메뉴 건너뛰기




Volumn 10, Issue 1, 2010, Pages 57-64

Immobilization of acetylcholinesterase in nanofibrous PVA/BSA membranes by electrospinning

Author keywords

Acetylcholinesterase; Electrospinning; Immobilization; Nanofiber; PVA

Indexed keywords

ACETYLCHOLINESTERASE; ACTIVITY RECOVERY; BATCH CYCLE; FREE ENZYME; INITIAL ACTIVITY; PH VALUE; STABILIZING ADDITIVES; VERSATILE METHODS;

EID: 77949500935     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.200900001     Document Type: Article
Times cited : (50)

References (41)
  • 1
    • 34447102668 scopus 로고    scopus 로고
    • Electrospun polyacrylonitrile nanofibrous membranes for lipase immobilization
    • Li, S. F., Chenb, J. P., Wu, W. T., Electrospun polyacrylonitrile nanofibrous membranes for lipase immobilization. J. Mol. Catal. B Enzym. 2007, 47, 117-127.
    • (2007) J. Mol. Catal. B Enzym , vol.47 , pp. 117-127
    • Li, S.F.1    Chenb, J.P.2    Wu, W.T.3
  • 2
    • 84907034314 scopus 로고
    • strategy for stabilizing enzymes part one: Increasing stability of enzymes via their multi-point interaction with a support
    • Mozhaev, V. V., Melik-Nubarov, N. S., Sergeeva, M. V., Siksnis, V., Martinek, K., strategy for stabilizing enzymes part one: increasing stability of enzymes via their multi-point interaction with a support. Biocatal. Biotransfor. 1990, 3, 179-187.
    • (1990) Biocatal. Biotransfor , vol.3 , pp. 179-187
    • Mozhaev, V.V.1    Melik-Nubarov, N.S.2    Sergeeva, M.V.3    Siksnis, V.4    Martinek, K.5
  • 3
    • 77949520869 scopus 로고
    • Immobilized enzyme principles
    • Wingard, L. B, Jr, Katchalski-Katzir, E, Goldstein, L, Eds, Academic Press, New York
    • Wingard, L. B., Jr., Katchalski-Katzir, E., Goldstein, L., (Eds.), Immobilized enzyme principles, in: Applied Biochemistry and Bioengineering, Academic Press, New York 1976, p. 364.
    • (1976) Applied Biochemistry and Bioengineering , pp. 364
  • 4
    • 0030232761 scopus 로고    scopus 로고
    • Nanometre diameter fibres of polymer, produced by electrospinning
    • Reneker, D. H., Chun, I., Nanometre diameter fibres of polymer, produced by electrospinning. Nanotechnology 1996, 7, 216-223.
    • (1996) Nanotechnology , vol.7 , pp. 216-223
    • Reneker, D.H.1    Chun, I.2
  • 5
    • 0037018364 scopus 로고    scopus 로고
    • Electrospinning of polyurethane fibers
    • Demir, M. M., Yilgor, I., Yilgor, E., Erman, B., Electrospinning of polyurethane fibers. Polymer 2002, 43, 3303-3309.
    • (2002) Polymer , vol.43 , pp. 3303-3309
    • Demir, M.M.1    Yilgor, I.2    Yilgor, E.3    Erman, B.4
  • 6
    • 4043075572 scopus 로고    scopus 로고
    • Electrospinning of nanofibers: Reinventing the wheel?
    • Li, D., Xia, Y., Electrospinning of nanofibers: reinventing the wheel? Adv. Mater. 2004, 16, 1151-1170.
    • (2004) Adv. Mater , vol.16 , pp. 1151-1170
    • Li, D.1    Xia, Y.2
  • 7
    • 0141683910 scopus 로고    scopus 로고
    • A review on polymer nanofibers by electrospinning and their applications in nanocomposites
    • Huang, Z. M., Zhang, Y. Z., Kotaki, M., Ramakrishna, S., A review on polymer nanofibers by electrospinning and their applications in nanocomposites. Compos. Sci. Technol. 2003, 63, 2223-2253.
    • (2003) Compos. Sci. Technol , vol.63 , pp. 2223-2253
    • Huang, Z.M.1    Zhang, Y.Z.2    Kotaki, M.3    Ramakrishna, S.4
  • 8
    • 36248959221 scopus 로고    scopus 로고
    • Functional electrospun nanofibrous scaffolds for biomedical applications
    • Liang, D., Hsiao, B. S., Chu, B., Functional electrospun nanofibrous scaffolds for biomedical applications. Adv. Drug Deliver. Rev. 2007, 59, 1392-1412.
    • (2007) Adv. Drug Deliver. Rev , vol.59 , pp. 1392-1412
    • Liang, D.1    Hsiao, B.S.2    Chu, B.3
  • 10
    • 20444447017 scopus 로고    scopus 로고
    • Chitosan-tethered poly(acrylonitrile-co-maleic acid) hollow fiber membrane for lipase immobilization
    • Ye, P., Xu, Z. K., Che, A. F., Wu, J., Seta, P., Chitosan-tethered poly(acrylonitrile-co-maleic acid) hollow fiber membrane for lipase immobilization. Biomaterials 2005, 26, 6394-6403.
    • (2005) Biomaterials , vol.26 , pp. 6394-6403
    • Ye, P.1    Xu, Z.K.2    Che, A.F.3    Wu, J.4    Seta, P.5
  • 11
    • 33748525836 scopus 로고    scopus 로고
    • Electrospun nanofibers modified with phospholipid moieties for enzyme immobilization
    • Huang, X. J., Xu, Z. K., Wan, L. S., Innocent, C., Seta, P., Electrospun nanofibers modified with phospholipid moieties for enzyme immobilization. Macromol. Rapid Commun. 2006, 27, 1341-1345.
    • (2006) Macromol. Rapid Commun , vol.27 , pp. 1341-1345
    • Huang, X.J.1    Xu, Z.K.2    Wan, L.S.3    Innocent, C.4    Seta, P.5
  • 12
    • 0038683278 scopus 로고    scopus 로고
    • Ultra-high surface fibrous membranes from electrospinning of natural proteins: Casein and lipase enzyme
    • Xie, J., Hsieh, Y. L., Ultra-high surface fibrous membranes from electrospinning of natural proteins: casein and lipase enzyme. J. Mater. Sci. 2003, 38, 2125-2133.
    • (2003) J. Mater. Sci , vol.38 , pp. 2125-2133
    • Xie, J.1    Hsieh, Y.L.2
  • 13
    • 0242408223 scopus 로고    scopus 로고
    • Surface modification of microporous polypropylene membranes by the grafting of poly(c-stearyl-L-glutamate)
    • Liu, Z. M., Xu, Z. K., Wang, J. Q., Yang, Q., Wu, J., Seta, P., Surface modification of microporous polypropylene membranes by the grafting of poly(c-stearyl-L-glutamate). Eur. Polym. J. 2003, 39, 2291-2299.
    • (2003) Eur. Polym. J , vol.39 , pp. 2291-2299
    • Liu, Z.M.1    Xu, Z.K.2    Wang, J.Q.3    Yang, Q.4    Wu, J.5    Seta, P.6
  • 14
    • 33646040441 scopus 로고    scopus 로고
    • Nanofibrous poly(acrylonitrile-co-maleic acid) membranes functionalized with gelatin and chitosan for lipase immobilization
    • Ye, P., Xu, Z. K., Wu, J., Innocent, C., Seta, P., Nanofibrous poly(acrylonitrile-co-maleic acid) membranes functionalized with gelatin and chitosan for lipase immobilization. Biomaterials 2006, 27, 4169-4176.
    • (2006) Biomaterials , vol.27 , pp. 4169-4176
    • Ye, P.1    Xu, Z.K.2    Wu, J.3    Innocent, C.4    Seta, P.5
  • 15
    • 12844283400 scopus 로고    scopus 로고
    • Comparison of hydrolytic activities in aqueous and organic media for lipases immobilized on poly(acrylonitrile-comaleic acid) ultrafiltration hollow fiber membrane
    • Ye, P., Xu, Z. K., Wang, Z. G., Wu, J., Denga, H. T., Seta, P., Comparison of hydrolytic activities in aqueous and organic media for lipases immobilized on poly(acrylonitrile-comaleic acid) ultrafiltration hollow fiber membrane. J. Mol. Catal. B Enzym. 2005, 32, 115-121.
    • (2005) J. Mol. Catal. B Enzym , vol.32 , pp. 115-121
    • Ye, P.1    Xu, Z.K.2    Wang, Z.G.3    Wu, J.4    Denga, H.T.5    Seta, P.6
  • 16
    • 33646164889 scopus 로고    scopus 로고
    • Entrusting poly(acrylonitrile-co-maleic acid) ultrafiltration hollow fiber membranes with biomimetic surfaces for lipase immobilization
    • Ye, P., Xu, Z. K., Wu, J., Innocent, C., Seta, P., Entrusting poly(acrylonitrile-co-maleic acid) ultrafiltration hollow fiber membranes with biomimetic surfaces for lipase immobilization. J. Mol. Catal. B Enzym. 2006, 40, 30-37.
    • (2006) J. Mol. Catal. B Enzym , vol.40 , pp. 30-37
    • Ye, P.1    Xu, Z.K.2    Wu, J.3    Innocent, C.4    Seta, P.5
  • 17
    • 0034692131 scopus 로고    scopus 로고
    • A membrane based reactor with an enzyme immobilized by an avidin-biotin molecular recognition in a polymer matrix
    • Amounas, M., Innocent, C., Cosnier, S., Seta, P., A membrane based reactor with an enzyme immobilized by an avidin-biotin molecular recognition in a polymer matrix. J. Membrane Sci. 2000, 176, 169-176.
    • (2000) J. Membrane Sci , vol.176 , pp. 169-176
    • Amounas, M.1    Innocent, C.2    Cosnier, S.3    Seta, P.4
  • 18
    • 0037557803 scopus 로고    scopus 로고
    • Preparation and characterization of nanoscale poly(vinyl alcohol) fibers via electrospinning
    • Ding, B., Kim, H. Y., Lee, S. C., Lee, D. R., Choi, K. J., Preparation and characterization of nanoscale poly(vinyl alcohol) fibers via electrospinning. Fiber Polym. 2002, 3, 73-79.
    • (2002) Fiber Polym , vol.3 , pp. 73-79
    • Ding, B.1    Kim, H.Y.2    Lee, S.C.3    Lee, D.R.4    Choi, K.J.5
  • 19
    • 0032143416 scopus 로고    scopus 로고
    • Poly (vinyl alcohol) cryogels employedas matrices for cell immobilization. 3. Overview of recent research and developments
    • Lozinsky, V. I., Plieva, F. M., Poly (vinyl alcohol) cryogels employedas matrices for cell immobilization. 3. Overview of recent research and developments. Enzyme Microb. Technol. 1998, 23, 227-242.
    • (1998) Enzyme Microb. Technol , vol.23 , pp. 227-242
    • Lozinsky, V.I.1    Plieva, F.M.2
  • 20
    • 20144373106 scopus 로고    scopus 로고
    • Poly(vinyl alcohol) nanofibers by electrospinning as a protein delivery system and the retardation of enzyme release by additional polymer coatings
    • Zeng, J., Aigner, A., Czubayko, F., Kissel, T., Wendorff, J. H., Greiner, A., Poly(vinyl alcohol) nanofibers by electrospinning as a protein delivery system and the retardation of enzyme release by additional polymer coatings. Biomacromolecules 2005, 6, 1484-1488.
    • (2005) Biomacromolecules , vol.6 , pp. 1484-1488
    • Zeng, J.1    Aigner, A.2    Czubayko, F.3    Kissel, T.4    Wendorff, J.H.5    Greiner, A.6
  • 21
    • 0242607168 scopus 로고    scopus 로고
    • Effect of molecular weight on fibrous PVA produced by electrospinning
    • Koski, A., Yim, K., Shivkumar, K., Effect of molecular weight on fibrous PVA produced by electrospinning. Mater. Lett. 2004, 58, 493-497.
    • (2004) Mater. Lett , vol.58 , pp. 493-497
    • Koski, A.1    Yim, K.2    Shivkumar, K.3
  • 22
    • 77949504568 scopus 로고    scopus 로고
    • Djennad, M., Benachour, D., Berger, H., Schom.acker, R., Poly (vinyl alcohol) ultrafiltration membranes: synthesis, characterization, the use for enzyme immobilization. Eng. Life Sci. 2003, 3, 446-452.
    • Djennad, M., Benachour, D., Berger, H., Schom.acker, R., Poly (vinyl alcohol) ultrafiltration membranes: synthesis, characterization, the use for enzyme immobilization. Eng. Life Sci. 2003, 3, 446-452.
  • 23
    • 14644442914 scopus 로고    scopus 로고
    • Immobilization of cellulase in nanofibrous PVA membranes by electrospinning
    • Wu, L., Yuan, X., Sheng, J., Immobilization of cellulase in nanofibrous PVA membranes by electrospinning. J. Membrane Sci. 2005, 250, 167-173.
    • (2005) J. Membrane Sci , vol.250 , pp. 167-173
    • Wu, L.1    Yuan, X.2    Sheng, J.3
  • 24
    • 33750988520 scopus 로고    scopus 로고
    • Electrospun poly(vinyl alcohol)/glucose oxidase biocomposite membranes for biosensor applications
    • Ren, G., Xu, X., Liu, Q., Cheng, J., Yuan, X., Wu, L., Wan, Y., Electrospun poly(vinyl alcohol)/glucose oxidase biocomposite membranes for biosensor applications. React. Funct. Polym. 2006, 66, 1559-1564.
    • (2006) React. Funct. Polym , vol.66 , pp. 1559-1564
    • Ren, G.1    Xu, X.2    Liu, Q.3    Cheng, J.4    Yuan, X.5    Wu, L.6    Wan, Y.7
  • 25
    • 37349035008 scopus 로고    scopus 로고
    • Immobilization of lipase enzyme in polyvinyl alcohol (PVA) nanofibrous membranes
    • Wang, Y., Hsieh, Y. L., Immobilization of lipase enzyme in polyvinyl alcohol (PVA) nanofibrous membranes. J. Membrane Sci. 2008, 309, 73-81.
    • (2008) J. Membrane Sci , vol.309 , pp. 73-81
    • Wang, Y.1    Hsieh, Y.L.2
  • 26
    • 33745328074 scopus 로고    scopus 로고
    • The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase
    • Ranaei-Siadat, S. O., Lougarre, A., Lamouroux, L., Ladurantie, C., Fournier, D., The effect of engineered disulfide bonds on the stability of Drosophila melanogaster acetylcholinesterase. BMC Biochem. 2006, 7, 12-18.
    • (2006) BMC Biochem , vol.7 , pp. 12-18
    • Ranaei-Siadat, S.O.1    Lougarre, A.2    Lamouroux, L.3    Ladurantie, C.4    Fournier, D.5
  • 27
    • 0039293206 scopus 로고    scopus 로고
    • Determination of organophosphate and carbamate pesticides in spiked samples of tap water and fruit juices by a biosensor with photothermal detection
    • Pogacnik, L., Franko, M., Determination of organophosphate and carbamate pesticides in spiked samples of tap water and fruit juices by a biosensor with photothermal detection. Biosens. Bioelectron. 1999, 14, 569-578.
    • (1999) Biosens. Bioelectron , vol.14 , pp. 569-578
    • Pogacnik, L.1    Franko, M.2
  • 28
    • 0032747193 scopus 로고    scopus 로고
    • Development of sensors for direct detection of organophosphates. Part I: Immobilization, characterization and stabilization of acetylcholinesterase and organophosphate hydrolase on silica supports
    • Singh, A. K., Flounders, A. W., Volponi, J. V., Ashley, C. S., Wally, K., Schoeniger, J. S., Development of sensors for direct detection of organophosphates. Part I: immobilization, characterization and stabilization of acetylcholinesterase and organophosphate hydrolase on silica supports. Biosens. Bioelectron. 1999, 14, 703-713.
    • (1999) Biosens. Bioelectron , vol.14 , pp. 703-713
    • Singh, A.K.1    Flounders, A.W.2    Volponi, J.V.3    Ashley, C.S.4    Wally, K.5    Schoeniger, J.S.6
  • 29
    • 31044455163 scopus 로고    scopus 로고
    • Enzyme inhibition-based biosensors for food safety and environmental monitoring
    • Amine, A., Mohammadi, H., Bourais, I., Palleschi, G., Enzyme inhibition-based biosensors for food safety and environmental monitoring. Biosens. Bioelectron. 2006, 21, 1405-1423.
    • (2006) Biosens. Bioelectron , vol.21 , pp. 1405-1423
    • Amine, A.1    Mohammadi, H.2    Bourais, I.3    Palleschi, G.4
  • 30
    • 0029081902 scopus 로고
    • Binding of acetylcholinesterase to multiwall carbon nanotube-cross-linked chitosan composite for flow-injection amperometric detection of an organophosphorous insecticide
    • Cremisini, C., Di Sario, S., Mela, J., Pilloton, R., Palleschi, G., Binding of acetylcholinesterase to multiwall carbon nanotube-cross-linked chitosan composite for flow-injection amperometric detection of an organophosphorous insecticide. Anal. Chim. Acta 1995, 311, 273-280.
    • (1995) Anal. Chim. Acta , vol.311 , pp. 273-280
    • Cremisini, C.1    Di Sario, S.2    Mela, J.3    Pilloton, R.4    Palleschi, G.5
  • 32
    • 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, 76, 248-254.
    • (1976) Anal. Biochem , vol.76 , pp. 248-254
    • Bradford, M.M.1
  • 33
  • 34
    • 0028172607 scopus 로고
    • Prospects for exploiting immobilization to modify enzyme activity
    • Clark, D. S., Prospects for exploiting immobilization to modify enzyme activity. Trends Biotechnol. 1994, 12, 439-445.
    • (1994) Trends Biotechnol , vol.12 , pp. 439-445
    • Clark, D.S.1
  • 35
    • 0027080386 scopus 로고
    • Replication inhibition by nucleoside analogues of a recombinant Autographa californica multicapsid nuclear polyhedrosis virus harboring the herpes thymidine kinase gene driven by the IE-1(0) promoter: A new way to select recombinant baculoviruses
    • Godeau, F., Saucier, C., Kourilsky, P., Replication inhibition by nucleoside analogues of a recombinant Autographa californica multicapsid nuclear polyhedrosis virus harboring the herpes thymidine kinase gene driven by the IE-1(0) promoter: a new way to select recombinant baculoviruses. Nucleic Acids Res. 1992, 20, 6239-6246.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6239-6246
    • Godeau, F.1    Saucier, C.2    Kourilsky, P.3
  • 37
    • 34547603971 scopus 로고    scopus 로고
    • Covalent attachment of cholesterol oxidase and horseradish peroxidase on perlite through silanization: Activity, stability and co-immobilization
    • Torabi, S. F., Khajeh, K., Ghasempur, S., Ghaemia, N., Ranaei Siadat, S. O., Covalent attachment of cholesterol oxidase and horseradish peroxidase on perlite through silanization: Activity, stability and co-immobilization. J. Biotechnol. 2007, 131, 111-120.
    • (2007) J. Biotechnol , vol.131 , pp. 111-120
    • Torabi, S.F.1    Khajeh, K.2    Ghasempur, S.3    Ghaemia, N.4    Ranaei Siadat, S.O.5
  • 38
    • 85131306304 scopus 로고    scopus 로고
    • Sahin, F., Demirel, G., T.umt .urk, H., A novel matrix for the immobilization of acetylcholinesterase. Int. J. Biol. Macromol. 2005, 37, 148-153.
    • Sahin, F., Demirel, G., T.umt .urk, H., A novel matrix for the immobilization of acetylcholinesterase. Int. J. Biol. Macromol. 2005, 37, 148-153.
  • 39
    • 0023935101 scopus 로고
    • Studies on the properties of immobilized urokinase: Effects of pH and temperature
    • Yabushita, I., Studies on the properties of immobilized urokinase: effects of pH and temperature. Biotechnol. Appl. Biochem. 1988, 10, 294-300.
    • (1988) Biotechnol. Appl. Biochem , vol.10 , pp. 294-300
    • Yabushita, I.1
  • 40
    • 0001431603 scopus 로고    scopus 로고
    • Effect of pH on the Adsorption of Bovine Serum Albumin at the Silica/Water Interface
    • Su, T. J., Lu, J. R., Thomas, R. K., Cui, Z. F., Effect of pH on the Adsorption of Bovine Serum Albumin at the Silica/Water Interface. J. Phys. Chem. B 1999, 103, 3727-3736.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3727-3736
    • Su, T.J.1    Lu, J.R.2    Thomas, R.K.3    Cui, Z.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.