Class II antimicrobial peptides from lactic acid bacteria

Biopolymers ◽  
2000 ◽  
Vol 55 (1) ◽  
pp. 50-61 ◽  
Author(s):  
Ingolf F. Nes ◽  
Helge Holo
Author(s):  
R. Geetha ◽  
C. T. Sathian ◽  
V. Prasad ◽  
V. L. Gleeja

A study was carried out to assess the efficacy of purified antimicrobial peptides of lactic acid bacteria (LAB), isolated from partially decayed samples of food items, against selected clinical isolates of mastitis bacterial pathogens, <italic>viz</italic>., <italic>Escherichia coli</italic> (<italic>E.coli</italic>), <italic>Staphylococcus aureus</italic> (<italic>S.aureus</italic>) and <italic>Streptococcus agalactiae</italic> (<italic>S.agalactiae</italic>). The crude culture extracts (CCE) from LAB isolates were concentrated and purified by salting out method followed by dialysis. Partially purified peptides (T-5 CR -2 CR -3) from three LAB isolated from tomato and carrot showed a significantly higher inhibitory spectrum, with zone of inhibition ranging from 11.66±0.33 to 12.66±0.33 mm diameter against different test pathogens. The inhibitory efficiency of all the three peptides was found to be significantly superior to the peptides from reference strain <italic>Lactococcus lactis</italic> NCIM-2114. Minimum inhibitory concentration (MIC) of the purified peptide samples ranged between 0.79±0.09 to 1.11±0.09 μg/ml against different test pathogens. The activity of peptides was completely lost after treatment with protease, thereby confining their protein character.


Author(s):  
Helge Holo ◽  
Ingolf Nes ◽  
Havard Hildeng Hauge ◽  
Gunnar Fimland ◽  
Jon Nissen Meyer

2013 ◽  
Vol 2 (11) ◽  
pp. 643-650 ◽  
Author(s):  
Katherine Volzing ◽  
Juan Borrero ◽  
Michael J. Sadowsky ◽  
Yiannis N. Kaznessis

2019 ◽  
Vol 2019 ◽  
pp. 1-12 ◽  
Author(s):  
Roger J. da Costa ◽  
Flávia L. S. Voloski ◽  
Rafael G. Mondadori ◽  
Eduarda H. Duval ◽  
Ângela M. Fiorentini

Bacteriocins are ribosomal-synthesized antimicrobial peptides that inhibit the growing of pathogenic and/or deteriorating bacteria. The most studied bacteriocin-producing microorganisms are lactic acid bacteria (LAB), as they have great potential application in food biopreservation, since the majority have GRAS (Generally Recognized as Safe) status. The LAB-producing bacteriocins and/or bacteriocins produced by these bacteria have been widely studied, with the emphasis on those derived from milk and dairy products. On the other hand, isolates from meat and meat products are less studied. The objective of this review is to address the main characteristics, classification, and mechanism of action of bacteriocins and their use in food, to highlight studies on the isolation of LAB with bacteriocinogenic potential from meat and meat products and also to characterize, purify, and apply these bacteriocins in meat products. In summary, most of the microorganisms studied areLactococcus,Enterococcus,Pediococcus, andLactobacillus, which produce bacteriocins such as nisin, enterocin, pediocin, pentocin, and sakacin, many with the potential for use in food biopreservation.


2002 ◽  
Vol 68 (12) ◽  
pp. 6451-6456 ◽  
Author(s):  
Franck Biet ◽  
Yves Cenatiempo ◽  
Christophe Fremaux

ABSTRACT A 2,665-bp cryptic plasmid, pTXL1, isolated from Leuconostoc mesenteroides subsp. mesenteroides Y110 was identified. This plasmid harbors a replicon localized on a 1,300-bp fragment. Two observations suggested that pTXL1 does not belong to rolling-circle replication (RCR)-type plasmids and most likely replicates via a theta mechanism. These hypotheses are supported by the observation that no detectable single-stranded intermediate was found for the replicon and that, unlike in RCR-type plasmids, the pTXL1 replicon sequence lacks an open reading frame encoding a replicase. The small-sized pTXL1 plasmid is stable and, according to its origin, can be considered in the “generally recognized as safe” category. Its ability to replicate in several lactic acid bacteria was exploited to develop a vector producing mesentericin Y105, a class II anti-Listeria bacteriocin. With this new vector, a recombinant industrial Leuconostoc cremoris strain able to produce mesentericin Y105 was constructed.


2021 ◽  
Author(s):  
S. Keerthini ◽  
R. Kapilan ◽  
S. Vasantharuba

Abstract BackgroundProbiotic, Lactic Acid Bacteria (LAB) are consumed by human through the traditional food products for several decades due to their beneficial health effects. LAB is Gram positive, non motile bacteria that produce antimicrobial peptides for their defense mechanism. Among the antimicrobial peptides, Bacteriocins are widely investigated because of their possible utilization in food sector especially food security actions, where bacteriocin kills or inhibits the growth of other bacteria. Usage of metabolic products of LAB and LAB are generally recognized as safe. Therefore, this study was aimed to isolate LAB species that produce bacteriocin showing wide spectrum antibacterial activity.Results Lactic acid bacteria were isolated from yoghurt, curd, dosa batter, idli batter and soaked and ground rice batter using (De Man, Rogosa and Sharpe agar) MRS agar and incubated at room temperature (30±2ºC) for 24-72 h aerobically and anaerobically. When agar well diffusion method was employed to detect the antibacterial activity of the twenty five isolates against food spoilage organisms (Enterococcus faecalis, Staphylococcus aureus, Pseudomonas aeruginosa, E.coli, Klebsiella pneumoniae, Serratia marcescens, Salmonella sp., Proteus sp., Micrococcus sp., and Bacillus sp.,). Three bacterial species showing broad spectrum of antibacterial activity, were identified and characterized by biochemical and molecular methods. The wide spectrum antibacterial bacterial species were identified as Lactobacillus reuteri AF182723 isolated from curd, Lactobacillus rhamnosus AY299488 isolated from rice batter and Lactobacillus acidophilus AF182726 isolated from yoghurt. Among all the isolates, Lactobacillus reuteri AF182723 showed significant wide spectrum antibacterial activity against diverse Gram positive and Gram negative bacterial species. Conclusion The production of bacteriocin from Lactobacillus reuteri AF182723 and incorporating it in the food would inhibit the food spoilage organisms. Usage of this bacteriocin at appropriate concentration in food needs to be studied further.


2001 ◽  
Vol 7 (4) ◽  
pp. 281-305 ◽  
Author(s):  
L. M. Cintas ◽  
M. P. Casaus ◽  
C. Herranz ◽  
I. F. Nes ◽  
P. E. Hernández

During the last few years, a large number of new bacteriocins produced by lactic acid bacteria (LAB) have been identified and characterized. LAB-bacteriocins comprise a heterogeneous group of physicochemically diverse ribosomally-synthesized peptides or proteins showing a narrow or broad antimicrobial activity spectrum against Gram-positive bacteria. Bacteriocins are classified into separate groups such as the lantibiotics (Class I); the small (<10 kDa) heat-stable postranslationally unmodified non-lantibiotics (Class II), further subdivided in the pediocin-like and anti Listeria bacteriocins (subclass IIa), the two-peptide bacteriocins (subclass IIb), and the sec-dependent bacteriocins (subclass IIc); and the large (>30 kDa) heat-labile non-lantibiotics (Class III). Most bacteriocins characterized to date belong to Class II and are synthesized as precursor peptides (preprobacteriocins) containing an N-terminal double-glycine leader peptide, which is cleaved off concomitantly with externalization of biologically active bacteriocins by a dedicated ABC-transporter and its accessory protein. However, the recently identified sec-dependent bacteriocins contain an N-terminal signal peptide that directs bacteriocin secretion through the general secretory pathway (GSP). Most LAB-bacteriocins act on sensitive cells by destabilization and permeabilization of the cytoplasmic membrane through the formation of transitory poration complexes or ionic channels that cause the reduction or dissipation of the proton motive force (PMF). Bacteriocin producing LAB strains protect themselves against the toxicity of their own bacteriocins by the expression of a specific immunity protein which is generally encoded in the bacteriocin operon. Bacteriocin production in LAB is frequently regulated by a three-component signal transduction system consisting of an induction factor (IF), and histidine protein kinase (HPK) and a response regulator (RR). This paper presents an updated review on the general knowledge about physicochemical properties, molecular mode of action, biosynthesis, regulation and genetics of LAB-bacteriocins.


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