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Volumn 28, Issue SUPPL. 1, 2006, Pages 121-131

Purification and amino acid sequence of a bacteriocins produced by Lactobacillus salivarius K7 isolated from chicken intestine

Author keywords

Bacteriocin; Chicken; Lactic acid bacteria

Indexed keywords


EID: 33646354638     PISSN: 01253395     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (26)

References (22)
  • 1
    • 0035882219 scopus 로고    scopus 로고
    • Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19
    • Atrih, A., Rekhif, N., Moir, A.J.G., Lebrihi, A., and Lefebvre, G. 2001. Mode of action, purification and amino acid sequence of plantaricin C19, an anti-Listeria bacteriocin produced by Lactobacillus plantarum C19. Inter. J. Food Microbiol., 68: 93-104.
    • (2001) Inter. J. Food Microbiol. , vol.68 , pp. 93-104
    • Atrih, A.1    Rekhif, N.2    Moir, A.J.G.3    Lebrihi, A.4    Lefebvre, G.5
  • 2
    • 0034111146 scopus 로고    scopus 로고
    • Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus feacalis BFE 1071
    • Balla, E., Dicks, L.M.T., Du Toit, M., Van Der Merwe, M.J. and Holzapfel, W.H. 2000. Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus feacalis BFE 1071. Appl. Environ. Microbiol., 66(4): 1298-1304.
    • (2000) Appl. Environ. Microbiol. , vol.66 , Issue.4 , pp. 1298-1304
    • Balla, E.1    Dicks, L.M.T.2    Du Toit, M.3    Van Der Merwe, M.J.4    Holzapfel, W.H.5
  • 3
    • 33646362702 scopus 로고    scopus 로고
    • Characterization of salivaricin B, A protein expressed by Lactobacillus salivarius M7
    • Cataloluk., O. and Gurakan, C.G. 2003. Characterization of salivaricin B, A protein expressed by Lactobacillus salivarius M7. Turk. J. Biol., 27: 131-136.
    • (2003) Turk. J. Biol. , vol.27 , pp. 131-136
    • Cataloluk, O.1    Gurakan, C.G.2
  • 4
    • 0035283752 scopus 로고    scopus 로고
    • Rapid PCR-based procedure to identify lactic acid bacteria: Application to six common Lactobacillus species
    • Chagnaud, P., Machinis, K., Coutte, L.A., Marecat, A. and Mercenier, A. 2001. Rapid PCR-based procedure to identify lactic acid bacteria: application to six common Lactobacillus species. J. Microbiol. Methods, 44: 139-148.
    • (2001) J. Microbiol. Methods , vol.44 , pp. 139-148
    • Chagnaud, P.1    Machinis, K.2    Coutte, L.A.3    Marecat, A.4    Mercenier, A.5
  • 6
    • 0034462540 scopus 로고    scopus 로고
    • Biochemical and genetic evidence that Enterococcus feacium L50 produces enterocin L50 A and L50 B, 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., Hernadez, P.E. and Nes, I.F. 2000. Biochemical and genetic evidence that Enterococcus feacium L50 produces enterocin L50 A and L50 B, the sec- dependent enterocin P, and a novel bacteriocin secreted without an N-terminal extension termed enterocin Q. J. Bacteriol., 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    Hernadez, P.E.6    Nes, I.F.7
  • 8
    • 0039967275 scopus 로고    scopus 로고
    • Investigation of bacetriocin production and purification from Nukadoko Isolates displaying anitimicrobial activity
    • Ennahar, S., Zendo, T., Sonomoto, K. and Ishizaki, A. 1999. Investigation of bacetriocin production and purification from Nukadoko Isolates displaying anitimicrobial activity. Jap. J. Lactic Acid Bacteria, 10: 29-36.
    • (1999) Jap. J. Lactic Acid Bacteria , vol.10 , pp. 29-36
    • Ennahar, S.1    Zendo, T.2    Sonomoto, K.3    Ishizaki, A.4
  • 10
    • 0036230805 scopus 로고    scopus 로고
    • Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp
    • Flynn, S., Sinderen, D.V., Thornton, G. M., Holo, H., Nes, I.F. and Collins, J.K. 2002. Characterization of the genetic locus responsible for the production of ABP-118, a novel bacteriocin produced by the probiotic bacterium Lactobacillus salivarius subsp. salivarius UCC118. Microbiol., 148: 973-984.
    • (2002) Salivarius UCC118. Microbiol. , vol.148 , pp. 973-984
    • Flynn, S.1    Sinderen, D.V.2    Thornton, G.M.3    Holo, H.4    Nes, I.F.5    Collins, J.K.6
  • 12
    • 0000219186 scopus 로고
    • Regular, nonsporing gram-positive rods
    • Sneath, P.H.A., Mair, N.S., Sharp M.E and Holt, J.G. (eds.). The Williams and Wilkins Co., Baltimore
    • Kandler, O. and Weiss, N. 1986. Regular, nonsporing gram-positive rods, pp 1208-1233. In: Sneath, P.H.A., Mair, N.S., Sharp M.E and Holt, J.G. (eds.). Bergey's Manual of systematic Bacteriology, vol. 2. The Williams and Wilkins Co., Baltimore.
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1208-1233
    • Kandler, O.1    Weiss, N.2
  • 13
    • 0028981814 scopus 로고
    • Evaluation of prokaryotic diversity by restrictase digestion of 16S rDNA directly amplified from hypersaline environments
    • Martinez-Murcia, A. J., Acinas, S. G. and Rodriguez-Valera, F. 1995. Evaluation of prokaryotic diversity by restrictase digestion of 16S rDNA directly amplified from hypersaline environments. FEMS Microbiol. Ecol. 17: 247-256.
    • (1995) FEMS Microbiol. Ecol. , vol.17 , pp. 247-256
    • Martinez-Murcia, A.J.1    Acinas, S.G.2    Rodriguez-Valera, F.3
  • 14
    • 0037196194 scopus 로고    scopus 로고
    • Inhibitory substances produced by Lactobacilli isolated from sourdoughs - A review
    • Messens, W. and De Vuyst, L. 2002. Inhibitory substances produced by Lactobacilli isolated from sourdoughs - a review. Int. J. Food Microbiol., 72: 31-43.
    • (2002) Int. J. Food Microbiol. , vol.72 , pp. 31-43
    • Messens, W.1    De Vuyst, L.2
  • 15
    • 0036589165 scopus 로고    scopus 로고
    • Potential of bacteriocin-producing lactic acid bacteria for improvements in food safety and quality
    • O' Sullivan, L., Ross, R.P. and Hill, C. 2002. Potential of bacteriocin-producing lactic acid bacteria for improvements in food safety and quality. Biochemie, 84: 593-604.
    • (2002) Biochemie , vol.84 , pp. 593-604
    • O'Sullivan, L.1    Ross, R.P.2    Hill, C.3
  • 16
    • 0028914567 scopus 로고
    • A comparison of methods for the measurement of bacteriocin activity
    • Parente, E., Brienza, C., Moles, M. and Ricciardi, A. 1995. A comparison of methods for the measurement of bacteriocin activity. J. Microbiol. Methods, 22: 95-108.
    • (1995) J. Microbiol. Methods , vol.22 , pp. 95-108
    • Parente, E.1    Brienza, C.2    Moles, M.3    Ricciardi, A.4
  • 17
    • 0032749389 scopus 로고    scopus 로고
    • Production, recovery and purification of bacteriocins from lactic acid bacteria
    • Parente, E., and Ricciardi, A. 1999. Production, recovery and purification of bacteriocins from lactic acid bacteria. App. Microbiol. Biotechnol., 52: 628-638.
    • (1999) App. Microbiol. Biotechnol. , vol.52 , pp. 628-638
    • Parente, E.1    Ricciardi, A.2
  • 18
    • 0029912668 scopus 로고    scopus 로고
    • Clinical uses of probiotics for stabilizing the gut mucosal barrier: Successful strains and future challenges
    • Salminen, S., Isolauri, E. and Salminen, E. 1996. Clinical uses of probiotics for stabilizing the gut mucosal barrier: successful strains and future challenges. Antonie Van Leeuwenhoek, 70: 251-262.
    • (1996) Antonie Van Leeuwenhoek , vol.70 , pp. 251-262
    • Salminen, S.1    Isolauri, E.2    Salminen, E.3
  • 20
    • 0142124980 scopus 로고    scopus 로고
    • Role of lactic acid bacteria (LAB) in food preservation and human health - A review
    • Soomro, A.H., Masud, T. and Anwaar, K. 2002. Role of lactic acid bacteria (LAB) in food preservation and human health - a review. Pakistan J. Nutrition, 1(1): 20-24.
    • (2002) Pakistan J. Nutrition , vol.1 , Issue.1 , pp. 20-24
    • Soomro, A.H.1    Masud, T.2    Anwaar, K.3
  • 21
    • 0036154401 scopus 로고    scopus 로고
    • Rapid two-step procedure for large-scale purification of pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium
    • Uteng, M., Hauge, H.H., Brondz, I., Meyer, J.N. and Fimland, G. 2002. Rapid two-step procedure for large-scale purification of pediocin-like bacteriocins and other cationic antimicrobial peptides from complex culture medium. Appl. Environ. Microbiol., 68: 952-956.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 952-956
    • Uteng, M.1    Hauge, H.H.2    Brondz, I.3    Meyer, J.N.4    Fimland, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.