메뉴 건너뛰기




Volumn 65, Issue 12, 2002, Pages 1916-1923

Lytic and nonlytic mechanism of inactivation of gram-positive bacteria by lysozyme under atmospheric and high hydrostatic pressure

Author keywords

[No Author keywords available]

Indexed keywords

LACTOBACILLUS; LACTOBACILLUS JOHNSONII; LISTERIA; LISTERIA INNOCUA; POSIBACTERIA; STAPHYLOCOCCUS; STAPHYLOCOCCUS AUREUS;

EID: 0036909240     PISSN: 0362028X     EISSN: None     Source Type: Journal    
DOI: 10.4315/0362-028X-65.12.1916     Document Type: Article
Times cited : (74)

References (45)
  • 1
    • 0029014984 scopus 로고
    • Pore-forming bacteriocins of gram-positive bacteria and self-protection mechanisms of producer organisms
    • Abee, T. 1995. Pore-forming bacteriocins of gram-positive bacteria and self-protection mechanisms of producer organisms. FEMS Microbiol. Lett. 129:1-10.
    • (1995) FEMS Microbiol. Lett. , vol.129 , pp. 1-10
    • Abee, T.1
  • 2
    • 0030801663 scopus 로고    scopus 로고
    • Bactericidal action of lysozymes attached with various sizes of hydrophobic peptides to the C-terminal using genetic modification
    • Arima, H., H. R. Ibrahim, T. Kinoshita, and A. Kato. 1997. Bactericidal action of lysozymes attached with various sizes of hydrophobic peptides to the C-terminal using genetic modification. FEBS Lett. 415:114-118.
    • (1997) FEBS Lett. , vol.415 , pp. 114-118
    • Arima, H.1    Ibrahim, H.R.2    Kinoshita, T.3    Kato, A.4
  • 3
    • 0032985757 scopus 로고    scopus 로고
    • Analysis of peptidoglycan structure from vegetative cells of Bacillus subtitis 168 and role of PBP 5 in peptidoglycan maturation
    • Atrih, A., G. Bacher, G. Allmaier, M. P. Williamson, and S. J. Foster. 1999. Analysis of peptidoglycan structure from vegetative cells of Bacillus subtitis 168 and role of PBP 5 in peptidoglycan maturation. J. Bacteriol. 181:3956-3966.
    • (1999) J. Bacteriol. , vol.181 , pp. 3956-3966
    • Atrih, A.1    Bacher, G.2    Allmaier, G.3    Williamson, M.P.4    Foster, S.J.5
  • 4
    • 0032189233 scopus 로고    scopus 로고
    • Synthesis and evaluation of lysozyme derivatives exhibiting an enhanced antimicrobial action
    • Bernkop-Schnurch, A., S. Krist, M. Vehabovic, and C. Valenta. 1998. Synthesis and evaluation of lysozyme derivatives exhibiting an enhanced antimicrobial action. Eur. J. Pharm. Sci. 6:301-306.
    • (1998) Eur. J. Pharm. Sci. , vol.6 , pp. 301-306
    • Bernkop-Schnurch, A.1    Krist, S.2    Vehabovic, M.3    Valenta, C.4
  • 5
    • 0026605558 scopus 로고
    • O-acetylated peptidoglycan: Its occurrence, pathobiological significance, and biosynthesis
    • Clarke, A., and C. Dupont. 1992. O-acetylated peptidoglycan: Its occurrence, pathobiological significance, and biosynthesis. Can. J. Microbiol. 38:85-91.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 85-91
    • Clarke, A.1    Dupont, C.2
  • 6
    • 0024021735 scopus 로고
    • Formation and regeneration of protoplasts and spheroplasts of gastrointestinal strains of lactobacilli
    • Connell, H., J. Lemmon, and G. W. Tannock. 1988. Formation and regeneration of protoplasts and spheroplasts of gastrointestinal strains of lactobacilli. Appl. Environ. Microbiol. 54:1615-1618.
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 1615-1618
    • Connell, H.1    Lemmon, J.2    Tannock, G.W.3
  • 8
    • 0345103456 scopus 로고    scopus 로고
    • Inactivation of Escherichia coli in milk by high hydrostatic pressure treatment in combination with antimicrobial peptides
    • García-Graells, C., B. Masschalck, and C. W. Michiels. 1999. Inactivation of Escherichia coli in milk by high hydrostatic pressure treatment in combination with antimicrobial peptides. J. Food Prot. 62:1248-1254.
    • (1999) J. Food Prot. , vol.62 , pp. 1248-1254
    • García-Graells, C.1    Masschalck, B.2    Michiels, C.W.3
  • 9
    • 0000864690 scopus 로고    scopus 로고
    • High pressure transient sensitization of Escherichia coli to lysozyme and nisin by disruption of outer membrane permeability
    • Hauben, K., E. Wuytack, C. Soontjens, and C. W. Michiels. 1996. High pressure transient sensitization of Escherichia coli to lysozyme and nisin by disruption of outer membrane permeability. J. Food Prot. 59:350-355.
    • (1996) J. Food Prot. , vol.59 , pp. 350-355
    • Hauben, K.1    Wuytack, E.2    Soontjens, C.3    Michiels, C.W.4
  • 10
    • 0002884888 scopus 로고
    • High pressure effects on biomolecules
    • D. A. Ledward, D. E. Johnston, R. G. Earnshaw, and A. P. M. Hasting (ed.). Nottingham University Press, Leicestershire, UK
    • Heremans, K. 1995. High pressure effects on biomolecules, p. 81-97. In D. A. Ledward, D. E. Johnston, R. G. Earnshaw, and A. P. M. Hasting (ed.), High Pressure Processing of Foods. Nottingham University Press, Leicestershire, UK.
    • (1995) High Pressure Processing of Foods , pp. 81-97
    • Heremans, K.1
  • 11
    • 0000432129 scopus 로고
    • Enhanced antimicrobial action of lysozyme against gram-negative and gram-positive bacteria due to modification with perillaldehyde
    • Ibrahim, H. R., H. Hatta, M. Fujiki, M. Kim, and T. Yamamoto. 1994. Enhanced antimicrobial action of lysozyme against gram-negative and gram-positive bacteria due to modification with perillaldehyde. J. Agric. Food Chem. 42:1813-1817.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1813-1817
    • Ibrahim, H.R.1    Hatta, H.2    Fujiki, M.3    Kim, M.4    Yamamoto, T.5
  • 12
    • 0001256923 scopus 로고    scopus 로고
    • Partially unfolded lysozyme at neutral pH agglutinates and kills gram-negative and gram-positive bacteria through membrane damage mechanism
    • Ibrahim, H. R., S. Higashiguchi, M. Koketsu, F. Juneja, M. Kim, T. Yamamoto, Y. Sugimoto, and T. Aoki. 1996. Partially unfolded lysozyme at neutral pH agglutinates and kills gram-negative and gram-positive bacteria through membrane damage mechanism. J. Agric. Chem. 44:3799-3806.
    • (1996) J. Agric. Chem. , vol.44 , pp. 3799-3806
    • Ibrahim, H.R.1    Higashiguchi, S.2    Koketsu, M.3    Juneja, F.4    Kim, M.5    Yamamoto, T.6    Sugimoto, Y.7    Aoki, T.8
  • 14
    • 0002857690 scopus 로고    scopus 로고
    • Role of divalent cations in the novel bactericidal activity of the partially unfolded lysozyme
    • Ibrahim, H. R., S. Higashiguchi, Y. Sugimoto, and T. Aoki. 1997. Role of divalent cations in the novel bactericidal activity of the partially unfolded lysozyme. J. Agric. Food Chem. 45:89-94.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 89-94
    • Ibrahim, H.R.1    Higashiguchi, S.2    Sugimoto, Y.3    Aoki, T.4
  • 15
    • 0001485251 scopus 로고
    • Antimicrobial effects of lysozyme against gram-negative bacteria due to covalent binding of palmitic acid
    • Ibrahim, H. R., A. Kato, and K. Kobayashi. 1991. Antimicrobial effects of lysozyme against gram-negative bacteria due to covalent binding of palmitic acid. J. Agric. Food Chem. 39:2077-2082.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 2077-2082
    • Ibrahim, H.R.1    Kato, A.2    Kobayashi, K.3
  • 16
    • 0001406217 scopus 로고
    • Length of hydrocarbon chain and antimicrobial action to gram-negative bacteria of fatty acylated lysozyme
    • Ibrahim, H. R., K. Kobayashi, and A. Kato. 1993. Length of hydrocarbon chain and antimicrobial action to gram-negative bacteria of fatty acylated lysozyme. J. Agric. Food Chem. 41:1164-1168.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1164-1168
    • Ibrahim, H.R.1    Kobayashi, K.2    Kato, A.3
  • 17
    • 0035964823 scopus 로고    scopus 로고
    • Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function
    • Ibrahim, H. R., T. Matsuzaki, and T. Aoki. 2001. Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function. FEBS Lett. 506:27-32.
    • (2001) FEBS Lett. , vol.506 , pp. 27-32
    • Ibrahim, H.R.1    Matsuzaki, T.2    Aoki, T.3
  • 18
    • 0026901107 scopus 로고
    • Bactericidal action of lysozyme against gram-negative bacteria due to insertion of a hydrophobic pentapeptide into its C-terminus
    • Ibrahim, H. R., M. Yamada, K. Kobayashi, and A. Kato. 1992. Bactericidal action of lysozyme against gram-negative bacteria due to insertion of a hydrophobic pentapeptide into its C-terminus. Biosci. Biotechnol. Biochem. 56:1361-1363.
    • (1992) Biosci. Biotechnol. Biochem. , vol.56 , pp. 1361-1363
    • Ibrahim, H.R.1    Yamada, M.2    Kobayashi, K.3    Kato, A.4
  • 19
    • 0030870671 scopus 로고    scopus 로고
    • Bactericidal activity of human lysozymes carrying various lengths of polyproline chain at the C-terminus
    • Ito, Y., O. H. Kwon, M. Ueda, A. Tanaka, and Y. Imanishi. 1997. Bactericidal activity of human lysozymes carrying various lengths of polyproline chain at the C-terminus. FEBS Lett. 415:285-288.
    • (1997) FEBS Lett. , vol.415 , pp. 285-288
    • Ito, Y.1    Kwon, O.H.2    Ueda, M.3    Tanaka, A.4    Imanishi, Y.5
  • 20
    • 0019452877 scopus 로고
    • The energized membrane and cellular autolysis in Bacillus subtilis
    • Jolliffe, L. K., R. J. Doyle, and N. Streips. 1981. The energized membrane and cellular autolysis in Bacillus subtilis. Cell 25:753-763.
    • (1981) Cell , vol.25 , pp. 753-763
    • Jolliffe, L.K.1    Doyle, R.J.2    Streips, N.3
  • 21
    • 0032052619 scopus 로고    scopus 로고
    • Interaction of hydrostatic pressure, time and temperature of pressurization and pediocin AcH on inactivation of foodborne bacteria
    • Kalchayanand, N., A. Sikes, C. P. Dunne, and B. Ray. 1998. Interaction of hydrostatic pressure, time and temperature of pressurization and pediocin AcH on inactivation of foodborne bacteria. J. Food Prot. 61:425-431.
    • (1998) J. Food Prot. , vol.61 , pp. 425-431
    • Kalchayanand, N.1    Sikes, A.2    Dunne, C.P.3    Ray, B.4
  • 22
    • 0028062817 scopus 로고
    • Hydrostatic pressure and electroporation efficiency in combination with bacteriocins
    • Kalchayanand, N., T. Sikes, C. P. Dunne, and B. Ray. 1994. Hydrostatic pressure and electroporation efficiency in combination with bacteriocins. Appl. Environ. Microbiol. 60:4174-4177.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 4174-4177
    • Kalchayanand, N.1    Sikes, T.2    Dunne, C.P.3    Ray, B.4
  • 23
    • 0027236008 scopus 로고
    • Proton motive force may regulate cell wall-associated enzymes of Bacillus subtilis
    • Kemper, M. A., M. M. Urrutia, T. J. Beveridge, A. K. Koch, and R. J. Doyle. 1993. Proton motive force may regulate cell wall-associated enzymes of Bacillus subtilis. J. Bacteriol. 175:5690-5696.
    • (1993) J. Bacteriol. , vol.175 , pp. 5690-5696
    • Kemper, M.A.1    Urrutia, M.M.2    Beveridge, T.J.3    Koch, A.K.4    Doyle, R.J.5
  • 24
    • 0021796925 scopus 로고
    • Bactericidal activity of human lysozyme, muramidase-inactive lysozyme, and cationic polypeptides against Streptococcus sanguis and Streptococcus faecalis: Inhibition by chitin oligosaccharides
    • Laible, N. J., and G. R. Germaine. 1985. Bactericidal activity of human lysozyme, muramidase-inactive lysozyme, and cationic polypeptides against Streptococcus sanguis and Streptococcus faecalis: Inhibition by chitin oligosaccharides. Infect. Immun. 48:720-728.
    • (1985) Infect. Immun. , vol.48 , pp. 720-728
    • Laible, N.J.1    Germaine, G.R.2
  • 25
    • 0014409087 scopus 로고
    • Studies on the permeability change produced in coliform bacteria by ethylenediaminetetraacetate
    • Leive, L. 1968. Studies on the permeability change produced in coliform bacteria by ethylenediaminetetraacetate. J. Biol. Chem. 243:2373-2380.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2373-2380
    • Leive, L.1
  • 26
    • 0032780720 scopus 로고    scopus 로고
    • The use of multiple indices of physiological activity to access viability in chlorine disinfected Escherichia coli O15:H7
    • Lisle, J. T., B. H. Pyle, and G. A. McFeters. 1999. The use of multiple indices of physiological activity to access viability in chlorine disinfected Escherichia coli O15:H7. Lett. Appt. Microbiol. 29:42-47.
    • (1999) Lett. Appt. Microbiol. , vol.29 , pp. 42-47
    • Lisle, J.T.1    Pyle, B.H.2    McFeters, G.A.3
  • 28
    • 0001142069 scopus 로고
    • Effects of high hydrostatic pressure on natural and artificial membranes
    • C. Balny, R. Hayashi, K. Heremans, and P. Masson (ed.). Colloques INSERM/John Libbey Eurotext Ltd., Montrouge, France
    • Macdonald, A. G. 1992. Effects of high hydrostatic pressure on natural and artificial membranes, p. 67-75. In C. Balny, R. Hayashi, K. Heremans, and P. Masson (ed.), High Pressure and Biotechnology. Colloques INSERM/John Libbey Eurotext Ltd., Montrouge, France.
    • (1992) High Pressure and Biotechnology , pp. 67-75
    • Macdonald, A.G.1
  • 31
    • 0035916960 scopus 로고    scopus 로고
    • High pressure increases bactericidal activity and spectrum of lactoferrin, lactoferricin and nisin
    • Masschalck, B., R. Van Houdt, and C. W. Michiels. 2001. High pressure increases bactericidal activity and spectrum of lactoferrin, lactoferricin and nisin. Int. J. Food Microbiol. 64:325-332.
    • (2001) Int. J. Food Microbiol. , vol.64 , pp. 325-332
    • Masschalck, B.1    Van Houdt, R.2    Michiels, C.W.3
  • 32
    • 0035158386 scopus 로고    scopus 로고
    • Inactivation of gram-negative bacteria by lysozyme, denatured lysozyme and lysozyme-derived peptides under high hydrostatic pressure
    • Masschalck, B., R. Van Houdt, E. G. R. Van Haver, and C. W. Michiels. 2001. Inactivation of gram-negative bacteria by lysozyme, denatured lysozyme and lysozyme-derived peptides under high hydrostatic pressure. Appl. Environ. Microbiol. 67:339-344.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 339-344
    • Masschalck, B.1    Van Houdt, R.2    Van Haver, E.G.R.3    Michiels, C.W.4
  • 33
    • 0015522563 scopus 로고
    • On the mode of in vivo assembly of the cell wall of Bacillus subtilis
    • Mauck, J., and L. Glaser. 1972. On the mode of in vivo assembly of the cell wall of Bacillus subtilis. J. Biol. Chem. 247:1180-1187.
    • (1972) J. Biol. Chem. , vol.247 , pp. 1180-1187
    • Mauck, J.1    Glaser, L.2
  • 34
    • 0029965071 scopus 로고    scopus 로고
    • Protective effect of lysozyme-galactomannan or lysozyme-palmitic acid conjugates against Edwardsiella tarda infection in carp, Cyprinus carpio. L.
    • Nakamura, S., Y. Gohya, J. N. Losso, S. Nakai, and A. Kato. 1996. Protective effect of lysozyme-galactomannan or lysozyme-palmitic acid conjugates against Edwardsiella tarda infection in carp, Cyprinus carpio. L. FEBS Lett. 383:251-254.
    • (1996) Febs Lett. , vol.383 , pp. 251-254
    • Nakamura, S.1    Gohya, Y.2    Losso, J.N.3    Nakai, S.4    Kato, A.5
  • 35
    • 33751391825 scopus 로고
    • Bifunctional lysozyme-galactomannan conjugate having excellent emulsifying properties and bactericidal effect
    • Nakamura, S., A. Kato, and K. Kobayashi. 1992. Bifunctional lysozyme-galactomannan conjugate having excellent emulsifying properties and bactericidal effect. J. Agric. Food Chem. 40:735-739.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 735-739
    • Nakamura, S.1    Kato, A.2    Kobayashi, K.3
  • 36
    • 0028052636 scopus 로고
    • Comparison of EDTA and apo-lactoferrin with lysozyme on the growth of foodborne pathogenic and spoilage bacteria
    • Payne, K. D., S. P. Oliver, and P. M. Davidson. 1994. Comparison of EDTA and apo-lactoferrin with lysozyme on the growth of foodborne pathogenic and spoilage bacteria. J. Food Prot. 57:62-65.
    • (1994) J. Food Prot. , vol.57 , pp. 62-65
    • Payne, K.D.1    Oliver, S.P.2    Davidson, P.M.3
  • 37
    • 0001673569 scopus 로고
    • Factors influencing lysis of frozen Escherichia coli cells by lysozyme
    • Ray, B., C. Johnson, and B. Wanismail. 1984. Factors influencing lysis of frozen Escherichia coli cells by lysozyme. Cryo Lett. 5:183-190.
    • (1984) Cryo Lett. , vol.5 , pp. 183-190
    • Ray, B.1    Johnson, C.2    Wanismail, B.3
  • 38
    • 0035348185 scopus 로고    scopus 로고
    • Morphological and physiological characterization of Listeria monocytogenes subjected to high hydrostatic pressure
    • Ritz, M., J. L. Tholozan, M. Federighi, and M. F. Pilet. 2001. Morphological and physiological characterization of Listeria monocytogenes subjected to high hydrostatic pressure. Appl. Environ. Microbiol. 67:2240-2247.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2240-2247
    • Ritz, M.1    Tholozan, J.L.2    Federighi, M.3    Pilet, M.F.4
  • 39
    • 0023491341 scopus 로고
    • Voltage-dependent depolarisation of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin
    • Sahl, H.-G., M. Kordel, and R. Benz. 1987. Voltage-dependent depolarisation of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin. Arch. Microbiol. 149:120-124.
    • (1987) Arch. Microbiol. , vol.149 , pp. 120-124
    • Sahl, H.-G.1    Kordel, M.2    Benz, R.3
  • 40
    • 77956866741 scopus 로고
    • Microbial peptidoglycan (murein) hydrolases
    • J. M. Ghuysen and R. Hakenbeck (ed.). Elsevier, London
    • Shockman, G. D., and J.-V. Höltje. 1994. Microbial peptidoglycan (murein) hydrolases, p. 131-166. In J. M. Ghuysen and R. Hakenbeck (ed.), Bacterial Cell Wall. Elsevier, London.
    • (1994) Bacterial Cell Wall , pp. 131-166
    • Shockman, G.D.1    Höltje, J.-V.2
  • 41
    • 0031895730 scopus 로고    scopus 로고
    • Flow cytometry demonstrates bacteriocin-induced injury to Listeria monocytogenes
    • Swarts, A. J., J. W. Hastings, R. F. Roberts, and A. von Holey. 1998. Flow cytometry demonstrates bacteriocin-induced injury to Listeria monocytogenes. Curr. Microbiol. 36:266-270.
    • (1998) Curr. Microbiol. , vol.36 , pp. 266-270
    • Swarts, A.J.1    Hastings, J.W.2    Roberts, R.F.3    Von Holey, A.4
  • 42
    • 0032850540 scopus 로고    scopus 로고
    • Synergistic actions of nisin, sublethal injury pressure, and reduced temperature on bacteria and yeast
    • ter Steeg, P. F., J. C. Hellemons, and A. E. Kok. 1999. Synergistic actions of nisin, sublethal injury pressure, and reduced temperature on bacteria and yeast. Appl. Environ. Microbiol. 65:4148-4154.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 4148-4154
    • Ter Steeg, P.F.1    Hellemons, J.C.2    Kok, A.E.3
  • 43
    • 0001327089 scopus 로고
    • Lysozyme, ovotransferrin and avidin
    • V. W. Dillon and R. G. Board (ed.). CAB International, Wallingford, Oxon, UK
    • Tranter, H. S. 1994. Lysozyme, ovotransferrin and avidin, p. 65-97. In V. W. Dillon and R. G. Board (ed.), Natural Antimicrobial Systems and Food Preservation. CAB International, Wallingford, Oxon, UK.
    • (1994) Natural Antimicrobial Systems and Food Preservation , pp. 65-97
    • Tranter, H.S.1
  • 44
    • 0000622943 scopus 로고
    • Involvement of membrane-lipids in cold shock-induced autolysis of Bacillus subtilis cells
    • Tsuchido, T., T. Nishino, Y. Kato, and M. Takano. 1995. Involvement of membrane-lipids in cold shock-induced autolysis of Bacillus subtilis cells. Biosci. Biotechnol. Biochem. 59:1636-1640.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 1636-1640
    • Tsuchido, T.1    Nishino, T.2    Kato, Y.3    Takano, M.4
  • 45
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara, M. 1992. Agents that increase the permeability of the outer membrane. Microbiol. Rev. 56:395-411.
    • (1992) Microbiol. Rev. , vol.56 , pp. 395-411
    • Vaara, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.