Bacteriocins: Properties and potential use as antimicrobials

Darbandi, Atieh; Asadi, Arezoo; Ari, Marzie Mahdizade; Ohadi, Elnaz; Talebi, Malihe; Zadeh, Masoume Halaj; Emamie, Amir Darb; Ghanavati, Roya; Kakanj, Maryam

doi:10.1002/jcla.24093

Cited by 105 publications

(23 citation statements)

References 269 publications

(409 reference statements)

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“…Finally, CFCS were treated with protease and peptidase to determine whether the antibacterial active substances were peptide; the result turns out that CFCS were sensitive to all proteases except pepsin, of which trypsin was the most sensitive. Bacteriocins produced by lactic acid bacteria are sensitive to protease, especially to trypsin [ 17 ]; thus, it is speculated that the peptide produced by L-36 might be bacteriocins and might play a major antibacterial role ( Figure 2 ).…”

Section: Resultsmentioning

confidence: 99%

Antibacterial Effect of Cell-Free Supernatant from Lactobacillus pentosus L-36 against Staphylococcus aureus from Bovine Mastitis

Wang

Zeng

2022

Molecules

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This study sought to analyze the main antibacterial active components of Lactobacillus pentosus (L. pentosus) L-36 cell-free culture supernatants (CFCS) in inhibiting the growth of Staphylococcus aureus (S. aureus), to explore its physicochemical properties and anti-bacterial mechanism. Firstly, the main antibacterial active substance in L-36 CFCS was peptides, which inferred by adjusting pH and enzyme treatment methods. Secondly, the physicochemical properties of the antibacterial active substances in L-36 CFCS were studied from heat, pH, and metal ions, respectively. It demonstrated good antibacterial activity when heated at 65 °C, 85 °C and 100 °C for 10 and 30 min, indicating that it had strong thermal stability. L-36 CFCS had antibacterial activity when the pH value was 2–6, and the antibacterial active substances became stable with the decrease in pH value. After 10 kinds of metal ions were treated, the antibacterial activity did not change significantly, indicating that it was insensitive to metal ions. Finally, scanning electron microscopy, transmission electron microscopy and fluorescence probe were used to reveal the antibacterial mechanism of S. aureus from the aspects of cell morphology and subcellular structure. The results demonstrated that L-36 CFCS could form 1.4–2.3 nm pores in the cell membrane of S. aureus, which increased the permeability of the bacterial cell membrane, resulting in the depolarization of cell membrane potential and leakage of nucleic acid protein and other cell contents. Meanwhile, a large number of ROS are produced and accumulated in the cells, causing damage to DNA, and with the increase in L-36 CFCS concentration, the effect is enhanced, and finally leads to the death of S. aureus. Our study suggests that the main antibacterial active substances of L-36 CFCS are peptides. L-36 CFCS are thermostable, active under acidic conditions, insensitive to metal ions, and exhibit antibacterial effects by damaging cell membranes, DNA and increasing ROS. Using lactic acid bacteria to inhibit S. aureus provides a theoretical basis for the discovery of new antibacterial substances, and will have great significance in the development of antibiotic substitutes, reducing bacterial resistance and ensuring animal food safety.

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Section: Resultsmentioning

confidence: 99%

Antibacterial Effect of Cell-Free Supernatant from Lactobacillus pentosus L-36 against Staphylococcus aureus from Bovine Mastitis

Wang

Zeng

2022

Molecules

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“…The activity was reduced when purified enterocin KAE01 FPLC fractions were exposed to proteases such as pepsin, trypsin, chymotrypsin, and proteinase K. Circular bacteriocins (head-to-tail-ligated cyclic antimicrobial peptides), including circularin A, Microcin J25, gassercin A, and AS-48, have been found to be extremely resistant to being broken down by some proteases [ 57 , 58 ]. The three-dimensional shape of these circular peptides may make recognition sites inaccessible, rather than the lack of enzyme digestion sites being the cause of this resistance.…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization, Purification, and Mode of Action of Enterocin KAE01 from Lactic Acid Bacteria and Its In Silico Analysis against MDR/ESBL Pseudomonas aeruginosa

Bashir

Ali

Bux

et al. 2022

Genes

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Bacteriocins are gaining immense importance in therapeutics since they show significant antibacterial potential. This study reports the bacteriocin KAE01 from Enterococcus faecium, along with its characterization, molecular modeling, and antibacterial potency, by targeting the matrix protein of Pseudomonas aeruginosa. The bacteriocin was purified by using ammonium sulfate precipitation and fast protein liquid chromatography (FPLC), and its molecular weight was estimated as 55 kDa by means of SDS-PAGE. The bacteriocin was found to show stability in a wide range of pH values (2.0–10.0) and temperatures (100 °C for 1 h and 121 °C for 15 min). Antimicrobial screening of the purified peptide against different strains of P. aeruginosa showed its significant antibacterial potential. Scanning electron microscopy of bacteriocin-induced bacterial cultures revealed significant changes in the cellular morphology of the pathogens. In silico molecular modeling of KAE01, followed by molecular docking of the matrix protein (qSA) of P. aeruginosa and KAE01, supported the antibacterial potency and SEM findings of this study.

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“…The earliest findings of their presence in AMPs are as old as 1941, when they were detected in gramicidin and tyrocidine [57], and many more followed, as summarized in Table 1. Several groups arise from Bacillus [58] and Streptomyces strains [59], and it is well known that Gram-positive bacteria use AMPs, termed bacteriocins [60], as a strategy to strive in an ecological niche with competition from other micro-organisms [61]. Other important sources of AMPs are fungi [62] and frog skin secretions [63].…”

Section: Antimicrobial Peptides (Amps) With D-amino Acidsmentioning

confidence: 99%

Polymer Conjugates of Antimicrobial Peptides (AMPs) with d-Amino Acids (d-aa): State of the Art and Future Opportunities

et al. 2022

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In recent years, antimicrobial peptides (AMPs) have enjoyed a renaissance, as the world is currently facing an emergency in terms of severe infections that evade antibiotics’ treatment. This is due to the increasing emergence and spread of resistance mechanisms. Covalent conjugation with polymers is an interesting strategy to modulate the pharmacokinetic profile of AMPs and enhance their biocompatibility profile. It can also be an effective approach to develop active coatings for medical implants and devices, and to avoid biofilm formation on their surface. In this concise review, we focus on the last 5 years’ progress in this area, pertaining in particular to AMPs that contain d-amino acids, as well as their role, and the advantages that may arise from their introduction into AMPs.

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Bacteriocins: Properties and potential use as antimicrobials

Cited by 105 publications

References 269 publications

Antibacterial Effect of Cell-Free Supernatant from Lactobacillus pentosus L-36 against Staphylococcus aureus from Bovine Mastitis

Antibacterial Effect of Cell-Free Supernatant from Lactobacillus pentosus L-36 against Staphylococcus aureus from Bovine Mastitis

Molecular Characterization, Purification, and Mode of Action of Enterocin KAE01 from Lactic Acid Bacteria and Its In Silico Analysis against MDR/ESBL Pseudomonas aeruginosa

Polymer Conjugates of Antimicrobial Peptides (AMPs) with d-Amino Acids (d-aa): State of the Art and Future Opportunities

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