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Volumn 115, Issue , 2012, Pages 172-176

Lipase immobilized on magnetic multi-walled carbon nanotubes

Author keywords

Immobilization; Lipase; Magnetic carbon nanotubes; Resolution

Indexed keywords

ENZYMATIC ACTIVITIES; IMMOBILIZED LIPASE; IMPREGNATION METHODS; MAGNETIC IRON OXIDE NANOPARTICLES; MAGNETIC NANOTUBES; STRUCTURAL CHANGE; XPS SPECTRA; XRD PATTERNS; YARROWIA LIPOLYTICA;

EID: 84861460395     PISSN: 09608524     EISSN: 18732976     Source Type: Journal    
DOI: 10.1016/j.biortech.2011.10.066     Document Type: Article
Times cited : (92)

References (38)
  • 1
    • 77955502497 scopus 로고    scopus 로고
    • Kinetic resolution of a drug precursor by Burkholderia cepacia lipase immobilized by different methodologies on superparamagnetic nanoparticles
    • Andrade L.H., Rebelo L.P., Nettob C.G.C.M., Toma H.E. Kinetic resolution of a drug precursor by Burkholderia cepacia lipase immobilized by different methodologies on superparamagnetic nanoparticles. J. Mol. Catal. B: Enzym. 2010, 66:55-62.
    • (2010) J. Mol. Catal. B: Enzym. , vol.66 , pp. 55-62
    • Andrade, L.H.1    Rebelo, L.P.2    Nettob, C.G.C.M.3    Toma, H.E.4
  • 3
    • 27144487754 scopus 로고    scopus 로고
    • Resolution of (±)-menthol by immobilized Candida rugosa lipase on superparamagnetic nanoparticles
    • Bai S., Guo Z., Liu W., Sun Y. Resolution of (±)-menthol by immobilized Candida rugosa lipase on superparamagnetic nanoparticles. Food Chem. 2006, 96:1-7.
    • (2006) Food Chem. , vol.96 , pp. 1-7
    • Bai, S.1    Guo, Z.2    Liu, W.3    Sun, Y.4
  • 5
    • 58149263264 scopus 로고    scopus 로고
    • Arthrobacter sp. lipase immobilization on magnetic sol-gel composite supports for enantioselectivity improvement
    • Chaubey A., Parshad R., Taneja S.C., Qazi G.N. Arthrobacter sp. lipase immobilization on magnetic sol-gel composite supports for enantioselectivity improvement. Process Biochem. 2009, 44:154-160.
    • (2009) Process Biochem. , vol.44 , pp. 154-160
    • Chaubey, A.1    Parshad, R.2    Taneja, S.C.3    Qazi, G.N.4
  • 8
    • 77956179565 scopus 로고    scopus 로고
    • Analysis of a reactive extraction process for biodiesel production using a lipase immobilized on magnetic nanostructures
    • Dussan K.J., Cardona C.A., Giraldo O.H., Gutiérrez L.F., Pérez V.H. Analysis of a reactive extraction process for biodiesel production using a lipase immobilized on magnetic nanostructures. Bioresour. Technol. 2011, 101:9542-9549.
    • (2011) Bioresour. Technol. , vol.101 , pp. 9542-9549
    • Dussan, K.J.1    Cardona, C.A.2    Giraldo, O.H.3    Gutiérrez, L.F.4    Pérez, V.H.5
  • 9
    • 41049111739 scopus 로고    scopus 로고
    • Application of multi-walled carbon nanotubes as efficient support to NiMo hydrotreating catalyst
    • Eswaramoorthi I., Sundaramurthy V., Das N., Dalai A.K., Adjaye J. Application of multi-walled carbon nanotubes as efficient support to NiMo hydrotreating catalyst. Appl. Catal., A: Gen. 2008, 339:187-195.
    • (2008) Appl. Catal., A: Gen. , vol.339 , pp. 187-195
    • Eswaramoorthi, I.1    Sundaramurthy, V.2    Das, N.3    Dalai, A.K.4    Adjaye, J.5
  • 10
    • 80053439206 scopus 로고    scopus 로고
    • Enzymes immobilized on carbon nanotubes
    • Feng W., Ji P. Enzymes immobilized on carbon nanotubes. Biotechnol. Adv. 2011, 29:889-895.
    • (2011) Biotechnol. Adv. , vol.29 , pp. 889-895
    • Feng, W.1    Ji, P.2
  • 11
    • 33645513452 scopus 로고    scopus 로고
    • A facile route for the preparation of superparamagnetic porous carbons
    • Fuertes A.B., Tartaj P. A facile route for the preparation of superparamagnetic porous carbons. Chem. Mater. 2006, 18:1675-1679.
    • (2006) Chem. Mater. , vol.18 , pp. 1675-1679
    • Fuertes, A.B.1    Tartaj, P.2
  • 12
    • 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. Bioconjug. Chem. 2008, 19:1945-1950.
    • (2008) Bioconjug. Chem. , vol.19 , pp. 1945-1950
    • Gao, Y.1    Kyratzis, I.2
  • 13
    • 77955548078 scopus 로고    scopus 로고
    • Hybrid nanogenerator for concurrently harvesting biomechanical and biochemical energy
    • Hansen B.J., Liu Y., Yang R., Wang Z. Hybrid nanogenerator for concurrently harvesting biomechanical and biochemical energy. ACSNANO 2010, 4:3647-3652.
    • (2010) ACSNANO , vol.4 , pp. 3647-3652
    • Hansen, B.J.1    Liu, Y.2    Yang, R.3    Wang, Z.4
  • 15
    • 67650257448 scopus 로고    scopus 로고
    • Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repeated use in enzymatic synthesis of Diltiazem intermediate
    • Hu B., Pan J., Yu H.L., Liu J.W., Xu J.H. Immobilization of Serratia marcescens lipase onto amino-functionalized magnetic nanoparticles for repeated use in enzymatic synthesis of Diltiazem intermediate. Process Biochem. 2009, 44:1019-1024.
    • (2009) Process Biochem. , vol.44 , pp. 1019-1024
    • Hu, B.1    Pan, J.2    Yu, H.L.3    Liu, J.W.4    Xu, J.H.5
  • 16
    • 66149103717 scopus 로고    scopus 로고
    • Enzymatic synthesis of esculin ester in ionic liquids buffered with organic solvents
    • Hu Y., Guo Z., Lue B.M., Xu X.B. Enzymatic synthesis of esculin ester in ionic liquids buffered with organic solvents. J. Agric. Food. Chem. 2009, 57:3845-3852.
    • (2009) J. Agric. Food. Chem. , vol.57 , pp. 3845-3852
    • Hu, Y.1    Guo, Z.2    Lue, B.M.3    Xu, X.B.4
  • 17
    • 0036286862 scopus 로고    scopus 로고
    • Orientation and conformation of a lipase at an interface studied by molecular dynamics simulations
    • Jensen M.O., Jensen T.R., Kjaer K., Bjonholm T., Mouritsen O.G., Peters G.H. Orientation and conformation of a lipase at an interface studied by molecular dynamics simulations. Biophys. J. 2002, 83:98-111.
    • (2002) Biophys. J. , vol.83 , pp. 98-111
    • Jensen, M.O.1    Jensen, T.R.2    Kjaer, K.3    Bjonholm, T.4    Mouritsen, O.G.5    Peters, G.H.6
  • 18
    • 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. Lipase covalently attached to multiwalled carbon nanotubes as an efficient catalyst in organic solvent. AIChE J. 2010, 56:3005-3011.
    • (2010) AIChE J. , vol.56 , pp. 3005-3011
    • Ji, P.1    Tan, H.2    Xu, X.3    Feng, W.4
  • 19
    • 84861454653 scopus 로고    scopus 로고
    • Lipase immobilization on ionic liquid-modified magnetic nanoparticles: ionic liquids controlled esters hydrolysis at oil-water interface
    • Jiang, Y., Guo, C., Gao, H., Xia, H., Mahmood, I., Liu, C., Liu, H., 2011. Lipase immobilization on ionic liquid-modified magnetic nanoparticles: ionic liquids controlled esters hydrolysis at oil-water interface. AIChE J. available online.
    • (2011) AIChE J. available online
    • Jiang, Y.1    Guo, C.2    Gao, H.3    Xia, H.4    Mahmood, I.5    Liu, C.6    Liu, H.7
  • 20
    • 0142073274 scopus 로고    scopus 로고
    • Catalytic behaviors of enzymes attached to nanoparticles: the effect of particle mobility
    • Jia H., Zhu G., Wang P. Catalytic behaviors of enzymes attached to nanoparticles: the effect of particle mobility. Biotechnol. Bioeng. 2003, 84:406-414.
    • (2003) Biotechnol. Bioeng. , vol.84 , pp. 406-414
    • Jia, H.1    Zhu, G.2    Wang, P.3
  • 21
  • 22
    • 27844518415 scopus 로고    scopus 로고
    • Nanostructures for enzyme stabilization
    • Kim J.B., Grate J.W., Wang P. Nanostructures for enzyme stabilization. Chem. Eng. Sci. 2006, 61:1017-1026.
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 1017-1026
    • Kim, J.B.1    Grate, J.W.2    Wang, P.3
  • 23
    • 36649003070 scopus 로고    scopus 로고
    • Catalytic activity of lipase immobilized onto ultrathin films of cellulose esters
    • Kosaka P.M., Kawano Y., El Seoud O.A., Petri D.F.S. Catalytic activity of lipase immobilized onto ultrathin films of cellulose esters. Langmuir 2007, 23:12167-12173.
    • (2007) Langmuir , vol.23 , pp. 12167-12173
    • Kosaka, P.M.1    Kawano, Y.2    El Seoud, O.A.3    Petri, D.F.S.4
  • 27
    • 48749085963 scopus 로고    scopus 로고
    • Supramolecular architectures of β-cyclodextrin-modified chitosan and pyrene derivatives mediated by carbon nanotubes and their DNA condensation
    • Liu Y., Yu Z.L., Zhang Y.M., Guo D.S., Liu Y.P. Supramolecular architectures of β-cyclodextrin-modified chitosan and pyrene derivatives mediated by carbon nanotubes and their DNA condensation. J. Am. Chem. Soc. 2008, 130:10431-10439.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 10431-10439
    • Liu, Y.1    Yu, Z.L.2    Zhang, Y.M.3    Guo, D.S.4    Liu, Y.P.5
  • 29
    • 58149352673 scopus 로고    scopus 로고
    • Esterification and hydrolytic activities of Candida rugosa lipase isoform 1 (LIP1) immobilized on celite 545, duolite A7, and sephadex G-25
    • Lumor S.E., Akoh C.C. Esterification and hydrolytic activities of Candida rugosa lipase isoform 1 (LIP1) immobilized on celite 545, duolite A7, and sephadex G-25. J. Agric. Food Chem. 2008, 56:10396-10398.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 10396-10398
    • Lumor, S.E.1    Akoh, C.C.2
  • 30
    • 31544438604 scopus 로고    scopus 로고
    • Thermal conductance of an individual single-wall carbon nanotube above room temperature
    • Pop E., Mann D., Wang Q., Goodson K., Dai H. Thermal conductance of an individual single-wall carbon nanotube above room temperature. Nano Lett. 2006, 6:96-100.
    • (2006) Nano Lett. , vol.6 , pp. 96-100
    • Pop, E.1    Mann, D.2    Wang, Q.3    Goodson, K.4    Dai, H.5
  • 31
    • 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.M., Dai H.J. Functionalization of carbon nanotubes for biocompatibility and biomolecular recognition. Nano Lett. 2002, 2:285-288.
    • (2002) Nano Lett. , vol.2 , pp. 285-288
    • Shim, M.1    Kam, N.W.S.2    Chen, R.J.3    Li, Y.M.4    Dai, H.J.5
  • 34
    • 77957328836 scopus 로고    scopus 로고
    • Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes
    • Wang L., Wei L., Chen Y., Jiang R. Specific and reversible immobilization of NADH oxidase on functionalized carbon nanotubes. J. Biotechnol. 2010, 150:57-63.
    • (2010) J. Biotechnol. , vol.150 , pp. 57-63
    • Wang, L.1    Wei, L.2    Chen, Y.3    Jiang, R.4
  • 35
    • 33947366309 scopus 로고    scopus 로고
    • Nanostructured biosensors built by layer-by-layer electrostatic assembly of enzyme-coated single-walled carbon nanotubes and redox polymers
    • Wang Y.D., Joshi P.P., Hobbs K.L., Johnson M.B., Schmidtke D.W. Nanostructured biosensors built by layer-by-layer electrostatic assembly of enzyme-coated single-walled carbon nanotubes and redox polymers. Langmuir 2006, 22:9776-9783.
    • (2006) Langmuir , vol.22 , pp. 9776-9783
    • Wang, Y.D.1    Joshi, P.P.2    Hobbs, K.L.3    Johnson, M.B.4    Schmidtke, D.W.5
  • 36
    • 13844310039 scopus 로고    scopus 로고
    • Production of lipase by repeated batch fermentation with immobilized Rhizopus arrhizus
    • Yang, X.H., Wang, B.W., Cui, F.N., Tan, W.T., 2005. Production of lipase by repeated batch fermentation with immobilized Rhizopus arrhizus. Process Biochem.
    • (2005) Process Biochem.
    • Yang, X.H.1    Wang, B.W.2    Cui, F.N.3    Tan, W.T.4
  • 37
    • 79751532883 scopus 로고    scopus 로고
    • Immobilization of Candida rugosa lipase on magnetic sol-gel composite supports for enzymatic resolution of (R, S)-naproxen methyl ester
    • Yilmaz E., Sezgin M., Yilmaz M. Immobilization of Candida rugosa lipase on magnetic sol-gel composite supports for enzymatic resolution of (R, S)-naproxen methyl ester. J. Mol. Catal. B: Enzym. 2011, 69:35-41.
    • (2011) J. Mol. Catal. B: Enzym. , vol.69 , pp. 35-41
    • Yilmaz, E.1    Sezgin, M.2    Yilmaz, M.3
  • 38
    • 66749166478 scopus 로고    scopus 로고
    • Functionalized carbon nanotubes specifically bind to α-chymotrypsin's catalytic site and regulate its enzymatic function
    • Zhang B., Xing Y., Li Z., Zhou H., Mu Q., Yan B. Functionalized carbon nanotubes specifically bind to α-chymotrypsin's catalytic site and regulate its enzymatic function. Nano Lett. 2009, 9:2280-2284.
    • (2009) Nano Lett. , vol.9 , pp. 2280-2284
    • Zhang, B.1    Xing, Y.2    Li, Z.3    Zhou, H.4    Mu, Q.5    Yan, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.