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Volumn 45, Issue 10, 2010, Pages 1692-1698

Heterofunctional supports for the one-step purification, immobilization and stabilization of large multimeric enzymes: Amino-glyoxyl versus amino-epoxy supports

Author keywords

Intramolecular covalent attachment of adsorbed enzymes; Selective immobilization of very large proteins; Stabilization of multimeric enzymes

Indexed keywords

ALKALINITY; CATALYST ACTIVITY; PURIFICATION; STABILIZATION;

EID: 77956170052     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2010.07.001     Document Type: Article
Times cited : (57)

References (36)
  • 1
    • 0030586740 scopus 로고    scopus 로고
    • Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state
    • Anchordoquy T.J., Carpenter J.F. Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state. Arch Biochem Biophys 1996, 332(2):231-238.
    • (1996) Arch Biochem Biophys , vol.332 , Issue.2 , pp. 231-238
    • Anchordoquy, T.J.1    Carpenter, J.F.2
  • 2
    • 23044493437 scopus 로고    scopus 로고
    • A mechanism for Ca2+/calmodulin-dependent protein kinase II clustering at synaptic and nonsynaptic sites based on self-association
    • Hudmon A., LeBel E., Roy H., Sik A., Schulman H., Waxham M.N., De Koninck P. A mechanism for Ca2+/calmodulin-dependent protein kinase II clustering at synaptic and nonsynaptic sites based on self-association. J Neurosci 2005, 25(30):6971-6983.
    • (2005) J Neurosci , vol.25 , Issue.30 , pp. 6971-6983
    • Hudmon, A.1    LeBel, E.2    Roy, H.3    Sik, A.4    Schulman, H.5    Waxham, M.N.6    De Koninck, P.7
  • 3
    • 0037133522 scopus 로고    scopus 로고
    • Guanidinium chloride- and urea-induced unfolding of the dimeric enzyme glucose oxidase
    • Akhtar Md.S., Ahmad A., Bhakuni V. Guanidinium chloride- and urea-induced unfolding of the dimeric enzyme glucose oxidase. Biochemistry 2002, 41(11):3819-3827.
    • (2002) Biochemistry , vol.41 , Issue.11 , pp. 3819-3827
    • Akhtar, M.1    Ahmad, A.2    Bhakuni, V.3
  • 4
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: strategies to prevent subunit dissociation
    • Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb Technol 2009, 45(6-7):405-418.
    • (2009) Enzyme Microb Technol , vol.45 , Issue.6-7 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 5
    • 0038796679 scopus 로고    scopus 로고
    • Preparation of a stable biocatalyst of bovine liver catalase using immobilization and post-immobilization techniques
    • Betancor L., Hidalgo A., Fernández-Lorente G., Mateo C., Fernández-Lafuente R., Guisan J.M. Preparation of a stable biocatalyst of bovine liver catalase using immobilization and post-immobilization techniques. Biotechnol Prog 2003, 19(3):763-767.
    • (2003) Biotechnol Prog , vol.19 , Issue.3 , pp. 763-767
    • Betancor, L.1    Hidalgo, A.2    Fernández-Lorente, G.3    Mateo, C.4    Fernández-Lafuente, R.5    Guisan, J.M.6
  • 6
    • 65249157035 scopus 로고    scopus 로고
    • Coating of soluble and immobilized enzymes with ionic polymers: full stabilization of the quaternary structure of multimeric enzymes
    • Bolivar J.M., Rocha-Martin J., Mateo C., Cava F., Berenguer J., Fernandez-Lafuente R., Guisan J.M. Coating of soluble and immobilized enzymes with ionic polymers: full stabilization of the quaternary structure of multimeric enzymes. Biomacromolecules 2009, 10(4):742-747.
    • (2009) Biomacromolecules , vol.10 , Issue.4 , pp. 742-747
    • Bolivar, J.M.1    Rocha-Martin, J.2    Mateo, C.3    Cava, F.4    Berenguer, J.5    Fernandez-Lafuente, R.6    Guisan, J.M.7
  • 8
    • 0033523004 scopus 로고    scopus 로고
    • Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface
    • Lebbink J.H.G., Knapp S., Van Der Oost J., Rice D., Ladenstein R., De Vos W.M. Engineering activity and stability of Thermotoga maritima glutamate dehydrogenase. II: construction of a 16-residue ion-pair network at the subunit interface. J Mol Biol 1999, 289(2):357-369.
    • (1999) J Mol Biol , vol.289 , Issue.2 , pp. 357-369
    • Lebbink, J.H.G.1    Knapp, S.2    Van Der Oost, J.3    Rice, D.4    Ladenstein, R.5    De Vos, W.M.6
  • 9
    • 0032015035 scopus 로고    scopus 로고
    • Dissociative thermal inactivation, stability, and activity of oligomeric enzymes
    • Poltorak O.M., Chukhray E.S., Torshin I.Y. Dissociative thermal inactivation, stability, and activity of oligomeric enzymes. Biochemistry (Moscow) 1998, 63(3):303-311.
    • (1998) Biochemistry (Moscow) , vol.63 , Issue.3 , pp. 303-311
    • Poltorak, O.M.1    Chukhray, E.S.2    Torshin, I.Y.3
  • 10
    • 0029797773 scopus 로고    scopus 로고
    • Streptavidins with intersubunit crosslinks have enhanced stability
    • Reznik G.O., Vajda S., Smith C.L., Cantor C.R., Sano T. Streptavidins with intersubunit crosslinks have enhanced stability. Nat Biotechnol 1996, 14(8):1007-1011.
    • (1996) Nat Biotechnol , vol.14 , Issue.8 , pp. 1007-1011
    • Reznik, G.O.1    Vajda, S.2    Smith, C.L.3    Cantor, C.R.4    Sano, T.5
  • 11
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger C.D., Schildbach J.F., Sauer R.T. Are buried salt bridges important for protein stability and conformational specificity?. Nat Struct Biol 1995, 2(2):122-128.
    • (1995) Nat Struct Biol , vol.2 , Issue.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 12
    • 0028080502 scopus 로고
    • Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds
    • Wakarchuk W.W., Sung W.L., Campbell R.L., Cunningham A., Watson D.C., Yaguchi M. Thermostabilization of the Bacillus circulans xylanase by the introduction of disulfide bonds. Protein Eng 1994, 7(11):1379-1386.
    • (1994) Protein Eng , vol.7 , Issue.11 , pp. 1379-1386
    • Wakarchuk, W.W.1    Sung, W.L.2    Campbell, R.L.3    Cunningham, A.4    Watson, D.C.5    Yaguchi, M.6
  • 13
    • 0000259836 scopus 로고
    • Control of oligomeric enzyme thermostability by protein engineering
    • Ahern T.J., Casal J.I., Petsko G.A. Control of oligomeric enzyme thermostability by protein engineering. PNAS 1987, 84(3):675-679.
    • (1987) PNAS , vol.84 , Issue.3 , pp. 675-679
    • Ahern, T.J.1    Casal, J.I.2    Petsko, G.A.3
  • 14
    • 58149296120 scopus 로고    scopus 로고
    • The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits: stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports
    • Bolivar J.M., Mateo C., Rocha-Martin J., Cava F., Berenguer J., Fernandez-Lafuente R., Guisan J.M. The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits: stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports. Enzyme Microb Technol 2009, 44:139-144.
    • (2009) Enzyme Microb Technol , vol.44 , pp. 139-144
    • Bolivar, J.M.1    Mateo, C.2    Rocha-Martin, J.3    Cava, F.4    Berenguer, J.5    Fernandez-Lafuente, R.6    Guisan, J.M.7
  • 15
    • 0024029957 scopus 로고
    • Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes
    • Guisán J.M. Aldehyde-agarose gels as activated supports for immobilization-stabilization of enzymes. Enzyme Microb Technol 1988, 10(6):375-382.
    • (1988) Enzyme Microb Technol , vol.10 , Issue.6 , pp. 375-382
    • Guisán, J.M.1
  • 18
    • 33745184478 scopus 로고    scopus 로고
    • Purification and very strong reversible immobilization of large proteins on anionic exchangers by controlling the support and the immobilization conditions
    • Pessela B.C.C., Fuentes M., Mateo C., Munilla R., Carrascosa A.V., Fernandez-Lafuente R., Guisan J.M. Purification and very strong reversible immobilization of large proteins on anionic exchangers by controlling the support and the immobilization conditions. Enzyme Microb Technol 2006, 39(4):909-915.
    • (2006) Enzyme Microb Technol , vol.39 , Issue.4 , pp. 909-915
    • Pessela, B.C.C.1    Fuentes, M.2    Mateo, C.3    Munilla, R.4    Carrascosa, A.V.5    Fernandez-Lafuente, R.6    Guisan, J.M.7
  • 20
    • 0034748951 scopus 로고    scopus 로고
    • Effects of temperature and pH on the catalytic activity of the immobilized β-galactosidase from Kluyveromyces lactis
    • Zhou Q.Z.K., Chen X.D. Effects of temperature and pH on the catalytic activity of the immobilized β-galactosidase from Kluyveromyces lactis. Biochem Eng J 2001, 9(1):33-40.
    • (2001) Biochem Eng J , vol.9 , Issue.1 , pp. 33-40
    • Zhou, Q.Z.K.1    Chen, X.D.2
  • 21
    • 75149156955 scopus 로고    scopus 로고
    • Lactose hydrolysis by β-galactosidase immobilized on concanavalin A-cellulose in batch and continuous mode
    • Ansari S.A., Husain Q. Lactose hydrolysis by β-galactosidase immobilized on concanavalin A-cellulose in batch and continuous mode. J Mol Catal B: Enzym 2010, 63(1-2):68-74.
    • (2010) J Mol Catal B: Enzym , vol.63 , Issue.1-2 , pp. 68-74
    • Ansari, S.A.1    Husain, Q.2
  • 22
    • 76749169409 scopus 로고    scopus 로고
    • β-galactosidases and their potential applications: a review
    • Husain Q. β-galactosidases and their potential applications: a review. Crit Rev Biotechnol 2010, 30(1):41-62.
    • (2010) Crit Rev Biotechnol , vol.30 , Issue.1 , pp. 41-62
    • Husain, Q.1
  • 23
    • 1142269586 scopus 로고    scopus 로고
    • Stabilization of a multimeric β-galactosidase from Thermus sp. strain T2 by immobilization on novel heterofunctional epoxy supports plus aldehyde-dextran cross-linking
    • Pessela B.C.C., Mateo C., Fuentes M., Vian A., García J.L., Carrascosa A.V., Guisán J.M., Fernández-Lafuente R. Stabilization of a multimeric β-galactosidase from Thermus sp. strain T2 by immobilization on novel heterofunctional epoxy supports plus aldehyde-dextran cross-linking. Biotechnol Prog 2004, 20:388-392.
    • (2004) Biotechnol Prog , vol.20 , pp. 388-392
    • Pessela, B.C.C.1    Mateo, C.2    Fuentes, M.3    Vian, A.4    García, J.L.5    Carrascosa, A.V.6    Guisán, J.M.7    Fernández-Lafuente, R.8
  • 24
    • 0016636179 scopus 로고
    • An improved 2,4,6 trinitrobenzenesulfonic acid method for the determination of amines
    • Snyder S.L., Sobocinski P.Z. An improved 2,4,6 trinitrobenzenesulfonic acid method for the determination of amines. Anal Biochem 1975, 64:284-288.
    • (1975) Anal Biochem , vol.64 , pp. 284-288
    • Snyder, S.L.1    Sobocinski, P.Z.2
  • 25
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzenesulfonicacid
    • Habeeb A.F.S.A. Determination of free amino groups in proteins by trinitrobenzenesulfonicacid. Anal Biochem 1966, 14:328-336.
    • (1966) Anal Biochem , vol.14 , pp. 328-336
    • Habeeb, A.F.S.A.1
  • 26
    • 0027627662 scopus 로고
    • Preparation of activated supports containing low pK amino groups. A new tool for protein immobilization via the carboxyl coupling method
    • Fernandez-Lafuente R., Rosell C.M., Rodriguez V., Santana C., Soler G., Bastida A., Guisán J.M. Preparation of activated supports containing low pK amino groups. A new tool for protein immobilization via the carboxyl coupling method. Enzyme Microb Technol 1993, 15:546-550.
    • (1993) Enzyme Microb Technol , vol.15 , pp. 546-550
    • Fernandez-Lafuente, R.1    Rosell, C.M.2    Rodriguez, V.3    Santana, C.4    Soler, G.5    Bastida, A.6    Guisán, J.M.7
  • 27
    • 0344394382 scopus 로고    scopus 로고
    • Novel bifunctional epoxy/thiol-reactive support to immobilize thiol containing proteins by the epoxy chemistry
    • Grazú V., Abian O., Mateo C., Batista-Viera F., Fernández-Lafuente R., Guisán J.M. Novel bifunctional epoxy/thiol-reactive support to immobilize thiol containing proteins by the epoxy chemistry. Biomacromolecules 2003, 4:1495-1501.
    • (2003) Biomacromolecules , vol.4 , pp. 1495-1501
    • Grazú, V.1    Abian, O.2    Mateo, C.3    Batista-Viera, F.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 28
    • 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
  • 29
    • 0024677047 scopus 로고
    • Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives
    • Blanco R.M., Guisan J.M. Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives. Enzyme Microb Technol 1989, 11(6):360-366.
    • (1989) Enzyme Microb Technol , vol.11 , Issue.6 , pp. 360-366
    • Blanco, R.M.1    Guisan, J.M.2
  • 30
    • 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, 27:680-685.
    • (1970) Nature , vol.27 , pp. 680-685
    • Laemmli, U.K.1
  • 31
  • 32
    • 33847619328 scopus 로고    scopus 로고
    • Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme-support linkages and thermal stability
    • Pedroche J., Yust M., Mateo C., Fernández-Lafuente R., Girón-Calle J., Alaiz M., Vioque J., Guisán J.M., Millán F. Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme-support linkages and thermal stability. Enzyme Microb Technol 2007, 40:1160-1166.
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1160-1166
    • Pedroche, J.1    Yust, M.2    Mateo, C.3    Fernández-Lafuente, R.4    Girón-Calle, J.5    Alaiz, M.6    Vioque, J.7    Guisán, J.M.8    Millán, F.9
  • 33
    • 0034575018 scopus 로고    scopus 로고
    • Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage
    • Mateo C., Fernández-Lorente G., Abian O., Fernández-Lafuente R., Guisán J.M. Multifunctional epoxy supports: a new tool to improve the covalent immobilization of proteins. The promotion of physical adsorptions of proteins on the supports before their covalent linkage. Biomacromolecules 2000, 1:739-745.
    • (2000) Biomacromolecules , vol.1 , pp. 739-745
    • Mateo, C.1    Fernández-Lorente, G.2    Abian, O.3    Fernández-Lafuente, R.4    Guisán, J.M.5
  • 34
    • 0017882127 scopus 로고
    • Methacrylate gels with epoxide groups as supports for immobilization of enzymes in pH range 3-12
    • Turkova J., Blaha K., Malanikova M. Methacrylate gels with epoxide groups as supports for immobilization of enzymes in pH range 3-12. Biochim Biophys Acta 1978, 524(1):162-169.
    • (1978) Biochim Biophys Acta , vol.524 , Issue.1 , pp. 162-169
    • Turkova, J.1    Blaha, K.2    Malanikova, M.3
  • 35
    • 63249128248 scopus 로고    scopus 로고
    • Purification and stabilization of a glutamate dehygrogenase from Thermus thermophilus via oriented multisubunit plus multipoint covalent immobilization
    • Bolivar J.M., Rocha-Martin J., Mateo C., Cava F., Berenguer J., Vega D., Fernandez-Lafuente R., Guisan J.M. Purification and stabilization of a glutamate dehygrogenase from Thermus thermophilus via oriented multisubunit plus multipoint covalent immobilization. J Mol Catal B: Enzym 2009, 58(1-4):158-163.
    • (2009) J Mol Catal B: Enzym , vol.58 , Issue.1-4 , pp. 158-163
    • Bolivar, J.M.1    Rocha-Martin, J.2    Mateo, C.3    Cava, F.4    Berenguer, J.5    Vega, D.6    Fernandez-Lafuente, R.7    Guisan, J.M.8
  • 36
    • 70449631056 scopus 로고    scopus 로고
    • Complete reactivation of immobilized derivatives of a trimeric glutamate dehydrogenase from Thermus thermophillus
    • Bolivar J.M., Rocha-Martin J., Godoy C., Rodrigues R.C., Guisan J.M. Complete reactivation of immobilized derivatives of a trimeric glutamate dehydrogenase from Thermus thermophillus. Process Biochem 2010, 45(1):107-113.
    • (2010) Process Biochem , vol.45 , Issue.1 , pp. 107-113
    • Bolivar, J.M.1    Rocha-Martin, J.2    Godoy, C.3    Rodrigues, R.C.4    Guisan, J.M.5


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