메뉴 건너뛰기




Volumn 115, Issue , 2012, Pages 164-171

Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials

Author keywords

Carbon nanotubes; Esterase; Graphene oxide; Immobilization; Lipase

Indexed keywords

BIOCHEMICAL CHARACTERIZATION; CARBON-BASED; CATALYTIC BEHAVIOR; ESTERASE; ESTERIFICATION ACTIVITIES; FUNCTIONALIZED; GRAPHENE OXIDES; HELICAL CONTENT; IMMOBILIZATION SUPPORT; IMMOBILIZED ENZYME; NANOMATERIAL; OPERATIONAL STABILITY; SECONDARY STRUCTURES;

EID: 84858340798     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2011.11.007     Document Type: Article
Times cited : (141)

References (36)
  • 1
    • 36649017886 scopus 로고    scopus 로고
    • Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes
    • Asuri P., Bale S.S., Pangule R.C., Shah D.A., Kane R.S., Dordick J.S. Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes. Langmuir 2007, 23(24):12318-12321.
    • (2007) Langmuir , vol.23 , Issue.24 , pp. 12318-12321
    • Asuri, P.1    Bale, S.S.2    Pangule, R.C.3    Shah, D.A.4    Kane, R.S.5    Dordick, J.S.6
  • 3
    • 33745748175 scopus 로고    scopus 로고
    • Increasing protein stability through control of the nanoscale environment
    • Asuri P., Karajanagi S.S., Yang H., Yim T.J., Kane R.S., Dordick J.S. Increasing protein stability through control of the nanoscale environment. Langmuir 2006, 22(13):5833-5836.
    • (2006) Langmuir , vol.22 , Issue.13 , 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
  • 4
    • 27744504244 scopus 로고    scopus 로고
    • Applications of carbon nanotubes in drug delivery
    • Bianco A., Kostarelos K., Prato M. Applications of carbon nanotubes in drug delivery. Curr. Opin. Chem. Biol. 2005, 9(6):674-679.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , Issue.6 , pp. 674-679
    • Bianco, A.1    Kostarelos, K.2    Prato, M.3
  • 5
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: classification, properties and application in biocatalysis
    • Bornscheuer U.T. Microbial carboxyl esterases: classification, properties and application in biocatalysis. FEMS Microbiol. Rev. 2002, 26(1):73-81.
    • (2002) FEMS Microbiol. Rev. , vol.26 , Issue.1 , pp. 73-81
    • Bornscheuer, U.T.1
  • 6
    • 0041841504 scopus 로고    scopus 로고
    • Graphite oxide: chemical reduction to graphite and surface modification with primary aliphatic amines and amino acids
    • Bourlinos A.B., Gournis D., Petridis D., Szabó T., Szeri A., Dékány I. Graphite oxide: chemical reduction to graphite and surface modification with primary aliphatic amines and amino acids. Langmuir 2003, 19(15):6050-6055.
    • (2003) Langmuir , vol.19 , Issue.15 , pp. 6050-6055
    • Bourlinos, A.B.1    Gournis, D.2    Petridis, D.3    Szabó, T.4    Szeri, A.5    Dékány, I.6
  • 7
    • 67649194837 scopus 로고    scopus 로고
    • The influence of carbon nanotubes on enzyme activity and structure: investigation of different immobilization procedures through enzyme kinetics and circular dichroism studies
    • Cang-Rong J.T., Pastorin G. The influence of carbon nanotubes on enzyme activity and structure: investigation of different immobilization procedures through enzyme kinetics and circular dichroism studies. Nanotechnology 2009, 20(25).
    • (2009) Nanotechnology , vol.20 , Issue.25
    • Cang-Rong, J.T.1    Pastorin, G.2
  • 8
    • 33744901695 scopus 로고    scopus 로고
    • Multi-walled carbon nanotubes reinforced nylon 6 composites
    • Chen G.-X., Kim H.-S., Park B.H., Yoon J.-S. Multi-walled carbon nanotubes reinforced nylon 6 composites. Polymer 2006, 47(13):4760-4767.
    • (2006) Polymer , vol.47 , Issue.13 , pp. 4760-4767
    • Chen, G.-X.1    Kim, H.-S.2    Park, B.H.3    Yoon, J.-S.4
  • 9
    • 55249126836 scopus 로고    scopus 로고
    • Covalent immobilization of proteins on carbon nanotubes using the cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide - a critical assessment
    • Gao Y., Kyratzis I. Covalent immobilization of proteins on carbon nanotubes using the cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide - a critical assessment. Bioconj. Chem. 2008, 19(10):1945-1950.
    • (2008) Bioconj. Chem. , vol.19 , Issue.10 , pp. 1945-1950
    • Gao, Y.1    Kyratzis, I.2
  • 10
    • 0037008979 scopus 로고    scopus 로고
    • Activity of lipases and esterases towards tertiary alcohols: insights into structure-function relationships
    • Henke E., Pleiss J., Bornscheuer U.T. Activity of lipases and esterases towards tertiary alcohols: insights into structure-function relationships. Angew. Chem., Int. Ed. 2002, 41(17):3211-3213.
    • (2002) Angew. Chem., Int. Ed. , vol.41 , Issue.17 , pp. 3211-3213
    • Henke, E.1    Pleiss, J.2    Bornscheuer, U.T.3
  • 11
    • 0036324633 scopus 로고    scopus 로고
    • Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon
    • Hotta Y., Ezaki S., Atomi H., Imanaka T. Extremely stable and versatile carboxylesterase from a hyperthermophilic archaeon. Appl. Environ. Microbiol. 2002, 68(8):3925-3931.
    • (2002) Appl. Environ. Microbiol. , vol.68 , Issue.8 , pp. 3925-3931
    • Hotta, Y.1    Ezaki, S.2    Atomi, H.3    Imanaka, T.4
  • 13
    • 11144230048 scopus 로고    scopus 로고
    • Structure and function of enzymes adsorbed onto single-walled carbon nanotubes
    • Karajanagi S.S., Vertegel A.A., Kane R.S., Dordick J.S. Structure and function of enzymes adsorbed onto single-walled carbon nanotubes. Langmuir 2004, 20(26):11594-11599.
    • (2004) Langmuir , vol.20 , Issue.26 , pp. 11594-11599
    • Karajanagi, S.S.1    Vertegel, A.A.2    Kane, R.S.3    Dordick, J.S.4
  • 14
    • 77958071557 scopus 로고    scopus 로고
    • Graphene versus carbon nanotubes for chemical sensor and fuel cell applications
    • Kauffman D.R., Star A. Graphene versus carbon nanotubes for chemical sensor and fuel cell applications. Analyst 2010, 135(11):2790-2797.
    • (2010) Analyst , vol.135 , Issue.11 , pp. 2790-2797
    • Kauffman, D.R.1    Star, A.2
  • 15
    • 53949106970 scopus 로고    scopus 로고
    • Nanobiocatalysis and its potential applications
    • Kim J., Grate J.W., Wang P. Nanobiocatalysis and its potential applications. Trends Biotechnol. 2008, 26(11):639-646.
    • (2008) Trends Biotechnol. , vol.26 , Issue.11 , pp. 639-646
    • Kim, J.1    Grate, J.W.2    Wang, P.3
  • 17
    • 50349099708 scopus 로고    scopus 로고
    • An electrochemical sensor for detection of laccase activities from Penicillium simplicissimum in compost based on carbon nanotube modified glassy carbon electrode
    • Liu J.X., Zhou W.J., Gong J.L., Tang L., Zhang Y., Yu H.Y., Wang B., Xu X.M., Zeng G.M. An electrochemical sensor for detection of laccase activities from Penicillium simplicissimum in compost based on carbon nanotube modified glassy carbon electrode. Bioresour. Technol. 2008, 99(18):8748-8751.
    • (2008) Bioresour. Technol. , vol.99 , Issue.18 , pp. 8748-8751
    • Liu, J.X.1    Zhou, W.J.2    Gong, J.L.3    Tang, L.4    Zhang, Y.5    Yu, H.Y.6    Wang, B.7    Xu, X.M.8    Zeng, G.M.9
  • 18
    • 42049092775 scopus 로고    scopus 로고
    • Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses
    • Menaa B., Herrero M., Rives V., Lavrenko M., Eggers D.K. Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses. Biomaterials 2008, 29(18):2710-2718.
    • (2008) Biomaterials , vol.29 , Issue.18 , pp. 2710-2718
    • Menaa, B.1    Herrero, M.2    Rives, V.3    Lavrenko, M.4    Eggers, D.K.5
  • 20
    • 41749116115 scopus 로고    scopus 로고
    • Protein binding by functionalized multiwalled carbon nanotubes is governed by the surface chemistry of both parties and the nanotube diameter
    • Mu Q., Liu W., Xing Y., Zhou H., Li Z., Zhang Y., Ji L., Wang F., Si Z., Zhang B., Yan B. Protein binding by functionalized multiwalled carbon nanotubes is governed by the surface chemistry of both parties and the nanotube diameter. J. Phys. Chem. C 2008, 112(9):3300-3307.
    • (2008) J. Phys. Chem. C , vol.112 , Issue.9 , pp. 3300-3307
    • Mu, Q.1    Liu, W.2    Xing, Y.3    Zhou, H.4    Li, Z.5    Zhang, Y.6    Ji, L.7    Wang, F.8    Si, Z.9    Zhang, B.10    Yan, B.11
  • 21
    • 12844274977 scopus 로고    scopus 로고
    • Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy
    • Natalello A., Ami D., Brocca S., Lotti M., Doglia S.M. Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy. Biochem. J. 2005, 385(2):511-517.
    • (2005) Biochem. J. , vol.385 , Issue.2 , pp. 511-517
    • Natalello, A.1    Ami, D.2    Brocca, S.3    Lotti, M.4    Doglia, S.M.5
  • 22
    • 67049114637 scopus 로고    scopus 로고
    • Chemical methods for the production of graphenes
    • Park S., Ruoff R.S. Chemical methods for the production of graphenes. Nat. Nanotechnol. 2009, 4(4):217-224.
    • (2009) Nat. Nanotechnol. , vol.4 , Issue.4 , pp. 217-224
    • Park, S.1    Ruoff, R.S.2
  • 24
    • 77955614043 scopus 로고    scopus 로고
    • Water-in-ionic liquid microemulsion-based organogels as novel matrices for enzyme immobilization
    • Pavlidis I.V., Tzafestas K., Stamatis H. Water-in-ionic liquid microemulsion-based organogels as novel matrices for enzyme immobilization. Biotechnol. J. 2010, 5(8):805-812.
    • (2010) Biotechnol. J. , vol.5 , Issue.8 , pp. 805-812
    • Pavlidis, I.V.1    Tzafestas, K.2    Stamatis, H.3
  • 26
    • 67649814702 scopus 로고    scopus 로고
    • XPS study and physico-chemical properties of nitrogen-enriched microporous activated carbon from high volatile bituminous coal
    • Pietrzak R. XPS study and physico-chemical properties of nitrogen-enriched microporous activated carbon from high volatile bituminous coal. Fuel 2009, 88(10):1871-1877.
    • (2009) Fuel , vol.88 , Issue.10 , pp. 1871-1877
    • Pietrzak, R.1
  • 28
    • 34247487327 scopus 로고    scopus 로고
    • Can an inactivating agent increase enzyme activity in organic solvent? Effects of 18-crown-6 on lipase activity, enantioselectivity, and conformation
    • Secundo F., Barletta G.L., Dumitriu E., Carrea G. Can an inactivating agent increase enzyme activity in organic solvent? Effects of 18-crown-6 on lipase activity, enantioselectivity, and conformation. Biotechnol. Bioeng. 2007, 97(1):12-18.
    • (2007) Biotechnol. Bioeng. , vol.97 , Issue.1 , pp. 12-18
    • Secundo, F.1    Barletta, G.L.2    Dumitriu, E.3    Carrea, G.4
  • 29
    • 0002990922 scopus 로고    scopus 로고
    • Functionalization of carbon nanotubes for biocompatibility and biomolecular recognition
    • Shim M., Kam N.W.S., Chen R.J., Li Y., Dai H. Functionalization of carbon nanotubes for biocompatibility and biomolecular recognition. Nano Lett. 2002, 2(4):285-288.
    • (2002) Nano Lett. , vol.2 , Issue.4 , pp. 285-288
    • Shim, M.1    Kam, N.W.S.2    Chen, R.J.3    Li, Y.4    Dai, H.5
  • 30
    • 0022186670 scopus 로고
    • Measurement of protein using bicinchoninic acid
    • Smith P.K., Krohn R.I., Hermanson G.T. Measurement of protein using bicinchoninic acid. Anal. Biochem. 1985, 150(1):76-85.
    • (1985) Anal. Biochem. , vol.150 , Issue.1 , pp. 76-85
    • Smith, P.K.1    Krohn, R.I.2    Hermanson, G.T.3
  • 31
    • 34347206354 scopus 로고    scopus 로고
    • Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt
    • Soliman N.A., Knoll M., Abdel-Fattah Y.R., Schmid R.D., Lange S. Molecular cloning and characterization of thermostable esterase and lipase from Geobacillus thermoleovorans YN isolated from desert soil in Egypt. Process Biochem. 2007, 42(7):1090-1100.
    • (2007) Process Biochem. , vol.42 , Issue.7 , pp. 1090-1100
    • Soliman, N.A.1    Knoll, M.2    Abdel-Fattah, Y.R.3    Schmid, R.D.4    Lange, S.5
  • 33
    • 77955627031 scopus 로고    scopus 로고
    • Lipase immobilization on smectite nanoclays: characterization and application to the epoxidation of α-pinene
    • Tzialla A.A., Pavlidis I.V., Felicissimo M.P., Rudolf P., Gournis D., Stamatis H. Lipase immobilization on smectite nanoclays: characterization and application to the epoxidation of α-pinene. Bioresour. Technol. 2010, 101:1587-1594.
    • (2010) Bioresour. Technol. , vol.101 , pp. 1587-1594
    • Tzialla, A.A.1    Pavlidis, I.V.2    Felicissimo, M.P.3    Rudolf, P.4    Gournis, D.5    Stamatis, H.6
  • 35
    • 64849106445 scopus 로고    scopus 로고
    • 4-chitosan nanoparticles for lipase immobilization by cross-linking and oxidation in aqueous solution
    • 4-chitosan nanoparticles for lipase immobilization by cross-linking and oxidation in aqueous solution. Bioresour. Technol. 2009, 100(14):3459-3464.
    • (2009) Bioresour. Technol. , vol.100 , Issue.14 , pp. 3459-3464
    • Wu, Y.1    Wang, Y.2    Luo, G.3    Dai, Y.4
  • 36
    • 77951678756 scopus 로고    scopus 로고
    • Graphene oxide as a matrix for enzyme immobilization
    • Zhang J., Zhang F., Yang H., Huang X., Liu H., Guo S. Graphene oxide as a matrix for enzyme immobilization. Langmuir 2010, 26(9):6083-6085.
    • (2010) Langmuir , vol.26 , Issue.9 , pp. 6083-6085
    • Zhang, J.1    Zhang, F.2    Yang, H.3    Huang, X.4    Liu, H.5    Guo, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.