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Volumn 60, Issue , 2012, Pages 74-80

Primary recovery of lipase derived from Burkholderia cenocepacia strain ST8 and recycling of phase components in an aqueous two-phase system

Author keywords

Aqueous two phase; Bioseparations; Enzymes; Lipase; Protein recovery; Purification

Indexed keywords

AQUEOUS TWO PHASE; AQUEOUS TWO PHASE SYSTEM; BIO SEPARATION; BURKHOLDERIA; CONCENTRATED SOLUTION; PHASE COMPONENT; PHOSPHATE SOLUTIONS; POTASSIUM PHOSPHATE; PRIMARY SYSTEMS; PROTEIN RECOVERY; PURIFICATION FACTORS; RANDOM COPOLYMER; SECONDARY SYSTEM; TIE-LINE; TWO PHASE SYSTEMS; VOLUME RATIO; WATER SOLUTIONS;

EID: 83555165947     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2011.10.005     Document Type: Article
Times cited : (53)

References (44)
  • 1
    • 4544317397 scopus 로고    scopus 로고
    • Evaluation of an alternative source of dextran as a phase forming polymer for aqueous two-phase extractive system
    • Ghosh S., Vijayalakshmi R., Swaminathan T. Evaluation of an alternative source of dextran as a phase forming polymer for aqueous two-phase extractive system. Biochem. Eng. J. 2004, 21:241-252.
    • (2004) Biochem. Eng. J. , vol.21 , pp. 241-252
    • Ghosh, S.1    Vijayalakshmi, R.2    Swaminathan, T.3
  • 2
    • 79952817767 scopus 로고    scopus 로고
    • Three-phase partitioning for concentration and purification of laccase produced by submerged cultures of Ganoderma sp. WR-1
    • Rajeeva S., Lele S.S. Three-phase partitioning for concentration and purification of laccase produced by submerged cultures of Ganoderma sp. WR-1. Biochem. Eng. J. 2011, 54:103-110.
    • (2011) Biochem. Eng. J. , vol.54 , pp. 103-110
    • Rajeeva, S.1    Lele, S.S.2
  • 3
    • 0037731214 scopus 로고    scopus 로고
    • Aqueous two-phase extraction using thermoseparating polymer: a new system for the separation of endo-polygalacturonase
    • Pereira M., Wu Y.T., Venâncio A., Teixeira J. Aqueous two-phase extraction using thermoseparating polymer: a new system for the separation of endo-polygalacturonase. Biochem. Eng. J. 2003, 15:131-138.
    • (2003) Biochem. Eng. J. , vol.15 , pp. 131-138
    • Pereira, M.1    Wu, Y.T.2    Venâncio, A.3    Teixeira, J.4
  • 4
    • 17544396435 scopus 로고    scopus 로고
    • Effects of fused tryptophan rich peptides to a recombinant protein A domain on the partitioning in polyethylene glycol-dextran and Ucon-dextran aqueous two-phase systems
    • Carlsson M., Berggren K., Linse P., Veide A., Tjerneld F. Effects of fused tryptophan rich peptides to a recombinant protein A domain on the partitioning in polyethylene glycol-dextran and Ucon-dextran aqueous two-phase systems. J. Chromatogr. A 1996, 756:107-117.
    • (1996) J. Chromatogr. A , vol.756 , pp. 107-117
    • Carlsson, M.1    Berggren, K.2    Linse, P.3    Veide, A.4    Tjerneld, F.5
  • 5
    • 0027976435 scopus 로고
    • Application of temperature-induced phase partitioning at ambient temperature for enzyme purification
    • Alred P.A., Kozlowski A., Harris J.M., Tjerneld F. Application of temperature-induced phase partitioning at ambient temperature for enzyme purification. J. Chromatogr. A 1994, 659:289-298.
    • (1994) J. Chromatogr. A , vol.659 , pp. 289-298
    • Alred, P.A.1    Kozlowski, A.2    Harris, J.M.3    Tjerneld, F.4
  • 6
    • 0030971323 scopus 로고    scopus 로고
    • Temperature-induced phase partitioning of peptides in water solutions of ethylene oxide and propylene oxide random copolymers
    • Johansson H.O., Karlström G., Tjerneld F. Temperature-induced phase partitioning of peptides in water solutions of ethylene oxide and propylene oxide random copolymers. Biochim. Biophys. Acta Gen. Subj. 1997, 1335:315-325.
    • (1997) Biochim. Biophys. Acta Gen. Subj. , vol.1335 , pp. 315-325
    • Johansson, H.O.1    Karlström, G.2    Tjerneld, F.3
  • 8
    • 33646481808 scopus 로고    scopus 로고
    • Direct recovery of alcohol dehydrogenase from unclarified yeast cell homogenate by IDEBAC using an improved scheme for elution
    • Chang Y.-K., Chen J.-P., Sheu J.-R., Cheng P.-J., Su C.-H., Chou S.-Y. Direct recovery of alcohol dehydrogenase from unclarified yeast cell homogenate by IDEBAC using an improved scheme for elution. Biochem. Eng. J. 2006, 30:1-10.
    • (2006) Biochem. Eng. J. , vol.30 , pp. 1-10
    • Chang, Y.-K.1    Chen, J.-P.2    Sheu, J.-R.3    Cheng, P.-J.4    Su, C.-H.5    Chou, S.-Y.6
  • 9
    • 78650523852 scopus 로고    scopus 로고
    • A novel thermoactive and alkaline lipase from Talaromyces thermophilus fungus for use in laundry detergents
    • Romdhane I.B.-B., Fendri A., Gargouri Y., Gargouri A., Belghith H. A novel thermoactive and alkaline lipase from Talaromyces thermophilus fungus for use in laundry detergents. Biochem. Eng. J. 2010, 53:112-120.
    • (2010) Biochem. Eng. J. , vol.53 , pp. 112-120
    • Romdhane, I.B.-B.1    Fendri, A.2    Gargouri, Y.3    Gargouri, A.4    Belghith, H.5
  • 10
    • 77954309544 scopus 로고    scopus 로고
    • Recycling of phase components during lysozyme extraction from hen egg white in the EO50PO50/K2HPO4 aqueous two-phase system
    • Dembczynski R., Bialas W., Jankowski T. Recycling of phase components during lysozyme extraction from hen egg white in the EO50PO50/K2HPO4 aqueous two-phase system. Biochem. Eng. J. 2010, 51:24-31.
    • (2010) Biochem. Eng. J. , vol.51 , pp. 24-31
    • Dembczynski, R.1    Bialas, W.2    Jankowski, T.3
  • 11
    • 0033396212 scopus 로고    scopus 로고
    • Thermoseparating water/polymer system: a novel one-polymer aqueous two-phase system for protein purification
    • Johansson H.O., Persson J., Tjerneld F. Thermoseparating water/polymer system: a novel one-polymer aqueous two-phase system for protein purification. Biotechnol. Bioeng. 1999, 66:247-257.
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 247-257
    • Johansson, H.O.1    Persson, J.2    Tjerneld, F.3
  • 12
    • 79952816834 scopus 로고    scopus 로고
    • Expression, purification of a novel alkaline Staphylococcus xylosus lipase acting at high temperature
    • Bouaziz A., Horchani H., Ben Salem N., Gargouri Y., Sayari A. Expression, purification of a novel alkaline Staphylococcus xylosus lipase acting at high temperature. Biochem. Eng. J. 2011, 54:93-102.
    • (2011) Biochem. Eng. J. , vol.54 , pp. 93-102
    • Bouaziz, A.1    Horchani, H.2    Ben Salem, N.3    Gargouri, Y.4    Sayari, A.5
  • 14
    • 44449161817 scopus 로고    scopus 로고
    • Refolding of a recombinant organic solvent-stable lipase, which is overexpressed and forms an inclusion body, and activation with lipase-specific foldase
    • Ogino H., Inoue S., Akagi R., Yasuda M., Doukyu N., Ishimi K. Refolding of a recombinant organic solvent-stable lipase, which is overexpressed and forms an inclusion body, and activation with lipase-specific foldase. Biochem. Eng. J. 2008, 40:507-511.
    • (2008) Biochem. Eng. J. , vol.40 , pp. 507-511
    • Ogino, H.1    Inoue, S.2    Akagi, R.3    Yasuda, M.4    Doukyu, N.5    Ishimi, K.6
  • 15
    • 33947590455 scopus 로고    scopus 로고
    • Neutral lipase from aqueous solutions on chitosan nano-particles
    • Tang Z.-X., Shi L.-E., Qian J.-Q. Neutral lipase from aqueous solutions on chitosan nano-particles. Biochem. Eng. J. 2007, 34:217-223.
    • (2007) Biochem. Eng. J. , vol.34 , pp. 217-223
    • Tang, Z.-X.1    Shi, L.-E.2    Qian, J.-Q.3
  • 17
    • 67651098843 scopus 로고    scopus 로고
    • Influence of temperature on the activity and enantioselectivity of Burkholderia cepacia lipase in the kinetic resolution of mandelic acid enantiomers
    • Dabkowska K., Szewczyk K.W. Influence of temperature on the activity and enantioselectivity of Burkholderia cepacia lipase in the kinetic resolution of mandelic acid enantiomers. Biochem. Eng. J. 2009, 46:147-153.
    • (2009) Biochem. Eng. J. , vol.46 , pp. 147-153
    • Dabkowska, K.1    Szewczyk, K.W.2
  • 18
    • 58149479855 scopus 로고    scopus 로고
    • Burkholderia cepacia complex: epithelial cell-pathogen confrontations and potential for therapeutic intervention
    • McClean S., Callaghan M. Burkholderia cepacia complex: epithelial cell-pathogen confrontations and potential for therapeutic intervention. Med. Microbiol. J. 2009, 58:1-12.
    • (2009) Med. Microbiol. J. , vol.58 , pp. 1-12
    • McClean, S.1    Callaghan, M.2
  • 19
    • 77957948573 scopus 로고    scopus 로고
    • Gas phase enantioselective reduction catalyzed by immobilized ketoreductase: Effects of water activity and reaction temperature
    • Nagayama K., Spiess A.C., Büchs J. Gas phase enantioselective reduction catalyzed by immobilized ketoreductase: Effects of water activity and reaction temperature. Biochem. Eng. J. 2010, 52:301-303.
    • (2010) Biochem. Eng. J. , vol.52 , pp. 301-303
    • Nagayama, K.1    Spiess, A.C.2    Büchs, J.3
  • 20
    • 75349100918 scopus 로고    scopus 로고
    • Organic solvent-tolerant enzymes
    • Doukyu N., Ogino H. Organic solvent-tolerant enzymes. Biochem. Eng. J. 2010, 48:270-282.
    • (2010) Biochem. Eng. J. , vol.48 , pp. 270-282
    • Doukyu, N.1    Ogino, H.2
  • 21
    • 79952814199 scopus 로고    scopus 로고
    • Comparison of the biochemical properties of a recombinant lipase extract from Rhizopus oryzae expressed in Pichia pastoris with a native extract
    • Guillén M., Benaiges M.D., Valero F. Comparison of the biochemical properties of a recombinant lipase extract from Rhizopus oryzae expressed in Pichia pastoris with a native extract. Biochem. Eng. J. 2011, 54:117-123.
    • (2011) Biochem. Eng. J. , vol.54 , pp. 117-123
    • Guillén, M.1    Benaiges, M.D.2    Valero, F.3
  • 22
    • 79960720997 scopus 로고    scopus 로고
    • Production and optimization of alkalostable lipase by alkalophilic Burkholderia cenocepacia ST8
    • Lau H.L., Ariff A., Woo K.K., Ling T.C., Hii S.L. Production and optimization of alkalostable lipase by alkalophilic Burkholderia cenocepacia ST8. Afr. J. Biotechnol. 2011, 10:7002-7009.
    • (2011) Afr. J. Biotechnol. , vol.10 , pp. 7002-7009
    • Lau, H.L.1    Ariff, A.2    Woo, K.K.3    Ling, T.C.4    Hii, S.L.5
  • 23
    • 78650232497 scopus 로고    scopus 로고
    • Extractive fermentation using aqueous two-phase systems for integrated production and purification of extracellular lipase derived from Burkholderia pseudomallei
    • Ooi C.W., Hii S.L., Kamal S.M.M., Ariff A., Ling T.C. Extractive fermentation using aqueous two-phase systems for integrated production and purification of extracellular lipase derived from Burkholderia pseudomallei. Process Biochem. 2011, 46:68-73.
    • (2011) Process Biochem. , vol.46 , pp. 68-73
    • Ooi, C.W.1    Hii, S.L.2    Kamal, S.M.M.3    Ariff, A.4    Ling, T.C.5
  • 25
    • 69249222636 scopus 로고    scopus 로고
    • Purification of lipase derived from Burkholderia pseudomallei with alcohol/salt-based aqueous two-phase systems
    • Ooi C.W., Tey B.T., Hii S.L., Kamal S.M.M., Lan J.C.W., Ariff A., Ling T.C. Purification of lipase derived from Burkholderia pseudomallei with alcohol/salt-based aqueous two-phase systems. Process Biochem. 2009, 44:1083-1087.
    • (2009) Process Biochem. , vol.44 , pp. 1083-1087
    • Ooi, C.W.1    Tey, B.T.2    Hii, S.L.3    Kamal, S.M.M.4    Lan, J.C.W.5    Ariff, A.6    Ling, T.C.7
  • 26
    • 79961021132 scopus 로고    scopus 로고
    • Direct recovery of lipase derived from Burkholderia cepacia in recycling aqueous two-phase flotation
    • Show P.L., Tan C.P., Anuar M.S., Ariff A., Yusof Y.A., Chen S.K., Ling T.C. Direct recovery of lipase derived from Burkholderia cepacia in recycling aqueous two-phase flotation. Sep. Purif. Technol. 2011, 80:577-584.
    • (2011) Sep. Purif. Technol. , vol.80 , pp. 577-584
    • Show, P.L.1    Tan, C.P.2    Anuar, M.S.3    Ariff, A.4    Yusof, Y.A.5    Chen, S.K.6    Ling, T.C.7
  • 27
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • Smith P.K., Krohn R.I., Hermanson G.T. Measurement of protein using bicinchoninic acid. Anal. Biochem. 1985, 150:76-85.
    • (1985) Anal. Biochem. , vol.150 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 29
    • 58049218870 scopus 로고    scopus 로고
    • Aqueous two-phase extraction of 2,3-butanediol from fermentation broths using an ethanol/phosphate system
    • Jiang B., Li Z.G., Dai J.Y., Zhang D.J., Xiu Z.L. Aqueous two-phase extraction of 2,3-butanediol from fermentation broths using an ethanol/phosphate system. Process Biochem. 2009, 44:112-117.
    • (2009) Process Biochem. , vol.44 , pp. 112-117
    • Jiang, B.1    Li, Z.G.2    Dai, J.Y.3    Zhang, D.J.4    Xiu, Z.L.5
  • 31
    • 0032703909 scopus 로고    scopus 로고
    • Purification of protein and recycling of polymers in a new aqueous two-phase system using two thermoseparating polymers
    • Persson J., Johansson H.O., Tjerneld F. Purification of protein and recycling of polymers in a new aqueous two-phase system using two thermoseparating polymers. J. Chromatogr. A 1999, 864:31-48.
    • (1999) J. Chromatogr. A , vol.864 , pp. 31-48
    • Persson, J.1    Johansson, H.O.2    Tjerneld, F.3
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 2642572488 scopus 로고    scopus 로고
    • Purification of hyperthermophilic archaeal amylolytic enzyme (MJA1) using thermoseparating aqueous two-phase systems
    • Li M., Peeples T.L. Purification of hyperthermophilic archaeal amylolytic enzyme (MJA1) using thermoseparating aqueous two-phase systems. J.Chromatogr. B: Anal. Technol. Biomed. Life Sci. 2004, 807:69-74.
    • (2004) J.Chromatogr. B: Anal. Technol. Biomed. Life Sci. , vol.807 , pp. 69-74
    • Li, M.1    Peeples, T.L.2
  • 34
    • 78049275440 scopus 로고    scopus 로고
    • Application of the aqueous two-phase thermoseparating systems of Dehypon® LS 54-the waxy maize starch for protein extraction
    • Fero A.B.J., Jahim J.M. Application of the aqueous two-phase thermoseparating systems of Dehypon® LS 54-the waxy maize starch for protein extraction. J. Appl. Sci. 2010, 10:2596-2601.
    • (2010) J. Appl. Sci. , vol.10 , pp. 2596-2601
    • Fero, A.B.J.1    Jahim, J.M.2
  • 35
    • 47949108470 scopus 로고    scopus 로고
    • Aqueous two-phase poly(ethylene glycol)-poly(acrylic acid) system for protein partitioning: Influence of molecular weight, pH and temperature
    • Saravanan S., Rao J.R., Nair B.U., Ramasami T. Aqueous two-phase poly(ethylene glycol)-poly(acrylic acid) system for protein partitioning: Influence of molecular weight, pH and temperature. Process Biochem. 2008, 43:905-911.
    • (2008) Process Biochem. , vol.43 , pp. 905-911
    • Saravanan, S.1    Rao, J.R.2    Nair, B.U.3    Ramasami, T.4
  • 36
    • 0028800165 scopus 로고
    • Effects of salts and the surface hydrophobicity of proteins on partitioning in aqueous two-phase systems containing thermoseparating ethylene oxide-propylene oxide copolymers
    • Berggren K., Johansson H.O., Tjerneld F. Effects of salts and the surface hydrophobicity of proteins on partitioning in aqueous two-phase systems containing thermoseparating ethylene oxide-propylene oxide copolymers. J. Chromatogr. A 1995, 718:67-79.
    • (1995) J. Chromatogr. A , vol.718 , pp. 67-79
    • Berggren, K.1    Johansson, H.O.2    Tjerneld, F.3
  • 37
    • 1542268883 scopus 로고    scopus 로고
    • Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents
    • Lima V.M.G., Krieger N., Mitchell D.A., Fontana J.D. Activity and stability of a crude lipase from Penicillium aurantiogriseum in aqueous media and organic solvents. Biochem. Eng. J. 2004, 18:65-71.
    • (2004) Biochem. Eng. J. , vol.18 , pp. 65-71
    • Lima, V.M.G.1    Krieger, N.2    Mitchell, D.A.3    Fontana, J.D.4
  • 38
    • 40849120992 scopus 로고    scopus 로고
    • Optimization of fibrinolytic enzyme production by Bacillus subtilis DC-2 in aqueous two-phase system (poly-ethylene glycol 4000 and sodium sulfate)
    • Ashipala O.K., He Q. Optimization of fibrinolytic enzyme production by Bacillus subtilis DC-2 in aqueous two-phase system (poly-ethylene glycol 4000 and sodium sulfate). Bioresour. Technol. 2008, 99:4112-4119.
    • (2008) Bioresour. Technol. , vol.99 , pp. 4112-4119
    • Ashipala, O.K.1    He, Q.2
  • 39
    • 0030087616 scopus 로고    scopus 로고
    • Partitioning of a Bacillus alkaline protease in aqueous two-phase systems
    • Sinha R., Singh S.P., Ahmed S., Garg S.K. Partitioning of a Bacillus alkaline protease in aqueous two-phase systems. Bioresour. Technol. 1996, 55:163-166.
    • (1996) Bioresour. Technol. , vol.55 , pp. 163-166
    • Sinha, R.1    Singh, S.P.2    Ahmed, S.3    Garg, S.K.4
  • 40
    • 0028765391 scopus 로고
    • Partitioning of pristinamycins in aqueous two-phase systems: A first step toward the development of antibiotic production by extractive fermentation
    • Paquet V., Myint M., Roque C., Soucaille P. Partitioning of pristinamycins in aqueous two-phase systems: A first step toward the development of antibiotic production by extractive fermentation. Biotechnol. Bioeng. 1994, 44:445-451.
    • (1994) Biotechnol. Bioeng. , vol.44 , pp. 445-451
    • Paquet, V.1    Myint, M.2    Roque, C.3    Soucaille, P.4
  • 41
    • 0029968162 scopus 로고    scopus 로고
    • A closed concept for purification of the membrane-bound cholesterol oxidase from Nocardia rhodochrous by surfactant-based cloud-point extraction, organic-solvent extraction and anion-exchange chromatography
    • Minuth T., Thömmes J., Kula M.R. A closed concept for purification of the membrane-bound cholesterol oxidase from Nocardia rhodochrous by surfactant-based cloud-point extraction, organic-solvent extraction and anion-exchange chromatography. Biotech. Appl. Biochem. 1996, 23:107-116.
    • (1996) Biotech. Appl. Biochem. , vol.23 , pp. 107-116
    • Minuth, T.1    Thömmes, J.2    Kula, M.R.3
  • 42
    • 69249181739 scopus 로고    scopus 로고
    • Burkholderia cepacia lipase is an excellent enzyme for the enantioselective hydrolysis of β-heteroaryl-β-amino esters
    • Tasnádi G., Forró E., Fülöp F. Burkholderia cepacia lipase is an excellent enzyme for the enantioselective hydrolysis of β-heteroaryl-β-amino esters. Tetrahedron Asymmetry 2009, 20:1771-1777.
    • (2009) Tetrahedron Asymmetry , vol.20 , pp. 1771-1777
    • Tasnádi, G.1    Forró, E.2    Fülöp, F.3
  • 43
    • 0038119852 scopus 로고    scopus 로고
    • Pilot-scale extraction of an intracellular recombinant cutinase from E. coli cell homogenate using a thermoseparating aqueous two-phase system
    • Kepka C., Collet E., Persson J., Ståhl Å., Lagerstedt T., Tjerneld F., Veide A. Pilot-scale extraction of an intracellular recombinant cutinase from E. coli cell homogenate using a thermoseparating aqueous two-phase system. J. Biotechnol. 2003, 103:165-181.
    • (2003) J. Biotechnol. , vol.103 , pp. 165-181
    • Kepka, C.1    Collet, E.2    Persson, J.3    Ståhl, Å.4    Lagerstedt, T.5    Tjerneld, F.6    Veide, A.7
  • 44
    • 0034705763 scopus 로고    scopus 로고
    • Polymer recycling in aqueous two-phase extractions using thermoseparating ethylene oxide-propylene oxide copolymers
    • Persson J., Kaul A., Tjerneld F. Polymer recycling in aqueous two-phase extractions using thermoseparating ethylene oxide-propylene oxide copolymers. J. Chromatogr. B Biomed. Sci. Appl. 2000, 743:115-126.
    • (2000) J. Chromatogr. B Biomed. Sci. Appl. , vol.743 , pp. 115-126
    • Persson, J.1    Kaul, A.2    Tjerneld, F.3


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