메뉴 건너뛰기




Volumn 12, Issue 102, 2015, Pages

Nanobiocatalyst advancements and bioprocessing applications

Author keywords

Bioprocess; Enzyme; Immobilization; Nanobiocatalysts; Nanocarrier

Indexed keywords

CATALYST ACTIVITY; CROSSLINKING; ENZYME ACTIVITY; ENZYMES; NANOMAGNETICS; NANOPARTICLES; RADIOACTIVE WASTE VITRIFICATION; SYNTHESIS (CHEMICAL);

EID: 84964314887     PISSN: 17425689     EISSN: 17425662     Source Type: Journal    
DOI: 10.1098/rsif.2014.0891     Document Type: Article
Times cited : (209)

References (152)
  • 1
    • 79956080802 scopus 로고    scopus 로고
    • Immobilization of Aspergillus oryzae beta galactosidase on zinc oxide nanoparticles via simple adsorption mechanism
    • Husain Q, Ansari SA, Alam F, Azam A. 2011 Immobilization of Aspergillus oryzae beta galactosidase on zinc oxide nanoparticles via simple adsorption mechanism. Int. J. Biol. Macromol. 49, 37-43. (doi:10.1016/j.ijbiomac.2011.03.011)
    • (2011) Int. J. Biol. Macromol. , vol.49 , pp. 37-43
    • Husain, Q.1    Ansari, S.A.2    Alam, F.3    Azam, A.4
  • 2
    • 84880150502 scopus 로고    scopus 로고
    • Enzyme immobilization an overview on techniques and support
    • Datta S, Christena LR, Rajaram YRS. 2012 Enzyme immobilization an overview on techniques and support. Biotechnol. Adv. 3, 1-9. (doi:10.1007/s13205-012-0071-7)
    • (2012) Biotechnol. Adv. , vol.3 , pp. 1-9
    • Datta, S.1    Christena, L.R.2    Rajaram, Y.R.S.3
  • 5
    • 51249110348 scopus 로고    scopus 로고
    • Bioinspired enzyme encapsulation for biocatalysis
    • Betancor L, Luckarift HR. 2008 Bioinspired enzyme encapsulation for biocatalysis. Trends Biotechnol. 26, 566-572. (doi:10.1016/j.tibtech.2008.06.009)
    • (2008) Trends Biotechnol. , vol.26 , pp. 566-572
    • Betancor, L.1    Luckarift, H.R.2
  • 6
    • 84875537701 scopus 로고    scopus 로고
    • Immobilization of commercial hydrolytic enzymes on poly (acrylonitrile) nanofibers for anti-biofilm activity
    • Plessis DM, Botes M, Dicks LMT, Cloete TE. 2012 Immobilization of commercial hydrolytic enzymes on poly (acrylonitrile) nanofibers for anti-biofilm activity. J. Chem. Technol. Biotechnol. 88, 585-593. (doi:10.1002/jctb.3866)
    • (2012) J. Chem. Technol. Biotechnol. , vol.88 , pp. 585-593
    • Plessis, D.M.1    Botes, M.2    Dicks, L.M.T.3    Cloete, T.E.4
  • 7
    • 80052643416 scopus 로고    scopus 로고
    • Reversible His-tagged enzyme immobilization on functionalized carbon nanotubes as nanoscale biocatalyst
    • Wang L, Jiang R. 2011 Reversible His-tagged enzyme immobilization on functionalized carbon nanotubes as nanoscale biocatalyst. Methods Mol. Biol. 743, 95-106. (doi:10.1007/978-1-61779-132-1-8)
    • (2011) Methods Mol. Biol. , vol.743 , pp. 95-106
    • Wang, L.1    Jiang, R.2
  • 8
    • 79952197637 scopus 로고    scopus 로고
    • Enzyme nanoparticle fabrication: Magnetic nanoparticle synthesis and enzyme immobilization
    • (ed. SD Minteer), New York, NY: Hanna Publisher
    • Johnson PA, Park HJ, Driscoll AJ. 2011 Enzyme nanoparticle fabrication: magnetic nanoparticle synthesis and enzyme immobilization. In Enzyme stabilization and immobilization methods in molecular biology (ed. SD Minteer), pp. 183-191. New York, NY: Hanna Publisher.
    • (2011) Enzyme Stabilization and Immobilization Methods in Molecular Biology , pp. 183-191
    • Johnson, P.A.1    Park, H.J.2    Driscoll, A.J.3
  • 9
    • 84862817808 scopus 로고    scopus 로고
    • Immobilization of Burkholderia sp. Lipase on a ferric silica nanocomposite for biodiesel production
    • Tran DT, Chen CL, Chang JS. 2012 Immobilization of Burkholderia sp. lipase on a ferric silica nanocomposite for biodiesel production. J. Biotechnol. 158, 112-119. (doi:10.1016/j.jbiotec.2012.01.018)
    • (2012) J. Biotechnol. , vol.158 , pp. 112-119
    • Tran, D.T.1    Chen, C.L.2    Chang, J.S.3
  • 10
    • 84862798508 scopus 로고    scopus 로고
    • Preparation and characterization of graphite nanosheets decorated with Fe3O4 nanoparticles used in the immobilization of glucoamylase
    • Ma Y-X, Li Y-F, Zhao G-H, Yang L-Q, Wang J-Z, Shan X, Yan X. 2012 Preparation and characterization of graphite nanosheets decorated with Fe3O4 nanoparticles used in the immobilization of glucoamylase. Carbon 50, 2976-2986. (doi:10.1016/j.carbon.2012.02.080)
    • (2012) Carbon , vol.50 , pp. 2976-2986
    • Ma, Y.-X.1    Li, Y.-F.2    Zhao, G.-H.3    Yang, L.-Q.4    Wang, J.-Z.5    Shan, X.6    Yan, X.7
  • 11
    • 43049123089 scopus 로고    scopus 로고
    • Covalent immobilization of lipase from Candida rugosa onto poly (acrylonitrile-co-2-hydroxyethyl methacrylate) electrospun fibrous membranes for potential bioreactor application
    • Huang X, Yu A, ZK X. 2008 Covalent immobilization of lipase from Candida rugosa onto poly (acrylonitrile-co-2-hydroxyethyl methacrylate) electrospun fibrous membranes for potential bioreactor application. Bioresour. Technol. 99, 5459-5465. (doi:10.1016/j.biortech.2007.11.009)
    • (2008) Bioresour. Technol. , vol.99 , pp. 5459-5465
    • Huang, X.1    Yu, A.2    Z.K., X.3
  • 12
    • 70350491449 scopus 로고    scopus 로고
    • Surface functionalization of silica-coated magnetic nanoparticles for covalent attachment of cholesterol oxidase
    • Sulek F, Drofenik M, Habulin M, Knez Z. 2010 Surface functionalization of silica-coated magnetic nanoparticles for covalent attachment of cholesterol oxidase. J. Magn. Magn. Mater. 322, 179-185. (doi:10.1016/j.jmmm.2009.07.075)
    • (2010) J. Magn. Magn. Mater. , vol.322 , pp. 179-185
    • Sulek, F.1    Drofenik, M.2    Habulin, M.3    Knez, Z.4
  • 14
    • 84870885611 scopus 로고    scopus 로고
    • Iron oxide filled magnetic carbon nanotube-enzyme conjugates for recycling of amyloglucosidase: Toward useful applications in biofuel production process
    • Goh WJ, Makam VS, Hu J, Kang L, Zheng M, Yoong SL, Udalagama CN, Pastorin G. 2012 Iron oxide filled magnetic carbon nanotube-enzyme conjugates for recycling of amyloglucosidase: toward useful applications in biofuel production process. Langmuir 28, 16 864-16 873. (doi:10.1021/la303046m)
    • (2012) Langmuir , vol.28 , pp. 16864-16873
    • Goh, W.J.1    Makam, V.S.2    Hu, J.3    Kang, L.4    Zheng, M.5    Yoong, S.L.6    Udalagama, C.N.7    Pastorin, G.8
  • 15
    • 77955662669 scopus 로고    scopus 로고
    • Magnetic mesoporous silica nanoparticles: Fabrication and their laccase immobilization performance
    • Wang F, Guo C, Yang LR, Liu CZ. 2010 Magnetic mesoporous silica nanoparticles: fabrication and their laccase immobilization performance. Bioresour. Technol. 101, 8931-8935. (doi:10.1016/j.biortech.2010.06.115)
    • (2010) Bioresour. Technol. , vol.101 , pp. 8931-8935
    • Wang, F.1    Guo, C.2    Yang, L.R.3    Liu, C.Z.4
  • 16
    • 84857501798 scopus 로고    scopus 로고
    • Potential applications of enzymes immobilized on/in nano materials: A review
    • Ansari SA, Husain Q. 2012 Potential applications of enzymes immobilized on/in nano materials: a review. Biotechnol. Adv. 30, 512-523. (doi:10.1016/j.biotechadv.2011.09.005)
    • (2012) Biotechnol. Adv. , vol.30 , pp. 512-523
    • Ansari, S.A.1    Husain, Q.2
  • 17
    • 84866151852 scopus 로고    scopus 로고
    • Food related applications of magnetic iron oxide nanoparticles: Enzyme immobilization, protein purification, and food analysis
    • Cao M, Li Z, Wang J, Ge W, Yue T, Li R, Colvin VL, Yu WW. 2012 Food related applications of magnetic iron oxide nanoparticles: enzyme immobilization, protein purification, and food analysis. Trends Food Sci. Technol. 27, 47-56. (doi:10.1016/j.tifs.2012.04.003)
    • (2012) Trends Food Sci. Technol. , vol.27 , pp. 47-56
    • Cao, M.1    Li, Z.2    Wang, J.3    Ge, W.4    Yue, T.5    Li, R.6    Colvin, V.L.7    Yu, W.W.8
  • 18
    • 84864914769 scopus 로고    scopus 로고
    • Harnessing the power of enzymes for environmental stewardship
    • Demarche P, Junghanns C, Nair RR, Agathos SN. 2012 Harnessing the power of enzymes for environmental stewardship. Biotechnol. Adv. 30, 933-953. (doi:10.1016/j.biotechadv.2011.05.013)
    • (2012) Biotechnol. Adv. , vol.30 , pp. 933-953
    • Demarche, P.1    Junghanns, C.2    Nair, R.R.3    Agathos, S.N.4
  • 19
    • 84872334138 scopus 로고    scopus 로고
    • Nanobiotechnology as a novel paradigm for enzyme immobilisation and stabilisation with potential applications in biodiesel production
    • Verma ML, Barrow CJ, Puri M. 2012 Nanobiotechnology as a novel paradigm for enzyme immobilisation and stabilisation with potential applications in biodiesel production. Appl. Microbiol. Biotechnol. 97, 23-39. (doi:10.1007/s00253-012-4535-9)
    • (2012) Appl. Microbiol. Biotechnol. , vol.97 , pp. 23-39
    • Verma, M.L.1    Barrow, C.J.2    Puri, M.3
  • 20
    • 84860176049 scopus 로고    scopus 로고
    • Enzymatic pretreatment of lignocellulosic wastes to improve biogas production
    • Zieminski K, Romanowska I, Kowalska M. 2012 Enzymatic pretreatment of lignocellulosic wastes to improve biogas production. Waste Manage. 32, 1131-1137. (doi:10.1016/j.wasman.2012.01.016)
    • (2012) Waste Manage. , vol.32 , pp. 1131-1137
    • Zieminski, K.1    Romanowska, I.2    Kowalska, M.3
  • 21
    • 80055048088 scopus 로고    scopus 로고
    • 4 nanoparticles for catalyzing transesterification reactions
    • 4 nanoparticles for catalyzing transesterification reactions. New J. Chem. 35, 2551. (doi:10.1039/c1nj20277d)
    • (2011) New J. Chem. , vol.35 , pp. 2551
    • Solanki, K.1    Gupta, M.N.2
  • 22
    • 84865186653 scopus 로고    scopus 로고
    • Recovery of high added-value components from food wastes: Conventional, emerging technologies and commercialized applications
    • Galanakis CM. 2012 Recovery of high added-value components from food wastes: conventional, emerging technologies and commercialized applications. Trends Food Sci. Technol. 26, 68-87. (doi:10.1016/j.tifs.2012.03.003)
    • (2012) Trends Food Sci. Technol. , vol.26 , pp. 68-87
    • Galanakis, C.M.1
  • 25
    • 68549096122 scopus 로고    scopus 로고
    • Electrospun microfibrous poly(styrene-alt-maleic anhydride)/ poly(styrene-co-maleic anhydride) mats tailored for enzymatic remediation of waters polluted by endocrine disruptors
    • Ignatova M, Stoilova O, Manolova N, Mita DG, Diano N, Nicolucci C, Rashkov I. 2009 Electrospun microfibrous poly(styrene-alt-maleic anhydride)/ poly(styrene-co-maleic anhydride) mats tailored for enzymatic remediation of waters polluted by endocrine disruptors. Eur. Polym. J. 45, 2494-2504. (doi:10.1016/j.eurpolymj.2009.06.010)
    • (2009) Eur. Polym. J. , vol.45 , pp. 2494-2504
    • Ignatova, M.1    Stoilova, O.2    Manolova, N.3    Mita, D.G.4    Diano, N.5    Nicolucci, C.6    Rashkov, I.7
  • 26
    • 84855428560 scopus 로고    scopus 로고
    • Electrospun polyacrylonitrileglycopolymer nanofibrous membranes for enzyme immobilization
    • Li Y, Quan J, White CB, Williams GR, Wu J-X, Zhu L-M. 2012 Electrospun polyacrylonitrileglycopolymer nanofibrous membranes for enzyme immobilization. J. Mol. Catal. B Enzymatic 76, 15-22. (doi:10.1016/j.molcatb.2011.12.003)
    • (2012) J. Mol. Catal. B Enzymatic , vol.76 , pp. 15-22
    • Li, Y.1    Quan, J.2    White, C.B.3    Williams, G.R.4    Wu, J.-X.5    Zhu, L.-M.6
  • 27
    • 84871414583 scopus 로고    scopus 로고
    • Immobilization of lysozyme-CLEA onto electrospun chitosan nanofiber for effective antibacterial applications
    • Park J-M, Kim M, Park H-S, Jang A, Min J, Kim Y-H. 2013 Immobilization of lysozyme-CLEA onto electrospun chitosan nanofiber for effective antibacterial applications. Int. J. Biol. Macromol. 54, 37-43. (doi:10.1016/j.ijbiomac.2012.11.025)
    • (2013) Int. J. Biol. Macromol. , vol.54 , pp. 37-43
    • Park, J.-M.1    Kim, M.2    Park, H.-S.3    Jang, A.4    Min, J.5    Kim, Y.-H.6
  • 28
    • 84868473398 scopus 로고    scopus 로고
    • Preparation and characterization of electro-spun nanofiber membranes and their possible applications in water treatment
    • Feng KCK, Matsuura T, Tabe S, Ismail AF. 2013 Preparation and characterization of electro-spun nanofiber membranes and their possible applications in water treatment. Sep. Purif. Technol. 102, 118-135. (doi:10.1016/j.seppur.2012.09.037)
    • (2013) Sep. Purif. Technol. , vol.102 , pp. 118-135
    • Feng, K.C.K.1    Matsuura, T.2    Tabe, S.3    Ismail, A.F.4
  • 29
    • 84887117043 scopus 로고    scopus 로고
    • Developing functionalized dendrimer-like silica nanoparticles with hierarchical pores as advanced delivery nanocarriers
    • Du X, Shi B, Liang J, Bi J, Dai S, Qiao SZ. 2013 Developing functionalized dendrimer-like silica nanoparticles with hierarchical pores as advanced delivery nanocarriers. Adv. Mater. 25, 5981-5985. (doi:10.1002/adma.201302189)
    • (2013) Adv. Mater. , vol.25 , pp. 5981-5985
    • Du, X.1    Shi, B.2    Liang, J.3    Bi, J.4    Dai, S.5    Qiao, S.Z.6
  • 30
    • 27844571788 scopus 로고    scopus 로고
    • Simple synthesis of hierarchically ordered mesocellular mesoporous silica materials hosting crosslinked enzyme aggregates
    • Lee J et al. 2005 Simple synthesis of hierarchically ordered mesocellular mesoporous silica materials hosting crosslinked enzyme aggregates. Small 1, 744-753. (doi:10.1002/smll.200500035)
    • (2005) Small , vol.1 , pp. 744-753
    • Lee, J.1
  • 31
    • 84884616336 scopus 로고    scopus 로고
    • Enzyme confined in silica-based nanocages for biocatalysis in a Pickering emulsion
    • Liu J, Lan G, Peng J, Li Y, Li C, Yang Q. 2013 Enzyme confined in silica-based nanocages for biocatalysis in a Pickering emulsion. Chem. Commun. 49, 9558. (doi:10.1039/c3cc45476b)
    • (2013) Chem. Commun. , vol.49 , pp. 9558
    • Liu, J.1    Lan, G.2    Peng, J.3    Li, Y.4    Li, C.5    Yang, Q.6
  • 32
    • 84863719219 scopus 로고    scopus 로고
    • Protein-inorganic hybrid nanoflowers
    • Ge J, Lei J, Zare RN. 2012 Protein-inorganic hybrid nanoflowers. Nat. Nanotechnol. 7, 428-432. (doi:10.1038/nnano.2012.80)
    • (2012) Nat. Nanotechnol. , vol.7 , pp. 428-432
    • Ge, J.1    Lei, J.2    Zare, R.N.3
  • 33
    • 68049146022 scopus 로고    scopus 로고
    • Spectro-electrochemical studies of acetylcholinesterase in carbon nanofiber-bioinspired silica nanocomposites for biosensor development
    • Hatzimarinaki M, Vamvakaki V, Chaniotakis N. 2009 Spectro-electrochemical studies of acetylcholinesterase in carbon nanofiber-bioinspired silica nanocomposites for biosensor development. J. Mater. Chem. 19, 428-433. (doi:10.1039/b811350e)
    • (2009) J. Mater. Chem. , vol.19 , pp. 428-433
    • Hatzimarinaki, M.1    Vamvakaki, V.2    Chaniotakis, N.3
  • 34
    • 84879374506 scopus 로고    scopus 로고
    • Colloidal silica nanoparticle-assisted structural control of cellulose nanofiber paper separators for lithium-ion batteries
    • Kim JH, Kim JH, Choi ES, Yu HK, Kim JH, Wu Q, Chun SJ, Lee SY, Lee SY. 2013 Colloidal silica nanoparticle-assisted structural control of cellulose nanofiber paper separators for lithium-ion batteries. J. Power Sources 242, 533-540. (doi:10.1016/j.jpowsour.2013.05.142)
    • (2013) J. Power Sources , vol.242 , pp. 533-540
    • Kim, J.H.1    Kim, J.H.2    Choi, E.S.3    Yu, H.K.4    Kim, J.H.5    Wu, Q.6    Chun, S.J.7    Lee, S.Y.8    Lee, S.Y.9
  • 35
    • 84893441516 scopus 로고    scopus 로고
    • Nanoparticle-on-nanofiber hybrid membrane separators for lithium-ion batteries via combining electrospraying and electrospinning techniques
    • Yanilmaz M, Lu Y, Dirican M, Fu K, Zhang X. 2014 Nanoparticle-on-nanofiber hybrid membrane separators for lithium-ion batteries via combining electrospraying and electrospinning techniques. J. Membr. Sci. 456, 57-65. (doi:10.1016/j.memsci.2014.01.022)
    • (2014) J. Membr. Sci. , vol.456 , pp. 57-65
    • Yanilmaz, M.1    Lu, Y.2    Dirican, M.3    Fu, K.4    Zhang, X.5
  • 36
    • 79954578667 scopus 로고    scopus 로고
    • Shape reformable polymeric nanofibers entrapped with QDs as a scaffold for enzyme stabilization
    • Hwang ET, Tatavarty R, Lee H, Kimb J, Gu MB. 2011 Shape reformable polymeric nanofibers entrapped with QDs as a scaffold for enzyme stabilization. J. Mater. Chem. 21, 5215-5218. (doi:10.1039/ c0jm02969f)
    • (2011) J. Mater. Chem. , vol.21 , pp. 5215-5218
    • Hwang, E.T.1    Tatavarty, R.2    Lee, H.3    Kimb, J.4    Gu, M.B.5
  • 37
    • 0036501464 scopus 로고    scopus 로고
    • Surface modification of carbon nanofibers
    • Ros T, van Dillen A, Geus J, Koningsberger D. 2002 Surface modification of carbon nanofibers. Chem. Eur. J 8, 1151-1162. (doi:10.1002/1521-3765(20020301)8:5, 1151::AID-CHEM1151 . 3.0.CO;2-#)
    • (2002) Chem. Eur. J , vol.8 , pp. 1151-1162
    • Ros, T.1    Van Dillen, A.2    Geus, J.3    Koningsberger, D.4
  • 38
    • 79952284546 scopus 로고    scopus 로고
    • Magnetic nanocomposites with mesoporous structures: Synthesis and applications
    • Liu J, Qiao SZ, Hu QH, Lu GQ. 2011 Magnetic nanocomposites with mesoporous structures: Synthesis and applications. Small 7, 425-443. (doi:10.1002/smll.201001402)
    • (2011) Small , vol.7 , pp. 425-443
    • Liu, J.1    Qiao, S.Z.2    Hu, Q.H.3    Lu, G.Q.4
  • 39
    • 77957587737 scopus 로고    scopus 로고
    • Stability and catalytic kinetics of horseradish peroxidase confined in nanoporous SBA-15
    • Ikemoto H, Chi Q, Ulstrup J. 2010 Stability and catalytic kinetics of horseradish peroxidase confined in nanoporous SBA-15. J. Phys. Chem. C 114, 16 174-16 180. (doi:10.1021/jp103137e)
    • (2010) J. Phys. Chem. C , vol.114 , pp. 16174-16180
    • Ikemoto, H.1    Chi, Q.2    Ulstrup, J.3
  • 40
    • 79952936113 scopus 로고    scopus 로고
    • Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores
    • Sang LC, Coppens MO. 2011 Effects of surface curvature and surface chemistry on the structure and activity of proteins adsorbed in nanopores. Phys. Chem. Chem. Phys. 13, 6689. (doi:10.1039/ c0cp02273j)
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 6689
    • Sang, L.C.1    Coppens, M.O.2
  • 41
    • 76749156605 scopus 로고    scopus 로고
    • Multifunctional mesoporous silica nanoparticles as labels for the preparation of ultrasensitive electrochemical immunosensors
    • Yang M, Li H, Javadi A, Gong S. 2010 Multifunctional mesoporous silica nanoparticles as labels for the preparation of ultrasensitive electrochemical immunosensors. Biomaterials 31, 3281-3286. (doi:10.1016/j.biomaterials.2010.01.033)
    • (2010) Biomaterials , vol.31 , pp. 3281-3286
    • Yang, M.1    Li, H.2    Javadi, A.3    Gong, S.4
  • 42
    • 73749088453 scopus 로고    scopus 로고
    • Stimuli-responsive nanoparticles, nanogels and capsules for integrated multifunctional intelligent systems
    • Motornov M, Roiter Y, Tokarev I, Minko S. 2010 Stimuli-responsive nanoparticles, nanogels and capsules for integrated multifunctional intelligent systems. Prog. Polym. Sci. 35, 174-211. (doi:10.1016/j.progpolymsci.2009.10.004)
    • (2010) Prog. Polym. Sci. , vol.35 , pp. 174-211
    • Motornov, M.1    Roiter, Y.2    Tokarev, I.3    Minko, S.4
  • 43
    • 78651364752 scopus 로고    scopus 로고
    • Photo-tunable protein release from biodegradable nanoparticles composed of cinnamic acid derivatives
    • Shi D, Matsusaki M, Akashi M. 2011 Photo-tunable protein release from biodegradable nanoparticles composed of cinnamic acid derivatives. J. Control. Release 149, 182-189. (doi:10.1016/j.jconrel.2010.08.009)
    • (2011) J. Control. Release , vol.149 , pp. 182-189
    • Shi, D.1    Matsusaki, M.2    Akashi, M.3
  • 44
    • 84877064712 scopus 로고    scopus 로고
    • Photo-crosslinked hyaluronic acid nanoparticles with improved stability for in vivo tumor-targeted drug delivery
    • Yoon HY, Koo H, Choi KY, Kwon IC, Choi K, Park JH, Kim K. 2013 Photo-crosslinked hyaluronic acid nanoparticles with improved stability for in vivo tumor-targeted drug delivery. Biomaterials 34, 5273-5280. (doi:10.1016/j.biomaterials.2013.03.050)
    • (2013) Biomaterials , vol.34 , pp. 5273-5280
    • Yoon, H.Y.1    Koo, H.2    Choi, K.Y.3    Kwon, I.C.4    Choi, K.5    Park, J.H.6    Kim, K.7
  • 45
    • 84871881666 scopus 로고    scopus 로고
    • Temperature- and pH-responsive nanoparticles of biocompatible polyurethanes for doxorubicin delivery
    • Wang A, Gao H, Sun Y, Sun Y, Yang Y-W, Wu G, Wang Y, Fan Y, Ma J. 2013 Temperature- and pH-responsive nanoparticles of biocompatible polyurethanes for doxorubicin delivery. Int. J. Pharm. 441, 30-39. (doi:10.1016/j.ijpharm.2012.12.021)
    • (2013) Int. J. Pharm. , vol.441 , pp. 30-39
    • Wang, A.1    Gao, H.2    Sun, Y.3    Sun, Y.4    Yang, Y.-W.5    Wu, G.6    Wang, Y.7    Fan, Y.8    Ma, J.9
  • 46
    • 78349312099 scopus 로고    scopus 로고
    • Biodegradable and thermosensitive chitosan-g-poly(N-vinylcaprolactam) nanoparticles as a 5-fluorouracil carrier
    • Rejinolda NS, Chennazhia KP, Naira SV, Tamurab H, Jayakumar R. 2011 Biodegradable and thermosensitive chitosan-g-poly(N-vinylcaprolactam) nanoparticles as a 5-fluorouracil carrier. Carbohydr. Polym. 83, 776-786. (doi:10.1016/j.carbpol.2010.08.052)
    • (2011) Carbohydr. Polym. , vol.83 , pp. 776-786
    • Rejinolda, N.S.1    Chennazhia, K.P.2    Naira, S.V.3    Tamurab, H.4    Jayakumar, R.5
  • 47
    • 84879497482 scopus 로고    scopus 로고
    • pH-responsive drug delivery of chitosan nanoparticles as tamoxifen carriers for effective anti-tumor activity in breast cancer cells
    • Viveka R, Babua VN, Thangama R, Subramanianc KS, Kannan S. 2013 pH-responsive drug delivery of chitosan nanoparticles as tamoxifen carriers for effective anti-tumor activity in breast cancer cells. Colloids Sur. B Biointerfaces 111, 117-123. (doi:10.1016/j.colsurfb.2013.05.018)
    • (2013) Colloids Sur. B Biointerfaces , vol.111 , pp. 117-123
    • Viveka, R.1    Babua, V.N.2    Thangama, R.3    Subramanianc, K.S.4    Kannan, S.5
  • 48
    • 80051544002 scopus 로고    scopus 로고
    • A pH-responsive mesoporous silica nanoparticles-based multi-drug delivery system for overcoming multi-drug resistance
    • Hea Q, Gao Y, Zhang L, Zhang Z, Gao F, Ji X, Li Y, Shi J. 2011 A pH-responsive mesoporous silica nanoparticles-based multi-drug delivery system for overcoming multi-drug resistance. Biomaterials 32, 7711-7720. (doi:10.1016/j.biomaterials.2011.06.066)
    • (2011) Biomaterials , vol.32 , pp. 7711-7720
    • Hea, Q.1    Gao, Y.2    Zhang, L.3    Zhang, Z.4    Gao, F.5    Ji, X.6    Li, Y.7    Shi, J.8
  • 49
    • 84884281722 scopus 로고    scopus 로고
    • Crosslinked ionic polysaccharides for stimulisensitive drug delivery
    • Lorenzo CA, Fernandez BB, Puga AM, Concheiro A. 2013 Crosslinked ionic polysaccharides for stimulisensitive drug delivery. Adv. Drug Deliv. Rev. 65, 1148-1171. (doi:10.1016/j.addr.2013.04.016)
    • (2013) Adv. Drug Deliv. Rev. , vol.65 , pp. 1148-1171
    • Lorenzo, C.A.1    Fernandez, B.B.2    Puga, A.M.3    Concheiro, A.4
  • 50
    • 58849144376 scopus 로고    scopus 로고
    • Stimuli-responsive interfaces and systems for the control of protein-surface and cell-surface interactions
    • Colea MA, Voelcker NH, Thissenc H, Griesser HJ. 2009 Stimuli-responsive interfaces and systems for the control of protein-surface and cell-surface interactions. Biomaterials 30, 1827-1850. (doi:10.1016/j.biomaterials.2008.12.026)
    • (2009) Biomaterials , vol.30 , pp. 1827-1850
    • Colea, M.A.1    Voelcker, N.H.2    Thissenc, H.3    Griesser, H.J.4
  • 51
    • 84886998752 scopus 로고    scopus 로고
    • Applicability of enzyme-responsive mesoporous silica supports capped with 2 bridged silsesquioxane for colon-specific drug delivery
    • Li X, Tang T, Zhou Y, Zhang Y, Sun Y. 2013 Applicability of enzyme-responsive mesoporous silica supports capped with 2 bridged silsesquioxane for colon-specific drug delivery. Microporous Mesoporous Mater. 184, 83-89.
    • (2013) Microporous Mesoporous Mater. , vol.184 , pp. 83-89
    • Li, X.1    Tang, T.2    Zhou, Y.3    Zhang, Y.4    Sun, Y.5
  • 52
    • 84864527570 scopus 로고    scopus 로고
    • Enzymeresponsive nanoparticles for drug release and diagnostics
    • Rica RDL, Aili D, Stevens MM. 2012 Enzymeresponsive nanoparticles for drug release and diagnostics. Adv. Drug Deliv. Rev. 64, 967-978.(doi:10.1016/j.addr.2012.01.002)
    • (2012) Adv. Drug Deliv. Rev. , vol.64 , pp. 967-978
    • Rica, R.D.L.1    Aili, D.2    Stevens, M.M.3
  • 53
    • 84888868249 scopus 로고    scopus 로고
    • Temperature-controlled encapsulation and release of an active enzyme in the cavity of a self-assembled DNA nanocage
    • Juul S et al. 2013 Temperature-controlled encapsulation and release of an active enzyme in the cavity of a self-assembled DNA nanocage. ACS Nano 7, 9724-9734. (doi:10.1021/nn4030543)
    • (2013) ACS Nano , vol.7 , pp. 9724-9734
    • Juul, S.1
  • 54
    • 79954685081 scopus 로고    scopus 로고
    • Covalent immobilization of recombinant Rhizobium etli CFN42 xylitol dehydrogenase onto modified silica nanoparticles
    • Zhang YW, Tiwari MK, Jeya M, Lee JK. 2011 Covalent immobilization of recombinant Rhizobium etli CFN42 xylitol dehydrogenase onto modified silica nanoparticles. Appl. Microbiol. Biotechnol. 90, 499-507. (doi:10.1007/s00253-011-3094-9)
    • (2011) Appl. Microbiol. Biotechnol. , vol.90 , pp. 499-507
    • Zhang, Y.W.1    Tiwari, M.K.2    Jeya, M.3    Lee, J.K.4
  • 55
    • 84862775519 scopus 로고    scopus 로고
    • Direct binding glucoamylase onto carboxyl-functioned magnetic nanoparticles
    • Guo C, Yunhui M, Pengfei S, Baishan F. 2012 Direct binding glucoamylase onto carboxyl-functioned magnetic nanoparticles. Biochem. Eng. J. 67, 120-125. (doi:10.1016/j.bej.2012.06.002)
    • (2012) Biochem. Eng. J. , vol.67 , pp. 120-125
    • Guo, C.1    Yunhui, M.2    Pengfei, S.3    Baishan, F.4
  • 57
    • 77954539727 scopus 로고    scopus 로고
    • Immobilization of Pseudomonas cepacia lipase onto electrospun polyacrylonitrile fibers through physical adsorption and application to transesterification in nonaqueous solvent
    • Sakai S, Liu Y, Yamaguchi T, Watanabe R, Kawabe M, Kawakami K. 2010 Immobilization of Pseudomonas cepacia lipase onto electrospun polyacrylonitrile fibers through physical adsorption and application to transesterification in nonaqueous solvent. Biotechnol. Lett. 32, 1059-1062. (doi:10.1007/s10529-010-0279-8)
    • (2010) Biotechnol. Lett. , vol.32 , pp. 1059-1062
    • Sakai, S.1    Liu, Y.2    Yamaguchi, T.3    Watanabe, R.4    Kawabe, M.5    Kawakami, K.6
  • 58
    • 80054948841 scopus 로고    scopus 로고
    • Apoferritin nanoparticle: A novel and biocompatible carrier for enzyme immobilization with enhanced activity and stability
    • Zhang Y, Tang Z, Wang J, Wu H, Lin C-T, Lin Y. 2011 Apoferritin nanoparticle: a novel and biocompatible carrier for enzyme immobilization with enhanced activity and stability. J. Mater. Chem. 21, 17 468-17 475. (doi:10.1039/c1jm11598g)
    • (2011) J. Mater. Chem. , vol.21 , pp. 17468-17475
    • Zhang, Y.1    Tang, Z.2    Wang, J.3    Wu, H.4    Lin, C.-T.5    Lin, Y.6
  • 59
    • 79953200775 scopus 로고    scopus 로고
    • Activity of diastase a-amylase immobilized on polyanilines (PANIs)
    • Ashly PC, Joseph MJ, Mohanan PV. 2011 Activity of diastase a-amylase immobilized on polyanilines (PANIs). Food Chem. 127, 1808-1813. (doi:10.1016/j.foodchem.2011.02.068)
    • (2011) Food Chem. , vol.127 , pp. 1808-1813
    • Ashly, P.C.1    Joseph, M.J.2    Mohanan, P.V.3
  • 61
    • 79952817928 scopus 로고    scopus 로고
    • Immobilized β-galactosidase onto magnetic particles coated with polyaniline: Support characterization and galactooligosaccharides production
    • Neri DFM, Balcão VM, Dourado FOQ, Oliveira JMB, Teixeira JA. 2011 Immobilized β-galactosidase onto magnetic particles coated with polyaniline: support characterization and galactooligosaccharides production. J. Mol. Catal. B Enzymatic 70, 74-80. (doi:10.1016/j.molcatb.2011.02.007)
    • (2011) J. Mol. Catal. B Enzymatic , vol.70 , pp. 74-80
    • Neri, D.F.M.1    Balcão, V.M.2    Dourado, F.O.Q.3    Oliveira, J.M.B.4    Teixeira, J.A.5
  • 62
    • 60749116567 scopus 로고    scopus 로고
    • Galacto-oligosaccharides production during lactose hydrolysis by free Aspergillus oryzae β-galactosidase and immobilized on magnetic polysiloxane-polyvinyl alcohol
    • Neri DFM, Balcao VM, Costa RS, Rocha ICAP, Ferreira EMFC, Torres DPM, Rodrigues LRM, Jr LBC, Teixeira JA. 2009 Galacto-oligosaccharides production during lactose hydrolysis by free Aspergillus oryzae β-galactosidase and immobilized on magnetic polysiloxane-polyvinyl alcohol. Food Chem. 115, 92-99. (doi:10.1016/j.foodchem.2008.11.068)
    • (2009) Food Chem. , vol.115 , pp. 92-99
    • Neri, D.F.M.1    Balcao, V.M.2    Costa, R.S.3    Rocha, I.C.A.P.4    Ferreira, E.M.F.C.5    Torres, D.P.M.6    Rodrigues, L.R.M.7    C., L.B.8    Teixeira, J.A.9
  • 63
    • 34447102668 scopus 로고    scopus 로고
    • Electrospun polyacrylonitrile nanofibrous membranes for lipase immobilization
    • Li S-F, Chen J-P, Wu W-T. 2007 Electrospun polyacrylonitrile nanofibrous membranes for lipase immobilization. J. Mol. Catal. B Enzymatic 47, 117-124. (doi:10.1016/j.molcatb.2007.04.010)
    • (2007) J. Mol. Catal. B Enzymatic , vol.47 , pp. 117-124
    • Li, S.-F.1    Chen, J.-P.2    Wu, W.-T.3
  • 64
    • 22944462986 scopus 로고    scopus 로고
    • Mesoporous silica particles as templates for preparing enzymeloaded biocompatible microcapsules
    • Yu A, Wang Y, Barlow E, Caruso F. 2005 Mesoporous silica particles as templates for preparing enzymeloaded biocompatible microcapsules. Adv. Mater. 17, 1737-1741. (doi:10.1002/adma.200402045)
    • (2005) Adv. Mater. , vol.17 , pp. 1737-1741
    • Yu, A.1    Wang, Y.2    Barlow, E.3    Caruso, F.4
  • 65
    • 84876474057 scopus 로고    scopus 로고
    • Immobilization of beta-glucosidase on a magnetic nanoparticle improves thermostability: Application in cellobiose hydrolysis
    • Verma ML, Chaudhary R, Tsuzuki T, Barrow CJ, Puri M. 2013 Immobilization of beta-glucosidase on a magnetic nanoparticle improves thermostability: application in cellobiose hydrolysis. Bioresour. Technol. 135, 2-6. (doi:10.1016/j.biortech.2013.01.047)
    • (2013) Bioresour. Technol. , vol.135 , pp. 2-6
    • Verma, M.L.1    Chaudhary, R.2    Tsuzuki, T.3    Barrow, C.J.4    Puri, M.5
  • 66
    • 80052393157 scopus 로고    scopus 로고
    • Enzyme-nanoporous gold biocomposite: Excellent biocatalyst with improved biocatalytic performance and stability
    • Wang X, Liu X, Yan X, Zhao P, Ding Y, Xu P. 2011 Enzyme-nanoporous gold biocomposite: excellent biocatalyst with improved biocatalytic performance and stability. PLoS ONE 6, e24207-e24207. (doi:10.1371/journal.pone.0024207)
    • (2011) PLoS ONE , vol.6 , pp. e24207-e24207
    • Wang, X.1    Liu, X.2    Yan, X.3    Zhao, P.4    Ding, Y.5    Xu, P.6
  • 67
    • 84864384352 scopus 로고    scopus 로고
    • Electrospun polystyrene-poly(styrene-co-maleicanhydride) nanofiber as a new aptasensor platform
    • Lee SJ, Rameshwar T, Gu M. 2012 Electrospun polystyrene-poly(styrene-co-maleicanhydride) nanofiber as a new aptasensor platform. Biosens. Bioelectron. 38, 302-307. (doi:10.1016/j.bios.2012.06.009)
    • (2012) Biosens. Bioelectron. , vol.38 , pp. 302-307
    • Lee, S.J.1    Rameshwar, T.2    Gu, M.3
  • 68
    • 84875332450 scopus 로고    scopus 로고
    • Laccase immobilization on chitosan/poly(vinyl alcohol) composite nanofibrous membranes for 2,4-dichlorophenol removal
    • Xu R, Zhou Q, Li F, Zhang B. 2013 Laccase immobilization on chitosan/poly(vinyl alcohol) composite nanofibrous membranes for 2,4-dichlorophenol removal. Chem. Eng. J. 222, 321-329. (doi:10.1016/j.cej.2013.02.074)
    • (2013) Chem. Eng. J. , vol.222 , pp. 321-329
    • Xu, R.1    Zhou, Q.2    Li, F.3    Zhang, B.4
  • 69
    • 14644442914 scopus 로고    scopus 로고
    • Immobilization of cellulase in nanofibrous PVA membranes by electrospinning
    • Wu L, Yuan X, Sheng J. 2005 Immobilization of cellulase in nanofibrous PVA membranes by electrospinning. J. Membr. Sci. 250, 167-173. (doi:10.1016/j.memsci.2004.10.024)
    • (2005) J. Membr. Sci. , vol.250 , pp. 167-173
    • Wu, L.1    Yuan, X.2    Sheng, J.3
  • 70
    • 84863280762 scopus 로고    scopus 로고
    • Magnetic enzyme nanogel (MENG): A universal synthetic route for biocatalysts
    • Lin M, Lu D, Zhu J, Yang C, Zhang Y, Liu Z. 2012 Magnetic enzyme nanogel (MENG): a universal synthetic route for biocatalysts. Chem. Commun. 48, 3315. (doi:10.1039/c2cc30189j)
    • (2012) Chem. Commun. , vol.48 , pp. 3315
    • Lin, M.1    Lu, D.2    Zhu, J.3    Yang, C.4    Zhang, Y.5    Liu, Z.6
  • 71
    • 84859968707 scopus 로고    scopus 로고
    • Applications of functionalized and nanoparticle-modified nanocrystalline cellulose
    • Lam E, Male KB, Chong JH, Leung AC, Luong JH. 2012 Applications of functionalized and nanoparticle-modified nanocrystalline cellulose. Trends Biotechnol. 30, 283-290. (doi:10.1016/j.tibtech.2012.02.001)
    • (2012) Trends Biotechnol. , vol.30 , pp. 283-290
    • Lam, E.1    Male, K.B.2    Chong, J.H.3    Leung, A.C.4    Luong, J.H.5
  • 72
    • 33748082007 scopus 로고    scopus 로고
    • Encapsulation of single enzyme in nanogel withenhanced biocatalytic activity and stability
    • Yan M, Ge J, Liu Z, Ouyang P. 2006 Encapsulation of single enzyme in nanogel withenhanced biocatalytic activity and stability. J. Am. Chem. Soc. 128, 11 008-11 009. (doi:10.1021/ja064126t)
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11008-11009
    • Yan, M.1    Ge, J.2    Liu, Z.3    Ouyang, P.4
  • 73
    • 37349029739 scopus 로고    scopus 로고
    • Covalent-bonded immobilization of enzyme on hydrophilic polymer covering magnetic nanogels
    • Hong J, Xu D, Gong P, Yu J, Ma H, Yao S. 2008 Covalent-bonded immobilization of enzyme on hydrophilic polymer covering magnetic nanogels. Microporous Mesoporous Mater. 109, 470-477. (doi:10.1016/j.micromeso.2007.05.052)
    • (2008) Microporous Mesoporous Mater. , vol.109 , pp. 470-477
    • Hong, J.1    Xu, D.2    Gong, P.3    Yu, J.4    Ma, H.5    Yao, S.6
  • 74
    • 84874652607 scopus 로고    scopus 로고
    • Biomimetic enzyme nanocomplexes and their use as antidotes and preventive measures for alcohol intoxication
    • Liu Y et al. 2013 Biomimetic enzyme nanocomplexes and their use as antidotes and preventive measures for alcohol intoxication. Nanotechnology 8, 187-192. (doi:10.1038/nnano.2012.264)
    • (2013) Nanotechnology , vol.8 , pp. 187-192
    • Liu, Y.1
  • 75
    • 80052626684 scopus 로고    scopus 로고
    • Preparation and characterization of single-enzyme nanogels
    • Ge J, Yan M, Lu D, Liu Z, Liu Z. 2011 Preparation and characterization of single-enzyme nanogels. Methods Mol. Biol. 743, 119-130. (doi:10.1007/978-1-61779-132-1-10)
    • (2011) Methods Mol. Biol. , vol.743 , pp. 119-130
    • Ge, J.1    Yan, M.2    Lu, D.3    Liu, Z.4    Liu, Z.5
  • 76
    • 84864949030 scopus 로고    scopus 로고
    • Optimum conditions for lipase immobilization on chitosan-coated Fe3O4 nanoparticles
    • Kuo C-H, Liu Y-C, Chang C-MJ, Chen J-H, Chang C, Shieh C-J. 2012 Optimum conditions for lipase immobilization on chitosan-coated Fe3O4 nanoparticles. Carbohydr. Polym. 87, 2538-2545. (doi:10.1016/j.carbpol.2011.11.026)
    • (2012) Carbohydr. Polym. , vol.87 , pp. 2538-2545
    • Kuo, C.-H.1    Liu, Y.-C.2    Chang, C.-M.J.3    Chen, J.-H.4    Chang, C.5    Shieh, C.-J.6
  • 77
    • 77951647619 scopus 로고    scopus 로고
    • Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization
    • Mahmoud KA, Male KB, Hrapovic S, Luong JHT. 2009 Cellulose nanocrystal/gold nanoparticle composite as a matrix for enzyme immobilization. ACS Appl. Mater. Interfaces 1, 1383-1386. (doi:10.1021/am900331d)
    • (2009) ACS Appl. Mater. Interfaces , vol.1 , pp. 1383-1386
    • Mahmoud, K.A.1    Male, K.B.2    Hrapovic, S.3    Luong, J.H.T.4
  • 78
    • 0034597419 scopus 로고    scopus 로고
    • Preparation and functional properties of trypsin modified by carboxymethylcellulose
    • Villalonga R, Villalonga ML, Gomez L. 2000 Preparation and functional properties of trypsin modified by carboxymethylcellulose. J. Mol. Catal. B Enzymatic 10, 483-490. (doi:10.1016/S1381-1177(00)00003-5)
    • (2000) J. Mol. Catal. B Enzymatic , vol.10 , pp. 483-490
    • Villalonga, R.1    Villalonga, M.L.2    Gomez, L.3
  • 79
    • 58249088885 scopus 로고    scopus 로고
    • Enzyme immobilization on electrospun polymer nanofibers: An overview
    • Wang ZG, Wan LS, Liu ZM, Huang XJ, Xu ZK. 2009 Enzyme immobilization on electrospun polymer nanofibers: an overview. J. Mol. Catal. B Enzymatic 56, 189-195. (doi:10.1016/j.molcatb.2008.05.005)
    • (2009) J. Mol. Catal. B Enzymatic , vol.56 , pp. 189-195
    • Wang, Z.G.1    Wan, L.S.2    Liu, Z.M.3    Huang, X.J.4    Xu, Z.K.5
  • 80
    • 77957372322 scopus 로고    scopus 로고
    • Functionalized electrospun mats from styrene-maleic anhydride copolymers for immobilization of acetylcholinesterase
    • Stoilova O, Ignatova M, Manolova N, Godjevargova T, Mita DG, Rashkov I. 2010 Functionalized electrospun mats from styrene-maleic anhydride copolymers for immobilization of acetylcholinesterase. Eur. Polym. J. 46, 1966-1974. (doi:10.1016/j.eurpolymj.2010.08.005)
    • (2010) Eur. Polym. J. , vol.46 , pp. 1966-1974
    • Stoilova, O.1    Ignatova, M.2    Manolova, N.3    Godjevargova, T.4    Mita, D.G.5    Rashkov, I.6
  • 81
    • 84893514240 scopus 로고    scopus 로고
    • Highly stabilized lipase in polyaniline nanofibers for surfactantmediated esterification of ibuprofen
    • Hong S-G, Kim HS, Kim J. 2014 Highly stabilized lipase in polyaniline nanofibers for surfactantmediated esterification of ibuprofen. Langmuir 30, 911-915. (doi:10.1021/la404189e)
    • (2014) Langmuir , vol.30 , pp. 911-915
    • Hong, S.-G.1    Kim, H.S.2    Kim, J.3
  • 82
    • 84890081307 scopus 로고    scopus 로고
    • Enabling multi-enzyme biocatalysis using coaxial-electrospun hollow nanofibers: Redesign of artificial cells
    • Ji X, Wang P, Su Z, Ma G, Zhang S. 2014 Enabling multi-enzyme biocatalysis using coaxial-electrospun hollow nanofibers: redesign of artificial cells. J. Mater. Chem. B 2, 181. (doi:10.1039/c3tb21232g)
    • (2014) J. Mater. Chem. B , vol.2 , pp. 181
    • Ji, X.1    Wang, P.2    Su, Z.3    Ma, G.4    Zhang, S.5
  • 83
    • 0034500248 scopus 로고    scopus 로고
    • Catalytic activity in organic solvents and stability of immobilized enzymes depend on the pore size and surface characteristics of mesoporous silica
    • Takahashi H, Li B, Sasaki T, Miyazaki C, Kajino T, Inagaki S. 2000 Catalytic activity in organic solvents and stability of immobilized enzymes depend on the pore size and surface characteristics of mesoporous silica. Chem. Mater. 12, 3301-3305. (doi:10.1021/cm000487a)
    • (2000) Chem. Mater. , vol.12 , pp. 3301-3305
    • Takahashi, H.1    Li, B.2    Sasaki, T.3    Miyazaki, C.4    Kajino, T.5    Inagaki, S.6
  • 84
    • 58149214047 scopus 로고    scopus 로고
    • Laccase immobilization on mesostructured cellular foams affords preparations with ultra high activity
    • Rekuc A, Bryjak J, Szymanska K, Jarzebski AB. 2009 Laccase immobilization on mesostructured cellular foams affords preparations with ultra high activity. Proc. Biochem. 44, 191-198. (doi:10.1016/j. procbio.2008.10.007)
    • (2009) Proc. Biochem. , vol.44 , pp. 191-198
    • Rekuc, A.1    Bryjak, J.2    Szymanska, K.3    Jarzebski, A.B.4
  • 85
    • 68549115472 scopus 로고    scopus 로고
    • Evaluation of a silica-coated magnetic nanoparticle for the immobilization of a His-tagged lipase
    • Kim H, Kwon H-S, Ahn J, Lee C-H, Ahn I-S. 2009 Evaluation of a silica-coated magnetic nanoparticle for the immobilization of a His-tagged lipase. Biocatal. Biotransform. 27, 246-253. (doi:10.1080/10242420903042627)
    • (2009) Biocatal. Biotransform. , vol.27 , pp. 246-253
    • Kim, H.1    Kwon, H.-S.2    Ahn, J.3    Lee, C.-H.4    Ahn, I.-S.5
  • 86
    • 84871851112 scopus 로고    scopus 로고
    • Modification of mesoporous silicates for immobilization of enzymes
    • Gaffney D, Cooney J, Magner E. 2012 Modification of mesoporous silicates for immobilization of enzymes. Top. Catal. 55, 1101-1106. (doi:10.1007/s11244-012-9899-7)
    • (2012) Top. Catal. , vol.55 , pp. 1101-1106
    • Gaffney, D.1    Cooney, J.2    Magner, E.3
  • 87
    • 76249098277 scopus 로고    scopus 로고
    • Tailored adsorption of His6-tagged protein onto nickel(II)-cyclam grafted mesoporous silica
    • Gaffney DA, O'Neill S, O'Loughlin MC, Hanefeld U, Cooney JC, Magner E. 2010 Tailored adsorption of His6-tagged protein onto nickel(II)-cyclam grafted mesoporous silica. Chem. Commun. 46, 1124-1126. (doi:10.1039/b915169a)
    • (2010) Chem. Commun. , vol.46 , pp. 1124-1126
    • Gaffney, D.A.1    O'Neill, S.2    O'Loughlin, M.C.3    Hanefeld, U.4    Cooney, J.C.5    Magner, E.6
  • 88
    • 79952198691 scopus 로고    scopus 로고
    • Nanoporous silica glass for the immobilization of interactive enzyme systems
    • Buthe A, Wu S, Wang P. 2011 Nanoporous silica glass for the immobilization of interactive enzyme systems. Methods Mol. Biol. 679, 37-48. (doi:10.1007/978-1-60761-895-9-5)
    • (2011) Methods Mol. Biol. , vol.679 , pp. 37-48
    • Buthe, A.1    Wu, S.2    Wang, P.3
  • 89
    • 65249178901 scopus 로고    scopus 로고
    • Immobilization of BSA on silica-coated magnetic iron oxide nanoparticle
    • Yu CH, Al-Saadi A, Shih SJ, Qiu L, Tam KY, Tsang SCT. 2009 Immobilization of BSA on silica-coated magnetic iron oxide nanoparticle. J. Phys. Chem. C 113, 537-543. (doi:10.1021/jp809662a)
    • (2009) J. Phys. Chem. C , vol.113 , pp. 537-543
    • Yu, C.H.1    Al-Saadi, A.2    Shih, S.J.3    Qiu, L.4    Tam, K.Y.5    Tsang, S.C.T.6
  • 90
    • 70049099385 scopus 로고    scopus 로고
    • An easy co-casting method to synthesize mesostructured carbon composites with high magnetic separability and acid resistance
    • Guo L, Zeng S, Li J, Cui F, Cui X, Bu W, Shi J. 2009 An easy co-casting method to synthesize mesostructured carbon composites with high magnetic separability and acid resistance. New J. Chem. 33, 1926-1931. (doi:10.1039/b906776k)
    • (2009) New J. Chem. , vol.33 , pp. 1926-1931
    • Guo, L.1    Zeng, S.2    Li, J.3    Cui, F.4    Cui, X.5    Bu, W.6    Shi, J.7
  • 91
    • 77958455868 scopus 로고    scopus 로고
    • Immobilization of enzyme biocatalyst on natural halloysite nanotubes
    • Zhai R, Zhang B, Liu L, Xie Y, Zhang H, Liu J. 2010 Immobilization of enzyme biocatalyst on natural halloysite nanotubes. Catal. Commun. 12, 259-263. (doi:10.1016/j.catcom.2010.09.030)
    • (2010) Catal. Commun. , vol.12 , pp. 259-263
    • Zhai, R.1    Zhang, B.2    Liu, L.3    Xie, Y.4    Zhang, H.5    Liu, J.6
  • 92
    • 11144277399 scopus 로고    scopus 로고
    • Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: Effect on the enzymatic activity in solvent-free ethyl oleate synthesis
    • Foresti ML, Alimenti GA, Ferreira ML. 2005 Interfacial activation and bioimprinting of Candida rugosa lipase immobilized on polypropylene: effect on the enzymatic activity in solvent-free ethyl oleate synthesis. Enzyme Microb. Technol. 36, 338-349. (doi:10.1016/j.enzmictec.2004.09.012)
    • (2005) Enzyme Microb. Technol. , vol.36 , pp. 338-349
    • Foresti, M.L.1    Alimenti, G.A.2    Ferreira, M.L.3
  • 95
    • 84878116553 scopus 로고    scopus 로고
    • Robust nanobioconjugates of Candida antarctica lipase B-multiwalled carbon nanotubes: Characterization and application for multiple usages in non-aqueous biocatalysis
    • Raghavendra T, Basak A, Manocha LM, Shah AR, Madamwar D. 2013 Robust nanobioconjugates of Candida antarctica lipase B-multiwalled carbon nanotubes: characterization and application for multiple usages in non-aqueous biocatalysis. Bioresour. Technol. 140, 103-110. (doi:10.1016/j. biortech.2013.04.071)
    • (2013) Bioresour. Technol. , vol.140 , pp. 103-110
    • Raghavendra, T.1    Basak, A.2    Manocha, L.M.3    Shah, A.R.4    Madamwar, D.5
  • 96
    • 78650330875 scopus 로고    scopus 로고
    • Lipase covalently attached to multiwalled carbon nanotubes as an efficient catalyst in organic solvent
    • Ji P, Tan H, Xu X, Feng W. 2010 Lipase covalently attached to multiwalled carbon nanotubes as an efficient catalyst in organic solvent. AIChE J. 56, 3005-3011. (doi:10.1002/aic.12180)
    • (2010) AIChE J. , vol.56 , pp. 3005-3011
    • Ji, P.1    Tan, H.2    Xu, X.3    Feng, W.4
  • 97
    • 84892985471 scopus 로고    scopus 로고
    • Biocatalytic carbon nanotube paper: A 'one-pot' route for fabrication of enzymeimmobilized membranes for organophosphate bioremediation
    • Mechrez G, Krepker MA, Harel Y, Lellouche J-P, Segal E. 2014 Biocatalytic carbon nanotube paper: a 'one-pot' route for fabrication of enzymeimmobilized membranes for organophosphate bioremediation. J. Mater. Chem. B 2, 915-922. (doi:10.1039/c3tb21439g)
    • (2014) J. Mater. Chem. B , vol.2 , pp. 915-922
    • Mechrez, G.1    Krepker, M.A.2    Harel, Y.3    Lellouche, J.-P.4    Segal, E.5
  • 98
    • 84893820288 scopus 로고    scopus 로고
    • Catalytic performance and molecular dynamic simulation of immobilized CC bond hydrolase based on carbon nanotube matrix
    • Zhou H, Qu Y, Kong C, Li D, Shen E, Ma Q, Zhang X, Wang J, Zhou J. 2014 Catalytic performance and molecular dynamic simulation of immobilized CC bond hydrolase based on carbon nanotube matrix. Colloids Surf. B Biointerfaces 116, 365-371. (doi:10.1016/j.colsurfb.2014.01.018)
    • (2014) Colloids Surf. B Biointerfaces , vol.116 , pp. 365-371
    • Zhou, H.1    Qu, Y.2    Kong, C.3    Li, D.4    Shen, E.5    Ma, Q.6    Zhang, X.7    Wang, J.8    Zhou, J.9
  • 101
    • 77957328836 scopus 로고    scopus 로고
    • Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes
    • Wang L, Wei L, Chen Y, Jiang R. 2010 Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes. J. Biotechnol. 150, 57-63. (doi:10.1016/j.jbiotec.2010.07.005)
    • (2010) J. Biotechnol. , vol.150 , pp. 57-63
    • Wang, L.1    Wei, L.2    Chen, Y.3    Jiang, R.4
  • 102
    • 71649087222 scopus 로고    scopus 로고
    • Immobilization of enzyme on detonation nanodiamond for highly efficient proteolysis
    • Wei L, Zhang W, Lu H, Yang P. 2010 Immobilization of enzyme on detonation nanodiamond for highly efficient proteolysis. Talanta 80, 1298-1304. (doi:10.1016/j.talanta.2009.09.029)
    • (2010) Talanta , vol.80 , pp. 1298-1304
    • Wei, L.1    Zhang, W.2    Lu, H.3    Yang, P.4
  • 103
    • 84899443582 scopus 로고    scopus 로고
    • Coimmobilization of multi-enzyme on control-reduced graphene oxide by non-covalent bonds: An artificial biocatalytic system for the one-pot production of gluconic acid from starch
    • Zhao F, Li H, Jiang Y, Wang X, Mu X. 2014 Coimmobilization of multi-enzyme on control-reduced graphene oxide by non-covalent bonds: an artificial biocatalytic system for the one-pot production of gluconic acid from starch. Green Chem. 16, 2558. (doi:10.1039/c3gc42545b)
    • (2014) Green Chem , vol.16 , pp. 2558
    • Zhao, F.1    Li, H.2    Jiang, Y.3    Wang, X.4    Mu, X.5
  • 104
    • 80052393157 scopus 로고    scopus 로고
    • Enzyme-nanoporous gold biocomposite: Excellent biocatalyst with improved biocatalytic performance and stability
    • Wang X, Liu X, Yan X, Zhao P, Ding Y, Xu P. 2011 Enzyme-nanoporous gold biocomposite: excellent biocatalyst with improved biocatalytic performance and stability. PLoS ONE 6, e24207. (doi:10.1371/journal.pone.0024207)
    • (2011) PLoS ONE , vol.6
    • Wang, X.1    Liu, X.2    Yan, X.3    Zhao, P.4    Ding, Y.5    Xu, P.6
  • 105
    • 13644250281 scopus 로고    scopus 로고
    • Examination of cholesterol oxidase attachment to magnetic nanoparticles
    • Kouassi GK, Irudayaraj J, McCarty G. 2005 Examination of cholesterol oxidase attachment to magnetic nanoparticles. J. Nanobiotechnol. 3, 1. (doi:10.1186/1477-3155-3-1)
    • (2005) J. Nanobiotechnol. , vol.3 , pp. 1
    • Kouassi, G.K.1    Irudayaraj, J.2    McCarty, G.3
  • 106
    • 33847216926 scopus 로고    scopus 로고
    • Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability
    • Li D, He Q, Cui Y, Duan L, Li J. 2007 Immobilization of glucose oxidase onto gold nanoparticles with enhanced thermostability. Biochem. Biophys. Res. Commun. 355, 488-493. (doi:10.1016/j.bbrc.2007.01.183)
    • (2007) Biochem. Biophys. Res. Commun. , vol.355 , pp. 488-493
    • Li, D.1    He, Q.2    Cui, Y.3    Duan, L.4    Li, J.5
  • 107
    • 33947433255 scopus 로고    scopus 로고
    • Application of thiolated gold nanoparticles for the enhancement of glucose oxidase activity
    • Pandey P, Singh SP, Arya SK, Gupta V, Datta M, Singh S, Malhotra BD. 2007 Application of thiolated gold nanoparticles for the enhancement of glucose oxidase activity. Langmuir 23, 3333-3337. (doi:10.1021/la062901c)
    • (2007) Langmuir , vol.23 , pp. 3333-3337
    • Pandey, P.1    Singh, S.P.2    Arya, S.K.3    Gupta, V.4    Datta, M.5    Singh, S.6    Malhotra, B.D.7
  • 108
    • 84859427635 scopus 로고    scopus 로고
    • Enzyme-magnetic nanoparticle hybrids: New effective catalysts for the production of high value chemicals
    • Yiu HHP, Keane MA. 2012 Enzyme-magnetic nanoparticle hybrids: new effective catalysts for the production of high value chemicals. J. Chem. Technol. Biotechnol. 87, 583-594. (doi:10.1002/jctb.3735)
    • (2012) J. Chem. Technol. Biotechnol. , vol.87 , pp. 583-594
    • Yiu, H.H.P.1    Keane, M.A.2
  • 110
    • 34250215648 scopus 로고    scopus 로고
    • Gold nanoparticles bound on microgel particles and their application as an enzyme support
    • Xu J, Zeng F, Wu S, Liu X, Hou C. 2007 Gold nanoparticles bound on microgel particles and their application as an enzyme support. Nanotechnology 18, 265-273. (doi:10.1088/0957-4484/18/26/265704)
    • (2007) Nanotechnology , vol.18 , pp. 265-273
    • Xu, J.1    Zeng, F.2    Wu, S.3    Liu, X.4    Hou, C.5
  • 112
    • 79957783524 scopus 로고    scopus 로고
    • Catalase-coupled gold nanoparticles: Comparison between the carbodiimide and biotin-streptavidin methods
    • Chirra HD, Sexton T, Biswal D, Hersh LB, Hilt JZ. 2011 Catalase-coupled gold nanoparticles: comparison between the carbodiimide and biotin-streptavidin methods. Acta Biomater. 7, 2865-2872. (doi:10.1016/j.actbio.2011.01.003)
    • (2011) Acta Biomater , vol.7 , pp. 2865-2872
    • Chirra, H.D.1    Sexton, T.2    Biswal, D.3    Hersh, L.B.4    Hilt, J.Z.5
  • 113
    • 67650106144 scopus 로고    scopus 로고
    • Directed self-immobilization of alkaline phosphatase on micro-patterned substrates via genetically fused metal-binding peptide
    • Kacar T, Zin MT, So C, Wilson B, Ma H, Gul-Karaguler N, Jen AK-Y, Sarikaya M, Tamerler C. 2009 Directed self-immobilization of alkaline phosphatase on micro-patterned substrates via genetically fused metal-binding peptide. Biotechnol. Bioeng. 103, 696-705. (doi:10.1002/bit.22282)
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 696-705
    • Kacar, T.1    Zin, M.T.2    So, C.3    Wilson, B.4    Ma, H.5    Gul-Karaguler, N.6    Jen, A.K.-Y.7    Sarikaya, M.8    Tamerler, C.9
  • 114
    • 66849108669 scopus 로고    scopus 로고
    • Multifunctional ligands based on dihydrolipoic acid and polyethylene glycol to promote biocompatibility of quantum dots
    • Susumu K, Mei BC, Mattoussi H. 2009 Multifunctional ligands based on dihydrolipoic acid and polyethylene glycol to promote biocompatibility of quantum dots. Nat. Protoc. 4, 424-436. (doi:10.1038/nprot.2008.247)
    • (2009) Nat. Protoc. , vol.4 , pp. 424-436
    • Susumu, K.1    Mei, B.C.2    Mattoussi, H.3
  • 115
    • 4344649335 scopus 로고    scopus 로고
    • Design of large-pore mesoporous materials for immobilization of penicillin G acylase biocatalyst
    • Chong ASM, Zhao XS. 2004 Design of large-pore mesoporous materials for immobilization of penicillin G acylase biocatalyst. Catal. Today 93-95, 293-299. (doi:10.1016/j.cattod.2004.06.064)
    • (2004) Catal. Today , vol.93-95 , pp. 293-299
    • Chong, A.S.M.1    Zhao, X.S.2
  • 116
    • 84898889702 scopus 로고    scopus 로고
    • Understanding enzymatic acceleration at nanoparticle interfaces: Approaches and challenges
    • Johnson BJ, Russ Algar W, Malanoski AP, Ancona MG, Medintz IL. 2014 Understanding enzymatic acceleration at nanoparticle interfaces: approaches and challenges. Nano Today 9, 102-131. (doi:10.1016/j.nantod.2014.02.005)
    • (2014) Nano Today , vol.9 , pp. 102-131
    • Johnson, B.J.1    Russ Algar, W.2    Malanoski, A.P.3    Ancona, M.G.4    Medintz, I.L.5
  • 117
    • 78650191419 scopus 로고    scopus 로고
    • Enzyme:Nanoparticle bioconjugates with two sequential enzymes: Stoichiometry and activity of malate dehydrogenase and citrate synthase on Au nanoparticles
    • Keighron JD, Keating CD. 2010 Enzyme:nanoparticle bioconjugates with two sequential enzymes: stoichiometry and activity of malate dehydrogenase and citrate synthase on Au nanoparticles. Langmuir 26, 18 992-19 000. (doi:10.1021/la1040882)
    • (2010) Langmuir , vol.26 , pp. 18992-19000
    • Keighron, J.D.1    Keating, C.D.2
  • 118
    • 55349136999 scopus 로고    scopus 로고
    • An enzymatic kinetics investigation into the significantly enhanced activity of functionalized gold nanoparticles
    • Wu C-S, Wu C-T, Yang Y-S, Ko F-H. 2008 An enzymatic kinetics investigation into the significantly enhanced activity of functionalized gold nanoparticles. Chem. Commun., 5327-5329. (doi:10.1039/b810889g)
    • (2008) Chem. Commun. , pp. 5327-5329
    • Wu, C.-S.1    Wu, C.-T.2    Yang, Y.-S.3    Ko, F.-H.4
  • 119
    • 77949917705 scopus 로고    scopus 로고
    • Nickel-impregnated silica nanoparticle synthesis and their evaluation for biocatalyst immobilization
    • Prakasham R, Devi GS, Rao C, Sivakumar VSS, Sathish T, Sarma PN. 2010 Nickel-impregnated silica nanoparticle synthesis and their evaluation for biocatalyst immobilization. Appl. Biochem. Biotechnol. 160, 1888-1895. (doi:10.1007/s12010-009-8726-5)
    • (2010) Appl. Biochem. Biotechnol. , vol.160 , pp. 1888-1895
    • Prakasham, R.1    Devi, G.S.2    Rao, C.3    Sivakumar, V.S.S.4    Sathish, T.5    Sarma, P.N.6
  • 120
    • 84873821085 scopus 로고    scopus 로고
    • A new nanobiocatalytic system based on allosteric effect with dramatically enhanced enzymatic performance
    • Wang LB, Wang YC, He R, Zhuang A, Wang X, Zeng J, Hou JG. 2013 A new nanobiocatalytic system based on allosteric effect with dramatically enhanced enzymatic performance. J. Am. Chem. Soc. 135, 1272-1275. (doi:10.1021/ja3120136)
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 1272-1275
    • Wang, L.B.1    Wang, Y.C.2    He, R.3    Zhuang, A.4    Wang, X.5    Zeng, J.6    Hou, J.G.7
  • 121
    • 0037010728 scopus 로고    scopus 로고
    • Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): Immobilization, hyperactivation and stabilization of the open form of lipases
    • Palomo JM, Muñoz G, Fernández-Lorente G, Mateo C, Fernández-Lafuente R, Guisán JM. 2002 Interfacial adsorption of lipases on very hydrophobic support (octadecyl-Sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases. J. Mol. Catal. B Enzymatic 19-20, 279-286. (doi:10.1016/S1381-1177 (02)00178-9)
    • (2002) J. Mol. Catal. B Enzymatic 1 , vol.19-20 , pp. 279-286
    • Palomo, J.M.1    Muñoz, G.2    Fernández-Lorente, G.3    Mateo, C.4    Fernández-Lafuente, R.5    Guisá6    n, J.M.7
  • 122
    • 50849121367 scopus 로고    scopus 로고
    • Immobilization of lipases on hydrophobilized zirconia nanoparticles: Highly enantioselective and reusable biocatalysts
    • Chen YZ, Yang CT, Ching CB, Xu R. 2008 Immobilization of lipases on hydrophobilized zirconia nanoparticles: highly enantioselective and reusable biocatalysts. Langmuir 24, 8877-8884. (doi:10.1021/la801384c)
    • (2008) Langmuir , vol.24 , pp. 8877-8884
    • Chen, Y.Z.1    Yang, C.T.2    Ching, C.B.3    Xu, R.4
  • 123
    • 84861458813 scopus 로고    scopus 로고
    • Process technology for multi-enzymatic reaction systems
    • Xue R, Woodley JM. 2012 Process technology for multi-enzymatic reaction systems. Bioresour. Technol. 115, 183-195. (doi:10.1016/j.biortech.2012.03.033)
    • (2012) Bioresour. Technol. , vol.115 , pp. 183-195
    • Xue, R.1    Woodley, J.M.2
  • 124
    • 33745748175 scopus 로고    scopus 로고
    • Increasing protein stability through control of the nanoscale environment
    • Asuri P, Karajanagi SS, Yang H, Yim T-J, Kane RS, Dordick JS. 2006 Increasing protein stability through control of the nanoscale environment. Langmuir 22, 5833-5836. (doi:10.1021/la0528450)
    • (2006) Langmuir , vol.22 , pp. 5833-5836
    • Asuri, P.1    Karajanagi, S.S.2    Yang, H.3    Yim, T.-J.4    Kane, R.S.5    Dordick, J.S.6
  • 125
    • 84875523288 scopus 로고    scopus 로고
    • Enzyme immobilization on nanomaterials for biofuel production
    • Puri M, Barrow CJ, Verma ML. 2013 Enzyme immobilization on nanomaterials for biofuel production. Trends Biotechnol. y, 1-2. (doi:10.1016/j.biortech.2013)
    • (2013) Trends Biotechnol. Y , pp. 1-2
    • Puri, M.1    Barrow, C.J.2    Verma, M.L.3
  • 126
    • 78650512355 scopus 로고    scopus 로고
    • Preparation and characterization of cellulase-bound magnetite nanoparticles
    • Jordan J, Kumar CSSR, Theegala C. 2011 Preparation and characterization of cellulase-bound magnetite nanoparticles. J. Mol. Catal. B Enzymatic 68, 139-146. (doi:10.1016/j.molcatb.2010.09.010)
    • (2011) J. Mol. Catal. B Enzymatic , vol.68 , pp. 139-146
    • Jordan, J.1    Kumar, C.S.S.R.2    Theegala, C.3
  • 127
    • 77149121079 scopus 로고    scopus 로고
    • Nanobiocatalysis for protein digestion in proteomic analysis
    • Kim J, Kim BC, Lopez Ferrer D, Petritis K, Smith RD. 2010 Nanobiocatalysis for protein digestion in proteomic analysis. Proteomics 10, 687-699. (doi:10.1002/pmic.200900519)
    • (2010) Proteomics , vol.10 , pp. 687-699
    • Kim, J.1    Kim, B.C.2    Lopez Ferrer, D.3    Petritis, K.4    Smith, R.D.5
  • 128
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: Strategies to prevent subunit dissociation
    • Fernandez-Lafuente R. 2009 Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb. Technol. 45, 405-418. (doi:10.1016/j.enzmictec.2009.08.009)
    • (2009) Enzyme Microb. Technol. , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 129
    • 84861398902 scopus 로고    scopus 로고
    • Self-assembly of a catalytic multivalent peptide-nanoparticle complex
    • Zaramella D, Scrimin P, Prins LJ. 2012 Self-assembly of a catalytic multivalent peptide-nanoparticle complex. Am. Chem. Soc. 134, 8396-8399. (doi:10.1021/ja302754h)
    • (2012) Am. Chem. Soc. , vol.134 , pp. 8396-8399
    • Zaramella, D.1    Scrimin, P.2    Prins, L.J.3
  • 130
    • 84915807906 scopus 로고
    • Colloidal gold: Principles, methods, and applications
    • (ed. MA Hayat), Wilmington, DE: Wiley Periodicals, Inc
    • Robenek H. 1990 Colloidal gold: principles, methods, and applications. In Scanning (ed. MA Hayat), pp. 244. Wilmington, DE: Wiley Periodicals, Inc.
    • (1990) Scanning , pp. 244
    • Robenek, H.1
  • 131
    • 33750991600 scopus 로고    scopus 로고
    • Modulation of the catalytic behavior of a-chymotrypsin at monolayer-protected nanoparticle surfaces
    • You C-C, Agasti SS, Mrinmoy De MJK, Rotello VM. 2006 Modulation of the catalytic behavior of a-chymotrypsin at monolayer-protected nanoparticle surfaces. J. Am. Chem. Soc. 128, 14 612-14 618. (doi:10.1021/ja064433z)
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14612-14618
    • You, C.-C.1    Agasti, S.S.2    Mrinmoy De, M.J.K.3    Rotello, V.M.4
  • 132
    • 80052585852 scopus 로고    scopus 로고
    • Multilayer enzyme-coupled magnetic nanoparticles as efficient, reusable biocatalysts and biosensors
    • Garcia J, Zhang Y, Taylor H, Cespedes O, Webb ME, Zhou D. 2011 Multilayer enzyme-coupled magnetic nanoparticles as efficient, reusable biocatalysts and biosensors. Nanoscale 3, 3721. (doi:10.1039/c1nr10411j)
    • (2011) Nanoscale , vol.3 , pp. 3721
    • Garcia, J.1    Zhang, Y.2    Taylor, H.3    Cespedes, O.4    Webb, M.E.5    Zhou, D.6
  • 133
    • 84877787360 scopus 로고    scopus 로고
    • Nanotechnology enabled enhancement of enzyme activity and thermostability: Study on impaired pectate lyase from attenuated Macrophomina phaseolina in presence of hydroxyapatite nanoparticle
    • Dutta N, Mukhopadhyay A, Dasgupta AK, Chakrabarti K. 2013 Nanotechnology enabled enhancement of enzyme activity and thermostability: study on impaired pectate lyase from attenuated Macrophomina phaseolina in presence of hydroxyapatite nanoparticle. PLoS ONE 8, e63567. (doi:10.1371/journal.pone.0063567)
    • (2013) PLoS ONE , vol.8
    • Dutta, N.1    Mukhopadhyay, A.2    Dasgupta, A.K.3    Chakrabarti, K.4
  • 134
    • 33847065929 scopus 로고    scopus 로고
    • Monodisperse carbon-polymer mesoporous spheres with magnetic functionality and adjustable pore-size distribution
    • Fuertes A, Tartaj P. 2007 Monodisperse carbon-polymer mesoporous spheres with magnetic functionality and adjustable pore-size distribution. Small 3, 275-279. (doi:10.1002/smll.200600487)
    • (2007) Small , vol.3 , pp. 275-279
    • Fuertes, A.1    Tartaj, P.2
  • 135
    • 84860000296 scopus 로고    scopus 로고
    • Reversible clustering of magnetic nanobiocatalysts for highperformance biocatalysis and easy catalyst recycling
    • Ngo TPN, Zhang W, Wang W, Li Z. 2012 Reversible clustering of magnetic nanobiocatalysts for highperformance biocatalysis and easy catalyst recycling. Chem. Commun. 48, 4585. (doi:10.1039/ c2cc30953j)
    • (2012) Chem. Commun. , vol.48 , pp. 4585
    • Ngo, T.P.N.1    Zhang, W.2    Wang, W.3    Li, Z.4
  • 136
    • 84055182856 scopus 로고    scopus 로고
    • Co-immobilization of three cellulases on Au-doped magnetic silica nanoparticles for the degradation of cellulose
    • Cho EJ, Jung S, Kim HJ, Lee YG, Nam KC, Lee HJ, Bae HJ. 2012 Co-immobilization of three cellulases on Au-doped magnetic silica nanoparticles for the degradation of cellulose. Chem. Commun. Camb. 48, 886-888. (doi:10.1039/c2cc16661e)
    • (2012) Chem. Commun. Camb. , vol.48 , pp. 886-888
    • Cho, E.J.1    Jung, S.2    Kim, H.J.3    Lee, Y.G.4    Nam, K.C.5    Lee, H.J.6    Bae, H.J.7
  • 137
    • 84877251282 scopus 로고    scopus 로고
    • Industrial upscaling of electrospinning and applications of polymer nanofibers: A review
    • Persano L, Camposeo A, Tekmen C, Pisignano D. 2013 Industrial upscaling of electrospinning and applications of polymer nanofibers: a review. Macromol. Mater. Eng. 298, 504-520. (doi:10.1002/mame.201200290)
    • (2013) Macromol. Mater. Eng. , vol.298 , pp. 504-520
    • Persano, L.1    Camposeo, A.2    Tekmen, C.3    Pisignano, D.4
  • 138
    • 84874971757 scopus 로고    scopus 로고
    • Electrospun cellulose acetate nanofibers: The present status and gamut of biotechnological applications
    • Konwarh R, Karak N, Misra M. 2013 Electrospun cellulose acetate nanofibers: the present status and gamut of biotechnological applications. Biotechnol. Adv. 31, 421-437. (doi:10.1016/j.biotechadv.2013.01.002)
    • (2013) Biotechnol. Adv. , vol.31 , pp. 421-437
    • Konwarh, R.1    Karak, N.2    Misra, M.3
  • 139
    • 53949106970 scopus 로고    scopus 로고
    • Nanobiocatalysis and its potential applications
    • Kim J, Grate JW, Wang P. 2008 Nanobiocatalysis and its potential applications. Trends Biotechnol. 26, 639-646. (doi:10.1016/j.tibtech.2008.07.009)
    • (2008) Trends Biotechnol. , vol.26 , pp. 639-646
    • Kim, J.1    Grate, J.W.2    Wang, P.3
  • 140
    • 78049264276 scopus 로고    scopus 로고
    • Polyaniline nanofiber coated monolith reactor for enzymatic bioconversion
    • Joo H, Lee JH. 2010 Polyaniline nanofiber coated monolith reactor for enzymatic bioconversion. J. Mol. Catal. B Enzymatic 67, 179-183. (doi:10.1016/j.molcatb.2010.08.001)
    • (2010) J. Mol. Catal. B Enzymatic , vol.67 , pp. 179-183
    • Joo, H.1    Lee, J.H.2
  • 141
    • 79955025068 scopus 로고    scopus 로고
    • Biodiesel production in packed-bed reactors using lipase-nanoparticle biocomposite
    • Wang X, Liu X, Zhao C, Ding Y, Xu P. 2011 Biodiesel production in packed-bed reactors using lipase-nanoparticle biocomposite. Bioresour. Technol. 102, 6352-6355. (doi:10.1016/j.biortech.2011.03.003)
    • (2011) Bioresour. Technol. , vol.102 , pp. 6352-6355
    • Wang, X.1    Liu, X.2    Zhao, C.3    Ding, Y.4    Xu, P.5
  • 142
    • 34247637888 scopus 로고    scopus 로고
    • Improving biocatalytic activity of enzyme-loaded nanofibers by dispersing entangled nanofiber structure
    • Nair S, Kim J, Crawford B, Kim SH. 2007 Improving biocatalytic activity of enzyme-loaded nanofibers by dispersing entangled nanofiber structure. Biomacromolecules 8, 1266-1270. (doi:10.1021/bm061004k)
    • (2007) Biomacromolecules , vol.8 , pp. 1266-1270
    • Nair, S.1    Kim, J.2    Crawford, B.3    Kim, S.H.4
  • 144
    • 79959359174 scopus 로고    scopus 로고
    • Immobilization of cellulase enzyme on superparamagnetic nanoparticles and determination of its activity and stability
    • Khoshnevisan K, Bordbar AK, Zare D, Davoodi D, Noruzi M, Barkhi M, Tabatabaei M. 2011 Immobilization of cellulase enzyme on superparamagnetic nanoparticles and determination of its activity and stability. Chem. Eng. J. 171, 669-673. (doi:10.1016/j.cej.2011.04.039)
    • (2011) Chem. Eng. J. , vol.171 , pp. 669-673
    • Khoshnevisan, K.1    Bordbar, A.K.2    Zare, D.3    Davoodi, D.4    Noruzi, M.5    Barkhi, M.6    Tabatabaei, M.7
  • 145
    • 80052970365 scopus 로고    scopus 로고
    • Immobilization of Pseudomonas cepacia lipase onto the electrospun PAN nanofibrous membranes for transesterification reaction
    • Li S-F, Fan Y-H, Hu J-F, Huang Y-S, Wu W-T. 2011 Immobilization of Pseudomonas cepacia lipase onto the electrospun PAN nanofibrous membranes for transesterification reaction. J. Mol. Catal. B Enzymatic 73, 98-103. (doi:10.1016/j.molcatb.2011.08.005)
    • (2011) J. Mol. Catal. B Enzymatic , vol.73 , pp. 98-103
    • Li, S.-F.1    Fan, Y.-H.2    Hu, J.-F.3    Huang, Y.-S.4    Wu, W.-T.5
  • 146
    • 84863008786 scopus 로고    scopus 로고
    • Reversible immobilization of K. Fragilis β-galactosidase onto magnetic polyethylenimine-grafted nanospheres for synthesis of galactooligosaccharide
    • Liu J-F, Liu H, Tan B, Chen Y-H, Yang R-J. 2012 Reversible immobilization of K. fragilis β -galactosidase onto magnetic polyethylenimine-grafted nanospheres for synthesis of galactooligosaccharide. J. Mol. Catal. B Enzymatic 82, 64-70. (doi:10.1016/j.molcatb.2012.06.001)
    • (2012) J. Mol. Catal. B Enzymatic , vol.82 , pp. 64-70
    • Liu, J.-F.1    Liu, H.2    Tan, B.3    Chen, Y.-H.4    Yang, R.-J.5
  • 147
    • 77949268947 scopus 로고    scopus 로고
    • Hydrolysis of granular starch at sub-gelatinization temperature using a mixture of amylolytic enzymes
    • Uthumporn U, Zaidul ISM, Karim AA. 2010 Hydrolysis of granular starch at sub-gelatinization temperature using a mixture of amylolytic enzymes. Food Bioproducts Process. 88, 47-54. (doi:10.1016/j.fbp.2009.10.001)
    • (2010) Food Bioproducts Process , vol.88 , pp. 47-54
    • Uthumporn, U.1    Zaidul, I.S.M.2    Karim, A.A.3
  • 148
    • 84859486494 scopus 로고    scopus 로고
    • Silver nanoparticles: A potential nanocatalyst for the rapid degradation of starch hydrolysis by alpha-amylase
    • Ernest V, Shiny PJ, Mukherjee A, Chandrasekaran N. 2012 Silver nanoparticles: a potential nanocatalyst for the rapid degradation of starch hydrolysis by alpha-amylase. Carbohydrate Res. 352, 60-64. (doi:10.1016/j.carres.2012.02.009)
    • (2012) Carbohydrate Res , vol.352 , pp. 60-64
    • Ernest, V.1    Shiny, P.J.2    Mukherjee, A.3    Chandrasekaran, N.4
  • 150
    • 84870355400 scopus 로고    scopus 로고
    • Covalent immobilization of Kluyveromyces fragilis beta-galactosidase on magnetic nanosized epoxy support for synthesis of galacto-oligosaccharide
    • Liu H, Liu J, Tan B, Zhou F, Qin Y, Yang R. 2012 Covalent immobilization of Kluyveromyces fragilis beta-galactosidase on magnetic nanosized epoxy support for synthesis of galacto-oligosaccharide. Bioprocess Biosyst. Eng. 35, 1287-1295. (doi:10.1007/s00449-012-0716-2)
    • (2012) Bioprocess Biosyst. Eng. , vol.35 , pp. 1287-1295
    • Liu, H.1    Liu, J.2    Tan, B.3    Zhou, F.4    Qin, Y.5    Yang, R.6
  • 151
    • 84862795741 scopus 로고    scopus 로고
    • B-Galactosidase-immobilised microreactor fabricated using a novel technique for enzyme immobilization and its application for continuous synthesis of lactulose
    • Song YS, Shin HY, Lee JY, Park C, Kim SW. 2012 b-Galactosidase-immobilised microreactor fabricated using a novel technique for enzyme immobilization and its application for continuous synthesis of lactulose. Food Chem. 133, 611-617. (doi:10.1016/j.foodchem.2012.01.096)
    • (2012) Food Chem , vol.133 , pp. 611-617
    • Song, Y.S.1    Shin, H.Y.2    Lee, J.Y.3    Park, C.4    Kim, S.W.5
  • 152
    • 84864283778 scopus 로고    scopus 로고
    • Recyclable biocatalytic composites of lipaselinked magnetic macro-/nano-particles for glycerol carbonate synthesis
    • Tudorache M, Protesescu L, Negoi A, Parvulescu VI. 2012 Recyclable biocatalytic composites of lipaselinked magnetic macro-/nano-particles for glycerol carbonate synthesis. Appl. Catal. A Gen. 437-438, 90-95. (doi:10.1016/j.apcata.2012.06.016)
    • (2012) Appl. Catal. A Gen. , vol.437-438 , pp. 90-95
    • Tudorache, M.1    Protesescu, L.2    Negoi, A.3    Parvulescu, V.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.