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Volumn 44, Issue 10, 2009, Pages 1144-1151

Production and characterization of a C15-surfactin-O-methyl ester by a lipopeptide producing strain Bacillus subtilis HSO121

Author keywords

Bacillus subtilis; Carboxyl group; Hela cell; Structure; Surface activity; Surfactin

Indexed keywords

BACILLUS SUBTILIS; CARBOXYL GROUP; HELA CELL; STRUCTURE; SURFACE ACTIVITY; SURFACTIN;

EID: 69249218967     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2009.06.014     Document Type: Article
Times cited : (60)

References (50)
  • 2
    • 33744969621 scopus 로고    scopus 로고
    • Molecular structures of microbial lipopeptides
    • Liu X.Y., Yang S.Z., and Mu B.Z. Molecular structures of microbial lipopeptides. Biotechnol Bull (2005) 18-26
    • (2005) Biotechnol Bull , pp. 18-26
    • Liu, X.Y.1    Yang, S.Z.2    Mu, B.Z.3
  • 3
    • 42149129522 scopus 로고    scopus 로고
    • Lipopeptide secondary metabolites from the phytopathogenic bacterium Pseudomonas syringae
    • Upadhyay R.K. (Ed), Kluwer Academic/Plenum Publishers, New York
    • Grgurina I. Lipopeptide secondary metabolites from the phytopathogenic bacterium Pseudomonas syringae. In: Upadhyay R.K. (Ed). Advances in microbial toxin research and its biotechnological exploitation (2002), Kluwer Academic/Plenum Publishers, New York 105-140
    • (2002) Advances in microbial toxin research and its biotechnological exploitation , pp. 105-140
    • Grgurina, I.1
  • 4
    • 29244459093 scopus 로고    scopus 로고
    • Natural products to drugs: daptomycin and related lipopeptide antibiotics
    • Baltz R.H., Miao V., and Wrigley S.K. Natural products to drugs: daptomycin and related lipopeptide antibiotics. Nat Prod Rep 22 (2005) 717-741
    • (2005) Nat Prod Rep , vol.22 , pp. 717-741
    • Baltz, R.H.1    Miao, V.2    Wrigley, S.K.3
  • 5
    • 0032831422 scopus 로고    scopus 로고
    • High- and low-molecular-mass microbial surfactants
    • Rosenberg E., and Ron E.Z. High- and low-molecular-mass microbial surfactants. Appl Microbiol Biotechnol 52 (1999) 154-162
    • (1999) Appl Microbiol Biotechnol , vol.52 , pp. 154-162
    • Rosenberg, E.1    Ron, E.Z.2
  • 7
    • 1242270554 scopus 로고    scopus 로고
    • Potential applications of microbial surfactants in biomedical sciences
    • Singh P., and Cameotra S.S. Potential applications of microbial surfactants in biomedical sciences. Trends Biotechnol 22 (2004) 142-146
    • (2004) Trends Biotechnol , vol.22 , pp. 142-146
    • Singh, P.1    Cameotra, S.S.2
  • 8
    • 2942560687 scopus 로고    scopus 로고
    • Recent applications of biosurfactants as biological and immunological molecules
    • Cameotra S.S., and Makkar R.S. Recent applications of biosurfactants as biological and immunological molecules. Curr Opin Microbiol 7 (2004) 262-266
    • (2004) Curr Opin Microbiol , vol.7 , pp. 262-266
    • Cameotra, S.S.1    Makkar, R.S.2
  • 9
    • 0020619631 scopus 로고
    • Acylpeptides, the inhibitors of cyclic adenosine 3′, 5′-monophosphate phosphodiesterase. III. Inhibition of cyclic AMP phosphodiesterase
    • Hosono K., and Suzuki H. Acylpeptides, the inhibitors of cyclic adenosine 3′, 5′-monophosphate phosphodiesterase. III. Inhibition of cyclic AMP phosphodiesterase. J Antibiot 36 (1983) 679-683
    • (1983) J Antibiot , vol.36 , pp. 679-683
    • Hosono, K.1    Suzuki, H.2
  • 10
    • 0031008172 scopus 로고    scopus 로고
    • Inhibition of alkaline phosphatase by surfactin, a natural chelating lipopeptide from Bacillus subtilis
    • Bortolato M., Besson F., and Roux B. Inhibition of alkaline phosphatase by surfactin, a natural chelating lipopeptide from Bacillus subtilis. Biotechnol Lett 19 (1997) 433-435
    • (1997) Biotechnol Lett , vol.19 , pp. 433-435
    • Bortolato, M.1    Besson, F.2    Roux, B.3
  • 11
    • 33846042565 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding and neutralizing activities of surfactin C in experimental models of septic shock
    • Hwang Y.H., Park B.K., Lim J.H., Kim M.S., Park S.C., Hwang M.H., et al. Lipopolysaccharide-binding and neutralizing activities of surfactin C in experimental models of septic shock. Eur J Pharmacol 556 (2007) 166-171
    • (2007) Eur J Pharmacol , vol.556 , pp. 166-171
    • Hwang, Y.H.1    Park, B.K.2    Lim, J.H.3    Kim, M.S.4    Park, S.C.5    Hwang, M.H.6
  • 12
    • 33644523413 scopus 로고    scopus 로고
    • Inhibition of lipopolysaccharide activity by a bacterial cyclic lipopeptide surfactin
    • Takahashi T., Ohno O., Ikeda Y., Sawa R., Homma Y., Igarashi M., et al. Inhibition of lipopolysaccharide activity by a bacterial cyclic lipopeptide surfactin. J Antibiot 59 (2006) 35-43
    • (2006) J Antibiot , vol.59 , pp. 35-43
    • Takahashi, T.1    Ohno, O.2    Ikeda, Y.3    Sawa, R.4    Homma, Y.5    Igarashi, M.6
  • 13
    • 0141736923 scopus 로고    scopus 로고
    • Diversity among microbial cyclic lipopeptides: iturins and surfactins. Activity-structure relationships to design new bioactive agents
    • Bonmatin J.M., Laprevote O., and Peypoux F. Diversity among microbial cyclic lipopeptides: iturins and surfactins. Activity-structure relationships to design new bioactive agents. Comb Chem High Throughput Screen 6 (2003) 541-556
    • (2003) Comb Chem High Throughput Screen , vol.6 , pp. 541-556
    • Bonmatin, J.M.1    Laprevote, O.2    Peypoux, F.3
  • 14
    • 33747345019 scopus 로고    scopus 로고
    • In vivo biocombinatorial synthesis of lipopeptides by COM domain-mediated reprogramming of the surfactin biosynthetic complex
    • Chiocchini C., Linne U., and Stachelhaus T. In vivo biocombinatorial synthesis of lipopeptides by COM domain-mediated reprogramming of the surfactin biosynthetic complex. Chem Biol 13 (2006) 899-908
    • (2006) Chem Biol , vol.13 , pp. 899-908
    • Chiocchini, C.1    Linne, U.2    Stachelhaus, T.3
  • 15
    • 0036878177 scopus 로고    scopus 로고
    • Modification of biologically active peptides: production of a novel lipohexapeptide after engineering of Bacillus subtilis surfactin synthetase
    • Symmank H., Franke P., Saenger W., and Bernhard F. Modification of biologically active peptides: production of a novel lipohexapeptide after engineering of Bacillus subtilis surfactin synthetase. Protein Eng 15 (2002) 913-921
    • (2002) Protein Eng , vol.15 , pp. 913-921
    • Symmank, H.1    Franke, P.2    Saenger, W.3    Bernhard, F.4
  • 16
    • 0030023476 scopus 로고    scopus 로고
    • Effect of heterogeneity of hydrophobic moieties on surface activity of lichenysin A, a lipopeptide biosurfactant from Bacillus licheniformis BAS50
    • Yakimov M.M., Fredrickson H.L., and Timmis K.N. Effect of heterogeneity of hydrophobic moieties on surface activity of lichenysin A, a lipopeptide biosurfactant from Bacillus licheniformis BAS50. Biotechnol Appl Biochem 23 (1996) 13-18
    • (1996) Biotechnol Appl Biochem , vol.23 , pp. 13-18
    • Yakimov, M.M.1    Fredrickson, H.L.2    Timmis, K.N.3
  • 17
    • 0000903740 scopus 로고
    • Selective esterification of surfactin: preparation and properties of surfactin methyl esters
    • Thimon L., Peypoux F., Das B.C., Wallach J., and Michel G. Selective esterification of surfactin: preparation and properties of surfactin methyl esters. Biotechnol Appl Biochem 20 (1994) 415-423
    • (1994) Biotechnol Appl Biochem , vol.20 , pp. 415-423
    • Thimon, L.1    Peypoux, F.2    Das, B.C.3    Wallach, J.4    Michel, G.5
  • 19
    • 41449109987 scopus 로고    scopus 로고
    • Surfactin isoforms from Bacillus subtilus HSO121: separation and characterization
    • Haddad N.I.A., Liu X.Y., Yang S.Z., and Mu B.Z. Surfactin isoforms from Bacillus subtilus HSO121: separation and characterization. Protein Pept Lett 15 (2008) 265-269
    • (2008) Protein Pept Lett , vol.15 , pp. 265-269
    • Haddad, N.I.A.1    Liu, X.Y.2    Yang, S.Z.3    Mu, B.Z.4
  • 20
    • 34548713440 scopus 로고    scopus 로고
    • Structural characterization of eight cyclic lipopeptides produced by Bacillus subtilis HSO121
    • Liu X.Y., Namir I.A.H., Yang S.Z., and Mu B.Z. Structural characterization of eight cyclic lipopeptides produced by Bacillus subtilis HSO121. Protein Pept Lett 14 (2007) 766-773
    • (2007) Protein Pept Lett , vol.14 , pp. 766-773
    • Liu, X.Y.1    Namir, I.A.H.2    Yang, S.Z.3    Mu, B.Z.4
  • 21
    • 48249155037 scopus 로고    scopus 로고
    • Isolation and characterization of a C12-lipopeptide produced by Bacillus subtilis HSO121
    • Liu X.Y., Yang S.Z., and Mu BZ. Isolation and characterization of a C12-lipopeptide produced by Bacillus subtilis HSO121. J Pept Sci 14 (2008) 864-875
    • (2008) J Pept Sci , vol.14 , pp. 864-875
    • Liu, X.Y.1    Yang, S.Z.2    Mu BZ3
  • 22
    • 33744987001 scopus 로고    scopus 로고
    • Isolation and identification of a lipopeptide
    • Lü Y.N., Yang S.Z., and Mu B.Z. Isolation and identification of a lipopeptide. Microbiology 32 (2005) 67-73
    • (2005) Microbiology , vol.32 , pp. 67-73
    • Lü, Y.N.1    Yang, S.Z.2    Mu, B.Z.3
  • 24
    • 33847610231 scopus 로고    scopus 로고
    • Determination of the structure of the fatty acid chain in a cyclic lipopeptide using GC-MS
    • Yang S.Z., Wei D.Z., and Mu B.Z. Determination of the structure of the fatty acid chain in a cyclic lipopeptide using GC-MS. J Biochem Biophys Methods 70 (2006) 519-523
    • (2006) J Biochem Biophys Methods , vol.70 , pp. 519-523
    • Yang, S.Z.1    Wei, D.Z.2    Mu, B.Z.3
  • 25
    • 33745003659 scopus 로고    scopus 로고
    • Determination of the amino acid sequence in a cyclic lipopeptide using MS with DHT mechanism
    • Yang S.Z., Wei D.Z., and Mu B.Z. Determination of the amino acid sequence in a cyclic lipopeptide using MS with DHT mechanism. J Biochem Biophys Methods 68 (2006) 69-74
    • (2006) J Biochem Biophys Methods , vol.68 , pp. 69-74
    • Yang, S.Z.1    Wei, D.Z.2    Mu, B.Z.3
  • 26
    • 0345708406 scopus 로고    scopus 로고
    • A novel lipopeptide, an inhibitor of bacterial adhesion, from the thermophilic and halotolerant subsurface Bacillus licheniformis strain 603
    • Batrakov S.G., Rodionova T.A., Esipov S.E., Polyakov N.B., Sheichenko V.I., Shekhovtsova N.V., et al. A novel lipopeptide, an inhibitor of bacterial adhesion, from the thermophilic and halotolerant subsurface Bacillus licheniformis strain 603. Biochim Biophys Acta 1634 (2003) 107-115
    • (2003) Biochim Biophys Acta , vol.1634 , pp. 107-115
    • Batrakov, S.G.1    Rodionova, T.A.2    Esipov, S.E.3    Polyakov, N.B.4    Sheichenko, V.I.5    Shekhovtsova, N.V.6
  • 27
    • 0032146421 scopus 로고    scopus 로고
    • Separation and characterization of surfactin isoforms produced by Bacillus subtilis OKB 105
    • Kowall M., Vater J., Kluge B., Stein T., Franke P., and Ziessow D. Separation and characterization of surfactin isoforms produced by Bacillus subtilis OKB 105. J Colloid Interf Sci 204 (1998) 1-8
    • (1998) J Colloid Interf Sci , vol.204 , pp. 1-8
    • Kowall, M.1    Vater, J.2    Kluge, B.3    Stein, T.4    Franke, P.5    Ziessow, D.6
  • 28
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 65 (1983) 55-63
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 30
    • 33747224297 scopus 로고    scopus 로고
    • Bioreactor design for enhanced carrier-assisted surfactin production with Bacillus subtilis
    • Yeh M.S., Wei Y.H., and Chang J.S. Bioreactor design for enhanced carrier-assisted surfactin production with Bacillus subtilis. Process Biochem 41 (2006) 1799-1805
    • (2006) Process Biochem , vol.41 , pp. 1799-1805
    • Yeh, M.S.1    Wei, Y.H.2    Chang, J.S.3
  • 31
    • 22544473053 scopus 로고    scopus 로고
    • Characterization of concentration and purification parameters and operating conditions for the small-scale recovery of surfactin
    • Sen R., and Swaminathan T. Characterization of concentration and purification parameters and operating conditions for the small-scale recovery of surfactin. Process Biochem 40 (2005) 2953-2958
    • (2005) Process Biochem , vol.40 , pp. 2953-2958
    • Sen, R.1    Swaminathan, T.2
  • 32
    • 33750940983 scopus 로고    scopus 로고
    • Using Taguchi experimental design methods to optimize trace element composition for enhanced surfactin production by Bacillus subtilis ATCC 21332
    • Wei Y.H., Lai C.C., and Chang J.S. Using Taguchi experimental design methods to optimize trace element composition for enhanced surfactin production by Bacillus subtilis ATCC 21332. Process Biochem 42 (2007) 40-45
    • (2007) Process Biochem , vol.42 , pp. 40-45
    • Wei, Y.H.1    Lai, C.C.2    Chang, J.S.3
  • 33
    • 0030777161 scopus 로고    scopus 로고
    • Production and properties of a lipopeptide biosurfactant from Bacillus subtilis C9
    • Kim H.-S., Yoon B.-D., Lee C.-H., Suh H.-H., Oh H.-M., Katsuragi T., et al. Production and properties of a lipopeptide biosurfactant from Bacillus subtilis C9. J Ferment Bioeng 84 (1997) 41-46
    • (1997) J Ferment Bioeng , vol.84 , pp. 41-46
    • Kim, H.-S.1    Yoon, B.-D.2    Lee, C.-H.3    Suh, H.-H.4    Oh, H.-M.5    Katsuragi, T.6
  • 34
    • 0025427315 scopus 로고
    • The characteristics of the biosynthesis of surface-active lipids by a Bacillus sp. culture
    • (in Russian)
    • Eliseev S.A., Shul'ga A.P., and Karpenko E.V. The characteristics of the biosynthesis of surface-active lipids by a Bacillus sp. culture. Mikrobiol Zh 52 (1990) 41-44 (in Russian)
    • (1990) Mikrobiol Zh , vol.52 , pp. 41-44
    • Eliseev, S.A.1    Shul'ga, A.P.2    Karpenko, E.V.3
  • 35
    • 0001620446 scopus 로고
    • The production of surfactin by Bacillus subtilis grown on peat hydrolysate
    • Sheppard J.D., and Mulligan C.N. The production of surfactin by Bacillus subtilis grown on peat hydrolysate. Appl Microbiol Biotechnol 27 (1987) 110-116
    • (1987) Appl Microbiol Biotechnol , vol.27 , pp. 110-116
    • Sheppard, J.D.1    Mulligan, C.N.2
  • 37
    • 0026077172 scopus 로고
    • Isolation and characterization of a new variant of surfactin, the [Val7]surfactin
    • Peypoux F., Bonmatin J.M., Labbe H., Das B.C., Ptak M., and Michel G. Isolation and characterization of a new variant of surfactin, the [Val7]surfactin. Eur J Biochem 202 (1991) 101-106
    • (1991) Eur J Biochem , vol.202 , pp. 101-106
    • Peypoux, F.1    Bonmatin, J.M.2    Labbe, H.3    Das, B.C.4    Ptak, M.5    Michel, G.6
  • 38
    • 0030798111 scopus 로고
    • Isolation of new variants of surfactin by a recombinant Bacillus subtilis
    • Nakayama S., Takahashi S., Hirai M., and Shoda M. Isolation of new variants of surfactin by a recombinant Bacillus subtilis. Appl Microbiol Biotechnol 48 (1991) 80-82
    • (1991) Appl Microbiol Biotechnol , vol.48 , pp. 80-82
    • Nakayama, S.1    Takahashi, S.2    Hirai, M.3    Shoda, M.4
  • 39
    • 33748063995 scopus 로고    scopus 로고
    • Biosynthesis of the (2S, 3R)-3-methyl glutamate residue of nonribosomal lipopeptides
    • Milne C., Powell A., Jim J., AlNakeeb M., Smith C.P., and Micklefield J. Biosynthesis of the (2S, 3R)-3-methyl glutamate residue of nonribosomal lipopeptides. J Am Chem Soc 128 (2006) 11250-11259
    • (2006) J Am Chem Soc , vol.128 , pp. 11250-11259
    • Milne, C.1    Powell, A.2    Jim, J.3    AlNakeeb, M.4    Smith, C.P.5    Micklefield, J.6
  • 40
    • 0037416878 scopus 로고    scopus 로고
    • Total synthesis and NMR conformational study of signal peptidase II inhibitors, globomycin and SF-1902 A(5)
    • Kiho T., Nakayama M., and Kogen H. Total synthesis and NMR conformational study of signal peptidase II inhibitors, globomycin and SF-1902 A(5). Tetrahedron 59 (2003) 1685-1697
    • (2003) Tetrahedron , vol.59 , pp. 1685-1697
    • Kiho, T.1    Nakayama, M.2    Kogen, H.3
  • 41
    • 0023273989 scopus 로고
    • Isolation and characterization of news iturins: iturin D and iturin E
    • Besson F., and Michel G. Isolation and characterization of news iturins: iturin D and iturin E. J Antibiot 40 (1987) 437-442
    • (1987) J Antibiot , vol.40 , pp. 437-442
    • Besson, F.1    Michel, G.2
  • 42
    • 0025373211 scopus 로고
    • A54145, a new lipopeptide antibiotic complex: isolation and characterization
    • Fukuda D.S., Dubus R.H., Baker P.J., Berry D.M., and Mynderse J.S. A54145, a new lipopeptide antibiotic complex: isolation and characterization. J Antibiot 43 (1990) 594-600
    • (1990) J Antibiot , vol.43 , pp. 594-600
    • Fukuda, D.S.1    Dubus, R.H.2    Baker, P.J.3    Berry, D.M.4    Mynderse, J.S.5
  • 44
    • 0032767622 scopus 로고    scopus 로고
    • Antiviral and hemolytic activities of surfactin isoforms and their methyl ester derivatives
    • Kracht M., Rokos H., Ozel M., Kowall M., Pauli G., and Vater J. Antiviral and hemolytic activities of surfactin isoforms and their methyl ester derivatives. J Antibiot (Tokyo) 52 (1999) 613-619
    • (1999) J Antibiot (Tokyo) , vol.52 , pp. 613-619
    • Kracht, M.1    Rokos, H.2    Ozel, M.3    Kowall, M.4    Pauli, G.5    Vater, J.6
  • 45
    • 0016159471 scopus 로고
    • Antitumor activity of bacillus natto. V. Isolation and characterization of surfactin in the culture medium of Bacillus natto KMD 2311
    • Kameda Y., Oira S., Matsui K., Kanatomo S., and Hase T. Antitumor activity of bacillus natto. V. Isolation and characterization of surfactin in the culture medium of Bacillus natto KMD 2311. Chem Pharm Bull (Tokyo) 22 (1974) 938-944
    • (1974) Chem Pharm Bull (Tokyo) , vol.22 , pp. 938-944
    • Kameda, Y.1    Oira, S.2    Matsui, K.3    Kanatomo, S.4    Hase, T.5
  • 46
    • 34447638323 scopus 로고    scopus 로고
    • Induction of apoptosis in human leukemia K562 cells by cyclic lipopeptide from Bacillus subtilis natto T-2
    • Wang C.L., Ng T.B., Yuan F., Liu Z.K., and Liu F. Induction of apoptosis in human leukemia K562 cells by cyclic lipopeptide from Bacillus subtilis natto T-2. Peptides 28 (2007) 1344-1350
    • (2007) Peptides , vol.28 , pp. 1344-1350
    • Wang, C.L.1    Ng, T.B.2    Yuan, F.3    Liu, Z.K.4    Liu, F.5
  • 47
    • 33847100500 scopus 로고    scopus 로고
    • Surfactin from Bacillus subtilis displays anti-proliferative effect via apoptosis induction, cell cycle arrest and survival signaling suppression
    • Kim S.Y., Kim J.Y., Kim S.H., Bae H.J., Yi H., Yoon S.H., et al. Surfactin from Bacillus subtilis displays anti-proliferative effect via apoptosis induction, cell cycle arrest and survival signaling suppression. FEBS Lett 581 (2007) 865-871
    • (2007) FEBS Lett , vol.581 , pp. 865-871
    • Kim, S.Y.1    Kim, J.Y.2    Kim, S.H.3    Bae, H.J.4    Yi, H.5    Yoon, S.H.6
  • 48
    • 0037193181 scopus 로고    scopus 로고
    • Enhancement of plasminogen activation by surfactin C: augmentation of fibrinolysis in vitro and in vivo
    • Kikuchi T., and Hasumi K. Enhancement of plasminogen activation by surfactin C: augmentation of fibrinolysis in vitro and in vivo. Biochim Biophys Acta 1596 (2002) 234-245
    • (2002) Biochim Biophys Acta , vol.1596 , pp. 234-245
    • Kikuchi, T.1    Hasumi, K.2
  • 49
    • 0029610597 scopus 로고
    • Inhibition of Acyl-CoA: cholesterol acyltransferase by isohalobacillin, a complex of novel cyclic acylpeptides produced by Bacillus sp. A1236
    • Hasumi K., Takizawa K., Takahashi F., Park J.K., and Endo A. Inhibition of Acyl-CoA: cholesterol acyltransferase by isohalobacillin, a complex of novel cyclic acylpeptides produced by Bacillus sp. A1236. J Antibiot 48 (1995) 1419-1424
    • (1995) J Antibiot , vol.48 , pp. 1419-1424
    • Hasumi, K.1    Takizawa, K.2    Takahashi, F.3    Park, J.K.4    Endo, A.5
  • 50
    • 0032055265 scopus 로고    scopus 로고
    • Suppression of inflammatory responses by surfactin, a selective inhibitor of platelet cytosolic phospholipase A2
    • Kim K., Jung S.Y., Lee D.K., Jung J.K., Park J.K., Kim D.K., et al. Suppression of inflammatory responses by surfactin, a selective inhibitor of platelet cytosolic phospholipase A2. Biochem Pharmacol 55 (1998) 975-985
    • (1998) Biochem Pharmacol , vol.55 , pp. 975-985
    • Kim, K.1    Jung, S.Y.2    Lee, D.K.3    Jung, J.K.4    Park, J.K.5    Kim, D.K.6


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