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Volumn 11, Issue 1, 2012, Pages 92-97

Changes in the antimicrobial potential of egg albumen during the early stages of incubation and its impact response of Salmonella on the growth and virulence Enteritidis

Author keywords

Antimicrobial activity; Antimicrobial protein; Egg albumen; Incubation; Salmonella enteritidis

Indexed keywords

BACTERIA (MICROORGANISMS); SALMONELLA; SALMONELLA ENTERITIDIS;

EID: 84863651462     PISSN: 15944077     EISSN: None     Source Type: Journal    
DOI: 10.4081/ijas.2012.e17     Document Type: Article
Times cited : (13)

References (33)
  • 1
    • 78651320084 scopus 로고    scopus 로고
    • Role of incubation conditions and protein fraction on the antimicrobial activity of egg white against Salmonella Enteritidis and Escherichia coil
    • Alabdeh, M., Lechevalier, V., Nau, F., Gautier, M., Cochet, M.F., Gonnet, F., Jan, S., Baron, F., 2011. Role of incubation conditions and protein fraction on the antimicrobial activity of egg white against Salmonella Enteritidis and Escherichia coil. J. Food Protect. 74:24-31.
    • (2011) J. Food Protect , vol.74 , pp. 24-31
    • Alabdeh, M.1    Lechevalier, V.2    Nau, F.3    Gautier, M.4    Cochet, M.F.5    Gonnet, F.6    Jan, S.7    Baron, F.8
  • 2
    • 84863684108 scopus 로고    scopus 로고
    • Study of the changes of protein and lysozyme of egg white on embryonic development and storage
    • Kyushu Tokai University Ed
    • Araki, T., Kuwamura, Y., Kuwahara, H., Masuda, S., Torikata, T., 2000. Study of the changes of protein and lysozyme of egg white on embryonic development and storage. Proc. School of Agriculture, Kyushu Tokai University Ed., 19:29-36.
    • (2000) Proc. School of Agriculture , vol.19 , pp. 29-36
    • Araki, T.1    Kuwamura, Y.2    Kuwahara, H.3    Masuda, S.4    Torikata, T.5
  • 3
    • 0029416946 scopus 로고
    • Hil A is a novel ompR/toxR family member that activates the expression of Salmonella typhimurium invasion genes
    • Bajaj, V., Hwang, C., Lee, C.A., 1995. Hil A is a novel ompR/toxR family member that activates the expression of Salmonella typhimurium invasion genes. Mol. Microbiol. 18:715-727.
    • (1995) Mol. Microbiol , vol.18 , pp. 715-727
    • Bajaj, V.1    Hwang, C.2    Lee, C.A.3
  • 4
    • 0029828325 scopus 로고    scopus 로고
    • Co-ordinate regulation of Salmonella typhimurium invasion genes by environmental and regulatory factors is mediated by control of hilA expression
    • Bajaj, V., Lucas, R.L., Hwang, C., Lee, C.A., 1996. Co-ordinate regulation of Salmonella typhimurium invasion genes by environmental and regulatory factors is mediated by control of hilA expression. Mol. Microbiol. 22:703-714.
    • (1996) Mol. Microbiol , vol.22 , pp. 703-714
    • Bajaj, V.1    Lucas, R.L.2    Hwang, C.3    Lee, C.A.4
  • 5
    • 0030828683 scopus 로고    scopus 로고
    • Factors involved in the inhibition of growth of Salmonella enteritidis in liquid egg white
    • Baron, F., Gautier, M., Brule, G., 1997. Factors involved in the inhibition of growth of Salmonella enteritidis in liquid egg white. J. Food. Protect. 60:1318-1323.
    • (1997) J. Food. Protect , vol.60 , pp. 1318-1323
    • Baron, F.1    Gautier, M.2    Brule, G.3
  • 6
    • 0035404546 scopus 로고    scopus 로고
    • Effects of presence of a blastoderm on albumen height and pH of broiler hatching eggs
    • Benton, C.E., Walsh, T.J., Brake, J., 2001. Effects of presence of a blastoderm on albumen height and pH of broiler hatching eggs. Poultry Sci. 80:955-957.
    • (2001) Poultry Sci , vol.80 , pp. 955-957
    • Benton, C.E.1    Walsh, T.J.2    Brake, J.3
  • 7
    • 13444282403 scopus 로고    scopus 로고
    • Why are pathogenic staphy-lococci so lysozyme resistant? The peptido-glycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus
    • Bera, A., Herbert, S., Jakob, A., Vollmer, W., Götz, F., 2005. Why are pathogenic staphy-lococci so lysozyme resistant? The peptido-glycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol. Microbiol. 55:778-787.
    • (2005) Mol. Microbiol , vol.55 , pp. 778-787
    • Bera, A.1    Herbert, S.2    Jakob, A.3    Vollmer, W.4    Götz, F.5
  • 8
    • 0015950632 scopus 로고
    • Non-specific antimicrobial defences of the avian egg, embryo and neonate
    • Boarad, R. G., Fuller, R., 1974. Non-specific antimicrobial defences of the avian egg, embryo and neonate. Biol. Rev. 49:15-49.
    • (1974) Biol. Rev , vol.49 , pp. 15-49
    • Boarad, R.G.1    Fuller, R.2
  • 10
    • 12244276358 scopus 로고    scopus 로고
    • Microbial infection affects egg viability and incubation behavior in a tropical passerine
    • Cook, M.I., Beissinger, S.R., Toranzos, G.A., Rodriguez, R.A., Arendt, W.J., 2005. Microbial infection affects egg viability and incubation behavior in a tropical passerine. Behav. Ecol. 16:30-36.
    • (2005) Behav. Ecol , vol.16 , pp. 30-36
    • Cook, M.I.1    Beissinger, S.R.2    Toranzos, G.A.3    Rodriguez, R.A.4    Arendt, W.J.5
  • 11
    • 0033026022 scopus 로고    scopus 로고
    • Proteolytic activity in the yolk sac membrane of quail eggs
    • Gerhartz, B., Kolb, H.J., Wittmann, J., 1999. Proteolytic activity in the yolk sac membrane of quail eggs. Comp. Biochem. Phys. A 123:1-8.
    • (1999) Comp. Biochem. Phys. A , vol.123 , pp. 1-8
    • Gerhartz, B.1    Kolb, H.J.2    Wittmann, J.3
  • 12
    • 0028711662 scopus 로고
    • Changes in hydration in chicken and duck eggs during incubation
    • Holub, A., Baranyiova, E., Ponizilova, E., 1994. Changes in hydration in chicken and duck eggs during incubation. Vet. Med. 39:605-614.
    • (1994) Vet. Med , vol.39 , pp. 605-614
    • Holub, A.1    Baranyiova, E.2    Ponizilova, E.3
  • 13
    • 84858339613 scopus 로고    scopus 로고
    • A simple assay for measurement of ovotransferrin-a marker of inflammation and infection in birds
    • Horrocks, N.P.C., Tieleman, I.B., Matson, K.D., 2011. A simple assay for measurement of ovotransferrin-a marker of inflammation and infection in birds. Method. Ecol. Evol. 2:518-526.
    • (2011) Method. Ecol. Evol , vol.2 , pp. 518-526
    • Horrocks, N.P.C.1    Tieleman, I.B.2    Matson, K.D.3
  • 14
    • 15944400604 scopus 로고    scopus 로고
    • Salmonella invasion gene regulation: A story of environmental awareness
    • Jones, B.D., 2005. Salmonella invasion gene regulation: A story of environmental awareness. J. Microbiol. 43:110-117.
    • (2005) J. Microbiol , vol.43 , pp. 110-117
    • Jones, B.D.1
  • 15
    • 33748336302 scopus 로고    scopus 로고
    • Survival characteristics of Salmonella enterica serovar Enteritidis in chicken egg albumen
    • Kang, H., Loui, C., Clavijo, R.I., Riley, L.W., Lu, S., 2006. Survival characteristics of Salmonella enterica serovar Enteritidis in chicken egg albumen. Epidemiol. Infect. 134:967-976.
    • (2006) Epidemiol. Infect , vol.134 , pp. 967-976
    • Kang, H.1    Loui, C.2    Clavijo, R.I.3    Riley, L.W.4    Lu, S.5
  • 16
    • 27744563959 scopus 로고    scopus 로고
    • Advances in the value of eggs and egg components for human health
    • Kovacs-Nolan, J., Phillips, M., Mine, Y., 2005. Advances in the value of eggs and egg components for human health. J. Agr. Food Chem. 53:8421-8431.
    • (2005) J. Agr. Food Chem , vol.53 , pp. 8421-8431
    • Kovacs-Nolan, J.1    Phillips, M.2    Mine, Y.3
  • 17
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using realtime quantitative PCR and the 2-[Delta Delta C(T)] method
    • Livak, K.J., Schmittgen, T.D., 2001. Analysis of relative gene expression data using realtime quantitative PCR and the 2-[Delta Delta C(T)] method. Methods 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 18
    • 59849115829 scopus 로고    scopus 로고
    • A study into measuring the antibacterial activity of lysozyme-containing foods
    • Maidment, C., Dyson, A., Beard, J., 2009. A study into measuring the antibacterial activity of lysozyme-containing foods. Nutr. Food Sci. 39:29-35.
    • (2009) Nutr. Food Sci , vol.39 , pp. 29-35
    • Maidment, C.1    Dyson, A.2    Beard, J.3
  • 19
    • 85014275836 scopus 로고    scopus 로고
    • Biologically active hen egg components in human health and disease
    • Mine, Y., Kovacs-Nolan, J., 2004. Biologically active hen egg components in human health and disease. J. Poultry Sci. 41:1-29.
    • (2004) J. Poultry Sci , vol.41 , pp. 1-29
    • Mine, Y.1    Kovacs-Nolan, J.2
  • 20
    • 1542347593 scopus 로고    scopus 로고
    • Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme
    • Mine, Y., Ma, F.P., Lauriau, S., 2004. Antimicrobial peptides released by enzymatic hydrolysis of hen egg white lysozyme. J. Agr. Food Chem. 52:1088-1094.
    • (2004) J. Agr. Food Chem , vol.52 , pp. 1088-1094
    • Mine, Y.1    Ma, F.P.2    Lauriau, S.3
  • 22
    • 0009539811 scopus 로고    scopus 로고
    • Effect of storage temperature and time on egg white protein
    • Schäfer, A., Drewes, W., Schwägele, F., 1999. Effect of storage temperature and time on egg white protein. Nahrung 43:86-89.
    • (1999) Nahrung , vol.43 , pp. 86-89
    • Schäfer, A.1    Drewes, W.2    Schwägele, F.3
  • 24
    • 77958143617 scopus 로고    scopus 로고
    • The battle for iron between bacterial pathogens and their vertebrate hosts
    • Skaar, E.P., 2010. The battle for iron between bacterial pathogens and their vertebrate hosts. Plos Pathog. 6:e1000949.
    • (2010) Plos Pathog , vol.6
    • Skaar, E.P.1
  • 25
    • 0029715684 scopus 로고    scopus 로고
    • Egg proteins: What are their functions?
    • Stevens, L., 1996. Egg proteins: what are their functions? Sci. Prog. 79:65-87.
    • (1996) Sci. Prog , vol.79 , pp. 65-87
    • Stevens, L.1
  • 26
    • 0033574609 scopus 로고    scopus 로고
    • Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability
    • Sugimoto, Y., Sanuki, S., Ohsako, S., Higashimoto, Y., Kondo, M., Kurawaki, J., Ibrahim, H.R., Aoki, T., Kusakabe, T., Koga, K., 1999. Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability. J. Biol. Chem. 274:11030-11037.
    • (1999) J. Biol. Chem , vol.274 , pp. 11030-11037
    • Sugimoto, Y.1    Sanuki, S.2    Ohsako, S.3    Higashimoto, Y.4    Kondo, M.5    Kurawaki, J.6    Ibrahim, H.R.7    Aoki, T.8    Kusakabe, T.9    Koga, K.10
  • 28
    • 0021344328 scopus 로고
    • The influence of incubation temperature and pH on the antimicrobial properties of hen egg albumen
    • Tranter, H. S., Board, R. G., 1984. The influence of incubation temperature and pH on the antimicrobial properties of hen egg albumen. J. Appl. Bacteriol. 56:53-61.
    • (1984) J. Appl. Bacteriol , vol.56 , pp. 53-61
    • Tranter, H.S.1    Board, R.G.2
  • 29
    • 79961202825 scopus 로고    scopus 로고
    • Stress-induced survival strategies enable Salmonella Enteritidis to persistently colonize the chicken oviduct tissue and cope with antimicrobial factors in egg white: A hypothesis to explain a pandemic
    • Van Immerseel, F., 2010. Stress-induced survival strategies enable Salmonella Enteritidis to persistently colonize the chicken oviduct tissue and cope with antimicrobial factors in egg white: A hypothesis to explain a pandemic. Gut Pathog. 2:23.
    • (2010) Gut Pathog , vol.2 , pp. 23
    • van Immerseel, F.1
  • 30
    • 34748879992 scopus 로고    scopus 로고
    • Avian antimicrobial proteins: Structure, distribution and activity
    • Wellman-Labadie, O., Picman, J., Hincke, M.T., 2007. Avian antimicrobial proteins: structure, distribution and activity. World. Poultry Sci. J. 63:421-438.
    • (2007) World. Poultry Sci. J , vol.63 , pp. 421-438
    • Wellman-Labadie, O.1    Picman, J.2    Hincke, M.T.3
  • 31
    • 0038283515 scopus 로고
    • Mechanism of egg white resistance to bacterial growth
    • Yadav, N.K., Vadehra, D.V., 1977. Mechanism of egg white resistance to bacterial growth. J. Food Sci. 42:97-99.
    • (1977) J. Food Sci , vol.42 , pp. 97-99
    • Yadav, N.K.1    Vadehra, D.V.2
  • 32
    • 0036720725 scopus 로고    scopus 로고
    • Modification of fully automated total iron-binding capacity (TIBC) assay in serum and comparison with dimension TIBC method
    • Yamanishi, H., Iyama, S., Yamaguchi, Y., Kanakura, Y., Iwatani, Y., 2002. Modification of fully automated total iron-binding capacity (TIBC) assay in serum and comparison with dimension TIBC method. Clin. Chem. 48:1565-1570.
    • (2002) Clin. Chem , vol.48 , pp. 1565-1570
    • Yamanishi, H.1    Iyama, S.2    Yamaguchi, Y.3    Kanakura, Y.4    Iwatani, Y.5
  • 33
    • 0036164773 scopus 로고    scopus 로고
    • Absorption, transportation and digestion of egg white in quail embryos
    • Yoshizaki, N., Ito, Y., Hori, H., Saito, H., Iwasawa, A., 2002. Absorption, transportation and digestion of egg white in quail embryos. Dev. Growth Differ. 44:11-22.
    • (2002) Dev. Growth Differ , vol.44 , pp. 11-22
    • Yoshizaki, N.1    Ito, Y.2    Hori, H.3    Saito, H.4    Iwasawa, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.