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Natural Preservatives
Published in Philip A. Geis, Cosmetic Microbiology, 2020
Nisin, a 34 amino acid bacteriocin shown in Figure 3.7 (22), produced by Lactococcus lactis and among the most studied of bacteriocins due to its use in the food industry, is inhibitory to a range of vegetative and spore-forming Gram-positive bacteria, including Bacillus, Clostridium, and Listeria. Some studies suggest that the range of antimicrobial activity can be extended to Gram-negative bacteria via the use of potentiators such as chelants (23) and hurdle technologies.
Cell-Cell Communication in Lactic Acid Bacteria
Published in Marcela Albuquerque Cavalcanti de Albuquerque, Alejandra de Moreno de LeBlanc, Jean Guy LeBlanc, Raquel Bedani, Lactic Acid Bacteria, 2020
Emília Maria França Lima, Beatriz Ximena Valencia Quecán, Luciana Rodrigues da Cunha, Bernadette Dora Gombossy de Melo Franco, Uelinton Manoel Pinto
Nisin was the first bacteriocin produced by a LAB to be approved for use in foods, and has been considered as an excellent preservative, because it has the capacity to act as an inhibitor of several types of Gram-positive bacteria such as strains of Streptococcus, Enterococcus, Staphylococcus, Micrococcus, Pediococcus, Lactobacillus, Listeria and Mycobacterium, but not in Gram-negative bacteria due to their outer membrane barrier (Williams and Delves-Broughton 2003, Arauz et al. 2009, Punyauppa-path et al. 2015, Jung et al. 2018). This is an antimicrobial agent considered as GRAS (Generally Recognized as Safe) and it was evaluated to be safe for use in foods by the Joint Food and Agriculture Organization/World Health Organization (FAO/WHO) (Arauz et al. 2009, Rul and Monnet 2015, Jung et al. 2018).
Natural and physical preservative systems
Published in R. M. Baird, S. F. Bloomfield, Microbial quality assurance in cosmetics, toiletries and non-sterile Pharmaceuticals, 2017
Nisin, a bacteriocin produced by Lactococcus lactis has been widely used as a food preservative for many years. (Delves-Broughton et al. 1992). Nisin and Pep 5, another peptide antibiotic, have been shown to have activity against Gram-positive bacteria but little or no activity against Gram-negative bacteria and fungi. This resistance is due to lack of penetration of the peptide into the outer membrane of Gram-negative bacteria (Sahl et al. 1986). However, recent studies have shown that disruption of the outer membrane of Gram-negative bacteria by the use of chelating agents can make them susceptible to the bactericidal effect of nisin (Stevens et al. 1991).
Blautia—a new functional genus with potential probiotic properties?
Published in Gut Microbes, 2021
Xuemei Liu, Bingyong Mao, Jiayu Gu, Jiaying Wu, Shumao Cui, Gang Wang, Jianxin Zhao, Hao Zhang, Wei Chen
Secondary metabolites are biologically active compounds produced by microorganisms during growth and metabolism and widely used in antibacterial and anticancer drugs, herbicides, and insecticides, which were also an important source of microbial drug development.86,87 According to the categories, there were more than 20 kinds of secondary metabolites, such as polyketides (PKS), non-ribosomal peptides (NRPS), lantipeptides/lantibiotics, bacteriocins, and terpenes.88 As early as 1980, bacteriocins produced by bifidobacteria were reported to possess antibacterial activity against pathogenic microorganisms such as Listeria monocytogenes, Clostridium perfringens, and Escherichia coli.89 Nisin, which is produced by Lactococcus lactis, is used as a natural food preservative.90 According to the chemical structures and mechanisms of action, bacteriocins are divided into four classes, and sactipeptides and lanthipeptides are post-translationally modified antibacterial peptides belonging to class I bacteriocins.91
Inhibition and eradication of Salmonella Typhimurium biofilm using P22 bacteriophage, EDTA and nisin
Published in Biofouling, 2018
Fatma Neslihan Yüksel, Sencer Buzrul, Mustafa Akçelik, Nefise Akçelik
As expected, eradication of biofilm was more difficult than inhibition and the maximum biofilm reduction achieved was only 51% by the use of 20 mM of EDTA and 150 µg ml−1 of nisin. The major problem in combating Salmonella is its outer membrane (OM) which contains a lipopolysaccharide lipid bilayer. This layer acts as a barrier against many compounds including antibiotics, hydrophobic compounds, detergents and dyes (Vaara 1992, Raetz and Whitfield 2002). The anionic lipopolysaccharide lipid bilayer is stabilized with divalent cations. If these cations are removed, the lipopolysaccharide molecules are released from OM and the integrity of the OM is disrupted (Vaara 1992). When only nisin is used, it is generally ineffective against Gram-negative microorganisms. However, if the nisin is used with a chelating agent such as EDTA, penetration of the antimicrobial agent into the bacterial cell is provided by opening of the porin channels (Chaudhary and Payasi 2012).
Improving the attrition rate of Lanthipeptide discovery for commercial applications
Published in Expert Opinion on Drug Discovery, 2018
Nisin has been used as food preservative for over 50 years without inducing significant resistance [49]. However, it has poor pharmacokinetics and is susceptible to proteolytic degradation and oxidation. The half-life of nisin was determined to be 0.9 h and nisin was not detectable after 3 h in a mouse model [50]. Nisin can be inactivated by chymotrypsin, trypsin, and thermolysin. The trypsin digestion of nisin yielded a proteolytic stable N-terminal fragment 1–12 containing rings A and B [51]. By attaching a series of lipids to the C-terminus of trypsin digested nisin, a subset of synthesized compounds was demonstrated to possess similar antibiotic activity with enhanced stability [52]. After 24 h incubation of nisin with human serum, only 33% of nisin remained intact, while up to 94% of four semisynthetic nisin variants remained intact, as determined by the peak area ratio corresponding to intact peptide. Nisin is also susceptible to oxidation, due to the presence of methionine residues. Exposure to hydrogen peroxide for 72 h resulted in a 60% loss of activity for nisin A, which contains two methionine residues, while only a 36% loss of activity for nisin Q, which contains only one methionine residue [53]. Amino acid substitutions at these positions need to be further evaluated in the future to determine whether these mutations can further improve its stability. Another type I lanthipeptide, mutacin 1140, which has potent activity against all tested gram-positive bacteria, is also susceptible to trypsin digestion and has poor pharmacokinetics. In a rat intravenously injection model, mutacin 1140 was administered at final dose of 12.5 or 25 mg/kg rat body weight. Blood was collected at times 1, 5, 10, 20, 30 min, 1, 2, 4, and 6 h post-dosing, and was analyzed by LC–MS to detect the concentration of mutacin 1140 within plasma. The half-life of mutacin 1140 was calculated to be around 1.6 h [54].