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Volumn 45, Issue 10, 2010, Pages 1664-1671

Purification of plant-esterase in PEG1000/NaH2PO4 aqueous two-phase system by a two-step extraction

Author keywords

Aqueous two phase system; Partition; PEG; Plant esterase; Purification; Salt

Indexed keywords

AQUEOUS TWO PHASE SYSTEM; AQUEOUS TWO-PHASE EXTRACTION; EFFICIENT PROCESS; NEUTRAL SALTS; OPTIMIZED CONDITIONS; ORGANOPHOSPHORUS COMPOUNDS; PARTITION; PEG; PLANT-ESTERASE; POLYMER-SALT SYSTEMS; PROCESS PARAMETERS; SALTING-OUT; TWO-STEP EXTRACTION;

EID: 77956171000     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.06.018     Document Type: Article
Times cited : (52)

References (45)
  • 1
    • 34347358392 scopus 로고    scopus 로고
    • PVDF coated quartz crystal microbalance sensor for DMMP vapor detection
    • Ying Z.H., Jiang Y.D., Du X.S., Xie G.Z., Yu J.S., Wang H. PVDF coated quartz crystal microbalance sensor for DMMP vapor detection. Sens Actuators B 2007, 125:167-172.
    • (2007) Sens Actuators B , vol.125 , pp. 167-172
    • Ying, Z.H.1    Jiang, Y.D.2    Du, X.S.3    Xie, G.Z.4    Yu, J.S.5    Wang, H.6
  • 2
    • 15744365262 scopus 로고    scopus 로고
    • Nanoparticle-based optical biosensors for the direct detection of organophosphate chemical warfare agents and pesticides
    • Simonian A.L., Good T.A., Wang S.-S., Wild J.R. Nanoparticle-based optical biosensors for the direct detection of organophosphate chemical warfare agents and pesticides. Anal Chim Acta 2005, 534:69-77.
    • (2005) Anal Chim Acta , vol.534 , pp. 69-77
    • Simonian, A.L.1    Good, T.A.2    Wang, S.-S.3    Wild, J.R.4
  • 3
    • 29144469442 scopus 로고    scopus 로고
    • Screen-printed bienzymatic sensor based on sol-gel immobilized Nippostronylus brasiliensis acetylcholinesterase and a cytochrome P450 BM-3 (CYP 102-A1) mutant
    • Waibel M., Schulze H., Huber N., Bachmann T.T. Screen-printed bienzymatic sensor based on sol-gel immobilized Nippostronylus brasiliensis acetylcholinesterase and a cytochrome P450 BM-3 (CYP 102-A1) mutant. Biosens Bioelectron 2006, 21:1132-1140.
    • (2006) Biosens Bioelectron , vol.21 , pp. 1132-1140
    • Waibel, M.1    Schulze, H.2    Huber, N.3    Bachmann, T.T.4
  • 4
    • 33646564967 scopus 로고    scopus 로고
    • An optical biosensor for dichlovos using stacked sol-gel films containing acetylcholinesterase and a lipophilic chromoionophore
    • Wong F.C.M., Ahmad M., Heng L.Y., Peng L.B. An optical biosensor for dichlovos using stacked sol-gel films containing acetylcholinesterase and a lipophilic chromoionophore. Talanta 2006, 69:888-893.
    • (2006) Talanta , vol.69 , pp. 888-893
    • Wong, F.C.M.1    Ahmad, M.2    Heng, L.Y.3    Peng, L.B.4
  • 5
    • 67649217264 scopus 로고    scopus 로고
    • Optical detection of dimethyl methyl-phosphonate with monosulfonate tetraphenyl porphyrin-plant-esterase complex
    • Huo D.Q., Yang L.M., Hou C.J. Optical detection of dimethyl methyl-phosphonate with monosulfonate tetraphenyl porphyrin-plant-esterase complex. Sens Lett 2009, 7:72-78.
    • (2009) Sens Lett , vol.7 , pp. 72-78
    • Huo, D.Q.1    Yang, L.M.2    Hou, C.J.3
  • 6
    • 64949180616 scopus 로고    scopus 로고
    • Comparative study of two rapid detection methods for organophosphorus pesticide residues in vegetables
    • Huang Z.Y., Yuan Y., Lv Y.Z. Comparative study of two rapid detection methods for organophosphorus pesticide residues in vegetables. Food Sci 2003, 24:135-137.
    • (2003) Food Sci , vol.24 , pp. 135-137
    • Huang, Z.Y.1    Yuan, Y.2    Lv, Y.Z.3
  • 7
    • 33846928747 scopus 로고    scopus 로고
    • Rapid detection of chlorpyrifos residues using a plant hydrolase
    • Chen F., Chen H.L. Rapid detection of chlorpyrifos residues using a plant hydrolase. Environ Sci Technol 2005, 28:48-51.
    • (2005) Environ Sci Technol , vol.28 , pp. 48-51
    • Chen, F.1    Chen, H.L.2
  • 8
    • 50949098665 scopus 로고    scopus 로고
    • Studies on sensitivity and detection limit of pesticides residues with phytoesterase
    • Wen Y.X., Li J.K., Zhang X.M., Xu J. Studies on sensitivity and detection limit of pesticides residues with phytoesterase. Food Sci 2006, 27:186-188.
    • (2006) Food Sci , vol.27 , pp. 186-188
    • Wen, Y.X.1    Li, J.K.2    Zhang, X.M.3    Xu, J.4
  • 9
    • 77956174444 scopus 로고    scopus 로고
    • Study on purification and properties of soybean esterase
    • Wen Y.X., Lan W.L., Li J.K. Study on purification and properties of soybean esterase. Food Sci 2008, 29:292-294.
    • (2008) Food Sci , vol.29 , pp. 292-294
    • Wen, Y.X.1    Lan, W.L.2    Li, J.K.3
  • 10
    • 77956177788 scopus 로고    scopus 로고
    • Study on purification and characterization of plant-esterase for detecting the residues of organophosphate pesticides
    • Zhou Y.M., Liu D., Hu R., E W, Wang X., Li X.N., et al. Study on purification and characterization of plant-esterase for detecting the residues of organophosphate pesticides. Food Sci Technol 2008, 3:52-56.
    • (2008) Food Sci Technol , vol.3 , pp. 52-56
    • Zhou, Y.M.1    Liu, D.2    Hu, R.3    E, W.4    Wang, X.5    Li, X.N.6
  • 11
    • 77956174123 scopus 로고    scopus 로고
    • Separation and characterization of soybean esterase isozyme involved in pesticide residues detection
    • Zhou Y.L., Li J.K. Separation and characterization of soybean esterase isozyme involved in pesticide residues detection. J Chin Cereals Oils Assoc 2008, 23:72-75.
    • (2008) J Chin Cereals Oils Assoc , vol.23 , pp. 72-75
    • Zhou, Y.L.1    Li, J.K.2
  • 12
    • 64949108862 scopus 로고    scopus 로고
    • Study on part purification of botanical esterase for detection of pesticide residue
    • Weng X., Meng L., Liu C.J. Study on part purification of botanical esterase for detection of pesticide residue. Chem Bioeng 2006, 23:22-24.
    • (2006) Chem Bioeng , vol.23 , pp. 22-24
    • Weng, X.1    Meng, L.2    Liu, C.J.3
  • 13
    • 0002025694 scopus 로고
    • Purification of enzymes by liquid-liquid extraction
    • Kula M.R., Kroner K.H., Hustedt H. Purification of enzymes by liquid-liquid extraction. Adv Biochem Eng 1982, 24:73-118.
    • (1982) Adv Biochem Eng , vol.24 , pp. 73-118
    • Kula, M.R.1    Kroner, K.H.2    Hustedt, H.3
  • 14
    • 0027013383 scopus 로고
    • Aqueous two-phase systems for biomolecule separation
    • Diamond A.D., Hsu J.T. Aqueous two-phase systems for biomolecule separation. Adv Biochem Eng Biotechnol 1992, 47:89-135.
    • (1992) Adv Biochem Eng Biotechnol , vol.47 , pp. 89-135
    • Diamond, A.D.1    Hsu, J.T.2
  • 17
    • 74549152642 scopus 로고    scopus 로고
    • Lysozyme extraction from hen egg white in an aqueous two-phase system composed of ethylene oxide-propylene oxide thermoseparating copolymer and potassium phosphate
    • Dembczyński R., Biaías W., Regulski K., Jankowski T. Lysozyme extraction from hen egg white in an aqueous two-phase system composed of ethylene oxide-propylene oxide thermoseparating copolymer and potassium phosphate. Process Biochem 2010, 45:369-374.
    • (2010) Process Biochem , vol.45 , pp. 369-374
    • Dembczyński, R.1    Biaías, W.2    Regulski, K.3    Jankowski, T.4
  • 18
    • 67749143575 scopus 로고    scopus 로고
    • Purfication of CBS 819.72 α-amylase by aqueous two-phase systems: modelling using response surface methodology
    • Kammoun R., Chouayekh H., Abid H., Naili B., Bejar S. Purfication of CBS 819.72 α-amylase by aqueous two-phase systems: modelling using response surface methodology. Biochem Eng J 2010, 46:306-312.
    • (2010) Biochem Eng J , vol.46 , pp. 306-312
    • Kammoun, R.1    Chouayekh, H.2    Abid, H.3    Naili, B.4    Bejar, S.5
  • 19
    • 75349103002 scopus 로고    scopus 로고
    • Dual affinity method for plasmid DNA purification in aqueous two-phase systems
    • Barbosa H.S.C., Hine A.V., Brocchini S., Slater N.K.H., Marcos J.C. Dual affinity method for plasmid DNA purification in aqueous two-phase systems. J Chromatogr A 2010, 1217:1429-1436.
    • (2010) J Chromatogr A , vol.1217 , pp. 1429-1436
    • Barbosa, H.S.C.1    Hine, A.V.2    Brocchini, S.3    Slater, N.K.H.4    Marcos, J.C.5
  • 20
    • 22544434368 scopus 로고    scopus 로고
    • Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems
    • Klomklao S., Benjakul S., Visessanguan W., Simpson B.K., Kishimura H. Partitioning and recovery of proteinase from tuna spleen by aqueous two-phase systems. Process Biochem 2005, 40:3061-3067.
    • (2005) Process Biochem , vol.40 , pp. 3061-3067
    • Klomklao, S.1    Benjakul, S.2    Visessanguan, W.3    Simpson, B.K.4    Kishimura, H.5
  • 21
    • 34250879050 scopus 로고    scopus 로고
    • Purification of recombinant phenylalanine dehydrogenase by partitioning in aqueous two-phase systems
    • Mohamadi H.S., Omidinia E. Purification of recombinant phenylalanine dehydrogenase by partitioning in aqueous two-phase systems. J Chromatogr B 2007, 854:273-278.
    • (2007) J Chromatogr B , vol.854 , pp. 273-278
    • Mohamadi, H.S.1    Omidinia, E.2
  • 22
    • 0343953539 scopus 로고    scopus 로고
    • Partitioning of bovine serum albumin in an aqueous two-phase system: optimization of partition coefficient
    • Gunduz U. Partitioning of bovine serum albumin in an aqueous two-phase system: optimization of partition coefficient. J Chromatogr B 2000, 743:259-262.
    • (2000) J Chromatogr B , vol.743 , pp. 259-262
    • Gunduz, U.1
  • 23
    • 0030569902 scopus 로고    scopus 로고
    • Conservative chemical modification of proteins to study the effects of a single protein property on partitioning in aqueous two-phase systems
    • Franco T.T., Andrews A.T., Asenjo J.A. Conservative chemical modification of proteins to study the effects of a single protein property on partitioning in aqueous two-phase systems. Biotechnol Bioeng 1995, 49:290-299.
    • (1995) Biotechnol Bioeng , vol.49 , pp. 290-299
    • Franco, T.T.1    Andrews, A.T.2    Asenjo, J.A.3
  • 24
    • 2642511370 scopus 로고    scopus 로고
    • Bromelain partitioning in two-phase aqueous systems containing PEO-PPO-PEO block copolymers
    • Rabelo A.P.B., Tambourgi E.B., Pessoa A. Bromelain partitioning in two-phase aqueous systems containing PEO-PPO-PEO block copolymers. J Chromatogr B 2004, 807:61-68.
    • (2004) J Chromatogr B , vol.807 , pp. 61-68
    • Rabelo, A.P.B.1    Tambourgi, E.B.2    Pessoa, A.3
  • 25
    • 74549152642 scopus 로고    scopus 로고
    • Lysozyme extraction from hen egg white in an aqueous two-phase system composed of ethylene oxide-propylene oxide thermoseparating copolymer and potassium phosphate
    • Dembczyński R., Bialas W., Regulski K., Jankowski T. Lysozyme extraction from hen egg white in an aqueous two-phase system composed of ethylene oxide-propylene oxide thermoseparating copolymer and potassium phosphate. Process Biochem 2010, 45:369-374.
    • (2010) Process Biochem , vol.45 , pp. 369-374
    • Dembczyński, R.1    Bialas, W.2    Regulski, K.3    Jankowski, T.4
  • 26
    • 33645910088 scopus 로고
    • A study of house fly esterase by means of a sensitive colorimetric method
    • Van Asperen K. A study of house fly esterase by means of a sensitive colorimetric method. J Insect Physiol 1962, 8:401-416.
    • (1962) J Insect Physiol , vol.8 , pp. 401-416
    • Van Asperen, K.1
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976, 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0342595317 scopus 로고
    • Methods in enzymology guide to protein purification; purification procedures
    • Deutscher M. Methods in enzymology guide to protein purification; purification procedures. Electrophor Meth 1990, 182:425-488.
    • (1990) Electrophor Meth , vol.182 , pp. 425-488
    • Deutscher, M.1
  • 29
    • 0035166234 scopus 로고    scopus 로고
    • Aqueous two-phase systems
    • Hatti-Kaul R. Aqueous two-phase systems. Mol Biotechnol 2001, 19:269-277.
    • (2001) Mol Biotechnol , vol.19 , pp. 269-277
    • Hatti-Kaul, R.1
  • 30
    • 0022731197 scopus 로고
    • Partitioning in aqueous two-phase systems: an overview
    • Walter H., Jobansson G. Partitioning in aqueous two-phase systems: an overview. Anal Biochem 1986, 155:215-242.
    • (1986) Anal Biochem , vol.155 , pp. 215-242
    • Walter, H.1    Jobansson, G.2
  • 31
    • 2642531799 scopus 로고    scopus 로고
    • Practical application of aqueous two-phase partition to process development for the recovery of biological products
    • Ratio-Palomares M. Practical application of aqueous two-phase partition to process development for the recovery of biological products. J Chromatogr B 2004, 807:3-11.
    • (2004) J Chromatogr B , vol.807 , pp. 3-11
    • Ratio-Palomares, M.1
  • 32
    • 0027572103 scopus 로고
    • Enhancement effect of polyethylene glycol on enzymatic synthesis of cephalexin
    • Hyun C.K., Choi J.M., Kim J.M., Ryu D.Y. Enhancement effect of polyethylene glycol on enzymatic synthesis of cephalexin. Biotechnol Bioeng 1993, 41:654-658.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 654-658
    • Hyun, C.K.1    Choi, J.M.2    Kim, J.M.3    Ryu, D.Y.4
  • 33
    • 0032569064 scopus 로고    scopus 로고
    • Influence of system and process parameters on partitioning of cheese whey proteins in aqueous two phase systems
    • Rito-Palomares M., Hernandez M. Influence of system and process parameters on partitioning of cheese whey proteins in aqueous two phase systems. J Chromatogr B 1998, 711:81-90.
    • (1998) J Chromatogr B , vol.711 , pp. 81-90
    • Rito-Palomares, M.1    Hernandez, M.2
  • 34
    • 0030569902 scopus 로고    scopus 로고
    • Conservative chemical modification of proteins to study the effects of a single protein property on partitioning in aqueous two-phase systems
    • Franco T.T., Andrews A.T., Asenjo J.A. Conservative chemical modification of proteins to study the effects of a single protein property on partitioning in aqueous two-phase systems. Biotechnol Bioeng 1996, 49:290-299.
    • (1996) Biotechnol Bioeng , vol.49 , pp. 290-299
    • Franco, T.T.1    Andrews, A.T.2    Asenjo, J.A.3
  • 35
    • 0026146746 scopus 로고
    • Solvent modulation in hydrophobic interaction chromatography
    • Arakawa T., Narhi L.O. Solvent modulation in hydrophobic interaction chromatography. Biotechnol Appl Biochem 1991, 13:151-172.
    • (1991) Biotechnol Appl Biochem , vol.13 , pp. 151-172
    • Arakawa, T.1    Narhi, L.O.2
  • 36
    • 0037175436 scopus 로고    scopus 로고
    • Isolation of alpha-1-antitrypsin from human plasma by partitioning in aqueous biphasic systems of polyethyleneglycol-phosphate
    • Reh G., Nerli B., Pico G. Isolation of alpha-1-antitrypsin from human plasma by partitioning in aqueous biphasic systems of polyethyleneglycol-phosphate. J Chromatogr B 2002, 780:89-96.
    • (2002) J Chromatogr B , vol.780 , pp. 89-96
    • Reh, G.1    Nerli, B.2    Pico, G.3
  • 37
    • 0037735116 scopus 로고    scopus 로고
    • Biphasic aqueous media containing polyethylene glycol for the enzymatic synthesis of oligosaccharides from lactose
    • Del-Val M.I., Otero C. Biphasic aqueous media containing polyethylene glycol for the enzymatic synthesis of oligosaccharides from lactose. Enzyme Microbiol Technol 2003, 33:118-126.
    • (2003) Enzyme Microbiol Technol , vol.33 , pp. 118-126
    • Del-Val, M.I.1    Otero, C.2
  • 38
    • 0035871923 scopus 로고    scopus 로고
    • Rapid process for purification of an extracellular beta-xylosidase by aqueous two-phase extraction
    • Pan I.H., Li Y.K. Rapid process for purification of an extracellular beta-xylosidase by aqueous two-phase extraction. J Chromatogr B 2001, 754:179-184.
    • (2001) J Chromatogr B , vol.754 , pp. 179-184
    • Pan, I.H.1    Li, Y.K.2
  • 39
    • 0029897576 scopus 로고    scopus 로고
    • Protein partition between the different phases comprising poly(ethylene glycol)-salt aqueous two-phase systems, hydrophobic interaction chromatography and precipitation: a generic description in terms of salting-out effects
    • Huddleston J.G., Abelaira J.C., Wang R., Lyddiatt A. Protein partition between the different phases comprising poly(ethylene glycol)-salt aqueous two-phase systems, hydrophobic interaction chromatography and precipitation: a generic description in terms of salting-out effects. J Chromatogr B 1996, 680:31-41.
    • (1996) J Chromatogr B , vol.680 , pp. 31-41
    • Huddleston, J.G.1    Abelaira, J.C.2    Wang, R.3    Lyddiatt, A.4
  • 40
    • 0026059521 scopus 로고
    • Influence of system and molecular parameters upon fractionation of intracellular proteins from Saccharomyces by aqueous two-phase partition
    • Huddleston J.G., Ottomar K.W., Ngonyani D.M., Lyddiatt A. Influence of system and molecular parameters upon fractionation of intracellular proteins from Saccharomyces by aqueous two-phase partition. Enzyme Microbiol Technol 1991, 13:24-32.
    • (1991) Enzyme Microbiol Technol , vol.13 , pp. 24-32
    • Huddleston, J.G.1    Ottomar, K.W.2    Ngonyani, D.M.3    Lyddiatt, A.4
  • 41
    • 0026203774 scopus 로고
    • Partitioning and purification of thaumatinin aqueous two-phase systems
    • Cascone O., Andrews B.A., Asenjo J.A. Partitioning and purification of thaumatinin aqueous two-phase systems. Enzyme Microb Technol 1991, 13:629-635.
    • (1991) Enzyme Microb Technol , vol.13 , pp. 629-635
    • Cascone, O.1    Andrews, B.A.2    Asenjo, J.A.3
  • 42
    • 0037193196 scopus 로고    scopus 로고
    • The surface exposed amino acid residues of monomeric proteins determine the partitioning in aqueous two-phase systems
    • Berggren K., Wolf A., Asenjo J.A., Andrews B.A., Tjerneld F. The surface exposed amino acid residues of monomeric proteins determine the partitioning in aqueous two-phase systems. Biochim Biophys Acta 2002, 1596:253-268.
    • (2002) Biochim Biophys Acta , vol.1596 , pp. 253-268
    • Berggren, K.1    Wolf, A.2    Asenjo, J.A.3    Andrews, B.A.4    Tjerneld, F.5
  • 43
    • 19844375733 scopus 로고    scopus 로고
    • Influence of pH on the partition of glucose-6-phosphate dehydrogenase and hexokinase in aqueous two-phase system
    • Silva D.P., Pontes M.Z.R., Souza M.A., Vitolo M., Silva J.B., Pessoa-Junior A. Influence of pH on the partition of glucose-6-phosphate dehydrogenase and hexokinase in aqueous two-phase system. Braz J Microbiol 2002, 33:196-201.
    • (2002) Braz J Microbiol , vol.33 , pp. 196-201
    • Silva, D.P.1    Pontes, M.Z.R.2    Souza, M.A.3    Vitolo, M.4    Silva, J.B.5    Pessoa-Junior, A.6
  • 44
    • 0011118570 scopus 로고
    • Separation of particles and macromolecules by phase partition
    • Albertsson P.Å. Separation of particles and macromolecules by phase partition. Endeavour 1977, 1:69-74.
    • (1977) Endeavour , vol.1 , pp. 69-74
    • Albertsson, P.Å.1
  • 45
    • 64949172290 scopus 로고    scopus 로고
    • Research on the purification of plant-esterase
    • Ji S.J., Zhang A.L., Liu L., Wei B.D. Research on the purification of plant-esterase. Food Technol 2005, 26:70-72.
    • (2005) Food Technol , vol.26 , pp. 70-72
    • Ji, S.J.1    Zhang, A.L.2    Liu, L.3    Wei, B.D.4


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