메뉴 건너뛰기




Volumn 81, Issue 3, 2011, Pages 339-346

Green fluorescent protein extraction and LPS removal from escherichia coli fermentation medium using aqueous two-phase micellar system

Author keywords

Green fluorescent protein; Liquid liquid extraction; LPS removal; Protein purification; Triton X 114

Indexed keywords

BIOTECHNOLOGY; ESCHERICHIA COLI; EXTRACTION; FLUORESCENCE; MICELLES; MOLECULAR BIOLOGY; PURIFICATION; RECOMBINANT PROTEINS; FERMENTATION;

EID: 84865710488     PISSN: 13835866     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.seppur.2011.07.043     Document Type: Article
Times cited : (29)

References (61)
  • 2
    • 0032900403 scopus 로고    scopus 로고
    • Xylanase recovery: Effect of extraction conditions on the aot reversed micellar systems using experimental design
    • E.M.G. Rodrigues, A.M.F. Milagres, A. Pessoa-Júnior, Xylanase recovery: effect of extraction conditions on the AOT reversed micellar systems using experimental design, P. Biochem. 3 (1999) 121-125.
    • (1999) P. Biochem. , vol.3 , pp. 121-125
    • Rodrigues, E.M.G.1    Milagres, A.M.F.2    Pessoa-Júnior, A.3
  • 3
    • 77956870628 scopus 로고    scopus 로고
    • Interaction of histidine-tagged human proinsulin with immobilized nickel ion: Effect of chelating ligand and thermodynamics analysis
    • L.C. Góes, E.A. Miranda, S.M.A. Bueno, Interaction of histidine-tagged human proinsulin with immobilized nickel ion: effect of chelating ligand and thermodynamics analysis, Colloids Surf. A 369 (2010) 176-185.
    • (2010) Colloids Surf. A , vol.369 , pp. 176-185
    • Góes, L.C.1    Miranda, E.A.2    Bueno, S.M.A.3
  • 4
    • 0026062620 scopus 로고
    • Gramnegative endotoxin: An extraordinary lipid with profound effects on eukaryotic signal transduction
    • C.R. Raetz, R.J. Ulevitch, S.D. Wright, C.H. Sibley, A. Ding, C.F. Nathan, Gramnegative endotoxin: an extraordinary lipid with profound effects on eukaryotic signal transduction, FASEB J. 12 (1991) 2652-2660.
    • (1991) FASEB J. , vol.12 , pp. 2652-2660
    • Raetz, C.R.1    Ulevitch, R.J.2    Wright, S.D.3    Sibley, C.H.4    Ding, A.5    Nathan, C.F.6
  • 5
    • 0037027896 scopus 로고    scopus 로고
    • Chromatographic removal of endotoxin from protein solutions by polymer particles
    • C. Hirayama, M. Sakata, Chromatographic removal of endotoxin from protein solutions by polymer particles, J. Chromatogr. B 781 (2002) 419-432.
    • (2002) J. Chromatogr. B , vol.781 , pp. 419-432
    • Hirayama, C.1    Sakata, M.2
  • 6
    • 5344241926 scopus 로고    scopus 로고
    • Evaluation of the bacterial endotoxin test for quantification of endotoxin contamination of porcine vaccines
    • Y. Ogikubo, M. Norimatsu, K. Noda, J. Takahashi, M. Inotsume, M. Tsuchiya, Y. Tamura, Evaluation of the bacterial endotoxin test for quantification of endotoxin contamination of porcine vaccines, Biologicals 32 (2004) 88-93.
    • (2004) Biologicals , vol.32 , pp. 88-93
    • Ogikubo, Y.1    Norimatsu, M.2    Noda, K.3    Takahashi, J.4    Inotsume, M.5    Tsuchiya, M.6    Tamura, Y.7
  • 7
    • 77958153489 scopus 로고    scopus 로고
    • Expressed protein ligation for the preparation of fusion proteins with cell penetrating peptides for endotoxin removal and intracellular delivery
    • H.H. Yu, I. Nakase, S. Pujals, H. Hirose, G. Tanaka, S. Katayama, M. Imanishi, S. Futaki, Expressed protein ligation for the preparation of fusion proteins with cell penetrating peptides for endotoxin removal and intracellular delivery, Biochim. Biophys. Acta 1798 (2010) 2249-2257.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 2249-2257
    • Yu, H.H.1    Nakase, I.2    Pujals, S.3    Hirose, H.4    Tanaka, G.5    Katayama, S.6    Imanishi, M.7    Futaki, S.8
  • 8
    • 79951474949 scopus 로고    scopus 로고
    • Selective removal of endotoxin from a dna solution by cross-linked cyclodextrin beads
    • G. Sakata, K. Yoshimura, I. Sakamoto, M. Todokoro, M. Kunitake, Selective removal of endotoxin from a DNA solution by cross-linked cyclodextrin beads, Anal. Sci. 27 (2011) 213-216.
    • (2011) Anal. Sci. , vol.27 , pp. 213-216
    • Sakata, G.1    Yoshimura, K.2    Sakamoto, I.3    Todokoro, M.4    Kunitake, M.5
  • 9
    • 0033991321 scopus 로고    scopus 로고
    • Endotoxin removal from protein solutions
    • D. Petsch, F.B. Anspach, Endotoxin removal from protein solutions, J. Biotechnol. 76 (2000) 97-119.
    • (2000) J. Biotechnol. , vol.76 , pp. 97-119
    • Petsch, D.1    Anspach, F.B.2
  • 10
    • 0033037301 scopus 로고    scopus 로고
    • Outer membrane permeability barrier in escherichia coli mutants that are defective in the late acyltransferases of lipid a biosyn thesis, antimicrob
    • M. Vaara, M. Nurminen, Outer membrane permeability barrier in Escherichia coli mutants that are defective in the late acyltransferases of lipid A biosynthesis, Antimicrob. Agents Chemother. 43 (1999) 1459-1462.
    • (1999) Agents Chemother. , vol.43 , pp. 1459-1462
    • Vaara, M.1    Nurminen, M.2
  • 11
    • 84755160974 scopus 로고    scopus 로고
    • Endotoxin elimination in sepsis: Physiology and therapeutic application langenbecks
    • K. Buttenschoen, P. Radermacher, H. Bracht, Endotoxin elimination in sepsis: physiology and therapeutic application, Langenbecks Arch. Surg. 395 (2010) 597-605.
    • (2010) Arch. Surg. , vol.395 , pp. 597-605
    • Buttenschoen, K.1    Radermacher, P.2    Bracht, H.3
  • 14
    • 33645409827 scopus 로고    scopus 로고
    • Single step protocol to purify recombinant proteins with low endotoxin contents protein
    • P. Reichelt, C. Schwarz, M. Donzeau, Single step protocol to purify recombinant proteins with low endotoxin contents, Protein Expr. Purif. 46 (2006) 483-488.
    • (2006) Expr. Purif. , vol.46 , pp. 483-488
    • Reichelt, P.1    Schwarz, C.2    Donzeau, M.3
  • 15
    • 0022658657 scopus 로고
    • Endotoxin detection and elimination in biotechnology
    • S.K. Sharma, Endotoxin detection and elimination in biotechnology, Biotechnol. Appl. Biochem. 1 (1986) 5-22.
    • (1986) Biotechnol. Appl. Biochem. , vol.1 , pp. 5-22
    • Sharma, S.K.1
  • 16
    • 0018910648 scopus 로고
    • The effects of prostacyclin (pg12) on endotoxin shock and endotoxin-induced platelet aggregation in dogs
    • J.R. Fletcher, P.W. Ramwell, The effects of prostacyclin (PG12) on endotoxin shock and endotoxin-induced platelet aggregation in dogs, Circ. Shock. 7 (1980) 299-308.
    • (1980) Circ. Shock. , vol.7 , pp. 299-308
    • Fletcher, J.R.1    Ramwell, P.W.2
  • 17
    • 0023688110 scopus 로고
    • Tolerance to tumor necrosis factor in rats and the relationship to endotoxin tolerance and toxicity
    • D.L. Fraker, M.C. Stovroff, M.J. Merino, J.A. Norton, Tolerance to tumor necrosis factor in rats and the relationship to endotoxin tolerance and toxicity, J. Exp. Med. 168 (1988) 95-105.
    • (1988) J. Exp. Med. , vol.168 , pp. 95-105
    • Fraker, D.L.1    Stovroff, M.C.2    Merino, M.J.3    Norton, J.A.4
  • 18
    • 0031786128 scopus 로고    scopus 로고
    • Effect of plyss on the production of bioadhesive precursor protein by fed-batch cultivation of recombinant escherichia coli
    • Y.C. Kim, S. Kwon, S.Y. Lee, H.N. Chang, Effect of pLysS on the production of bioadhesive precursor protein by fed-batch cultivation of recombinant Escherichia coli, Biotechnol. Lett. 20 (1998) 799-803.
    • (1998) Biotechnol. Lett. , vol.20 , pp. 799-803
    • Kim, Y.C.1    Kwon, S.2    Lee, S.Y.3    Chang, H.N.4
  • 19
    • 0034597709 scopus 로고    scopus 로고
    • High level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies
    • J.H. Lee, High level expression of antimicrobial peptide mediated by a fusion partner reinforcing formation of inclusion bodies, Biochem. Biophys. Res. Comm. 277 (2000) 575-680.
    • (2000) Biochem. Biophys. Res. Comm. , vol.277 , pp. 575-680
    • Lee, J.H.1
  • 20
    • 0034816503 scopus 로고    scopus 로고
    • A large-scale purification of recombinant histone h1.5 from escherichia coli protein
    • S.H. Pyo, J.H. Lee, H.B. Park, S.S. Hong, J.H. Kim, A large-scale purification of recombinant histone H1.5 from Escherichia coli, Protein Expr. Purif. 23 (2001) 38-44.
    • (2001) Expr. Purif. , vol.23 , pp. 38-44
    • Pyo, S.H.1    Lee, J.H.2    Park, H.B.3    Hong, S.S.4    Kim, J.H.5
  • 21
    • 79955458160 scopus 로고    scopus 로고
    • Endotoxin removing method based on lipopolysaccharide binding protein and polyhydroxyalkanoate binding protein phap
    • J. Li, G. Shang, M. You, S. Peng, Z. Wang, H. Wu, G.Q. Chen, Endotoxin Removing Method Based on Lipopolysaccharide Binding Protein and Polyhydroxyalkanoate Binding Protein PhaP, Biomacromolecules 12 (2011) 602-608.
    • (2011) Biomacromolecules , vol.12 , pp. 602-608
    • Li, J.1    Shang, G.2    You, M.3    Peng, S.4    Wang, Z.5    Wu, H.6    Chen, G.Q.7
  • 22
    • 0031835746 scopus 로고    scopus 로고
    • Chromatographic removal of endotoxin from hemoglobin preparations effects of solution conditions on endotoxin removal efficiency and protein recovery
    • Y. Kang, R.G. Luo, Chromatographic removal of endotoxin from hemoglobin preparations effects of solution conditions on endotoxin removal efficiency and protein recovery, J. Chromatogr. A 809 (1998) 13-20.
    • (1998) J. Chromatogr. A , vol.809 , pp. 13-20
    • Kang, Y.1    Luo, R.G.2
  • 25
    • 27844581254 scopus 로고    scopus 로고
    • Production of recombinant proteins by high cell density culture of escherichia coli
    • J.H. Choi, K.C. Keum, S.Y. Lee, Production of recombinant proteins by high cell density culture of Escherichia coli, Chem. Eng. Sci. 61 (2006) 876-885.
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 876-885
    • Choi, J.H.1    Keum, K.C.2    Lee, S.Y.3
  • 26
    • 79955160817 scopus 로고    scopus 로고
    • Endotoxin removal during the purification process of human-like collagen
    • R. Ma, D.D. Fan, W.J. Xue, J.Y. Xing, C.H. Zhu, X.X. Ma, Endotoxin removal during the purification process of human-like collagen, Sep. Sci. Technol. 45 (2010) 2400-2405.
    • (2010) Sep. Sci. Technol. , vol.45 , pp. 2400-2405
    • Ma, R.1    Fan, D.D.2    Xue, W.J.3    Xing, J.Y.4    Zhu, C.H.5    Ma, X.X.6
  • 28
    • 0029084380 scopus 로고
    • Removal of endotoxins by affinity sorbents
    • F.B. Anspach, O. Hilbeck, Removal of endotoxins by affinity sorbents, J. Chrom. A 711 (1995) 81-92.
    • (1995) J. Chrom. A , vol.711 , pp. 81-92
    • Anspach, F.B.1    Hilbeck, O.2
  • 29
    • 34249748433 scopus 로고    scopus 로고
    • Studies on endotoxin removal mechanism of adsorbents with amino acid ligands
    • Z. Wei, W. Huang, J. Li, G. Hou, J. Fang, Z. Yuan, Studies on endotoxin removal mechanism of adsorbents with amino acid ligands, J. Chromatogr. B 852 (2007) 288-292.
    • (2007) J. Chromatogr. B , vol.852 , pp. 288-292
    • Wei, Z.1    Huang, W.2    Li, J.3    Hou, G.4    Fang, J.5    Yuan, Z.6
  • 30
    • 0037681802 scopus 로고    scopus 로고
    • Optimization of buffer conditions for the removal of endotoxins using q-sepharose
    • S.H. Lee, J.S. Kim, C.W. Kim, Optimization of buffer conditions for the removal of endotoxins using Q-sepharose, Process Biochem. 38 (2003) 1091-1098.
    • (2003) Process Biochem. , vol.38 , pp. 1091-1098
    • Lee, S.H.1    Kim, J.S.2    Kim, C.W.3
  • 31
    • 0024997246 scopus 로고
    • Removal of endotoxin from protein solutions by phase separation using triton x-114 j
    • Y. Aida, M.J. Pabst, Removal of endotoxin from protein solutions by phase separation using Triton X-114, J. Immunol. Methods 14 (1990) 191-195.
    • (1990) Immunol. Methods , vol.14 , pp. 191-195
    • Aida, Y.1    Pabst, M.J.2
  • 32
    • 0028466386 scopus 로고
    • Lipopolysaccharide is a frequent contaminant of plasmid dna preparations and can be toxic to primary human cells in the presence of adenovirus
    • M. Cotten, A. Baker, M. Saltik, E. Wagner, M. Buschle, Lipopolysaccharide is a frequent contaminant of plasmid DNA preparations and can be toxic to primary human cells in the presence of adenovirus, Gene Ther. 1 (1994) 239- 246.
    • (1994) Gene Ther , vol.1 , pp. 239-246
    • Cotten, M.1    Baker, A.2    Saltik, M.3    Wagner, E.4    Buschle, M.5
  • 33
    • 0028918896 scopus 로고
    • A non-degradative route for the removal of endotoxin from exopolysaccharides
    • O. Adam, A. Vercellone, F. Paul, P.F. Monsan, G. Puzo, A non-degradative route for the removal of endotoxin from exopolysaccharides, Anal. Biochem. 225 (1995) 321-327.
    • (1995) Anal. Biochem. , vol.225 , pp. 321-327
    • Adam, O.1    Vercellone, A.2    Paul, F.3    Monsan, P.F.4    Puzo, G.5
  • 34
    • 43049156554 scopus 로고    scopus 로고
    • The biological activity of a recombinantly expressed (his)6-tagged peanut allergen (rara h 1) is unaffected by endotoxin removal
    • L.B. Jensen, A.M. Torp, S.B. Andersen, P.S. Skov, L.K. Poulsen, E.F. Knol, E. van Hoffen, The biological activity of a recombinantly expressed (His)6-tagged peanut allergen (rAra h 1) is unaffected by endotoxin removal, J. Immunol. Methods 335 (2008) 116-120.
    • (2008) J. Immunol. Methods , vol.335 , pp. 116-120
    • Jensen, L.B.1    Torp, A.M.2    Andersen, S.B.3    Skov, P.S.4    Poulsen, L.K.5    Knol, E.F.6    Van Hoffen, E.7
  • 35
    • 48449096698 scopus 로고    scopus 로고
    • Discovery of the dual polysaccharide composition of emulsan and the isolation of the emulsion stabilizing component
    • M.P. Mercaldi, H. Dams-Kozlowska, B. Panilaitis, A.P. Joyce, D.L. Kaplan, Discovery of the Dual Polysaccharide Composition of Emulsan and the Isolation of the Emulsion Stabilizing Component, Biomacromolecules 9 (2008) 1988-1996.
    • (2008) Biomacromolecules , vol.9 , pp. 1988-1996
    • Mercaldi, M.P.1    Dams-Kozlowska, H.2    Panilaitis, B.3    Joyce, A.P.4    Kaplan, D.L.5
  • 36
    • 38449108659 scopus 로고    scopus 로고
    • Large-scale production of endotoxin-free plasmids for transient expression in mammalian cell culture
    • A. Rozkov, B. Larsson, S. Gillström, R. Björnestedt, S.R. Schmidt, Large-scale production of endotoxin-free plasmids for transient expression in mammalian cell culture, Biotechnol Bioeng. 99 (2008) 557-666.
    • (2008) Biotechnol Bioeng. , vol.99 , pp. 557-666
    • Rozkov, A.1    Larsson, B.2    Gillström, S.3    Björnestedt, R.4    Schmidt, S.R.5
  • 38
    • 60349109980 scopus 로고    scopus 로고
    • Refining hpv 16 l1 purification from e. Coli: Reducing endotoxin contaminations and their impact on immunogenicity
    • L. Schädlich, T. Senger, C.J. Kirschning, M. Müller, L. Gissmann, Refining HPV 16 L1 purification from E. coli: reducing endotoxin contaminations and their impact on immunogenicity, Vaccine 27 (2009) 1511-1522.
    • (2009) Vaccine , vol.27 , pp. 1511-1522
    • Schädlich, L.1    Senger, T.2    Kirschning, C.J.3    Müller, M.4    Gissmann, L.5
  • 40
    • 12444322142 scopus 로고    scopus 로고
    • Removal of lipopolysaccharides from protein-lipopolysaccharide complex by nonflammable solvents
    • M.F. Lin, C. Williams, M.V. Murray, P.A. Ropp, Removal of lipopolysaccharides from protein-lipopolysaccharide complex by nonflammable solvents, J. Chromatogr. B 816 (2005) 167-174.
    • (2005) J. Chromatogr. B , vol.816 , pp. 167-174
    • Lin, M.F.1    Williams, C.2    Murray, M.V.3    Ropp, P.A.4
  • 42
    • 10144238512 scopus 로고    scopus 로고
    • Novel bioseparations using two-phase aqueous micellar systems
    • C.L. Liu, Y.J. Nikas, D. Blankschtein, Novel bioseparations using two-phase aqueous micellar systems, Biotechnol. Bioeng. 52 (1996) 185-192.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 185-192
    • Liu, C.L.1    Nikas, Y.J.2    Blankschtein, D.3
  • 43
    • 78649447670 scopus 로고    scopus 로고
    • Micelle-mediated extraction of chlorogenic acid from morus laevigata w. Leaves
    • A.A. Memon, N. Memon, M.I. Bhangera, Micelle-mediated extraction of chlorogenic acid from Morus laevigata W. leaves, Sep. Purif. Technol. 76 (2010) 179-183.
    • (2010) Sep. Purif. Technol. , vol.76 , pp. 179-183
    • Memon, A.A.1    Memon, N.2    Bhangera, M.I.3
  • 44
    • 0036161197 scopus 로고    scopus 로고
    • Large-scale extraction of proteins
    • T. Cunha, R. Aires-Barros, Large-scale extraction of proteins, Mol. Biotechnol. 20 (2002) 29-40.
    • (2002) Mol. Biotechnol. , vol.20 , pp. 29-40
    • Cunha, T.1    Aires-Barros, R.2
  • 46
    • 34249113112 scopus 로고    scopus 로고
    • Study on the thermal stability of green fluorescent protein (gfp) in glucose parenteral formulations
    • M. Ishii, J.S. Kunimura, T.C.V. Penna, O. Cholewa, Study on the thermal stability of green fluorescent protein (GFP) in glucose parenteral formulations, Int. J. Pharm. 337 (2007) 109-117.
    • (2007) Int. J. Pharm. , vol.337 , pp. 109-117
    • Ishii, M.1    Kunimura, J.S.2    Penna, T.C.V.3    Cholewa, O.4
  • 49
    • 4744352796 scopus 로고    scopus 로고
    • A, permeation associated with three phase partitioning method on the release of green fluorescent protein (gfpuv) from escherichia coli
    • T.C.V. Penna, E. Chiarini, A. Pessoa Jr., A, Permeation associated with three phase partitioning method on the release of green fluorescent protein (GFPuv) from Escherichia coli, Appl. Biochem. Biotechnol. 105 (2003) 481- 491.
    • (2003) Appl. Biochem. Biotechnol. , vol.105 , pp. 481-491
    • Penna, T.C.V.1    Chiarini, E.2    Pessoa Jr., A.3
  • 51
    • 84865754118 scopus 로고    scopus 로고
    • United states pharmacopeia 24 and national formulary 19 bacterial endotoxins
    • United States Pharmacopeia 24 and National Formulary 19 Bacterial Endotoxins, Test. Suppl. 85 (2000) 2875-2879.
    • (2000) Test. Suppl. , vol.85 , pp. 2875-2879
  • 53
    • 36549099006 scopus 로고
    • Phenomenological theory of equilibrium thermodynamic properties and phase separation of micellar solutions
    • D. Blankschtein, G.M. Thurston, G.B. Benedek, Phenomenological theory of equilibrium thermodynamic properties and phase separation of micellar solutions, J. Chem. Phys. 85 (1986) 7268-7288.
    • (1986) J. Chem. Phys. , vol.85 , pp. 7268-7288
    • Blankschtein, D.1    Thurston, G.M.2    Benedek, G.B.3
  • 55
    • 0033829204 scopus 로고    scopus 로고
    • Enzyme activity and stability control by amphiphilic self-organizing systems in aqueous solutions
    • G. Savelli, N. Spreti, P. Di Profio, Enzyme activity and stability control by amphiphilic self-organizing systems in aqueous solutions, Curr. Opin. Colloid Interface Sci. 5 (2000) 111-117.
    • (2000) Curr. Opin. Colloid Interface Sci. , vol.5 , pp. 111-117
    • Savelli, G.1    Spreti, N.2    Di Profio, P.3
  • 56
    • 4344717466 scopus 로고    scopus 로고
    • What can we learn by studying enzymes in non-aqueous media?
    • P.J. Halling, What can we learn by studying enzymes in non-aqueous media?, Philos Trans. R. Soc. Lond. B Biol Sci. 359 (2004) 1287-1297.
    • (2004) Philos Trans. R. Soc. Lond. B Biol Sci. , vol.359 , pp. 1287-1297
    • Halling, P.J.1
  • 57
    • 0030243049 scopus 로고    scopus 로고
    • A liquid-state theory approach to modeling solute partitioning in phase-separated solutions
    • L. Lue, D. Blankschtein, A liquid-state theory approach to modeling solute partitioning in phase-separated solutions, Ind. Eng. Chem. Res. 35 (1996) 3032-3043.
    • (1996) Ind. Eng. Chem. Res. , vol.35 , pp. 3032-3043
    • Lue, L.1    Blankschtein, D.2
  • 58
    • 84865719318 scopus 로고    scopus 로고
    • National Formulary 25
    • United States Pharmacopoeia 30, National Formulary 25 (2007).
    • (2007) United States Pharmacopoeia , vol.30
  • 59
    • 84865764451 scopus 로고    scopus 로고
    • Agência Nacional de Vigilância Sanitária - ANVISA, Guia para qualidade em química analítica: uma assistência a acreditação, Brasília
    • Agência Nacional de Vigilância Sanitária - ANVISA, Guia para qualidade em química analítica: uma assistência a acreditação, Brasília, 2004, p. 80.
    • (2004) , pp. 80
  • 61
    • 85030498720 scopus 로고    scopus 로고
    • United States Pharmacopoeia 26, Rockville: United Stated Pharmacopeial Convention, 2002, p. 2569
    • United States Pharmacopoeia 26, Rockville: United Stated Pharmacopeial Convention, 2002, p. 2569.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.