메뉴 건너뛰기




Volumn 472, Issue , 2015, Pages 251-260

Nanofibrous membranes for single-step immobilization of hyperthermophilic enzymes

Author keywords

Chemical crosslinking; Electrospinning; Enzyme immobilization; Hyperthermophilic enzymes; Nanofibers

Indexed keywords

CATALYST ACTIVITY; CROSSLINKING; ELECTROSPINNING; ENZYME ACTIVITY; HIGH TEMPERATURE OPERATIONS; MASS TRANSFER; NANOFIBERS;

EID: 84908405848     PISSN: 03767388     EISSN: 18733123     Source Type: Journal    
DOI: 10.1016/j.memsci.2014.08.037     Document Type: Article
Times cited : (29)

References (75)
  • 4
    • 79961235658 scopus 로고    scopus 로고
    • Perspective on recent progress in immobilization of enzymes
    • Tran D.N., Balkus K.J. Perspective on recent progress in immobilization of enzymes. ACS Catal. 2011, 1:956-968.
    • (2011) ACS Catal. , vol.1 , pp. 956-968
    • Tran, D.N.1    Balkus, K.J.2
  • 5
    • 77956972987 scopus 로고    scopus 로고
    • N-terminal fusion of a hyperthermophilic chitin-binding domain to xylose isomerase from Thermotoga neapolitana enhances kinetics and thermostability of both free and immobilized enzymes
    • Harris J.M., Epting K.L., Kelly R.M. N-terminal fusion of a hyperthermophilic chitin-binding domain to xylose isomerase from Thermotoga neapolitana enhances kinetics and thermostability of both free and immobilized enzymes. Biotechnol. Prog. 2010, 26:993-1000.
    • (2010) Biotechnol. Prog. , vol.26 , pp. 993-1000
    • Harris, J.M.1    Epting, K.L.2    Kelly, R.M.3
  • 6
    • 34547747311 scopus 로고    scopus 로고
    • Hyperthermophlic enzymes - stability, activity and implementation strategies for high temperature applications
    • Unsworth L.D., van der Oost J., Koutsopoulos S. Hyperthermophlic enzymes - stability, activity and implementation strategies for high temperature applications. FEBS J. 2007, 274:4044-4056.
    • (2007) FEBS J. , vol.274 , pp. 4044-4056
    • Unsworth, L.D.1    van der Oost, J.2    Koutsopoulos, S.3
  • 7
    • 80051793850 scopus 로고    scopus 로고
    • Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization
    • Cowan D.A., Fernandez-Lafuente R. Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization. Enzym. Microb. Technol. 2011, 49:326-346.
    • (2011) Enzym. Microb. Technol. , vol.49 , pp. 326-346
    • Cowan, D.A.1    Fernandez-Lafuente, R.2
  • 8
    • 0002156239 scopus 로고    scopus 로고
    • Immobilized enzymes: methods and applications
    • Tischer W., Wedekind F. Immobilized enzymes: methods and applications. Top. Curr. Chem. 1999, 200:95-126.
    • (1999) Top. Curr. Chem. , vol.200 , pp. 95-126
    • Tischer, W.1    Wedekind, F.2
  • 9
    • 0041528514 scopus 로고    scopus 로고
    • Immobilizing enzymes: how to create more suitable biocatalysts
    • Bornscheuer U.T. Immobilizing enzymes: how to create more suitable biocatalysts. Angew. Chem. Int. Ed. 2003, 42:3336-3337.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 3336-3337
    • Bornscheuer, U.T.1
  • 10
    • 34547209337 scopus 로고    scopus 로고
    • Enzyme immobilization: the quest for optimum performance
    • Sheldon R.A. Enzyme immobilization: the quest for optimum performance. Adv. Synth. Catal. 2007, 349:1289-1307.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1289-1307
    • Sheldon, R.A.1
  • 11
    • 16244405562 scopus 로고    scopus 로고
    • Immobilised enzymes: science or art?
    • Cao L. Immobilised enzymes: science or art?. Curr. Opin. Chem. Biol. 2005, 9:217-226.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 217-226
    • Cao, L.1
  • 12
    • 14644442914 scopus 로고    scopus 로고
    • Immobilization of cellulose in nanofibrous PVA membranes by electrospinning
    • Wu L., Yuan X., Sheng J. Immobilization of cellulose in nanofibrous PVA membranes by electrospinning. J. Membr. Sci. 2005, 250:167-173.
    • (2005) J. Membr. Sci. , vol.250 , pp. 167-173
    • Wu, L.1    Yuan, X.2    Sheng, J.3
  • 13
    • 37349035008 scopus 로고    scopus 로고
    • Immobilization of lipase enzymes in polyvinyl alcohol (PVA) nanofibrous membranes
    • Wang Y., Hsieh Y.L. Immobilization of lipase enzymes in polyvinyl alcohol (PVA) nanofibrous membranes. J. Membr. Sci. 2008, 309:73-81.
    • (2008) J. Membr. Sci. , vol.309 , pp. 73-81
    • Wang, Y.1    Hsieh, Y.L.2
  • 14
    • 33749188740 scopus 로고    scopus 로고
    • Nanofibrous materials and their applications
    • Burger C., Hsiao B.S., Chu B. Nanofibrous materials and their applications. Annu. Rev. Mater. Res. 2006, 36:333-368.
    • (2006) Annu. Rev. Mater. Res. , vol.36 , pp. 333-368
    • Burger, C.1    Hsiao, B.S.2    Chu, B.3
  • 15
    • 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
  • 16
    • 0030232761 scopus 로고    scopus 로고
    • Nanometer diameter fibers of polymer, produced by electrospinning
    • Reneker D.H., Chun I. Nanometer diameter fibers of polymer, produced by electrospinning. Nanotechnology 1996, 7:216-223.
    • (1996) Nanotechnology , vol.7 , pp. 216-223
    • Reneker, D.H.1    Chun, I.2
  • 17
    • 0141683910 scopus 로고    scopus 로고
    • A review on polymer nanofibers by electrospinning and their applications in nanocomposites
    • Huang Z., 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.1    Zhang, Y.Z.2    Kotaki, M.3    Ramakrishna, S.4
  • 19
    • 65649114364 scopus 로고    scopus 로고
    • Electrospun nanoparticle-nanofiber composites via one-step synthesis
    • Saquing C., Manasco J.L., Khan S.A. Electrospun nanoparticle-nanofiber composites via one-step synthesis. Small 2009, 5:944-951.
    • (2009) Small , vol.5 , pp. 944-951
    • Saquing, C.1    Manasco, J.L.2    Khan, S.A.3
  • 20
    • 74849115025 scopus 로고    scopus 로고
    • In situ cross-linking of electrospun poly(vinyl alcohol) nanofibers
    • Tang C., Saquing C.D., Harding J.R., Khan S.A. In situ cross-linking of electrospun poly(vinyl alcohol) nanofibers. Macromolecules 2010, 43:630-637.
    • (2010) Macromolecules , vol.43 , pp. 630-637
    • Tang, C.1    Saquing, C.D.2    Harding, J.R.3    Khan, S.A.4
  • 21
    • 58249088885 scopus 로고    scopus 로고
    • Enzyme immobilization on electrospun polymer nanofibers: an overview
    • Wang Z., Wan L., Liu Z., Huang X., Xu Z. Enzyme immobilization on electrospun polymer nanofibers: an overview. J. Mol. Catal. B-Enzym. 2009, 56:189-195.
    • (2009) J. Mol. Catal. B-Enzym. , vol.56 , pp. 189-195
    • Wang, Z.1    Wan, L.2    Liu, Z.3    Huang, X.4    Xu, Z.5
  • 22
    • 84866324570 scopus 로고    scopus 로고
    • Electrospinning pure protein solutions in core-shell fibers
    • Tiwari S.K., Venkatraman S. Electrospinning pure protein solutions in core-shell fibers. Polym. Int. 2012, 61:1549-1555.
    • (2012) Polym. Int. , vol.61 , pp. 1549-1555
    • Tiwari, S.K.1    Venkatraman, S.2
  • 23
    • 47249148929 scopus 로고    scopus 로고
    • Encapsulation of enzymes in biodegradable tubular structures
    • Dror Y., Kuhn J., Avrahami R., Zussman E. Encapsulation of enzymes in biodegradable tubular structures. Macromolecules 2008, 41:4187-4192.
    • (2008) Macromolecules , vol.41 , pp. 4187-4192
    • Dror, Y.1    Kuhn, J.2    Avrahami, R.3    Zussman, E.4
  • 24
    • 62549140558 scopus 로고    scopus 로고
    • Activation of lactoperoxidase system in milk by glucose oxidase immobilized in electrospun polylactide microfibers
    • Zhou Y., Lim L.T. Activation of lactoperoxidase system in milk by glucose oxidase immobilized in electrospun polylactide microfibers. J. Food Sci. 2009, 74:C170-C176.
    • (2009) J. Food Sci. , vol.74 , pp. C170-C176
    • Zhou, Y.1    Lim, L.T.2
  • 25
    • 80055003730 scopus 로고    scopus 로고
    • In situ encapsulation of laccase in nanofibers by electrospinning for development of enyme biosensors for chlorophenol monitoring
    • Liu J., Niu J., Yin L., Jiang F. In situ encapsulation of laccase in nanofibers by electrospinning for development of enyme biosensors for chlorophenol monitoring. Analyst 2011, 136:4802-4808.
    • (2011) Analyst , vol.136 , pp. 4802-4808
    • Liu, J.1    Niu, J.2    Yin, L.3    Jiang, F.4
  • 28
    • 83455245879 scopus 로고    scopus 로고
    • Laccase-carrying electrospun fibrous membranes for adsorption and degredation of PAHs in shoal soils
    • Dai Y., Yin L., Niu J. Laccase-carrying electrospun fibrous membranes for adsorption and degredation of PAHs in shoal soils. Environ. Sci. Technol. 2011, 45:10611-10618.
    • (2011) Environ. Sci. Technol. , vol.45 , pp. 10611-10618
    • Dai, Y.1    Yin, L.2    Niu, J.3
  • 30
    • 84871851279 scopus 로고    scopus 로고
    • Enzyme immobilization via electrospinning
    • Tran D.N., Balkus K.J. Enzyme immobilization via electrospinning. Top. Catal. 2012, 55:1057-1069.
    • (2012) Top. Catal. , vol.55 , pp. 1057-1069
    • Tran, D.N.1    Balkus, K.J.2
  • 32
    • 0038683278 scopus 로고    scopus 로고
    • Ultra-high surface fibrous membranes from electrospinning of natural proteins: casein and lipase enzyme
    • Xie J., Hsieh Y. 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.2
  • 33
    • 33750988520 scopus 로고    scopus 로고
    • Optimizing partition-controlled drug release from electrospun core-shell fibers
    • Ren G., Xu X., Liu Q., Cheng J., Yuan X., Wu L., Wan Y. Optimizing partition-controlled drug release from electrospun core-shell fibers. 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
  • 34
    • 33744794047 scopus 로고    scopus 로고
    • In situ encapsulation of horseradish peroxidase in electrospun porous silica fibers for potential biosensor applications
    • Patel A.C., Li S., Yuan J., Wei T. In situ encapsulation of horseradish peroxidase in electrospun porous silica fibers for potential biosensor applications. Nano Lett. 2006, 6:1042-1046.
    • (2006) Nano Lett. , vol.6 , pp. 1042-1046
    • Patel, A.C.1    Li, S.2    Yuan, J.3    Wei, T.4
  • 35
    • 33947433621 scopus 로고    scopus 로고
    • Biochemical analysis of Thermotoga maritima GH36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases
    • Comfort D.A., Bobrov K.S., Ivanen D.R., Shabalin K.A., Harris J.M., Kulminskaya A.A., Brumer H., Kelly R.M. Biochemical analysis of Thermotoga maritima GH36 α-galactosidase (TmGalA) confirms the mechanistic commonality of clan GH-D glycoside hydrolases. Biochemistry 2007, 46:3319-3330.
    • (2007) Biochemistry , vol.46 , pp. 3319-3330
    • Comfort, D.A.1    Bobrov, K.S.2    Ivanen, D.R.3    Shabalin, K.A.4    Harris, J.M.5    Kulminskaya, A.A.6    Brumer, H.7    Kelly, R.M.8
  • 37
    • 0028876332 scopus 로고
    • Characterization of the celB gene coding for β-Glucoside from the hyperthermophilic arachaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli
    • Voorhorst W.G., Eggen R.I., Leusink E.J., de Vos W.M. Characterization of the celB gene coding for β-Glucoside from the hyperthermophilic arachaeon Pyrococcus furiosus and its expression and site-directed mutation in Escherichia coli. J. Bacteriol. 1995, 177:7105-7111.
    • (1995) J. Bacteriol. , vol.177 , pp. 7105-7111
    • Voorhorst, W.G.1    Eggen, R.I.2    Leusink, E.J.3    de Vos, W.M.4
  • 38
    • 0035143560 scopus 로고    scopus 로고
    • Glucosidase CelB from Pyrococcus furiousus: production by Escherichia coli, Purification, and in vitro evolution
    • Lebbink J.H.G., Kaper T., Kengen S.W.M., van der Oost J., de Vos W.M. Glucosidase CelB from Pyrococcus furiousus: production by Escherichia coli, Purification, and in vitro evolution. Method Enzymol. 2001, 330:364-379.
    • (2001) Method Enzymol. , vol.330 , pp. 364-379
    • Lebbink, J.H.G.1    Kaper, T.2    Kengen, S.W.M.3    van der Oost, J.4    de Vos, W.M.5
  • 39
    • 0040776974 scopus 로고    scopus 로고
    • Comparative structural analysis and substrate specificity engineering of the hyperthermostable β-Glucosidase CelB from Pyrococcus furiosus
    • Kaper T., Lebbink J.H.G., Pouwels J., Kopp J., Schulz G.E., van der Oost J., de Vos W.M. Comparative structural analysis and substrate specificity engineering of the hyperthermostable β-Glucosidase CelB from Pyrococcus furiosus. Biochemistry 2000, 39:4963-4970.
    • (2000) Biochemistry , vol.39 , pp. 4963-4970
    • Kaper, T.1    Lebbink, J.H.G.2    Pouwels, J.3    Kopp, J.4    Schulz, G.E.5    van der Oost, J.6    de Vos, W.M.7
  • 40
    • 0032472347 scopus 로고    scopus 로고
    • Preparation and characterization of urease bound on crosslinked poly(vinyl alcohol)
    • Rejikumar S., Devi S. Preparation and characterization of urease bound on crosslinked poly(vinyl alcohol). J. Mol. Catal. B-Enzym. 1998, 4:61-66.
    • (1998) J. Mol. Catal. B-Enzym. , vol.4 , pp. 61-66
    • Rejikumar, S.1    Devi, S.2
  • 41
    • 0242594589 scopus 로고    scopus 로고
    • Immobilization of a thermostable α-amylase onto reactive membranes: kinetics characterization and application to continuous starch hydrolysis
    • Bayramoglu G., Yilmaz M., Arica M.Y. Immobilization of a thermostable α-amylase onto reactive membranes: kinetics characterization and application to continuous starch hydrolysis. Food Chem. 2004, 84:591-599.
    • (2004) Food Chem. , vol.84 , pp. 591-599
    • Bayramoglu, G.1    Yilmaz, M.2    Arica, M.Y.3
  • 43
    • 6344268958 scopus 로고    scopus 로고
    • Characterization of a thermostable recombinant β-galactosidase from Thermotoga maritima
    • Kim C.S., Ji E.S., Oh D.K. Characterization of a thermostable recombinant β-galactosidase from Thermotoga maritima. J. Appl. Microbiol. 2004, 97:1006-1014.
    • (2004) J. Appl. Microbiol. , vol.97 , pp. 1006-1014
    • Kim, C.S.1    Ji, E.S.2    Oh, D.K.3
  • 45
    • 0035810688 scopus 로고    scopus 로고
    • Improved oligosaccharide synthesis by protein engineering of β-glucosidase CelB from hyperthermophilic Pyrococcus furiosus
    • Hansson T., Kaper T., van der Oost J., de Vos W.M., Adlercreutz P. Improved oligosaccharide synthesis by protein engineering of β-glucosidase CelB from hyperthermophilic Pyrococcus furiosus. Biotechnol. Bioeng. 2001, 73:203-210.
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 203-210
    • Hansson, T.1    Kaper, T.2    van der Oost, J.3    de Vos, W.M.4    Adlercreutz, P.5
  • 46
    • 33748538751 scopus 로고    scopus 로고
    • Correlation of physiochemical characteristics with pervaporation performance of poly(vinyl alcohol) membranes
    • Hyder M.N., Huang R.Y.M., Chen P. Correlation of physiochemical characteristics with pervaporation performance of poly(vinyl alcohol) membranes. J. Membr. Sci. 2006, 283:281-290.
    • (2006) J. Membr. Sci. , vol.283 , pp. 281-290
    • Hyder, M.N.1    Huang, R.Y.M.2    Chen, P.3
  • 47
    • 69249219259 scopus 로고    scopus 로고
    • Crosslinked poly(vinyl alcohol) membranes
    • Bolto B., Tran T., Hoang M., Xie Z. Crosslinked poly(vinyl alcohol) membranes. Prog. Polym. Sci. 2009, 34:969-981.
    • (2009) Prog. Polym. Sci. , vol.34 , pp. 969-981
    • Bolto, B.1    Tran, T.2    Hoang, M.3    Xie, Z.4
  • 48
    • 8444230519 scopus 로고    scopus 로고
    • Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and applications to enzyme crosslinking
    • Migneault I., Dartiguenave C., Bertrand M., Waldron K.C. Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and applications to enzyme crosslinking. BioTechniques 2004, 37:790-802.
    • (2004) BioTechniques , vol.37 , pp. 790-802
    • Migneault, I.1    Dartiguenave, C.2    Bertrand, M.3    Waldron, K.C.4
  • 49
    • 84861128240 scopus 로고    scopus 로고
    • Effect of pH on protein distribution in electrospun PVA/BSA composite nanofibers
    • Tang C., Ozcam A.E., Stout B., Khan S.A. Effect of pH on protein distribution in electrospun PVA/BSA composite nanofibers. Biomacromolecules 2012, 13:1269-1278.
    • (2012) Biomacromolecules , vol.13 , pp. 1269-1278
    • Tang, C.1    Ozcam, A.E.2    Stout, B.3    Khan, S.A.4
  • 50
    • 80055010578 scopus 로고    scopus 로고
    • Operational stabilization of fungal α-rhamnosyl-β-glucosidase by immobilization on chitosan composites
    • Pinuel L., Mazzaferro L.S., Breccia J.D. Operational stabilization of fungal α-rhamnosyl-β-glucosidase by immobilization on chitosan composites. Process Biochem. 2011, 46:2330-2335.
    • (2011) Process Biochem. , vol.46 , pp. 2330-2335
    • Pinuel, L.1    Mazzaferro, L.S.2    Breccia, J.D.3
  • 53
    • 27944460277 scopus 로고    scopus 로고
    • Immobilization of xylan-degrading enzymes from Scytalidium thermophilum on Eudragit L-100
    • Gaur R., Lata R., Khare S.K. Immobilization of xylan-degrading enzymes from Scytalidium thermophilum on Eudragit L-100. World J. Microbiol. Biotechnol. 2005, 21:1123-1128.
    • (2005) World J. Microbiol. Biotechnol. , vol.21 , pp. 1123-1128
    • Gaur, R.1    Lata, R.2    Khare, S.K.3
  • 54
    • 82955162467 scopus 로고    scopus 로고
    • Characterization and further stabilization of a new anti-prelog specific alcohol dehydrogenase from Thermus thermophilus HC27 for asymmetric reduction of carbonyl compounds
    • Rocha-Martin J., Vega D., Bolivar J.M., Hidalgo A., Berenguer J., Guisan Lopez J.M., Gallego F. Characterization and further stabilization of a new anti-prelog specific alcohol dehydrogenase from Thermus thermophilus HC27 for asymmetric reduction of carbonyl compounds. Bioresour. Technol. 2012, 103:343-350.
    • (2012) Bioresour. Technol. , vol.103 , pp. 343-350
    • Rocha-Martin, J.1    Vega, D.2    Bolivar, J.M.3    Hidalgo, A.4    Berenguer, J.5    Guisan Lopez, J.M.6    Gallego, F.7
  • 55
    • 0037357583 scopus 로고    scopus 로고
    • Enzymatic process for d-Tagatose production by an immobilized thermostable l-Arabinose isomerase in a packed-bed bioreactor
    • Kim H., Ryu S., Kim P., Oh D. Enzymatic process for d-Tagatose production by an immobilized thermostable l-Arabinose isomerase in a packed-bed bioreactor. Biotechnol. Prog. 2003, 19:400-404.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 400-404
    • Kim, H.1    Ryu, S.2    Kim, P.3    Oh, D.4
  • 56
    • 79951645821 scopus 로고    scopus 로고
    • Ultra-stable phosphoglucose isomerase through immobilization of cellulose-binding module-tagged thermophilic enzyme on low-cost high-capacity cellulosic adsorbant
    • Myung S., Zhang X., Zhang Y.P. Ultra-stable phosphoglucose isomerase through immobilization of cellulose-binding module-tagged thermophilic enzyme on low-cost high-capacity cellulosic adsorbant. Biotechnol. Prog. 2011, 27:969-975.
    • (2011) Biotechnol. Prog. , vol.27 , pp. 969-975
    • Myung, S.1    Zhang, X.2    Zhang, Y.P.3
  • 57
    • 50649091654 scopus 로고    scopus 로고
    • Tagatose production with pH control in a stirred tank reactor containing immobilized l-Arabinose isomerase from Thermotoga neapolitana
    • Lim B., Kim H., Oh D. Tagatose production with pH control in a stirred tank reactor containing immobilized l-Arabinose isomerase from Thermotoga neapolitana. Appl. Biochem. Biotechnol. 2008, 149:245-253.
    • (2008) Appl. Biochem. Biotechnol. , vol.149 , pp. 245-253
    • Lim, B.1    Kim, H.2    Oh, D.3
  • 58
    • 33747353616 scopus 로고    scopus 로고
    • Immobilization and characterization of a thermostable β-xylosidase to generate a reusable biocatalyst
    • Morana A., Mangione A., Maurelli L., Fiume I., Paris O., Cannio R., Rossi M. Immobilization and characterization of a thermostable β-xylosidase to generate a reusable biocatalyst. Enzym. Microb. Technol. 2006, 39:1205-1213.
    • (2006) Enzym. Microb. Technol. , vol.39 , pp. 1205-1213
    • Morana, A.1    Mangione, A.2    Maurelli, L.3    Fiume, I.4    Paris, O.5    Cannio, R.6    Rossi, M.7
  • 59
    • 1642323577 scopus 로고    scopus 로고
    • Glucose production from maltodextrins employing a thermophilic immobilized cell biocatalyst in a packed-bed reactor
    • Schiraldi C., Martino A., Costabile T., Generoso M., Marotta M., De Rosa M. Glucose production from maltodextrins employing a thermophilic immobilized cell biocatalyst in a packed-bed reactor. Enzym. Microb. Technol. 2004, 34:415-421.
    • (2004) Enzym. Microb. Technol. , vol.34 , pp. 415-421
    • Schiraldi, C.1    Martino, A.2    Costabile, T.3    Generoso, M.4    Marotta, M.5    De Rosa, M.6
  • 60
    • 70350223483 scopus 로고    scopus 로고
    • Improved reactivation of immobilized-stabilized lipase from Thermomyces lanuginosus by its coating with highly hydrophilic polymers
    • Rodrigues R.C., Bolivar J.M., Volpato G., Filice M., Godoy C., Fernandez-Lafuente R., Guisan J.M. Improved reactivation of immobilized-stabilized lipase from Thermomyces lanuginosus by its coating with highly hydrophilic polymers. J. Biotechnol. 2009, 144:113-119.
    • (2009) J. Biotechnol. , vol.144 , pp. 113-119
    • Rodrigues, R.C.1    Bolivar, J.M.2    Volpato, G.3    Filice, M.4    Godoy, C.5    Fernandez-Lafuente, R.6    Guisan, J.M.7
  • 61
    • 77954291511 scopus 로고    scopus 로고
    • Concentration gradients for substrate and acidic product in immobilized cephalosporin C amidase and their dependencies on carrier characteristics and reaction parameters
    • Boniello C., Mayr T., Kilmant I., Koenig B., Riethorst W., Nidetzky B. Concentration gradients for substrate and acidic product in immobilized cephalosporin C amidase and their dependencies on carrier characteristics and reaction parameters. Biotechnol. Bioeng. 2010, 106:528-540.
    • (2010) Biotechnol. Bioeng. , vol.106 , pp. 528-540
    • Boniello, C.1    Mayr, T.2    Kilmant, I.3    Koenig, B.4    Riethorst, W.5    Nidetzky, B.6
  • 63
    • 47049116004 scopus 로고    scopus 로고
    • Study of charge storage in the nanofibrous poly(ethylene terephthalate) electrets prepared by electrospinning or by corona discharge method
    • Ignatova M., Yovacheva T., Viraneva A., Mekishev G., Manolova N., Rashkov I. Study of charge storage in the nanofibrous poly(ethylene terephthalate) electrets prepared by electrospinning or by corona discharge method. Eur. Polym. J. 2008, 44:1962-1967.
    • (2008) Eur. Polym. J. , vol.44 , pp. 1962-1967
    • Ignatova, M.1    Yovacheva, T.2    Viraneva, A.3    Mekishev, G.4    Manolova, N.5    Rashkov, I.6
  • 64
    • 10044291720 scopus 로고    scopus 로고
    • Surface engineering of electrospun polyethylene terephthalate (PET) nanofibers towards development of a new material for blood vessel engineering
    • Ma Z., Kotaki M., Yong T., He W., Ramakrishna S. Surface engineering of electrospun polyethylene terephthalate (PET) nanofibers towards development of a new material for blood vessel engineering. Biomaterials 2005, 26:2527-2536.
    • (2005) Biomaterials , vol.26 , pp. 2527-2536
    • Ma, Z.1    Kotaki, M.2    Yong, T.3    He, W.4    Ramakrishna, S.5
  • 65
    • 33947301782 scopus 로고    scopus 로고
    • Immobilization of lipase with a special microstrucutre in composite hydrophilic CA/hydrophobic PTFE membrane for chiral separation of racemic ibuprofen
    • Wang Y., Hu Y., Xu J., Luo G., Dai Y. Immobilization of lipase with a special microstrucutre in composite hydrophilic CA/hydrophobic PTFE membrane for chiral separation of racemic ibuprofen. J. Membr. Sci. 2007, 293:133-141.
    • (2007) J. Membr. Sci. , vol.293 , pp. 133-141
    • Wang, Y.1    Hu, Y.2    Xu, J.3    Luo, G.4    Dai, Y.5
  • 66
    • 0027910084 scopus 로고
    • Immobilization of glucose oxidase in thin polypyrrole films: influence of polymerization conditions and film thickness on the activity and stability of the immobilized enzyme
    • Almeida N.F., Beckman E.J., Ataai M.M. Immobilization of glucose oxidase in thin polypyrrole films: influence of polymerization conditions and film thickness on the activity and stability of the immobilized enzyme. Biotechnol. Bioeng. 1993, 42:1037-1045.
    • (1993) Biotechnol. Bioeng. , vol.42 , pp. 1037-1045
    • Almeida, N.F.1    Beckman, E.J.2    Ataai, M.M.3
  • 67
    • 0000514066 scopus 로고
    • Importance of mass transfer and intraparticle diffusion in polymer-supported phase-transfer catalysis
    • Tomoi M., Ford W.T. Importance of mass transfer and intraparticle diffusion in polymer-supported phase-transfer catalysis. J. Am. Chem. Soc. 1980, 102:7140-7141.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 7140-7141
    • Tomoi, M.1    Ford, W.T.2
  • 68
    • 34447511000 scopus 로고    scopus 로고
    • Catalytic hydrolysis of p-nitrophenos acetate by electrospun polyacrylamidoxime nanofibers
    • Chen L., Bromberg L., Hatton T.A., Rutledge G.C. Catalytic hydrolysis of p-nitrophenos acetate by electrospun polyacrylamidoxime nanofibers. Polymer 2007, 48:4675-4682.
    • (2007) Polymer , vol.48 , pp. 4675-4682
    • Chen, L.1    Bromberg, L.2    Hatton, T.A.3    Rutledge, G.C.4
  • 69
    • 70449628878 scopus 로고    scopus 로고
    • A novel catalyst based on electrospun silver doped silica fibers with ribbon morphology
    • Kang H., Zhu Y., Yang X., Jing Y., Lengalova A., Li C. A novel catalyst based on electrospun silver doped silica fibers with ribbon morphology. J. Colloid Interface Sci 2010, 341:303-310.
    • (2010) J. Colloid Interface Sci , vol.341 , pp. 303-310
    • Kang, H.1    Zhu, Y.2    Yang, X.3    Jing, Y.4    Lengalova, A.5    Li, C.6
  • 70
    • 72449183180 scopus 로고
    • Interpretation of measurements in experimental catalysis
    • Weisz P.B., Prater C.D. Interpretation of measurements in experimental catalysis. Adv. Catal. 1954, 6:143-196.
    • (1954) Adv. Catal. , vol.6 , pp. 143-196
    • Weisz, P.B.1    Prater, C.D.2
  • 71
    • 0035303164 scopus 로고    scopus 로고
    • A kinetic model for enzyme-catalyzed self-epoxidation of oleic acid
    • Yadav G.D., Devi K.M. A kinetic model for enzyme-catalyzed self-epoxidation of oleic acid. J. Am. Oil Chem. Soc. 2001, 78:347-351.
    • (2001) J. Am. Oil Chem. Soc. , vol.78 , pp. 347-351
    • Yadav, G.D.1    Devi, K.M.2
  • 72
    • 0030394690 scopus 로고    scopus 로고
    • Solute diffusion in poly(vinyl alcohol)/poly(acrylic acid) interpenetrating netwoks
    • Peppas N.A., Wright S.L. Solute diffusion in poly(vinyl alcohol)/poly(acrylic acid) interpenetrating netwoks. Macromolecules 1996, 29:8798-8804.
    • (1996) Macromolecules , vol.29 , pp. 8798-8804
    • Peppas, N.A.1    Wright, S.L.2
  • 73
    • 0030615434 scopus 로고    scopus 로고
    • Analysis of solute diffusion in poly(vinyl alcohol) hydrogel membrane
    • Matsuyama H., Teramoto M., Urano H. Analysis of solute diffusion in poly(vinyl alcohol) hydrogel membrane. J. Membr. Sci. 1997, 126:151-160.
    • (1997) J. Membr. Sci. , vol.126 , pp. 151-160
    • Matsuyama, H.1    Teramoto, M.2    Urano, H.3
  • 74
    • 0022077568 scopus 로고
    • The role of cross-links, entanglements, and relaxations of the macromolecular carrier in the diffusional release of biologically active materials
    • Peppas N.A., Moynihan H.J. The role of cross-links, entanglements, and relaxations of the macromolecular carrier in the diffusional release of biologically active materials. J. Appl. Polym. Sci. 1985, 30:2589-2606.
    • (1985) J. Appl. Polym. Sci. , vol.30 , pp. 2589-2606
    • Peppas, N.A.1    Moynihan, H.J.2
  • 75
    • 0027465230 scopus 로고
    • Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen S.W.M., Luesink E.J., Stams A.J.M., Zehnder A.J.B. Purification and characterization of an extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem. 1993, 213:305-312.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 305-312
    • Kengen, S.W.M.1    Luesink, E.J.2    Stams, A.J.M.3    Zehnder, A.J.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.