Nisin

Last updated
Nisin
Nisin.png
Nisin 1WCO.png
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
ECHA InfoCard 100.014.370 OOjs UI icon edit-ltr-progressive.svg
E number E234 (preservatives)
PubChem CID
UNII
  • InChI=1S/C143H246N42O45S7/c1-22-68(10)104(148)134(220)183-111(76(18)193)140(226)173-93(57-189)127(213)179-107(70(12)24-3)138(224)172-91(55-187)125(211)166-86(45-66(6)7)120(206)175-98(62-235)132(218)184-112(77(19)194)142(228)185-41-31-35-99(185)133(219)152-53-103(198)158-94(58-231)128(214)161-81(33-26-29-39-145)117(203)181-108(73(15)190)135(221)153-51-101(196)156-71(13)113(199)165-85(44-65(4)5)119(205)162-82(36-42-236-20)115(201)151-52-102(197)159-95(59-232)129(215)168-89(48-100(147)195)122(208)163-83(37-43-237-21)116(202)160-80(32-25-28-38-144)118(204)182-109(74(16)191)139(225)157-72(14)114(200)180-110(75(17)192)141(227)176-97(61-234)130(216)167-87(46-78-49-149-63-154-78)121(207)174-96(60-233)131(217)170-92(56-188)126(212)178-106(69(11)23-2)137(223)169-88(47-79-50-150-64-155-79)123(209)177-105(67(8)9)136(222)171-90(54-186)124(210)164-84(143(229)230)34-27-30-40-146/h49-50,63-77,80-99,104-112,186-194,231-235H,22-48,51-62,144-146,148H2,1-21H3,(H2,147,195)(H,149,154)(H,150,155)(H,151,201)(H,152,219)(H,153,221)(H,156,196)(H,157,225)(H,158,198)(H,159,197)(H,160,202)(H,161,214)(H,162,205)(H,163,208)(H,164,210)(H,165,199)(H,166,211)(H,167,216)(H,168,215)(H,169,223)(H,170,217)(H,171,222)(H,172,224)(H,173,226)(H,174,207)(H,175,206)(H,176,227)(H,177,209)(H,178,212)(H,179,213)(H,180,200)(H,181,203)(H,182,204)(H,183,220)(H,184,218)(H,229,230) Yes check.svgY
    Key: WAMGWAJCUSJZNI-UHFFFAOYSA-N Yes check.svgY
  • InChI=1/C143H246N42O45S7/c1-22-68(10)104(148)134(220)183-111(76(18)193)140(226)173-93(57-189)127(213)179-107(70(12)24-3)138(224)172-91(55-187)125(211)166-86(45-66(6)7)120(206)175-98(62-235)132(218)184-112(77(19)194)142(228)185-41-31-35-99(185)133(219)152-53-103(198)158-94(58-231)128(214)161-81(33-26-29-39-145)117(203)181-108(73(15)190)135(221)153-51-101(196)156-71(13)113(199)165-85(44-65(4)5)119(205)162-82(36-42-236-20)115(201)151-52-102(197)159-95(59-232)129(215)168-89(48-100(147)195)122(208)163-83(37-43-237-21)116(202)160-80(32-25-28-38-144)118(204)182-109(74(16)191)139(225)157-72(14)114(200)180-110(75(17)192)141(227)176-97(61-234)130(216)167-87(46-78-49-149-63-154-78)121(207)174-96(60-233)131(217)170-92(56-188)126(212)178-106(69(11)23-2)137(223)169-88(47-79-50-150-64-155-79)123(209)177-105(67(8)9)136(222)171-90(54-186)124(210)164-84(143(229)230)34-27-30-40-146/h49-50,63-77,80-99,104-112,186-194,231-235H,22-48,51-62,144-146,148H2,1-21H3,(H2,147,195)(H,149,154)(H,150,155)(H,151,201)(H,152,219)(H,153,221)(H,156,196)(H,157,225)(H,158,198)(H,159,197)(H,160,202)(H,161,214)(H,162,205)(H,163,208)(H,164,210)(H,165,199)(H,166,211)(H,167,216)(H,168,215)(H,169,223)(H,170,217)(H,171,222)(H,172,224)(H,173,226)(H,174,207)(H,175,206)(H,176,227)(H,177,209)(H,178,212)(H,179,213)(H,180,200)(H,181,203)(H,182,204)(H,183,220)(H,184,218)(H,229,230)
    Key: WAMGWAJCUSJZNI-UHFFFAOYAB
  • C[C@H](CC)[C@@H](N)C(N/C(C(N[C@@H]1C(N[C@@H](C(NC(C(N[C@@H](C(N[C@@H](C(N[C@H](C(N2[C@@H](C(NC3)=O)CCC2)=O)[C@@H](C)SC[C@H](C(N[C@H](CCCCN)C(N[C@H](C(NCC(N[C@@H](C(N[C@H](CC(C)C)C(N[C@H](CCSC)C(NCC(N[C@@H](C(N[C@H](CC(N)=O)C(N[C@H](CCSC)C(N[C@H](CCCCN)C(N[C@@H]([C@@H](C)SC[C@@H](N6)C(N[C@H](CC5=CN=CN5)C(N[C@@H](C(N[C@H](CO)C(N[C@H]([C@@H](CC)C)C(N[C@H](CC8=CN=CN8)C(N[C@H]([C@@H](C)C)C(NC(C(N[C@H](CCCCN)C(O)=O)=O)=C)=O)=O)=O)=O)=O)CS[C@H](C)[C@H]7C6=O)=O)=O)C(N[C@H](C)C(N7)=O)=O)=O)=O)=O)=O)CS4)=O)=O)=O)=O)C)=O)=O)[C@H]4C)=O)=O)NC3=O)=O)CSC1)=O)CC(C)C)=O)=C)=O)[C@H](C)CC)=O)=O)=C\C)=O
Properties
C143H230N42O37S7
Molar mass 3354.07 g/mol
Appearancepowder
Density 1.402 g/mL
Boiling point 2,966 °C (5,371 °F; 3,239 K)
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Nisin is a polycyclic antibacterial peptide produced by the bacterium Lactococcus lactis that is used as a food preservative. It has 34 amino acid residues, including the uncommon amino acids lanthionine (Lan), methyllanthionine (MeLan), didehydroalanine (Dha), and didehydroaminobutyric acid (Dhb). These unusual amino acids are introduced by posttranslational modification of the precursor peptide. In these reactions a ribosomally synthesized 57-mer is converted to the final peptide. The unsaturated amino acids originate from serine and threonine, and the enzyme-catalysed addition of cysteine residues to the didehydro amino acids result in the multiple (5) thioether bridges.

Contents

Subtilin and epidermin are related to nisin. All are members of a class of molecules known as lantibiotics.

In the food industry, nisin is obtained from the culturing of L. lactis on natural substrates, such as dextrose, and it is not chemically synthesized.

It was originally isolated in the late 1930s, and produced since the 1950s as Nisaplin from naturally occurring sources by Aplin and Barrett in laboratories in Beaminster in Dorset (now owned by International Flavors & Fragrances), and approved as an additive for food use in the US in the late 1960s. [1]

Properties

While most bacteriocins generally inhibit only closely related species, nisin is a rare example of a "broad-spectrum" bacteriocin effective against many Gram-positive organisms, including lactic acid bacteria (commonly associated with avoiding food spoilage), Listeria monocytogenes (a known pathogen), Staphylococcus aureus , Bacillus cereus , Clostridium botulinum , etc. [2] It is also particularly effective against spores. Gram-negative bacteria are protected by their outer membrane but may become susceptible to nisin action after a heat shock or when this is coupled with the chelator EDTA. When used in combination with EDTA, nisin can inhibit E. coli O157:H7 and Salmonella enterica . [2] Nisin, as a class I bacteriocin, is very stable at acidic pHs and is more heat stable at lower pHs. [2] The mode of action of Nisin against pathogens such as L. monocytogenes is to dissipate the membrane potential and pH gradient. [2]

Nisin is soluble in water and effective at levels nearing the parts-per-billion range. Nisin concentration can be measured using various techniques such as chromatography or by a simple agar diffusion bioassay. [3]

Applications

Food production

Nisin is used in processed cheese, meats, beverages, etc. during production to extend shelf life by suppressing Gram-positive spoilage and pathogenic bacteria.[ citation needed ] In foods, it is common to use nisin at levels ranging from ~1-25 ppm, depending on the food type and regulatory approval. As a food additive, nisin has an E number of E234.

Other

Due to its naturally selective spectrum of activity, it is also employed as a selective agent in microbiological media to isolate gram-negative bacteria, yeast, and moulds.

Nisin has also been used in food packaging applications and can serve as a preservative by controlled release onto the food surface from the polymer packaging. [4]

In combination with miconazole it has been studied as a possible treatment for infections of Clostridium difficile .[ citation needed ]

Further reading

Related Research Articles

<span class="mw-page-title-main">Food preservation</span> Inhibition of microbial growth in food

Food preservation includes processes that make food more resistant to microorganism growth and slow the oxidation of fats. This slows down the decomposition and rancidification process. Food preservation may also include processes that inhibit visual deterioration, such as the enzymatic browning reaction in apples after they are cut during food preparation. By preserving food, food waste can be reduced, which is an important way to decrease production costs and increase the efficiency of food systems, improve food security and nutrition and contribute towards environmental sustainability. For instance, it can reduce the environmental impact of food production.

Peptidoglycan or murein is a unique large macromolecule, a polysaccharide, consisting of sugars and amino acids that forms a mesh-like peptidoglycan layer (sacculus) that surrounds the bacterial cytoplasmic membrane. The sugar component consists of alternating residues of β-(1,4) linked N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM). Attached to the N-acetylmuramic acid is an oligopeptide chain made of three to five amino acids. The peptide chain can be cross-linked to the peptide chain of another strand forming the 3D mesh-like layer. Peptidoglycan serves a structural role in the bacterial cell wall, giving structural strength, as well as counteracting the osmotic pressure of the cytoplasm. This repetitive linking results in a dense peptidoglycan layer which is critical for maintaining cell form and withstanding high osmotic pressures, and it is regularly replaced by peptidoglycan production. Peptidoglycan hydrolysis and synthesis are two processes that must occur in order for cells to grow and multiply, a technique carried out in three stages: clipping of current material, insertion of new material, and re-crosslinking of existing material to new material.

<span class="mw-page-title-main">Bacteriocin</span> Class of bacterially produced peptide antibiotics

Bacteriocins are proteinaceous or peptidic toxins produced by bacteria to inhibit the growth of similar or closely related bacterial strain(s). They are similar to yeast and paramecium killing factors, and are structurally, functionally, and ecologically diverse. Applications of bacteriocins are being tested to assess their application as narrow-spectrum antibiotics.

<span class="mw-page-title-main">Lanthionine</span> Chemical compound

Lanthionine is a nonproteinogenic amino acid with the chemical formula (HOOC-CH(NH2)-CH2-S-CH2-CH(NH2)-COOH). It is typically formed by a cysteine residue and a dehydrated serine residue. Despite its name, lanthionine does not contain the element lanthanum.

<span class="mw-page-title-main">Dehydroalanine</span> Chemical compound

Dehydroalanine is a dehydroamino acid. It does not exist in its free form, but it occurs naturally as a residue found in peptides of microbial origin. As an amino acid residue, it is unusual because it has an unsaturated backbone.

Lantibiotics are a class of polycyclic peptide antibiotics that contain the characteristic thioether amino acids lanthionine or methyllanthionine, as well as the unsaturated amino acids dehydroalanine, and 2-aminoisobutyric acid. They belong to ribosomally synthesized and post-translationally modified peptides.

<i>Lactococcus lactis</i> Species of bacterium

Lactococcus lactis is a gram-positive bacterium used extensively in the production of buttermilk and cheese, but has also become famous as the first genetically modified organism to be used alive for the treatment of human disease. L. lactis cells are cocci that group in pairs and short chains, and, depending on growth conditions, appear ovoid with a typical length of 0.5 - 1.5 µm. L. lactis does not produce spores (nonsporulating) and are not motile (nonmotile). They have a homofermentative metabolism, meaning they produce lactic acid from sugars. They've also been reported to produce exclusive L-(+)-lactic acid. However, reported D-(−)-lactic acid can be produced when cultured at low pH. The capability to produce lactic acid is one of the reasons why L. lactis is one of the most important microorganisms in the dairy industry. Based on its history in food fermentation, L. lactis has generally recognized as safe (GRAS) status, with few case reports of it being an opportunistic pathogen.

Mutacin 1140 is a bacteriocin produced by Streptococcus mutans. It has activity against a broad spectrum of Gram-positive bacteria. It is a member of the class of compounds known as lantibiotics.

<span class="mw-page-title-main">Lactic acid bacteria</span> Order of bacteria

Lactobacillales are an order of gram-positive, low-GC, acid-tolerant, generally nonsporulating, nonrespiring, either rod-shaped (bacilli) or spherical (cocci) bacteria that share common metabolic and physiological characteristics. These bacteria, usually found in decomposing plants and milk products, produce lactic acid as the major metabolic end product of carbohydrate fermentation, giving them the common name lactic acid bacteria (LAB).

<span class="mw-page-title-main">Food microbiology</span> Study of the microorganisms that inhibit, create, or contaminate food

Food microbiology is the study of the microorganisms that inhabit, create, or contaminate food. This includes the study of microorganisms causing food spoilage; pathogens that may cause disease ; microbes used to produce fermented foods such as cheese, yogurt, bread, beer, and wine; and microbes with other useful roles, such as producing probiotics.

<span class="mw-page-title-main">Class II bacteriocin</span>

Class II bacteriocins are a class of small peptides that inhibit the growth of various bacteria.

Sakacins are bacteriocins produced by Lactobacillus sakei. They are often clustered with the other lactic acid bacteriocins. The best known sakacins are sakacin A, G, K, P, and Q. In particular, sakacin A and P have been well characterized.

<span class="mw-page-title-main">Biopreservation</span>

Biopreservation is the use of natural or controlled microbiota or antimicrobials as a way of preserving food and extending its shelf life. The biopreservation of food, especially utilizing lactic acid bacteria (LAB) that are inhibitory to food spoilage microbes, has been practiced since early ages, at first unconsciously but eventually with an increasingly robust scientific foundation. Beneficial bacteria or the fermentation products produced by these bacteria are used in biopreservation to control spoilage and render pathogens inactive in food. There are a various modes of action through which microorganisms can interfere with the growth of others such as organic acid production, resulting in a reduction of pH and the antimicrobial activity of the un-dissociated acid molecules, a wide variety of small inhibitory molecules including hydrogen peroxide, etc. It is a benign ecological approach which is gaining increasing attention.

Hurdle technology is a method of ensuring that pathogens in food products can be eliminated or controlled. This means the food products will be safe for consumption, and their shelf life will be extended. Hurdle technology usually works by combining more than one approach. These approaches can be thought of as "hurdles" the pathogen has to overcome if it is to remain active in the food. The right combination of hurdles can ensure all pathogens are eliminated or rendered harmless in the final product.

<span class="mw-page-title-main">Food spoilage</span> Often due to bacteria and fungi

Food spoilage is the process where a food product becomes unsuitable to ingest by the consumer. The cause of such a process is due to many outside factors as a side-effect of the type of product it is, as well as how the product is packaged and stored. Due to food spoilage, one-third of the world's food produced for the consumption of humans is lost every year. Bacteria and various fungi are the cause of spoilage and can create serious consequences for the consumers, but there are preventive measures that can be taken.

Bisin is a naturally occurring lantibiotic discovered by University of Minnesota microbiologist Dan O'Sullivan. Unlike earlier lantibiotics discovered, such as nisin, bisin also kills Gram-negative bacteria, including E. coli, Salmonella and Listeria.

<i>Latilactobacillus sakei</i> Species of bacterium

Latilactobacillus sakei is the type species of the genus Latilactobacillus that was previously classified in the genus Lactobacillus. It is homofermentative; hexoses are metabolized via glycolysis to lactic acid as main metabolite; pentoses are fermented via the Phosphoketolase pathway to lactic and acetic acids.

Ribosomally synthesized and post-translationally modified peptides (RiPPs), also known as ribosomal natural products, are a diverse class of natural products of ribosomal origin. Consisting of more than 20 sub-classes, RiPPs are produced by a variety of organisms, including prokaryotes, eukaryotes, and archaea, and they possess a wide range of biological functions.

<span class="mw-page-title-main">Lipid II</span> Chemical compound

Lipid II is a precursor molecule in the synthesis of the cell wall of bacteria. It is a peptidoglycan, which is amphipathic and named for its bactoprenol hydrocarbon chain, which acts as a lipid anchor, embedding itself in the bacterial cell membrane. Lipid II must translocate across the cell membrane to deliver and incorporate its disaccharide-pentapeptide "building block" into the peptidoglycan mesh. Lipid II is the target of several antibiotics.

Proteobiotics are natural metabolites which are produced by fermentation process of specific probiotic strains. These small oligopeptides were originally discovered in and isolated from culture media used to grow probiotic bacteria and may account for some of the health benefits of probiotics.

References

  1. ↑ ageconsearch.umn.edu/bitstream/90779/2/CP%2001%2005%20Nisin%20Report.pdf
  2. 1 2 3 4 And, H. Chen; Hoover, D. G. (2003). "Bacteriocins and their Food Applications". Comprehensive Reviews in Food Science and Food Safety. 2 (3): 82–100. doi:10.1111/j.1541-4337.2003.tb00016.x. ISSN   1541-4337. PMID   33451234.
  3. ↑ Chandrasekar, Vaishnavi (2015). "Modeling development of inhibition zones in an agar diffusion bioassay". Food Science and Nutrition. 3 (5): 394–403. doi:10.1002/fsn3.232. PMC   4576963 . PMID   26405525.
  4. ↑ Chandrasekar, Vaishnavi (2017). "Release Kinetics of Nisin from Chitosan–Alginate Complex Films". Journal of Food Science. 81 (10): E2503–E2510. doi:10.1111/1750-3841.13443. PMID   27635864.
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