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Volumn 173, Issue , 2014, Pages 81-88

Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: Carnobacteriocin X and carnolysins A1 and A2

Author keywords

Bacteriocins; Carnobacteriocins; Carnobacterium; Listeria spp; Purification

Indexed keywords

BACTERIOCIN; CARNOBACTERIOCIN B1; CARNOBACTERIOCIN B2; CARNOBACTERIOCIN BM1; CARNOBACTERIOCIN X; CARNOLYSIN A1; CARNOLYSIN A2; RESIN; UNCLASSIFIED DRUG;

EID: 84891919526     PISSN: 01681605     EISSN: 18793460     Source Type: Journal    
DOI: 10.1016/j.ijfoodmicro.2013.12.019     Document Type: Article
Times cited : (32)

References (32)
  • 1
    • 26644468146 scopus 로고    scopus 로고
    • Antilisterial activity of a Carnobacterium piscicola isolated from Brazilian smoked fish (Surubim Pseudoplatystoma sp.) and its activity against a persistent strain of Listeria monocytogenes isolated from Surubim
    • Alves V.F., De Martinis E.C.P., Destro M.T., Vogel B.F., Gram L. Antilisterial activity of a Carnobacterium piscicola isolated from Brazilian smoked fish (Surubim Pseudoplatystoma sp.) and its activity against a persistent strain of Listeria monocytogenes isolated from Surubim. J. Food Prot. 2005, 68:2068-2077.
    • (2005) J. Food Prot. , vol.68 , pp. 2068-2077
    • Alves, V.F.1    De Martinis, E.C.P.2    Destro, M.T.3    Vogel, B.F.4    Gram, L.5
  • 2
    • 0029909789 scopus 로고    scopus 로고
    • Purification and amino acid sequences of piscicocins V1a and V1b, two class IIa bacteriocins secreted by Carnobacterium piscicola V1 that display significantly different levels of specific inhibitory activity
    • Bhugaloo-Vial P., Dousset X., Metivier A., Sorokine O., Anglade P., Boyaval P., Marion D. Purification and amino acid sequences of piscicocins V1a and V1b, two class IIa bacteriocins secreted by Carnobacterium piscicola V1 that display significantly different levels of specific inhibitory activity. Appl. Environ. Microbiol. 1996, 62:4410-4416.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 4410-4416
    • Bhugaloo-Vial, P.1    Dousset, X.2    Metivier, A.3    Sorokine, O.4    Anglade, P.5    Boyaval, P.6    Marion, D.7
  • 3
    • 0029786349 scopus 로고    scopus 로고
    • Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic
    • Booth M.C., Bogie C.P., Sahl H.G., Siezen R.J., Hatter K.L., Gilmore M.S. Structural analysis and proteolytic activation of Enterococcus faecalis cytolysin, a novel lantibiotic. Mol. Microbiol. 1996, 21:1175-1184.
    • (1996) Mol. Microbiol. , vol.21 , pp. 1175-1184
    • Booth, M.C.1    Bogie, C.P.2    Sahl, H.G.3    Siezen, R.J.4    Hatter, K.L.5    Gilmore, M.S.6
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0034462540 scopus 로고    scopus 로고
    • Biochemical and genetic evidence that Enterococcus faecium L50 produces enterocins L50A and L50B, the sec-dependent enterocin P, and a novel bacteriocin secreted without an N-terminal extension termed enterocin Q
    • Cintas L.M., Casaus P., Herranz C., Havarstein L.S., Holo H., Hernandez P.E., Nes I.F. Biochemical and genetic evidence that Enterococcus faecium L50 produces enterocins L50A and L50B, the sec-dependent enterocin P, and a novel bacteriocin secreted without an N-terminal extension termed enterocin Q. J. Bacteriol. 2000, 182:6806-6814.
    • (2000) J. Bacteriol. , vol.182 , pp. 6806-6814
    • Cintas, L.M.1    Casaus, P.2    Herranz, C.3    Havarstein, L.S.4    Holo, H.5    Hernandez, P.E.6    Nes, I.F.7
  • 7
    • 0141725789 scopus 로고    scopus 로고
    • The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells
    • Coburn P.S., Gilmore M.S. The Enterococcus faecalis cytolysin: a novel toxin active against eukaryotic and prokaryotic cells. Cell. Microbiol. 2003, 5:661-669.
    • (2003) Cell. Microbiol. , vol.5 , pp. 661-669
    • Coburn, P.S.1    Gilmore, M.S.2
  • 8
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: developing innate immunity for food
    • Cotter P.D., Hill C., Ross R.P. Bacteriocins: developing innate immunity for food. Nat. Rev. Microbiol. 2005, 3:777-788.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 9
    • 0025719296 scopus 로고
    • Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum
    • Hastings J.W., Sailer M., Johnson K., Roy K.L., Vederas J.C., Stiles M.E. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J. Bacteriol. 1991, 173:7491-7500.
    • (1991) J. Bacteriol. , vol.173 , pp. 7491-7500
    • Hastings, J.W.1    Sailer, M.2    Johnson, K.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6
  • 10
    • 0030834391 scopus 로고    scopus 로고
    • Characteristics and genetic determinants of bacteriocin activities produced by Carnobacterium piscicola CP5 isolated from cheese
    • Herbin S., Mathieu F., Brule F., Branlant C., Lefebvre G., Lebrihi A. Characteristics and genetic determinants of bacteriocin activities produced by Carnobacterium piscicola CP5 isolated from cheese. Curr. Microbiol. 1997, 35:319-326.
    • (1997) Curr. Microbiol. , vol.35 , pp. 319-326
    • Herbin, S.1    Mathieu, F.2    Brule, F.3    Branlant, C.4    Lefebvre, G.5    Lebrihi, A.6
  • 12
    • 0027199706 scopus 로고
    • Genetics of bacteriocins produced by lactic acid bacteria
    • Klaenhammer T.R. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev. 1994, 12:39-85.
    • (1994) FEMS Microbiol. Rev. , vol.12 , pp. 39-85
    • Klaenhammer, T.R.1
  • 13
    • 4544251455 scopus 로고    scopus 로고
    • Quorum sensing control of lantibiotic production; nisin and subtilin autoregulate their own biosynthesis
    • Kleerebezem M. Quorum sensing control of lantibiotic production; nisin and subtilin autoregulate their own biosynthesis. Peptides 2004, 25:1405-1414.
    • (2004) Peptides , vol.25 , pp. 1405-1414
    • Kleerebezem, M.1
  • 14
    • 84861649020 scopus 로고    scopus 로고
    • Discovery, biosynthesis and engineering of lantipeptides
    • Knerr P.J., van der Donk W.A. Discovery, biosynthesis and engineering of lantipeptides. Annu. Rev. Biochem. 2012, 81:479-505.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 479-505
    • Knerr, P.J.1    van der Donk, W.A.2
  • 16
    • 77956856274 scopus 로고
    • Methods for studying bacteriocins
    • Academic Press, New York, (Part A), J.R. Norris, D.W. Ribbons (Eds.)
    • Mayr-Harting A., Hedgesm A.J., Berkeley R.C.W. Methods for studying bacteriocins. Methods in Microbiology 1972, 7:315-422. Academic Press, New York, (Part A). J.R. Norris, D.W. Ribbons (Eds.).
    • (1972) Methods in Microbiology , vol.7 , pp. 315-422
    • Mayr-Harting, A.1    Hedgesm, A.J.2    Berkeley, R.C.W.3
  • 17
    • 80052212888 scopus 로고    scopus 로고
    • New developments and applications of bacteriocins and peptides in foods
    • Mills S., Stanton C., Hill C., Ross R.P. New developments and applications of bacteriocins and peptides in foods. Annu. Rev. Food Sci. Technol. 2011, 2:299-329.
    • (2011) Annu. Rev. Food Sci. Technol. , vol.2 , pp. 299-329
    • Mills, S.1    Stanton, C.2    Hill, C.3    Ross, R.P.4
  • 18
    • 0842287257 scopus 로고    scopus 로고
    • The contribution of bacteriocin to inhibition of Listeria monocytogenes by Carnobacterium piscicola strains in cold-smoked salmon systems
    • Nilsson L., Ng Y.Y., Christiansen J.N., Jorgensen B.L., Grotinum D., Gram L. The contribution of bacteriocin to inhibition of Listeria monocytogenes by Carnobacterium piscicola strains in cold-smoked salmon systems. J. Appl. Microbiol. 2004, 96:133-143.
    • (2004) J. Appl. Microbiol. , vol.96 , pp. 133-143
    • Nilsson, L.1    Ng, Y.Y.2    Christiansen, J.N.3    Jorgensen, B.L.4    Grotinum, D.5    Gram, L.6
  • 19
    • 0032749389 scopus 로고    scopus 로고
    • Production, recovery and purification of bacteriocins from lactic acid bacteria
    • Parente E., Ricciardi A. Production, recovery and purification of bacteriocins from lactic acid bacteria. Appl. Microbiol. Biotechnol. 1999, 52:628-638.
    • (1999) Appl. Microbiol. Biotechnol. , vol.52 , pp. 628-638
    • Parente, E.1    Ricciardi, A.2
  • 20
    • 0028363167 scopus 로고
    • Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B
    • Quadri L.E.N., Sailer M., Roy K.L., Vederas J.C., Stiles M.E. Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B. J. Biol. Chem. 1994, 269:12204-12211.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12204-12211
    • Quadri, L.E.N.1    Sailer, M.2    Roy, K.L.3    Vederas, J.C.4    Stiles, M.E.5
  • 21
    • 0028915914 scopus 로고
    • Characterization of the protein conferring immunity to the antimicrobial peptide carnobacteriocin B2 and expression of carnobacteriocins B2 and BM1
    • Quadri L.E.N., Sailer M., Terebiznik M.R., Roy K.L., Vederas J.C., Stiles M.E. Characterization of the protein conferring immunity to the antimicrobial peptide carnobacteriocin B2 and expression of carnobacteriocins B2 and BM1. J. Bacteriol. 1995, 177:1144-1151.
    • (1995) J. Bacteriol. , vol.177 , pp. 1144-1151
    • Quadri, L.E.N.1    Sailer, M.2    Terebiznik, M.R.3    Roy, K.L.4    Vederas, J.C.5    Stiles, M.E.6
  • 22
    • 0030930569 scopus 로고    scopus 로고
    • Characterization of a locus from Carnobacterium piscicola LV17B involved in bacteriocin production and immunity: evidence for global inducer-mediated transcriptional regulation
    • Quadri L.E.N., Kleerebezem M., Kuipers O.P., DeVos W.M., Roy K.L., Vederas J.C., Stiles M.E. Characterization of a locus from Carnobacterium piscicola LV17B involved in bacteriocin production and immunity: evidence for global inducer-mediated transcriptional regulation. J. Bacteriol. 1997, 179:6163-6171.
    • (1997) J. Bacteriol. , vol.179 , pp. 6163-6171
    • Quadri, L.E.N.1    Kleerebezem, M.2    Kuipers, O.P.3    DeVos, W.M.4    Roy, K.L.5    Vederas, J.C.6    Stiles, M.E.7
  • 23
    • 79954594997 scopus 로고    scopus 로고
    • Use of Carnobacterium maltaromaticum cultures and hydroalcoholic extract of Lippia sidoides Cham. against Listeria monocytogenes in fish model systems
    • Reis F.B., Souza V.M., Thomaz M.R.S., Fernandes L.P., Oliveira W.P., De Martinis E.C.P. Use of Carnobacterium maltaromaticum cultures and hydroalcoholic extract of Lippia sidoides Cham. against Listeria monocytogenes in fish model systems. Int. J. Food Microbiol. 2011, 146:228-234.
    • (2011) Int. J. Food Microbiol. , vol.146 , pp. 228-234
    • Reis, F.B.1    Souza, V.M.2    Thomaz, M.R.S.3    Fernandes, L.P.4    Oliveira, W.P.5    De Martinis, E.C.P.6
  • 24
    • 79251639867 scopus 로고    scopus 로고
    • Fundamental functionality: recent developments in understanding the structure- activity relationships of lantibiotic peptides
    • Ross A.C., Vederas J.C. Fundamental functionality: recent developments in understanding the structure- activity relationships of lantibiotic peptides. J. Antibiot. 2011, 64:27-34.
    • (2011) J. Antibiot. , vol.64 , pp. 27-34
    • Ross, A.C.1    Vederas, J.C.2
  • 27
    • 0034024616 scopus 로고    scopus 로고
    • Transposition in Lactobacillus sakei: inactivation of a second lactocin S operon by the insertion of IS1520, a new member of the IS3 family of insertion sequences
    • Skaugen M., Nes I.F. Transposition in Lactobacillus sakei: inactivation of a second lactocin S operon by the insertion of IS1520, a new member of the IS3 family of insertion sequences. Microbiology 2000, 146:1163-1169.
    • (2000) Microbiology , vol.146 , pp. 1163-1169
    • Skaugen, M.1    Nes, I.F.2
  • 28
    • 0030902941 scopus 로고    scopus 로고
    • Lactic acid bacteria of foods and their current taxonomy
    • Stiles M.E., Holzapfel W.H. Lactic acid bacteria of foods and their current taxonomy. Int. J. Food Microbiol. 1997, 36:1-29.
    • (1997) Int. J. Food Microbiol. , vol.36 , pp. 1-29
    • Stiles, M.E.1    Holzapfel, W.H.2
  • 30
    • 34547842488 scopus 로고    scopus 로고
    • Quorum-sensing based bacteriocin production is down-regulated by N-terminally truncated species of gene activators
    • Straume D., Kjos M., Nes I.F., Diep D.B. Quorum-sensing based bacteriocin production is down-regulated by N-terminally truncated species of gene activators. Mol. Gen. Genomics. 2007, 278:283-293.
    • (2007) Mol. Gen. Genomics. , vol.278 , pp. 283-293
    • Straume, D.1    Kjos, M.2    Nes, I.F.3    Diep, D.B.4
  • 31
    • 0030944568 scopus 로고    scopus 로고
    • Double-glycine-type leader peptides direct secretion of bacteriocins by ABC transporters: colicin V secretion in Lactococcus lactis
    • Van Belkum M.J., Worobo R.W., Stiles M.E. Double-glycine-type leader peptides direct secretion of bacteriocins by ABC transporters: colicin V secretion in Lactococcus lactis. Mol. Microbiol. 1997, 23:1293-1301.
    • (1997) Mol. Microbiol. , vol.23 , pp. 1293-1301
    • Van Belkum, M.J.1    Worobo, R.W.2    Stiles, M.E.3
  • 32
    • 12244269723 scopus 로고    scopus 로고
    • Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from surimi-associated Carnobacterium piscicola CS526
    • Yamazaki K., Suzuki M., Kawai Y., Inoue N., Montville T.J. Purification and characterization of a novel class IIa bacteriocin, piscicocin CS526, from surimi-associated Carnobacterium piscicola CS526. Appl. Environ. Microbiol. 2005, 71:554-557.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 554-557
    • Yamazaki, K.1    Suzuki, M.2    Kawai, Y.3    Inoue, N.4    Montville, T.J.5


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