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Nisin

February 27, 2023

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.

Nisin
Identifiers
  • 1414-45-5 Y
3D model (JSmol)
  • Interactive image
ChEBI
  • CHEBI:71629 N
ChEMBL
  • ChEMBL526744 N
ChemSpider
  • 21106355 Y
ECHA InfoCard 100.014.370
E number E234 (preservatives)
  • 16219761
UNII
  • EN8XKG133D Y
  • DTXSID20893678
  • 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) Y
    Key: WAMGWAJCUSJZNI-UHFFFAOYSA-N Y
  • 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
Appearance powder
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).
N verify (what is YN ?)

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 milk or 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 DuPont), and approved as an additive for food use in the US in the late 1960s.[1]

Properties

While in general most bacteriocins 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 to avoid 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 has the ability to 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 can be 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 for the isolation of 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

  • Fukase, Koichi; Kitazawa, Manabu; Sano, Akihiko; Shimbo, Kuniaki; Fujita, Hiroshi; Horimoto, Shingo; Wakamiya, Tateaki; Shiba, Tetsuo (1988). "Total synthesis of peptide antibiotic nisin". Tetrahedron Letters. 29 (7): 795–798. doi:10.1016/s0040-4039(00)80212-9. (Total synthesis)
  • Buchman, GW; Banerjee, S; Hansen, JN (1988). "Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic". J Biol Chem. 263 (31): 16260–6. doi:10.1016/S0021-9258(18)37587-2. PMID 3141403. (Biosynthesis)
  • http://medicalxpress.com/news/2012-10-common-food-tumor-growth.html
  • Encyclopedia of Food Microbiology - Page 187 books.google.ae/books?ISBN 0123847338

References

  1. ^ ageconsearch.umn.edu/bitstream/90779/2/CP%2001%2005%20Nisin%20Report.pdf
  2. ^ a b c d 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.

External links

  • Nisin A
  • Nisin Z
  • Nisin Q
  • Nisin F
  • Nisin U

February 27, 2023
nisin, polycyclic, antibacterial, peptide, produced, bacterium, lactococcus, lactis, that, used, food, preservative, amino, acid, residues, including, uncommon, amino, acids, lanthionine, methyllanthionine, melan, didehydroalanine, didehydroaminobutyric, acid,. 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 Nisin IdentifiersCAS Number 1414 45 5 Y3D model JSmol Interactive imageChEBI CHEBI 71629 NChEMBL ChEMBL526744 NChemSpider 21106355 YECHA InfoCard 100 014 370E number E234 preservatives PubChem CID 16219761UNII EN8XKG133D YCompTox Dashboard EPA DTXSID20893678InChI 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 YKey WAMGWAJCUSJZNI UHFFFAOYSA N YInChI 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 UHFFFAOYABSMILES 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 OPropertiesChemical formula C143H230N42O37S7Molar mass 3354 07 g molAppearance powderDensity 1 402 g mLBoiling 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 N verify what is Y N Infobox references 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 milk or 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 DuPont and approved as an additive for food use in the US in the late 1960s 1 Contents 1 Properties 2 Applications 2 1 Food production 2 2 Other 3 Further reading 4 References 5 External linksProperties EditWhile in general most bacteriocins 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 to avoid 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 has the ability to 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 can be 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 EditFood production Edit 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 Edit Due to its naturally selective spectrum of activity it is also employed as a selective agent in microbiological media for the isolation of 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 EditFukase Koichi Kitazawa Manabu Sano Akihiko Shimbo Kuniaki Fujita Hiroshi Horimoto Shingo Wakamiya Tateaki Shiba Tetsuo 1988 Total synthesis of peptide antibiotic nisin Tetrahedron Letters 29 7 795 798 doi 10 1016 s0040 4039 00 80212 9 Total synthesis Buchman GW Banerjee S Hansen JN 1988 Structure expression and evolution of a gene encoding the precursor of nisin a small protein antibiotic J Biol Chem 263 31 16260 6 doi 10 1016 S0021 9258 18 37587 2 PMID 3141403 Biosynthesis http medicalxpress com news 2012 10 common food tumor growth html Encyclopedia of Food Microbiology Page 187 books google ae books ISBN 0123847338References Edit ageconsearch wbr umn wbr edu wbr bitstream wbr 90779 wbr 2 wbr CP 2001 2005 20Nisin 20Report wbr pdf a b c d 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 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 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 External links EditNisin A Nisin Z Nisin Q Nisin F Nisin U Retrieved from https en wikipedia org w index php title Nisin amp oldid 1125597212, wikipedia, wiki, book, books, library,

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