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Modification of Nisin

Yıl 2017, Cilt: 8 Sayı: Ek (Suppl.) 1, 239 - 244, 16.11.2017
https://doi.org/10.29048/makufebed.342554

Öz

Bacteriocin nisin, an
antimicrobial lantibiotic peptide, is produced by Lactococcus lactis and is effective against Gram positive bacteria.
Nisin is used as a natural preservative to control the growth of
bacteria in foods, such as cheese, liquid egg, salad dressings, canned foods,
meat and meat products.
Nisin has been awarded the
"GRAS" (Generally Recognized as Safe) designation by the United States
Food and Drug Administration (FDA), and also has been approved as a food
additive by the World Health Organization (WHO) because of its non-toxic nature
to humans and other mammalians.
Although nisin is a natural preservative, its application as a food
preservative is limited due to its low solubility in neutral and slightly
alkaline solutions, restricted antibacterial spectrum, high production cost,
and high sensitivity to proteolytic enzymes.
Therefore, attempts are being made to overcome the
problems mentioned above with various applications including genetic and
chemical modifications. In this review, different methods applied in the
modification of nisin, and the findings obtained are discussed.

Kaynakça

  • Aasen, I. M., Markussen, S., Moretro, T., Katla, T., Axelsson, L., Naterstad, K. (2003). Interactions of the bacteriocins sakacin P and nisin with food constituents. International Journal of Food Microbiology 87: 35-43.
  • Abdullah, S. U., Badaruddin, M., Ali, R., Riaz, M. N. (2010). Effect of elementary and advanced glycation products of nisin on its preservative efficacy and digestibility. Food Chemistry 122: 1043-1046. doi: 10.1016/j.foodchem.2009.07.065
  • Bonev, B. B., Breukink, E., Swiezewska, E., De Kruijff, B., Watts, A. (2004). Targeting extracellular pyrophosphates underpins the high selectivity of nisin. Faseb Journal 18: 1862-1869. doi: 10.1096/fj.04-2358com
  • Breukink, E., de Kruijff, B. (1999). The lantibiotic nisin, a special case or not?. Biochimica Et Biophysica Acta-Biomembranes 1462: 223-234. doi: Doi 10.1016/S0005-2736(99)00208-4
  • Breukink, Eefjan, de Kruijff, Ben. (2006). Lipid II as a target for antibiotics. Nature reviews. Drug discovery 5: 321.
  • Brumfitt, W., Salton, M. R. J., Hamilton-Miller, J. M. T. (2002). Nisin, alone and combined with peptidoglycan-modulating antibiotics: activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci. Journal of Antimicrobial Chemotherapy 50: 731-734. doi: 10.1093/jac/dkf190
  • Cleveland, J., Montville, T. J., Nes, I. F., Chikindas, M. L. (2001). Bacteriocins: safe, natural antimicrobials for food preservation. International Journal of Food Microbiology 71: 1-20.
  • De Vuyst, Luc, Vandamme, Erick J 1994. Nisin, a lantibiotic produced by Lactococcus lactis subsp. lactis: properties, biosynthesis, fermentation and applications. In Bacteriocins of lactic acid bacteria, 151-221: Springer.
  • Dischinger, J., Chipalu, S. B., Bierbaum, G. (2014). Lantibiotics: Promising candidates for future applications in health care. International Journal of Medical Microbiology 304: 51-62. doi: 10.1016/j.ijmm.2013.09.003
  • Feeney, R. E., Yamasaki, R. B., Geoghegan, K. F. (1982). Chemical Modification of Proteins - an Overview. Advances in Chemistry Series: 3-55.
  • Field, D., Begley, M., O'Connor, P. M., Daly, K. M., Hugenholtz, F., Cotter, P. D., Hill, C., Ross, R. P. (2012). Bioengineered Nisin A Derivatives with Enhanced Activity against Both Gram Positive and Gram Negative Pathogens. Plos One 7. doi: ARTN e4688410.1371/journal.pone.0046884
  • Field, D., Connor, P. M. O., Cotter, P. D., Hill, C., Ross, R. P. (2008). The generation of nisin variants with enhanced activity against specific Gram-positive pathogens. Molecular Microbiology 69: 218-230.
  • Galvez, A., Abriouel, H., Lopez, R. L., Ben Omar, N. (2007). Bacteriocin-based strategies for food biopreservation. International Journal of Food Microbiology 120: 51-70.
  • Gross, Erhard, Morell, John L. (1971). Structure of nisin. Journal of the American Chemical Society 93: 4634-4635.
  • Guiotto, Andrea, Pozzobon, Michela, Canevari, Mirta, Manganelli, Riccardo, Scarin, Marino, Veronese, Francesco M. (2003). PEGylation of the antimicrobial peptide nisin A: problems and perspectives. Il Farmaco 58: 45-50.
  • Hansen, J. N. (1994). Nisin as a Model Food Preservative. Critical Reviews in Food Science and Nutrition 34: 69-93.
  • Klaenhammer, T. R. (1993). Genetics of Bacteriocins Produced by Lactic-Acid Bacteria. Fems Microbiology Reviews 12: 39-86.
  • Koponen, O., Tolonen, M., Qiao, M. Q., Wahlstrom, G., Helin, J., Saris, P. E. J. (2002). NisB is required for the dehydration and NisC for the lanthionine formation in the post-translational modification of nisin. Microbiology-Sgm 148: 3561-3568.
  • Kuipers, O. P., Rollema, H. S., Beerthuyzen, M. M., Siezen, R. J., deVos, W. M. (1995). Protein engineering and biosynthesis of nisin and regulation of transcription of the structural nisA gene. International Dairy Journal 5: 785-795.
  • Kuipers, Oscar P, Rollema, Harry S, Yap, WM, Boot, Hein J, Siezen, Roland J, de Vos, Willem M. (1992). Engineering dehydrated amino acid residues in the antimicrobial peptide nisin. Journal of Biological Chemistry 267: 24340-24346.
  • Liu, W., Hansen, J. N. (1990). Some Chemical and Physical-Properties of Nisin, a Small-Protein Antibiotic Produced by Lactococcus-Lactis. Applied and Environmental Microbiology 56: 2551-2558.
  • Lopes, Nathalie Almeida, Pinilla, Cristian Mauricio Barreto, Brandelli, Adriano. (2017). Pectin and polygalacturonic acid-coated liposomes as novel delivery system for nisin: Preparation, characterization and release behavior. Food Hydrocolloids 70: 1-7.
  • Maher, S., Vilk, G., Kelleher, F., Lajoie, G., McClean, S. (2009). Chemical Modification of the Carboxyl Terminal of Nisin A with Biotin does not Abolish Antimicrobial Activity Against the Indicator Organism, Kocuria rhizophila. International Journal of Peptide Research and Therapeutics 15: 219-226. doi: 10.1007/s10989-009-9179-y
  • Marth, E. H. (1998). Extended shelf life refrigerated foods: Microbiological quality and safety. Food Technology 52: 57-62.
  • Muppalla, S. R., Sonavale, R., Chawla, S. P., Sharma, A. (2012). Functional properties of nisin-carbohydrate conjugates formed by radiation induced Maillard reaction. Radiation Physics and Chemistry 81: 1917-1922. doi: 10.1016/j.radphyschem.2012.07.009
  • Parada, J. L., Caron, C. R., Medeiros, A. B. P., Soccol, C. R. (2007). Bacteriocins from lactic acid bacteria: Purification, properties and use as biopreservatives. Brazilian Archives of Biology and Technology 50: 521-542. doi: Doi 10.1590/S1516-89132007000300018
  • Plat, A., Kuipers, A., de Lange, J. G., Moll, G. N., Rink, R. (2011). Activity and Export of Engineered Nisin-(1-22) Analogs. Polymers 3: 1282-1296.
  • Rollema, H. S., Kuipers, O. P., Both, O., Devos, W. M., Siezen, R. J. (1995). Improvement of Solubility and Stability of the Antimicrobial Peptide Nisin by Protein Engineering. Applied and Environmental Microbiology 61: 2873-2878.
  • Slootweg, J. C., van der Wal, S., van Ufford, H. C. Q., Breukink, E., Liskamp, R. M. J., Rijkers, D. T. S. (2013). Synthesis, Antimicrobial Activity, and Membrane Permeabilizing Properties of C-Terminally Modified Nisin Conjugates Accessed by CuAAC. Bioconjugate Chemistry 24: 2058-2066. doi: 10.1021/bc400401k
  • Spicer, C. D., Davis, B. G. (2014). Selective chemical protein modification. Nature Communications 5.
  • van Kraaij, Cindy, Breukink, Eefjan, Rollema, Harry S, Bongers, Roger S, Kosters, Hans A, de Kruijff, Ben, Kuipers, Oscar P. (2000). Engineering a disulfide bond and free thiols in the lantibiotic nisin Z. European Journal of Biochemistry 267: 901-909.
  • Wilson-Stanford, S., Kalli, A., Hakansson, K., Kastrantas, J., Orugunty, R. S., Smith, L. (2009). Oxidation of Lanthionines Renders the Lantibiotic Nisin Inactive. Applied and Environmental Microbiology 75: 1381-1387. doi: 10.1128/Aem.01864-08
  • Yang, Shih-Chun, Lin, Chih-Hung, Sung, Calvin T, Fang, Jia-You. (2014). Antibacterial activities of bacteriocins: application in foods and pharmaceuticals. Frontiers in Microbiology 5: 241.
  • Yuan, J., Zhang, Z. Z., Chen, X. Z., Yang, W., Huan, L. D. (2004). Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants. Applied Microbiology and Biotechnology 64: 806-815. doi: 10.1007/s00253-004-1599-1
  • Zhou, Liang, Shao, Jinfeng, Li, Qian, van Heel, Auke J, de Vries, Marcel P, Broos, Jaap, Kuipers, Oscar P. (2016). Incorporation of tryptophan analogues into the lantibiotic nisin. Amino Acids 48: 1309-1318.

Nisinin Modifikasyonu

Yıl 2017, Cilt: 8 Sayı: Ek (Suppl.) 1, 239 - 244, 16.11.2017
https://doi.org/10.29048/makufebed.342554

Öz

Bakteriyosinlerin lantibiyotikler
sınıfında yer alan antimikrobiyal peptit nisin, Lactococcus lactis tarafından üretilir ve Gram pozitif bakterilere
karşı etkilidir. Nisin doğal bir koruyucu olarak, peynir, sıvı yumurta, salata
sosları, konserveler, et ve ürünleri gibi gıdalarda bakteri gelişimini kontrol
altına almak amacıyla kullanılmaktadır. İnsanlar ve diğer memeliler için toksik
etkisi bulunmayan nisin, Amerika Birleşik Devletleri Gıda ve İlaç Dairesi (FDA)
tarafından “GRAS” (Generally Recognized as Safe - Genel Olarak Güvenli Kabul
Edilebilir Ürün) statüsünde kabul edilmiş ve ayrıca Dünya Sağlık Örgütü (WHO)
tarafından da gıda katkı maddesi olarak onaylanmış bir bakteriyosindir. Doğal
bir koruyucu olmasına karşın nötr ve hafif alkali çözeltilerde çözünürlüğünün
düşük, antimikrobiyal spektrumunun sınırlı, üretim maliyetinin yüksek ve proteolitik
enzimler tarafından kolayca parçalanabilir olması gibi nedenlerle nisinin gıda
koruyucusu olarak uygulanabilirliği sınırlı kalmaktadır. Bu yüzden genetik ve
kimyasal modifikasyonları kapsayan çeşitli uygulamalarla sözü edilen
olumsuzluklar giderilmeye çalışılmaktadır. Bu derlemede doğal bir koruyucu olan
nisinin modifiye edilmesinde uygulanan farklı yöntemler ve elde edilen
bulgulara değinilmektedir.

Kaynakça

  • Aasen, I. M., Markussen, S., Moretro, T., Katla, T., Axelsson, L., Naterstad, K. (2003). Interactions of the bacteriocins sakacin P and nisin with food constituents. International Journal of Food Microbiology 87: 35-43.
  • Abdullah, S. U., Badaruddin, M., Ali, R., Riaz, M. N. (2010). Effect of elementary and advanced glycation products of nisin on its preservative efficacy and digestibility. Food Chemistry 122: 1043-1046. doi: 10.1016/j.foodchem.2009.07.065
  • Bonev, B. B., Breukink, E., Swiezewska, E., De Kruijff, B., Watts, A. (2004). Targeting extracellular pyrophosphates underpins the high selectivity of nisin. Faseb Journal 18: 1862-1869. doi: 10.1096/fj.04-2358com
  • Breukink, E., de Kruijff, B. (1999). The lantibiotic nisin, a special case or not?. Biochimica Et Biophysica Acta-Biomembranes 1462: 223-234. doi: Doi 10.1016/S0005-2736(99)00208-4
  • Breukink, Eefjan, de Kruijff, Ben. (2006). Lipid II as a target for antibiotics. Nature reviews. Drug discovery 5: 321.
  • Brumfitt, W., Salton, M. R. J., Hamilton-Miller, J. M. T. (2002). Nisin, alone and combined with peptidoglycan-modulating antibiotics: activity against methicillin-resistant Staphylococcus aureus and vancomycin-resistant enterococci. Journal of Antimicrobial Chemotherapy 50: 731-734. doi: 10.1093/jac/dkf190
  • Cleveland, J., Montville, T. J., Nes, I. F., Chikindas, M. L. (2001). Bacteriocins: safe, natural antimicrobials for food preservation. International Journal of Food Microbiology 71: 1-20.
  • De Vuyst, Luc, Vandamme, Erick J 1994. Nisin, a lantibiotic produced by Lactococcus lactis subsp. lactis: properties, biosynthesis, fermentation and applications. In Bacteriocins of lactic acid bacteria, 151-221: Springer.
  • Dischinger, J., Chipalu, S. B., Bierbaum, G. (2014). Lantibiotics: Promising candidates for future applications in health care. International Journal of Medical Microbiology 304: 51-62. doi: 10.1016/j.ijmm.2013.09.003
  • Feeney, R. E., Yamasaki, R. B., Geoghegan, K. F. (1982). Chemical Modification of Proteins - an Overview. Advances in Chemistry Series: 3-55.
  • Field, D., Begley, M., O'Connor, P. M., Daly, K. M., Hugenholtz, F., Cotter, P. D., Hill, C., Ross, R. P. (2012). Bioengineered Nisin A Derivatives with Enhanced Activity against Both Gram Positive and Gram Negative Pathogens. Plos One 7. doi: ARTN e4688410.1371/journal.pone.0046884
  • Field, D., Connor, P. M. O., Cotter, P. D., Hill, C., Ross, R. P. (2008). The generation of nisin variants with enhanced activity against specific Gram-positive pathogens. Molecular Microbiology 69: 218-230.
  • Galvez, A., Abriouel, H., Lopez, R. L., Ben Omar, N. (2007). Bacteriocin-based strategies for food biopreservation. International Journal of Food Microbiology 120: 51-70.
  • Gross, Erhard, Morell, John L. (1971). Structure of nisin. Journal of the American Chemical Society 93: 4634-4635.
  • Guiotto, Andrea, Pozzobon, Michela, Canevari, Mirta, Manganelli, Riccardo, Scarin, Marino, Veronese, Francesco M. (2003). PEGylation of the antimicrobial peptide nisin A: problems and perspectives. Il Farmaco 58: 45-50.
  • Hansen, J. N. (1994). Nisin as a Model Food Preservative. Critical Reviews in Food Science and Nutrition 34: 69-93.
  • Klaenhammer, T. R. (1993). Genetics of Bacteriocins Produced by Lactic-Acid Bacteria. Fems Microbiology Reviews 12: 39-86.
  • Koponen, O., Tolonen, M., Qiao, M. Q., Wahlstrom, G., Helin, J., Saris, P. E. J. (2002). NisB is required for the dehydration and NisC for the lanthionine formation in the post-translational modification of nisin. Microbiology-Sgm 148: 3561-3568.
  • Kuipers, O. P., Rollema, H. S., Beerthuyzen, M. M., Siezen, R. J., deVos, W. M. (1995). Protein engineering and biosynthesis of nisin and regulation of transcription of the structural nisA gene. International Dairy Journal 5: 785-795.
  • Kuipers, Oscar P, Rollema, Harry S, Yap, WM, Boot, Hein J, Siezen, Roland J, de Vos, Willem M. (1992). Engineering dehydrated amino acid residues in the antimicrobial peptide nisin. Journal of Biological Chemistry 267: 24340-24346.
  • Liu, W., Hansen, J. N. (1990). Some Chemical and Physical-Properties of Nisin, a Small-Protein Antibiotic Produced by Lactococcus-Lactis. Applied and Environmental Microbiology 56: 2551-2558.
  • Lopes, Nathalie Almeida, Pinilla, Cristian Mauricio Barreto, Brandelli, Adriano. (2017). Pectin and polygalacturonic acid-coated liposomes as novel delivery system for nisin: Preparation, characterization and release behavior. Food Hydrocolloids 70: 1-7.
  • Maher, S., Vilk, G., Kelleher, F., Lajoie, G., McClean, S. (2009). Chemical Modification of the Carboxyl Terminal of Nisin A with Biotin does not Abolish Antimicrobial Activity Against the Indicator Organism, Kocuria rhizophila. International Journal of Peptide Research and Therapeutics 15: 219-226. doi: 10.1007/s10989-009-9179-y
  • Marth, E. H. (1998). Extended shelf life refrigerated foods: Microbiological quality and safety. Food Technology 52: 57-62.
  • Muppalla, S. R., Sonavale, R., Chawla, S. P., Sharma, A. (2012). Functional properties of nisin-carbohydrate conjugates formed by radiation induced Maillard reaction. Radiation Physics and Chemistry 81: 1917-1922. doi: 10.1016/j.radphyschem.2012.07.009
  • Parada, J. L., Caron, C. R., Medeiros, A. B. P., Soccol, C. R. (2007). Bacteriocins from lactic acid bacteria: Purification, properties and use as biopreservatives. Brazilian Archives of Biology and Technology 50: 521-542. doi: Doi 10.1590/S1516-89132007000300018
  • Plat, A., Kuipers, A., de Lange, J. G., Moll, G. N., Rink, R. (2011). Activity and Export of Engineered Nisin-(1-22) Analogs. Polymers 3: 1282-1296.
  • Rollema, H. S., Kuipers, O. P., Both, O., Devos, W. M., Siezen, R. J. (1995). Improvement of Solubility and Stability of the Antimicrobial Peptide Nisin by Protein Engineering. Applied and Environmental Microbiology 61: 2873-2878.
  • Slootweg, J. C., van der Wal, S., van Ufford, H. C. Q., Breukink, E., Liskamp, R. M. J., Rijkers, D. T. S. (2013). Synthesis, Antimicrobial Activity, and Membrane Permeabilizing Properties of C-Terminally Modified Nisin Conjugates Accessed by CuAAC. Bioconjugate Chemistry 24: 2058-2066. doi: 10.1021/bc400401k
  • Spicer, C. D., Davis, B. G. (2014). Selective chemical protein modification. Nature Communications 5.
  • van Kraaij, Cindy, Breukink, Eefjan, Rollema, Harry S, Bongers, Roger S, Kosters, Hans A, de Kruijff, Ben, Kuipers, Oscar P. (2000). Engineering a disulfide bond and free thiols in the lantibiotic nisin Z. European Journal of Biochemistry 267: 901-909.
  • Wilson-Stanford, S., Kalli, A., Hakansson, K., Kastrantas, J., Orugunty, R. S., Smith, L. (2009). Oxidation of Lanthionines Renders the Lantibiotic Nisin Inactive. Applied and Environmental Microbiology 75: 1381-1387. doi: 10.1128/Aem.01864-08
  • Yang, Shih-Chun, Lin, Chih-Hung, Sung, Calvin T, Fang, Jia-You. (2014). Antibacterial activities of bacteriocins: application in foods and pharmaceuticals. Frontiers in Microbiology 5: 241.
  • Yuan, J., Zhang, Z. Z., Chen, X. Z., Yang, W., Huan, L. D. (2004). Site-directed mutagenesis of the hinge region of nisinZ and properties of nisinZ mutants. Applied Microbiology and Biotechnology 64: 806-815. doi: 10.1007/s00253-004-1599-1
  • Zhou, Liang, Shao, Jinfeng, Li, Qian, van Heel, Auke J, de Vries, Marcel P, Broos, Jaap, Kuipers, Oscar P. (2016). Incorporation of tryptophan analogues into the lantibiotic nisin. Amino Acids 48: 1309-1318.
Toplam 35 adet kaynakça vardır.

Ayrıntılar

Konular Mühendislik
Bölüm Araştırma Makalesi
Yazarlar

Ezgi Demir Özer

Metin Yıldırım

Yayımlanma Tarihi 16 Kasım 2017
Kabul Tarihi 9 Kasım 2017
Yayımlandığı Sayı Yıl 2017 Cilt: 8 Sayı: Ek (Suppl.) 1

Kaynak Göster

APA Demir Özer, E., & Yıldırım, M. (2017). Nisinin Modifikasyonu. Mehmet Akif Ersoy Üniversitesi Fen Bilimleri Enstitüsü Dergisi, 8(Ek (Suppl.) 1), 239-244. https://doi.org/10.29048/makufebed.342554