of Applied Microbiology",
title = "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68",
volume = "107",
number = "6",
pages = "2108-2115",
doi = "10.1111/j.1365-2672.2009.04539.x"
}
Dimitrijevic R, Stojanovic M, Zivkovic I, Petersen A, Jankov RM, Dimitrijevic L, Gavrović-Jankulović M. The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68. Journal of Applied Microbiology. 2009;107(6):2108-2115
Dimitrijevic, R., Stojanovic, M., Zivkovic, I., Petersen, A., Jankov, R. M., Dimitrijevic, L.,& Gavrović-Jankulović, M. (2009). The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68.
Journal of Applied MicrobiologyWiley-Blackwell, Hoboken., 107(6), 2108-2115.
https://doi.org/10.1111/j.1365-2672.2009.04539.x
Dimitrijevic R., Stojanovic M., Zivkovic I., Petersen A., Jankov Ratko M., Dimitrijevic L., Gavrović-Jankulović Marija, "The identification of a low molecular mass bacteriocin, rhamnosin A, produced by Lactobacillus rhamnosus strain 68" 107, no. 6 (2009):2108-2115,
https://doi.org/10.1111/j.1365-2672.2009.04539.x .

DSpace software copyright © 2002-2015  DuraSpace
About CHERRY - CHEmistry RepositoRY | Send Feedback

OpenAIRERCUB
 

 

All of DSpaceInstitutionsAuthorsTitlesSubjectsThis institutionAuthorsTitlesSubjects

Statistics

View Usage Statistics

DSpace software copyright © 2002-2015  DuraSpace
About CHERRY - CHEmistry RepositoRY | Send Feedback

OpenAIRERCUB