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Yıl 2014, Cilt: 30 Sayı: 5, 338 - 345, 01.10.2014

Öz

Topraktan izole edilen Bacillus amyloliquefaciens B10 morfolojik, biyokimyasal ve 16S rRNA sekans analizi sonuçlarına göre belirlenmiştir. Bacillus amyloliquefaciens B10’un ürettiği bakteriyosin benzeri peptit (BLP) Bacillus cereus ve Listeria monoctogenesis gibi patojenik Gram pozitif ve Candida albicans gibi fırsatçı patojenleri içeren mayalara karşı geniş antimikrobiyal aktivite gösterir. BLP katalaz hariç proteolitik proteinaz-K, lipaz, tripsin, α-amilaz enzimlerine hassastır (5 mg/ml). BLP aktivitesi 90°C’de 30dk. da stabil iken aktivite 90°C 2 saatde ve 121°C’de 20 dk. da kaybolmaktadır. BLP pH 3-9 arasında aktivite göstermesine rağmen, optimum aktivite pH 7’dir. BLP ethanol, hekzan, etil eter ve tween-80 gibi bazı organik çözücü ve deterjanlara karşı hassastır. Amonyum sülfat çöktürmesi (%70) ile yapılan kısmi saflaştırma sonucu BLP’nin yaklaşik 5 kDa ağırlığında olduğu tespit edilmiştir.

Kaynakça

  • Abriouel, H., Franz, C.M.A.P., Omar, N.B., Galvez, A. Diversity and applications of Bacillus bacteriocins. FEMS Microbiol. Rev., 35, 201-232, 2011.
  • Altschul, S.F., Gish, W., Miller, W., Myers, E.W., Lipman, D.J. Basic local alignment search tool. J. Mol. Biol., 215, 403–410, 1990.
  • Ayed, H.B., Hmidet, N., Bechet, M., Chollet, M., Chataigne, G., Leclere, P., Jacques, P., Nasri, M. Identification and biochemical characteristics of lipopeptides fromBacillus mojavensis A21. Process Biochemistry, 49, 1669-1707, 2014.
  • Banerjee, S., Hansen, J.N. Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic. J. Biol. Chem., 263, 9508–9514, 1988.
  • Benitez, L.B., Caumo, K., Brandalli, A., Rott, M.B. substance amyloliquefaciens shows remarkable inhibition of Acanthamoeba polyphaga. Parasitol. Res., 108, 687– 69, 2011. from Bacillus
  • Benson, D.A., Karsch-Mizrachi, I., Clark, K., Lipman, D.J., Ostell, J., Sayers, E.W. GenBank. Nucleic Acids Res., 40 (Database issue), D48–D53, 2002.
  • Beric, T., Stankovic, S., Draganic, V., Kojic, M., Lozo, J., Fira, D. Novel antilisterial bacteriocin licheniocin 50.2 fromBacillus licheniformis VPS50.2 isolated from soil sample. J. Appl. Microbiol., 116, 502-510, 2014.
  • Bizani, D., Brandelli, A. Characterization of a bacteriocin produced by a newly isolated Bacillus sp. strain 8 A. J. Appl. Microbiol., 93, 512-9, 2002.
  • Bizani, D., Dominguez, A.P., Brandelli, A. Purification and antimicrobial peptide cerein 8A. Lett. Appl. Microbiol., 41, 269-73, 2005.
  • characterization of the
  • Cherif, A., Ouzari, H., Daffonchio, D., Cherif, H., Ben Slama, K., Hassen, A., Jaoua, S., Boudabous, A. Thuricin 7: a novel bacteriocin produced by Bacillus thuringiensis BMG1.7, a new strain isolated from soil. Lett. Appl. Microbiol., 32, 243-7, 2001.
  • Cherif, A., Chehimi, S., Limem, F., Hansen, B.M., Hendriksen, N.B., Daffonchio, D., Boudabous, A. Detection and characterization of the novel bacteriocin entomocin 9, and safety evaluation of its producer Bacillus thuringiensis subsp. entomocidus HD9. J. Appl. Microbiol., 95, 990–1000, 2003.
  • Slepecky, R., Hemphill, E. The genus Bacillus. Nonmedical. The Prokaryotes, In: Dworkin M, Falkow S, Rosenberg E, Schleifer KH, Stackebrandt E (eds), Vol. 4, Springer, New York, pp. 530–562, 2006.
  • Stevens, K.A., Sheldon, B.W., Klapes, N.A., Klaenhammer, R. Nisin treatment for inactivation of Salmonella species and other gram negative bacteria. Appl. Environ. Microbiol., 57, 3613-15, 1991.
  • Grosu-Tudor, S.S., Stancu, M.M., Pelinescu, D., Zamfir, M. Characterization of some bacteriocins produced by lactic acid bacteria isolated from fermented foods. World J. Microbiol. Biotechnol., 30, 2459-2469, 2014.
  • He, L., Chen, W., Liu, Y. Production and partial characterization of bacteriocin-like pepitdes by Bacillus licheniformis ZJU12. Microbiol. Res., 161, 321-6, 2006.
  • Hiradate, S., Yoshida, S., Sugie, H., Yada, H., Fujii, Y. Mulberry anthracnose antagonists (iturins) produced by Bacillus amyloliquefaciens RC-2. Phytochemistry, 61, 693-698, 2002.
  • Izquerdo, E., Audrey, B., Christine, S., Yimin, C., Eric, M., Alain, V.D., Said, E. Production of Enterocins L50A, L50B, and IT, a New Enterocin, by Enterococcus faecium IT62, a Strain isolated from Italian Ryegrass in Japan. J. Antimicrob. Agents Chemother., 52, 1917- 1923, 2008.
  • Kamoun, F., Fguira, I., Hassen, N., Mejdoub, H., Lereclus, Characterization of a New Bacillus thuringiensis Bacteriocin Active Against Listeria monocytogenes, Bacillus cereus and Agrobacterium tumefaciens. Appl. Biochem. Biotechnol., 165, 300-314, 2011.
  • Kindoli, S., Lee, H.A., Kim, J.H. Properties of Bac W42, a bacteriocin produced by Bacillus subtilis W42 isolated Biotechnol., 22, 1092-100, 2012. J. Microbiol.
  • Laemmli, U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227, 680-685, 1970.
  • Lisboa, M.P., Bonatto, D., Bizani, D., Henriques, A. J.A.P., bacteriocin-like substance produced by ‘Bacillus amyloliquefaciens’ isolated from the Brazilian Atlantic forest. Int. Microbiol., 9, 111–118, 2006.
  • Lucas, R., Grande, M.A., Abriouel, H., Maqueda, M., Ben Omar, N., Valdivia, E., Martinez-Canamero, M., Galvez, A. Application of the broad-spectrum bacteriocin enterocin AS-48 to inhibit Bacillus coagulans in canned fruit and vegetable foods. Food Chem. Toxicol., 44, 1774-81, 2006.
  • Naclerio, G., Ricca, E., Sacco, M., De Felice, M. Antimicrobial activity of a newly identified bacteriocin of Bacillus cereus. Appl. Environ. Microbiol., 59, 4313-6, 1993.
  • Nicholson, W.L. Roles of Bacillus endospores in the environment. Cell Mol. Life Sci., 59, 410–416, 2002.
  • Priest, F.G., Goodfellow, M., Shute, L.A., Berkeley, R.C.W. Bacillus amyloliquefaciens sp. nov. norn. rev. Int. J. Syst. Bacteriol., 37, 69-71, 1987.
  • Sevim, E., Alpay Karaoglu, S., Sevim, A., Canakcı, S. Antimicrobial Activity of Bacillus Strains Isolated from Spring Water and A Novel Bacteriocin: RS108. J. Pure Appl. Microbiol., 7, 2757-2765, 2013.
  • Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M., Kumar, S. MEGA5: Molecular evolutionary genetics evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol., 28, 2731–2739, 2011.
  • Weisburg, W.G., Barns, S.M., Pelletier, D.A., Lane, D.J. 16S ribosomal DNA amplification for phylogenetic study. J. Bacteriol., 173, 697–703, 1991.
  • Xie, J., Zhang, R., Shang, C., Guo, Y. Isolation and characterization of a bacteriocin produced by an isolated Bacillus subtilis LFB112 that exhibits antimicrobial activity against domestic animal pathogens. Afr. J. Biotechnol., 8, 5611–5619, 2009.
  • Zheng, G., Yan, L.Z., Vederas, J.C., Zuber, P. Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin. J. Bacteriol., 181, 7346– 7355, 1999.

Production and Characterization of Bacteriocin-like Peptide Produced by Bacillus amyloliquefaciens B10

Yıl 2014, Cilt: 30 Sayı: 5, 338 - 345, 01.10.2014

Öz

Bacillus amyloliquefaciens B10 that was isolated from soil was identified according to data of morphological, biochemical and 16S rRNA sequence analyses. The bacteriocin like peptide (BLP) produced by B. amyloliquefaciens B10 shows extendend antimicrobial activity against gram-positive bacteria including some pathogenic bacteria such as B. cereus and L. monocytogenesis and yeast including opportunistic pathogen such as Candida albicans. The BLP was sensitive to proteolytic enzyme proteinase K, lipase, tripsin, α- amylase except for catalase (5 mg/ml). While the activity of BLP of B13 was stable at 90°C for 30 min, the activity was completely lost at 90°C for 2 h and 121°C 20 min. Although activity of BLP of B10 was stable pH range 3-9, optimum pH was 7.0. It was sensitive against some organic solvent and detergent such as ethanol, hexane, ethyl ether and tween-80. Partial purification of BLP of B10 performed 70% ammonium sulphate precipitation was shown that it has approximately 5 kDa molecular weight.

Kaynakça

  • Abriouel, H., Franz, C.M.A.P., Omar, N.B., Galvez, A. Diversity and applications of Bacillus bacteriocins. FEMS Microbiol. Rev., 35, 201-232, 2011.
  • Altschul, S.F., Gish, W., Miller, W., Myers, E.W., Lipman, D.J. Basic local alignment search tool. J. Mol. Biol., 215, 403–410, 1990.
  • Ayed, H.B., Hmidet, N., Bechet, M., Chollet, M., Chataigne, G., Leclere, P., Jacques, P., Nasri, M. Identification and biochemical characteristics of lipopeptides fromBacillus mojavensis A21. Process Biochemistry, 49, 1669-1707, 2014.
  • Banerjee, S., Hansen, J.N. Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic. J. Biol. Chem., 263, 9508–9514, 1988.
  • Benitez, L.B., Caumo, K., Brandalli, A., Rott, M.B. substance amyloliquefaciens shows remarkable inhibition of Acanthamoeba polyphaga. Parasitol. Res., 108, 687– 69, 2011. from Bacillus
  • Benson, D.A., Karsch-Mizrachi, I., Clark, K., Lipman, D.J., Ostell, J., Sayers, E.W. GenBank. Nucleic Acids Res., 40 (Database issue), D48–D53, 2002.
  • Beric, T., Stankovic, S., Draganic, V., Kojic, M., Lozo, J., Fira, D. Novel antilisterial bacteriocin licheniocin 50.2 fromBacillus licheniformis VPS50.2 isolated from soil sample. J. Appl. Microbiol., 116, 502-510, 2014.
  • Bizani, D., Brandelli, A. Characterization of a bacteriocin produced by a newly isolated Bacillus sp. strain 8 A. J. Appl. Microbiol., 93, 512-9, 2002.
  • Bizani, D., Dominguez, A.P., Brandelli, A. Purification and antimicrobial peptide cerein 8A. Lett. Appl. Microbiol., 41, 269-73, 2005.
  • characterization of the
  • Cherif, A., Ouzari, H., Daffonchio, D., Cherif, H., Ben Slama, K., Hassen, A., Jaoua, S., Boudabous, A. Thuricin 7: a novel bacteriocin produced by Bacillus thuringiensis BMG1.7, a new strain isolated from soil. Lett. Appl. Microbiol., 32, 243-7, 2001.
  • Cherif, A., Chehimi, S., Limem, F., Hansen, B.M., Hendriksen, N.B., Daffonchio, D., Boudabous, A. Detection and characterization of the novel bacteriocin entomocin 9, and safety evaluation of its producer Bacillus thuringiensis subsp. entomocidus HD9. J. Appl. Microbiol., 95, 990–1000, 2003.
  • Slepecky, R., Hemphill, E. The genus Bacillus. Nonmedical. The Prokaryotes, In: Dworkin M, Falkow S, Rosenberg E, Schleifer KH, Stackebrandt E (eds), Vol. 4, Springer, New York, pp. 530–562, 2006.
  • Stevens, K.A., Sheldon, B.W., Klapes, N.A., Klaenhammer, R. Nisin treatment for inactivation of Salmonella species and other gram negative bacteria. Appl. Environ. Microbiol., 57, 3613-15, 1991.
  • Grosu-Tudor, S.S., Stancu, M.M., Pelinescu, D., Zamfir, M. Characterization of some bacteriocins produced by lactic acid bacteria isolated from fermented foods. World J. Microbiol. Biotechnol., 30, 2459-2469, 2014.
  • He, L., Chen, W., Liu, Y. Production and partial characterization of bacteriocin-like pepitdes by Bacillus licheniformis ZJU12. Microbiol. Res., 161, 321-6, 2006.
  • Hiradate, S., Yoshida, S., Sugie, H., Yada, H., Fujii, Y. Mulberry anthracnose antagonists (iturins) produced by Bacillus amyloliquefaciens RC-2. Phytochemistry, 61, 693-698, 2002.
  • Izquerdo, E., Audrey, B., Christine, S., Yimin, C., Eric, M., Alain, V.D., Said, E. Production of Enterocins L50A, L50B, and IT, a New Enterocin, by Enterococcus faecium IT62, a Strain isolated from Italian Ryegrass in Japan. J. Antimicrob. Agents Chemother., 52, 1917- 1923, 2008.
  • Kamoun, F., Fguira, I., Hassen, N., Mejdoub, H., Lereclus, Characterization of a New Bacillus thuringiensis Bacteriocin Active Against Listeria monocytogenes, Bacillus cereus and Agrobacterium tumefaciens. Appl. Biochem. Biotechnol., 165, 300-314, 2011.
  • Kindoli, S., Lee, H.A., Kim, J.H. Properties of Bac W42, a bacteriocin produced by Bacillus subtilis W42 isolated Biotechnol., 22, 1092-100, 2012. J. Microbiol.
  • Laemmli, U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature, 227, 680-685, 1970.
  • Lisboa, M.P., Bonatto, D., Bizani, D., Henriques, A. J.A.P., bacteriocin-like substance produced by ‘Bacillus amyloliquefaciens’ isolated from the Brazilian Atlantic forest. Int. Microbiol., 9, 111–118, 2006.
  • Lucas, R., Grande, M.A., Abriouel, H., Maqueda, M., Ben Omar, N., Valdivia, E., Martinez-Canamero, M., Galvez, A. Application of the broad-spectrum bacteriocin enterocin AS-48 to inhibit Bacillus coagulans in canned fruit and vegetable foods. Food Chem. Toxicol., 44, 1774-81, 2006.
  • Naclerio, G., Ricca, E., Sacco, M., De Felice, M. Antimicrobial activity of a newly identified bacteriocin of Bacillus cereus. Appl. Environ. Microbiol., 59, 4313-6, 1993.
  • Nicholson, W.L. Roles of Bacillus endospores in the environment. Cell Mol. Life Sci., 59, 410–416, 2002.
  • Priest, F.G., Goodfellow, M., Shute, L.A., Berkeley, R.C.W. Bacillus amyloliquefaciens sp. nov. norn. rev. Int. J. Syst. Bacteriol., 37, 69-71, 1987.
  • Sevim, E., Alpay Karaoglu, S., Sevim, A., Canakcı, S. Antimicrobial Activity of Bacillus Strains Isolated from Spring Water and A Novel Bacteriocin: RS108. J. Pure Appl. Microbiol., 7, 2757-2765, 2013.
  • Tamura, K., Peterson, D., Peterson, N., Stecher, G., Nei, M., Kumar, S. MEGA5: Molecular evolutionary genetics evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol., 28, 2731–2739, 2011.
  • Weisburg, W.G., Barns, S.M., Pelletier, D.A., Lane, D.J. 16S ribosomal DNA amplification for phylogenetic study. J. Bacteriol., 173, 697–703, 1991.
  • Xie, J., Zhang, R., Shang, C., Guo, Y. Isolation and characterization of a bacteriocin produced by an isolated Bacillus subtilis LFB112 that exhibits antimicrobial activity against domestic animal pathogens. Afr. J. Biotechnol., 8, 5611–5619, 2009.
  • Zheng, G., Yan, L.Z., Vederas, J.C., Zuber, P. Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin. J. Bacteriol., 181, 7346– 7355, 1999.
Toplam 31 adet kaynakça vardır.

Ayrıntılar

Diğer ID JA79HD45ZC
Bölüm Makaleler
Yazarlar

Seyma Sensoy Karaoglu Bu kişi benim

Ali Sevim Bu kişi benim

Elif Sevim Bu kişi benim

Yayımlanma Tarihi 1 Ekim 2014
Yayımlandığı Sayı Yıl 2014 Cilt: 30 Sayı: 5

Kaynak Göster

APA Sensoy Karaoglu, S., Sevim, A., & Sevim, E. (2014). Production and Characterization of Bacteriocin-like Peptide Produced by Bacillus amyloliquefaciens B10. Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi, 30(5), 338-345.
AMA Sensoy Karaoglu S, Sevim A, Sevim E. Production and Characterization of Bacteriocin-like Peptide Produced by Bacillus amyloliquefaciens B10. Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi. Ekim 2014;30(5):338-345.
Chicago Sensoy Karaoglu, Seyma, Ali Sevim, ve Elif Sevim. “Production and Characterization of Bacteriocin-Like Peptide Produced by Bacillus Amyloliquefaciens B10”. Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi 30, sy. 5 (Ekim 2014): 338-45.
EndNote Sensoy Karaoglu S, Sevim A, Sevim E (01 Ekim 2014) Production and Characterization of Bacteriocin-like Peptide Produced by Bacillus amyloliquefaciens B10. Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi 30 5 338–345.
IEEE S. Sensoy Karaoglu, A. Sevim, ve E. Sevim, “Production and Characterization of Bacteriocin-like Peptide Produced by Bacillus amyloliquefaciens B10”, Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi, c. 30, sy. 5, ss. 338–345, 2014.
ISNAD Sensoy Karaoglu, Seyma vd. “Production and Characterization of Bacteriocin-Like Peptide Produced by Bacillus Amyloliquefaciens B10”. Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi 30/5 (Ekim 2014), 338-345.
JAMA Sensoy Karaoglu S, Sevim A, Sevim E. Production and Characterization of Bacteriocin-like Peptide Produced by Bacillus amyloliquefaciens B10. Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi. 2014;30:338–345.
MLA Sensoy Karaoglu, Seyma vd. “Production and Characterization of Bacteriocin-Like Peptide Produced by Bacillus Amyloliquefaciens B10”. Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi, c. 30, sy. 5, 2014, ss. 338-45.
Vancouver Sensoy Karaoglu S, Sevim A, Sevim E. Production and Characterization of Bacteriocin-like Peptide Produced by Bacillus amyloliquefaciens B10. Erciyes Üniversitesi Fen Bilimleri Enstitüsü Fen Bilimleri Dergisi. 2014;30(5):338-45.

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