Nisin, A Lantibiotic Produced by Lactococcus Lactis Subsp. Lactis: Properties, Biosynthesis, Fermentation and Applications

Vuyst, Luc De; Vandamme, Erick

doi:10.1007/978-1-4615-2668-1_5

Cited by 130 publications

(115 citation statements)

References 234 publications

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“…Furthermore, since GFP fluorescence is induced solely by photoactivation, no substrate addition is required. The simplicity of the GFP test allows analysis of hundreds of samples at the same time to detect 45 ng of nisin per ml in milk, 0.9 g of nisin per g in cheese, and 1 g of nisin per g in salad dressings, compared to the levels of more than 1 g/ml or 1 g/g used in food manufacturing (9,34), and makes it possible to analyze nisin in different kind of food matrices. Therefore, the GFP assay could be widely used in the food industry, as well as in basic research.…”

Section: Discussionmentioning

confidence: 99%

Microplate Bioassay for Nisin in Foods, Based on Nisin-Induced Green Fluorescent Protein Fluorescence

Reunanen

Saris

2003

Appl Environ Microbiol

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A plasmid coding for the nisin two-component regulatory proteins, NisK and NisR, was constructed; in this plasmid a gfp gene (encoding the green fluorescent protein) was placed under control of the nisin-inducible nisF promoter. The plasmid was transformed into non-nisin-producing Lactococcus lactis strain MG1614. The new strain could sense extracellular nisin and transduce it to green fluorescent protein fluorescence. The amount of fluorescence was dependent on the nisin concentration, and it could be measured easily. By using this strain, an assay for quantification of nisin was developed. With this method it was possible to measure as little as 2.5 ng of pure nisin per ml in culture supernatant, 45 ng of nisin per ml in milk, 0.9 g of nisin in cheese, and 1 g of nisin per ml in salad dressings.The type A lantibiotic nisin (16), produced by some Lactococcus lactis strains, is a small antimicrobial peptide that inhibits the growth of a wide range of gram-positive bacteria, such as Bacillus, Clostridium, Listeria, and Staphylococcus species. It is nontoxic to humans (19) and is broadly used as a food preservative (E234) (6) in more than 50 countries, including the United States, countries in the European Union, and the People's Republic of China. So far, two natural nisin variants, nisin A (4) and nisin Z (15, 25), which differ in a single amino acid residue, have been described. National laws concerning the presence and maximum levels of nisin in different food products vary greatly (1). Therefore, there is a demand by national food authorities for better methods to identify and quantify nisin reliably in different food matrices. The inhibitory effect of nisin on a given test organism (9) is the basis for most quantification methods that have been developed so far. The sensitivity and accuracy of the agar diffusion method (13,35) are affected by several parameters (38). Moreover, due to the better diffusion properties of nisin Z, it produces larger inhibition zones than equal amounts of nisin A produce (8). Immunological tests have also been described. Falahee et al. (12) described an enzyme-linked immunosorbent assay (ELISA) for nisin A in cheese based on sheep polyclonal antibodies. This method is considerably more sensitive than the agar diffusion assay, but it is not totally reliable due to cross-reactivity with the lantibiotic subtilin (11). Suárez et al. developed competitive direct ELISAs for nisin with polyclonal (31) and monoclonal (32) antibodies from mice. Bouksaim et al. (2) described an immunodot detection method in which rabbit antiserum against nisin Z in milk and whey is used. The same authors (3) also introduced an ELISA method in which affinity-purified polyclonal rabbit antibodies are used for quantification of nisin Z in complex media and milk. The flow injection immunoassay described by Nandakumar et al. (26) has an advantage over the other nisin quantification methods because it allows workers to monitor the concentration of nisin in a fermentation broth online. Dadoudi et al. (5) develope...

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Section: Discussionmentioning

confidence: 99%

Microplate Bioassay for Nisin in Foods, Based on Nisin-Induced Green Fluorescent Protein Fluorescence

Reunanen

Saris

2003

Appl Environ Microbiol

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“…In canned foods, there are two commonlyassociated spoilage organisms, B. stearothermophilus and C. thermosaccharolyticum. Addition of nisin in the range of100-200 IU g-1 controlled these pathogens and positively contributed to overall nutritional and organoleptic properties of the canned product (De Vuyst et a.,1994).Nisin was also used in high acid canned foods such as in canned tomato and fruit juices to control Clostridium pasteurianum and Bacillus spp. (Delves et al,1990).…”

Section: Potential Application Of Lab and Bacteriocins In The Food Inmentioning

confidence: 99%

Bacteriocin as an advanced technology in food industry

Delesa¹

2017

Int. J. Adv. Res. Biol. Sci.

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Concentration in novel biological preservation has increased during recent years, supported by research indicating that antagonistic microorganisms or their antimicrobial metabolites may have some potential as natural preservativesto control the growth of pathogenic bacteria in foods, andalso to control mycotoxinogenic fungi. Bacteriocins produced by lactic acid bacteria (LAB) are attracting considerable interest as food preservatives and safe alternatives to conventional antimicrobials in food industry as novel technology .The current global response to these useful bacteriocins needs to be improved by genetic or metabolic engineering. Due to the alarming rise in antibiotic resistance and adverse effects provoked by a number of antibiotics, bacteriocins have been applied in several fields: human health, food industry, animal health, and medicine, in particular as a substitution for the traditional growth promoters, antibiotics. Lactic Acid Bacteria (LAB) bacterocins are likely used because of their "safe" (GRAS) status, especially in food industry as bio-preservatives. Among these LAB bacteriocins, commercially marketed, nisin groups produced by Lactococcus lactis subsp. lactis and pediocins produced by Pediococcus sp., are the most characterized by their antibacterial property. Several LAB bacteriocins offer potential applications in food preservation, and the use of bacteriocins in the food industry can help to reduce the additionof chemical preservatives as well as the intensity of heat treatments, resulting in foods which are more naturallypreserved and richer in organoleptic and nutritional properties. This can be an alternative to satisfy the increasing consumers demands for safe, fresh-tasting, ready-to-eat, minimally-processed foods and also to develop "novel" food products (e.g. less acidic, or with a lower salt content). Therefore, this review paper is intention to discuss the novel and attractive application of bacteriocin producing by Lactic acid bacteria as innovative technology in food industry.

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“…However, certain strains of LAB are further known to produce bioactive molecules such as ethanol, formic acid, fatty acids, hydrogen peroxide, diacetyl, reuterin, and reutericyclin. Many strains also produce bacteriocins and bacteriocin-like molecules that display antibacterial activity [38][39][40]. Bacteriocins are generally considered to act at the cytoplasmic membrane and dissipate the proton motive force through the formation of pores in the membrane.…”

Section: Figure 3 Growth Inhibition Of Penicillium Candidum By Ppblsmentioning

confidence: 99%

Extending the Shelf Life of Camembert Cheese via Controlling Over-Ripening by Bacteriocin of Newly Lactic Acid Bacterial Isolate LAB100

Khider¹,

Elbanna²

2017

IJNFS

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Camembert cheese is a surface white mould ripened cheese; when full ripe the casein becomes liquefy as the intensive degradation occurs by proteinases from surface flora and results over-ripening and off flavor. To control this, partial purified bacteriocin like substances (PPBLS) from newly lactic acid bacterial isolate (LAB100) exhibited antifungal activity against Penicillium candidum (in vitro) were used. Inhibition (%) of P. candidum by PPBLS at concentrations of 2, 4, 8, 16 and 32 mg/ml was 34, 50, 79, 80 and 85%, respectively. Based on their superior antifungal potential activity; isolate LAB100 was phenotypically and genotypically characterized as newly Lactobacillus sp. For delaying the Camembert cheese over-ripening (in vivo), bacteriocin producing isolate LAB100 and its PPBLS were incorporated and applied in different camembert cheese treatments. Three treatments beside control were conducted; after brining all cheese treatments stored at 12±2°C to ripen for 12 days and then at 5±2°C for more 30 days to complete ripening. Organoleptic properties, pH values and nitrogen distribution were determined during ripening period. In addition, the proteolysis of treated Camembert cheese was monitored by gel electrophoresis. The cheese treatment (T2) made with bacteriocin producer isolate LAB 100 added as co-culture to main starter recorded the highest total score, followed by T3 and the lowest one was recorded for control (T1). The highest WSN/TN% was in T1; 5. 4, 22.87, 34.41 and 57.65% at 3, 10, 20, and 40 days after brining, respectively, while the lowest WSN/TN% was recorded for treatment that made with both bacteriocin producer strain LAB100 and sprayed by PPBLS solution after 3 days of brining (T3), where it was 5.05, 9.85, 13.82, and 31.74% at the same previous ages, respectively. These results were confirmed by gel electrophoresis, indicating that bacteriocin producer LAB100 and or its bacteriocin controlled the protein degradation. These results suggest that both bacteriocin producer strain and its PPBLS minimize the growth of P. candidum as a consequence the rate of proteolysis was controlled and hence extending the shelf life of Camembert cheese is occurred.

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Nisin, A Lantibiotic Produced by Lactococcus Lactis Subsp. Lactis: Properties, Biosynthesis, Fermentation and Applications

Cited by 130 publications

References 234 publications

Microplate Bioassay for Nisin in Foods, Based on Nisin-Induced Green Fluorescent Protein Fluorescence

Microplate Bioassay for Nisin in Foods, Based on Nisin-Induced Green Fluorescent Protein Fluorescence

Bacteriocin as an advanced technology in food industry

Extending the Shelf Life of Camembert Cheese via Controlling Over-Ripening by Bacteriocin of Newly Lactic Acid Bacterial Isolate LAB100

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