נגישות
menu      
Advanced Search
Syntax
Search...
Volcani treasures
About
Terms of use
Manage
Community:
אסיף מאגר המחקר החקלאי
Powered by ClearMash Solutions Ltd -
Purification, partial characterization and plasmid‐linkage of pediocin SJ‐1, a bacteriocin produced by Pediococcus acidilactici
Year:
1993
Source of publication :
Journal of Applied Bacteriology
Authors :
Lalazar, Avraham
;
.
Schved, Fernando
;
.
Volume :
74
Co-Authors:
Schved, F., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, Bet Dagan, Israel
Lalazar, A., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, Bet Dagan, Israel
Henis, Y., Department of Plant Pathology, Otto Warburg Centre for Biotechnology in Agriculture, Hebrew University of Jerusalem, Faculty of Agriculture, Rehovot, Israel
Juven, B.J., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, Bet Dagan, Israel
Facilitators :
From page:
67
To page:
77
(
Total pages:
11
)
Abstract:
Pediococcus acidilactici SJ‐1, isolated from a naturally‐fermented meat product, produced an antibacterial agent active against selected strains of Lactobacillus spp., Clostridium perfringens and Listeria monocytogenes. The agent was bactericidal against sensitive indicators, and sensitive to proteolytic enzymes; it was identified as a bacteriocin, and was designated as pediocin SJ‐1. It was stable over a wide pH range (3–9), and apparently most stable in the lower part of that range. At pH 3.6, pediocin SJ‐1 was stable at heat‐processing temperatures within the range 65–121°C; its activity decreased significantly, however, when it was heated at pH 7.0. The activity of pediocin SJ‐1 on sensitive indicator cells was lost in the presence of α‐amylase, suggesting that it contains a glyco moiety, necessary for its antibacterial action. Native pediocin SJ‐1 exists in the form of monomers and aggregates (with molecular weights in the range 80–150 kDa). Pediocin SJ‐1 was purified 262‐fold by direct application of cell‐free supernatant fluids to a cation‐exchange chromatography column, and was resolved by SDS‐PAGE as a single peptide band with a MW of ca 4 kDa. The original pediocin SJ‐1‐producing strain (bac+) harbours three plasmids of 4.6, 23.5, and 45.7 MDa. Production of pediocin SJ‐1, but not immunity to SJ‐1, is associated with the 4.6 MDa plasmid. Copyright © 1993, Wiley Blackwell. All rights reserved
Note:
Related Files :
bacteriocin
Bacteriocins
biosynthesis
Clostridium perfringens
Pediococcus
Plasmid
temperature
Show More
Related Content
More details
DOI :
10.1111/j.1365-2672.1993.tb02998.x
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
30962
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:58
You may also be interested in
Scientific Publication
Purification, partial characterization and plasmid‐linkage of pediocin SJ‐1, a bacteriocin produced by Pediococcus acidilactici
74
Schved, F., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, Bet Dagan, Israel
Lalazar, A., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, Bet Dagan, Israel
Henis, Y., Department of Plant Pathology, Otto Warburg Centre for Biotechnology in Agriculture, Hebrew University of Jerusalem, Faculty of Agriculture, Rehovot, Israel
Juven, B.J., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, Volcani Center, Bet Dagan, Israel
Purification, partial characterization and plasmid‐linkage of pediocin SJ‐1, a bacteriocin produced by Pediococcus acidilactici
Pediococcus acidilactici SJ‐1, isolated from a naturally‐fermented meat product, produced an antibacterial agent active against selected strains of Lactobacillus spp., Clostridium perfringens and Listeria monocytogenes. The agent was bactericidal against sensitive indicators, and sensitive to proteolytic enzymes; it was identified as a bacteriocin, and was designated as pediocin SJ‐1. It was stable over a wide pH range (3–9), and apparently most stable in the lower part of that range. At pH 3.6, pediocin SJ‐1 was stable at heat‐processing temperatures within the range 65–121°C; its activity decreased significantly, however, when it was heated at pH 7.0. The activity of pediocin SJ‐1 on sensitive indicator cells was lost in the presence of α‐amylase, suggesting that it contains a glyco moiety, necessary for its antibacterial action. Native pediocin SJ‐1 exists in the form of monomers and aggregates (with molecular weights in the range 80–150 kDa). Pediocin SJ‐1 was purified 262‐fold by direct application of cell‐free supernatant fluids to a cation‐exchange chromatography column, and was resolved by SDS‐PAGE as a single peptide band with a MW of ca 4 kDa. The original pediocin SJ‐1‐producing strain (bac+) harbours three plasmids of 4.6, 23.5, and 45.7 MDa. Production of pediocin SJ‐1, but not immunity to SJ‐1, is associated with the 4.6 MDa plasmid. Copyright © 1993, Wiley Blackwell. All rights reserved
Scientific Publication
You may also be interested in