메뉴 건너뛰기




Volumn 60, Issue , 2014, Pages 1-8

Improving the catalytic properties of immobilized Lecitase via physical coating with ionic polymers

Author keywords

Enzyme hyperactivation; Enzyme stabilization; Interfacial activation; Lecitase Ultra; Polyethylenimine; Sulfate dextran

Indexed keywords

ENZYME STABILIZATION; HYPERACTIVATION; INTERFACIAL ACTIVATION; LECITASE; POLYETHYLENIMINES;

EID: 84903365325     PISSN: 01410229     EISSN: 18790909     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2014.03.001     Document Type: Article
Times cited : (64)

References (44)
  • 1
    • 33645780387 scopus 로고    scopus 로고
    • Improving the foaming properties and heat stability of whey protein concentrates by phospholipase treatment
    • Havn S.S., Ipsen R., Nielsen P.M., Lilbæk H.M. Improving the foaming properties and heat stability of whey protein concentrates by phospholipase treatment. Milchwissenschaft 2006, 61:188-191.
    • (2006) Milchwissenschaft , vol.61 , pp. 188-191
    • Havn, S.S.1    Ipsen, R.2    Nielsen, P.M.3    Lilbæk, H.M.4
  • 3
    • 0025512648 scopus 로고
    • Synthesis of phosphatidylcholine with (n-3) fatty acids by phospholipase A 2 in microemulsion
    • Na A., Eriksson C., Eriksson S.G., Österberg E., Holmberg K. Synthesis of phosphatidylcholine with (n-3) fatty acids by phospholipase A 2 in microemulsion. J Am Oil Chem Soc 1990, 67:766-770.
    • (1990) J Am Oil Chem Soc , vol.67 , pp. 766-770
    • Na, A.1    Eriksson, C.2    Eriksson, S.G.3    Österberg, E.4    Holmberg, K.5
  • 4
    • 33746923464 scopus 로고    scopus 로고
    • Enzymatic hydrolysis of phospholipids from Isochrysis galbana for docosahexaenoic acid enrichment
    • Devos M., Poisson L., Ergan F., Pencreac'h G. Enzymatic hydrolysis of phospholipids from Isochrysis galbana for docosahexaenoic acid enrichment. Enzyme Microb Technol 2006, 39:548-554.
    • (2006) Enzyme Microb Technol , vol.39 , pp. 548-554
    • Devos, M.1    Poisson, L.2    Ergan, F.3    Pencreac'h, G.4
  • 5
    • 33746382870 scopus 로고    scopus 로고
    • Production of phosphatidylcholine containing conjugated linoleic acid mediated by phospholipase A2
    • Yamamoto Y., Hosokawa M., Miyashita K. Production of phosphatidylcholine containing conjugated linoleic acid mediated by phospholipase A2. J Mol Catal B: Enzym 2006, 41:92-96.
    • (2006) J Mol Catal B: Enzym , vol.41 , pp. 92-96
    • Yamamoto, Y.1    Hosokawa, M.2    Miyashita, K.3
  • 8
    • 33746892304 scopus 로고    scopus 로고
    • Optimization of enzymatic degumming process for rapeseed oil
    • Yang B., Wang Y.H., Yang J.G. Optimization of enzymatic degumming process for rapeseed oil. J Am Oil Chem Soc 2006, 83:653-658.
    • (2006) J Am Oil Chem Soc , vol.83 , pp. 653-658
    • Yang, B.1    Wang, Y.H.2    Yang, J.G.3
  • 9
    • 33847696154 scopus 로고    scopus 로고
    • Phospholipase A1-catalyzed synthesis of phospholipids enriched in n-3 polyunsaturated fatty acid residues
    • Kim I.H., Garcia H.S., Hill C.G. Phospholipase A1-catalyzed synthesis of phospholipids enriched in n-3 polyunsaturated fatty acid residues. Enzyme Microb Technol 2007, 40:1130-1135.
    • (2007) Enzyme Microb Technol , vol.40 , pp. 1130-1135
    • Kim, I.H.1    Garcia, H.S.2    Hill, C.G.3
  • 10
    • 84878294356 scopus 로고    scopus 로고
    • A comprehensive study on the activity and deactivation of immobilized lecitase ultra in esterifications of food waste streams to monoacylglycerols
    • Gonçalves K.M., Sutili F.K., Júnior I.I., Flores M.C., Soter De Mariz L., Miranda E., et al. A comprehensive study on the activity and deactivation of immobilized lecitase ultra in esterifications of food waste streams to monoacylglycerols. ChemSusChem 2013, 6:872-879.
    • (2013) ChemSusChem , vol.6 , pp. 872-879
    • Gonçalves, K.M.1    Sutili, F.K.2    Júnior, I.I.3    Flores, M.C.4    Soter De Mariz, L.5    Miranda, E.6
  • 11
    • 84871905734 scopus 로고    scopus 로고
    • ® Ultra onto a novel polystyrene DA-201 resin: characterization and biochemical properties
    • ® Ultra onto a novel polystyrene DA-201 resin: characterization and biochemical properties. Appl Biochem Biotechnol 2012, 168:1108-1120.
    • (2012) Appl Biochem Biotechnol , vol.168 , pp. 1108-1120
    • Liu, N.1    Fu, M.2    Wang, Y.3    Zhao, Q.4    Sun, W.5    Zhao, M.6
  • 12
    • 84862784878 scopus 로고    scopus 로고
    • Immobilisation of Lecitase® Ultra for production of diacylglycerols by glycerolysis of soybean oil
    • Liu N., Wang Y., Zhao Q., Cui C., Fu M., Zhao M. Immobilisation of Lecitase® Ultra for production of diacylglycerols by glycerolysis of soybean oil. Food Chem 2012, 134:301-307.
    • (2012) Food Chem , vol.134 , pp. 301-307
    • Liu, N.1    Wang, Y.2    Zhao, Q.3    Cui, C.4    Fu, M.5    Zhao, M.6
  • 13
    • 80051690019 scopus 로고    scopus 로고
    • Fast synthesis of 1 3-DAG by Lecitase® Ultra-catalyzed esterification in solvent-free system
    • Liu N., Wang Y., Zhao Q., Zhang Q., Zhao M. Fast synthesis of 1 3-DAG by Lecitase® Ultra-catalyzed esterification in solvent-free system. Eur J Lipid Sci Technol 2011, 113:973-979.
    • (2011) Eur J Lipid Sci Technol , vol.113 , pp. 973-979
    • Liu, N.1    Wang, Y.2    Zhao, Q.3    Zhang, Q.4    Zhao, M.5
  • 14
    • 79956120943 scopus 로고    scopus 로고
    • A porous vessel bioreactor for gel entrapped biocatalysts: kinetic resolution of trans-methyl (4-methoxyphenyl)glycidate by Lecitase® Ultra in gelatin organogel (Gelozyme)
    • Mishra M.K., Harini M., Kumaraguru T., Lakshmi Prasanna T., Fadnavis N.W. A porous vessel bioreactor for gel entrapped biocatalysts: kinetic resolution of trans-methyl (4-methoxyphenyl)glycidate by Lecitase® Ultra in gelatin organogel (Gelozyme). J Mol Catal B: Enzym 2011, 71:56-62.
    • (2011) J Mol Catal B: Enzym , vol.71 , pp. 56-62
    • Mishra, M.K.1    Harini, M.2    Kumaraguru, T.3    Lakshmi Prasanna, T.4    Fadnavis, N.W.5
  • 15
    • 77949492157 scopus 로고    scopus 로고
    • Partial hydrolysis of soybean oil by phospholipase A1 (Lecitase Ultra)
    • Wang Y., Zhao M., Song K., Wang L., Tang S., Riley W.W. Partial hydrolysis of soybean oil by phospholipase A1 (Lecitase Ultra). Food Chem 2010, 121:1066-1072.
    • (2010) Food Chem , vol.121 , pp. 1066-1072
    • Wang, Y.1    Zhao, M.2    Song, K.3    Wang, L.4    Tang, S.5    Riley, W.W.6
  • 16
    • 80054880910 scopus 로고    scopus 로고
    • Preparation of diacylglycerol-enriched oil from free fatty acids using lecitase ultra-catalyzed esterification
    • Wang L., Wang Y., Hu C., Cao Q., Yang X., Zhao M. Preparation of diacylglycerol-enriched oil from free fatty acids using lecitase ultra-catalyzed esterification. J Am Oil Chem Soc 2011, 88:1557-1565.
    • (2011) J Am Oil Chem Soc , vol.88 , pp. 1557-1565
    • Wang, L.1    Wang, Y.2    Hu, C.3    Cao, Q.4    Yang, X.5    Zhao, M.6
  • 19
    • 0028173902 scopus 로고
    • Current progress in crystallographic studies of new lipases from filamentous fungi
    • Derewenda U., Swenson L., Green R., Wei Y., Yamaguchi S., Joerger R., et al. Current progress in crystallographic studies of new lipases from filamentous fungi. Protein Eng 1994, 7:551-557.
    • (1994) Protein Eng , vol.7 , pp. 551-557
    • Derewenda, U.1    Swenson, L.2    Green, R.3    Wei, Y.4    Yamaguchi, S.5    Joerger, R.6
  • 22
    • 84859424745 scopus 로고    scopus 로고
    • Modulation of the properties of immobilized CALB by chemical modification with 2,3,4-trinitrobenzenesulfonate or ethylendiamine. Advantages of using adsorbed lipases on hydrophobic supports
    • Barbosa O., Ruiz M., Ortiz C., Fernández M., Torres R., Fernandez-Lafuente R. Modulation of the properties of immobilized CALB by chemical modification with 2,3,4-trinitrobenzenesulfonate or ethylendiamine. Advantages of using adsorbed lipases on hydrophobic supports. Process Biochem 2012, 47:867-876.
    • (2012) Process Biochem , vol.47 , pp. 867-876
    • Barbosa, O.1    Ruiz, M.2    Ortiz, C.3    Fernández, M.4    Torres, R.5    Fernandez-Lafuente, R.6
  • 23
    • 80051787511 scopus 로고    scopus 로고
    • Coupling chemical modification and immobilization to improve the catalytic performance of enzymes
    • Rodrigues R.C., Berenguer-Murcia Á., Fernandez-Lafuente R. Coupling chemical modification and immobilization to improve the catalytic performance of enzymes. Adv Synth Catal 2011, 353:2216-2238.
    • (2011) Adv Synth Catal , vol.353 , pp. 2216-2238
    • Rodrigues, R.C.1    Berenguer-Murcia, Á.2    Fernandez-Lafuente, R.3
  • 24
    • 84897915516 scopus 로고    scopus 로고
    • Tuning of Lecitase features via solid-phase chemical modification: effect of the immobilization protocol
    • Garcia-Galan C.J.C.S., Santos d., Barbosa O., Torres R., Pereira E.B., Corberan V.C., et al. Tuning of Lecitase features via solid-phase chemical modification: effect of the immobilization protocol. Process Biochem 2014, 49(4):604-616. 10.1016/j.procbio.01. 028.
    • (2014) Process Biochem , vol.49 , Issue.4 , pp. 604-616
    • Garcia-Galan, C.J.C.S.1    Santos, D.2    Barbosa, O.3    Torres, R.4    Pereira, E.B.5    Corberan, V.C.6
  • 25
    • 84855990869 scopus 로고    scopus 로고
    • Modulation of the selectivity of immobilized lipases by chemical and physical modifications: release of omega-3 fatty acids from fish oil
    • Fernández-Lorente G., Betancor L., Carrascosa A.V., Palomo J.M., Guisan J.M. Modulation of the selectivity of immobilized lipases by chemical and physical modifications: release of omega-3 fatty acids from fish oil. J Am Oil Chem Soc 2012, 89:97-102.
    • (2012) J Am Oil Chem Soc , vol.89 , pp. 97-102
    • Fernández-Lorente, G.1    Betancor, L.2    Carrascosa, A.V.3    Palomo, J.M.4    Guisan, J.M.5
  • 26
    • 77954214536 scopus 로고    scopus 로고
    • Highly enantioselective biocatalysts by coating immobilized lipases with polyethyleneimine
    • Cabrera Z., Gutarra M.L.E., Guisan J.M., Palomo J.M. Highly enantioselective biocatalysts by coating immobilized lipases with polyethyleneimine. Catal Commun 2010, 11:964-967.
    • (2010) Catal Commun , vol.11 , pp. 964-967
    • Cabrera, Z.1    Gutarra, M.L.E.2    Guisan, J.M.3    Palomo, J.M.4
  • 28
    • 4043112664 scopus 로고    scopus 로고
    • Reversible and strong immobilization of proteins by ionic exchange on supports coated with sulfate-dextran
    • Fuentes M., Pessela B.C.C., Maquiese J.V., Ortiz C., Segura R.L., Palomo J.M., et al. Reversible and strong immobilization of proteins by ionic exchange on supports coated with sulfate-dextran. Biotechnol Prog 2004, 20:1134-1139.
    • (2004) Biotechnol Prog , vol.20 , pp. 1134-1139
    • Fuentes, M.1    Pessela, B.C.C.2    Maquiese, J.V.3    Ortiz, C.4    Segura, R.L.5    Palomo, J.M.6
  • 29
    • 0034607269 scopus 로고    scopus 로고
    • Reversible enzyme immobilization via a very strong and nondistorting ionic adsorption on support-polyethylenimine composites
    • Mateo C., Abian O., Fernandez-Lafuente R., Guisan J.M. Reversible enzyme immobilization via a very strong and nondistorting ionic adsorption on support-polyethylenimine composites. Biotechnol Bioeng 2000, 68:98-105.
    • (2000) Biotechnol Bioeng , vol.68 , pp. 98-105
    • Mateo, C.1    Abian, O.2    Fernandez-Lafuente, R.3    Guisan, J.M.4
  • 30
    • 84875808954 scopus 로고    scopus 로고
    • Stabilization of the hexameric glutamate dehydrogenase from Escherichia coli by cations and polyethyleneimine
    • Garcia-Galan C., Barbosa O., Fernandez-Lafuente R. Stabilization of the hexameric glutamate dehydrogenase from Escherichia coli by cations and polyethyleneimine. Enzyme Microb Technol 2013, 52:211-217.
    • (2013) Enzyme Microb Technol , vol.52 , pp. 211-217
    • Garcia-Galan, C.1    Barbosa, O.2    Fernandez-Lafuente, R.3
  • 31
    • 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., et al. Coating of soluble and immobilized enzymes with ionic polymers: full stabilization of the quaternary structure of multimeric enzymes. Biomacromolecules 2009, 10:742-747.
    • (2009) Biomacromolecules , vol.10 , pp. 742-747
    • Bolivar, J.M.1    Rocha-Martin, J.2    Mateo, C.3    Cava, F.4    Berenguer, J.5    Fernandez-Lafuente, R.6
  • 32
    • 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, 45:405-418.
    • (2009) Enzyme Microb Technol , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 33
    • 0032669215 scopus 로고    scopus 로고
    • Protein stabilising effect of polyethyleneimine
    • Andersson M.M., Hatti-Kaul R. Protein stabilising effect of polyethyleneimine. J Biotechnol 1999, 72:21-31.
    • (1999) J Biotechnol , vol.72 , pp. 21-31
    • Andersson, M.M.1    Hatti-Kaul, R.2
  • 34
    • 0029153957 scopus 로고
    • Storage stabilization of enzyme activity by poly(ethyleneimine)
    • Bryjak J. Storage stabilization of enzyme activity by poly(ethyleneimine). Bioprocess Engineering 1995, 13:177-181.
    • (1995) Bioprocess Engineering , vol.13 , pp. 177-181
    • Bryjak, J.1
  • 35
    • 33644542090 scopus 로고    scopus 로고
    • Stabilisation of oxygen-labile nitrilases via co-aggregation with poly(ethyleneimine)
    • Mateo C., Fernandes B., Van Rantwijk F., Stolz A., Sheldon R.A. Stabilisation of oxygen-labile nitrilases via co-aggregation with poly(ethyleneimine). J Mol Catal B: Enzym 2006, 38:154-157.
    • (2006) J Mol Catal B: Enzym , vol.38 , pp. 154-157
    • Mateo, C.1    Fernandes, B.2    Van Rantwijk, F.3    Stolz, A.4    Sheldon, R.A.5
  • 36
    • 2542579376 scopus 로고    scopus 로고
    • Co-aggregation of penicillin G acylase and polyionic polymers: an easy methodology to prepare enzyme biocatalysts stable in organic media
    • Wilson L., Illanes A., Abián O., Pessela B.C.C., Fernández-Lafuente R., Guisán J.M. Co-aggregation of penicillin G acylase and polyionic polymers: an easy methodology to prepare enzyme biocatalysts stable in organic media. Biomacromolecules 2004, 5:852-857.
    • (2004) Biomacromolecules , vol.5 , pp. 852-857
    • Wilson, L.1    Illanes, A.2    Abián, O.3    Pessela, B.C.C.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 37
    • 0032890111 scopus 로고    scopus 로고
    • Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives: dramatic stabilization of penicillin acylase versus organic solvents
    • Fernandez-Lafuente R., Rosell C.M., Caanan-Haden L., Rodes L., Guisan J.M. Facile synthesis of artificial enzyme nano-environments via solid-phase chemistry of immobilized derivatives: dramatic stabilization of penicillin acylase versus organic solvents. Enzyme Microb Technol 1999, 24:96-103.
    • (1999) Enzyme Microb Technol , vol.24 , pp. 96-103
    • Fernandez-Lafuente, R.1    Rosell, C.M.2    Caanan-Haden, L.3    Rodes, L.4    Guisan, J.M.5
  • 39
    • 34547537549 scopus 로고    scopus 로고
    • Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports
    • Fernández-Lorente G., Palomo J.M., Cabrera Z., Guisán J.M., Fernández-Lafuente R. Specificity enhancement towards hydrophobic substrates by immobilization of lipases by interfacial activation on hydrophobic supports. Enzyme Microb Technol 2007, 41:565-569.
    • (2007) Enzyme Microb Technol , vol.41 , pp. 565-569
    • Fernández-Lorente, G.1    Palomo, J.M.2    Cabrera, Z.3    Guisán, J.M.4    Fernández-Lafuente, R.5
  • 40
    • 0017070145 scopus 로고
    • Immobilization of enzymes by covalent binding to amine supports via cyanogen bromide activation
    • Schnapp J., Shalitin Y. Immobilization of enzymes by covalent binding to amine supports via cyanogen bromide activation. Biochem Biophys Res Commun 1976, 70:8-14.
    • (1976) Biochem Biophys Res Commun , vol.70 , pp. 8-14
    • Schnapp, J.1    Shalitin, Y.2
  • 42
    • 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
  • 44
    • 33749545520 scopus 로고    scopus 로고
    • Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance
    • Fernández-Lorente G., Palomo J.M., Mateo C., Munilla R., Ortiz C., Cabrera Z., et al. Glutaraldehyde cross-linking of lipases adsorbed on aminated supports in the presence of detergents leads to improved performance. Biomacromolecules 2006, 7:2610-2615.
    • (2006) Biomacromolecules , vol.7 , pp. 2610-2615
    • Fernández-Lorente, G.1    Palomo, J.M.2    Mateo, C.3    Munilla, R.4    Ortiz, C.5    Cabrera, Z.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.