메뉴 건너뛰기




Volumn 30, Issue 4, 2014, Pages 828-836

Enhanced conjugation of Candida rugosa lipase onto multiwalled carbon nanotubes using reverse micelles as attachment medium and application in nonaqueous biocatalysis

Author keywords

Candida rugosa lipase; Multiwalled carbon nanotubes; Pentyl valerate; Reverse micelles

Indexed keywords

AMINATION; CANDIDA; ESTERIFICATION; ESTERS; FOURIER TRANSFORMS; MICELLES; MULTIWALLED CARBON NANOTUBES (MWCN); NANOTUBES; SPECTROSCOPIC ANALYSIS; TRANSMISSION ELECTRON MICROSCOPY;

EID: 84904743889     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1929     Document Type: Article
Times cited : (12)

References (41)
  • 1
    • 27844518415 scopus 로고    scopus 로고
    • Nanostructures for enzyme stabilization
    • Kim JB, Grate JW, 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
  • 2
    • 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
  • 3
    • 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
  • 4
    • 79956032803 scopus 로고    scopus 로고
    • High-purity carbon nanotube synthesis method by an arc discharging in magnetic field
    • Anazawa K, Shimotani K, Manabe C, Watanabe H, Shimizu M. High-purity carbon nanotube synthesis method by an arc discharging in magnetic field. Appl Phys Lett. 2002;81:739-741.
    • (2002) Appl Phys Lett. , vol.81 , pp. 739-741
    • Anazawa, K.1    Shimotani, K.2    Manabe, C.3    Watanabe, H.4    Shimizu, M.5
  • 5
  • 6
    • 0036377140 scopus 로고    scopus 로고
    • A scalable process for production of single-walled carbon nanotubes (SWNTS) by catalytic disproportionation of CO on a solid catalyst
    • Resasco D, Alvarez W, Pompeo F, Balzano L, Herrera J, Kitiyanan B. A scalable process for production of single-walled carbon nanotubes (SWNTS) by catalytic disproportionation of CO on a solid catalyst. J Nanopart Res. 2002;4:131-136.
    • (2002) J Nanopart Res. , vol.4 , pp. 131-136
    • Resasco, D.1    Alvarez, W.2    Pompeo, F.3    Balzano, L.4    Herrera, J.5    Kitiyanan, B.6
  • 10
    • 36749045733 scopus 로고    scopus 로고
    • Surface modification of multi-walled carbon nanotubes using 3-aminopropyltriethoxysilane
    • Kathi J, Rhee KY. Surface modification of multi-walled carbon nanotubes using 3-aminopropyltriethoxysilane. J Mater Sci. 2008;43:33-37.
    • (2008) J Mater Sci. , vol.43 , pp. 33-37
    • Kathi, J.1    Rhee, K.Y.2
  • 11
    • 0000308990 scopus 로고    scopus 로고
    • Attaching proteins to carbon nanotubes via diimide-activated amidation
    • Huang W, Taylor S, Fu K, Lin Y, Zhang D, Hanks TW. Attaching proteins to carbon nanotubes via diimide-activated amidation. Nano Lett. 2002;2:311-314.
    • (2002) Nano Lett. , vol.2 , pp. 311-314
    • Huang, W.1    Taylor, S.2    Fu, K.3    Lin, Y.4    Zhang, D.5    Hanks, T.W.6
  • 14
    • 0026143707 scopus 로고
    • Immobilization of acetylcholinesterase on solid surfaces: chemistry and activity studies
    • Bhatia S, Cooney M, Shriverlake L, Fare T, Ligler F. Immobilization of acetylcholinesterase on solid surfaces: chemistry and activity studies. Sens Actuators B. 1991;3:311-317.
    • (1991) Sens Actuators B , vol.3 , pp. 311-317
    • Bhatia, S.1    Cooney, M.2    Shriverlake, L.3    Fare, T.4    Ligler, F.5
  • 15
    • 77955708538 scopus 로고    scopus 로고
    • Immobilization of laccase onto 1-aminopyrene functionalized carbon nanotubes and their electrocatalytic activity for oxygen reduction
    • Pang HL, Liu J, Hu D, Zhang XH, Chen JH. Immobilization of laccase onto 1-aminopyrene functionalized carbon nanotubes and their electrocatalytic activity for oxygen reduction. Electrochim Acta. 2010;55:6611-6616.
    • (2010) Electrochim Acta. , vol.55 , pp. 6611-6616
    • Pang, H.L.1    Liu, J.2    Hu, D.3    Zhang, X.H.4    Chen, J.H.5
  • 16
    • 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
  • 17
    • 78649335075 scopus 로고    scopus 로고
    • Amperometric biosensor for aflatoxin B1 based on aflatoxin-oxidase immobilized on multiwalled carbon nanotubes
    • Li SC, Chen JH, Cao H, Yao DS, Liu DL. Amperometric biosensor for aflatoxin B1 based on aflatoxin-oxidase immobilized on multiwalled carbon nanotubes. Food Control. 2011;22:43-49.
    • (2011) Food Control. , vol.22 , pp. 43-49
    • Li, S.C.1    Chen, J.H.2    Cao, H.3    Yao, D.S.4    Liu, D.L.5
  • 18
    • 71849086388 scopus 로고    scopus 로고
    • Immobilization of horseradish peroxidase on multiwalled carbon nanotubes and its enzymatic stability
    • Kim BJ, Kang BK, Bahk YY, Yoo KH, Lim KJ. Immobilization of horseradish peroxidase on multiwalled carbon nanotubes and its enzymatic stability. Curr Appl Phys. 2009;9:263-265.
    • (2009) Curr Appl Phys. , vol.9 , pp. 263-265
    • Kim, B.J.1    Kang, B.K.2    Bahk, Y.Y.3    Yoo, K.H.4    Lim, K.J.5
  • 19
    • 38549083005 scopus 로고    scopus 로고
    • Enhancement of lipase activity in non-aqueous media upon immobilization on multi-walled carbon nanotubes
    • Shah S, Solanki K, Gupta MN. Enhancement of lipase activity in non-aqueous media upon immobilization on multi-walled carbon nanotubes. Chem Cent J. 2007;1:30.
    • (2007) Chem Cent J. , vol.1 , pp. 30
    • Shah, S.1    Solanki, K.2    Gupta, M.N.3
  • 20
    • 78650330875 scopus 로고    scopus 로고
    • Lipase covalently attached to multi-walled carbon nanotubes as an efficient catalyst in organic solvent
    • Ji P, Tan H, Xu X, Feng W. Lipase covalently attached to multi-walled 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
  • 21
    • 84858340798 scopus 로고    scopus 로고
    • Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials
    • Pavlidis IV, Vorhaben T, Tsoufis T, Rudolf P, Bornscheuer UT, Gournis D, Stamatis H. Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials. Bioresour Technol. 2012;115:164-171.
    • (2012) Bioresour Technol. , vol.115 , pp. 164-171
    • Pavlidis, I.V.1    Vorhaben, T.2    Tsoufis, T.3    Rudolf, P.4    Bornscheuer, U.T.5    Gournis, D.6    Stamatis, H.7
  • 22
    • 34748816278 scopus 로고    scopus 로고
    • Covalent functionalization of multi-walled carbon nanotubes by lipase
    • Shi Q, Yang D, Su Y, Li J, Jiang Z, Jiang Y, Yuan W. Covalent functionalization of multi-walled carbon nanotubes by lipase. J Nanopart Res. 2007;9:1205-1210.
    • (2007) J Nanopart Res. , vol.9 , pp. 1205-1210
    • Shi, Q.1    Yang, D.2    Su, Y.3    Li, J.4    Jiang, Z.5    Jiang, Y.6    Yuan, W.7
  • 23
    • 17444384812 scopus 로고    scopus 로고
    • A microwave-assisted microassay for lipases
    • Jain P, Jain S, Gupta MN. A microwave-assisted microassay for lipases. Anal Bioanal Chem. 2005;381:1480-1482.
    • (2005) Anal Bioanal Chem. , vol.381 , pp. 1480-1482
    • Jain, P.1    Jain, S.2    Gupta, M.N.3
  • 24
    • 75449100095 scopus 로고    scopus 로고
    • Synthesis of the 'green apple ester' ethyl valerate in organic solvents by Candida rugosa lipase immobilized in MBGs in organic solvents: effects of immobilization and reaction parameters
    • Raghavendra T, Sayania D, Madamwar D. Synthesis of the 'green apple ester' ethyl valerate in organic solvents by Candida rugosa lipase immobilized in MBGs in organic solvents: effects of immobilization and reaction parameters. J Mol Catal B. 2010;63:31-38.
    • (2010) J Mol Catal B. , vol.63 , pp. 31-38
    • Raghavendra, T.1    Sayania, D.2    Madamwar, D.3
  • 25
    • 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. Robust nanobioconjugates of Candida antarctica lipase B-multiwalled carbon nanotubes: characterization and application for multiple usages in non-aqueous biocatalysis. Bioresour Technol. 2013;140:103-110.
    • (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
  • 26
    • 33947512734 scopus 로고    scopus 로고
    • Functionalized multi-walled carbon nanotubes as affinity ligands
    • Yu L, Li CM, Zhou Q, Gan Y, Bao QL. Functionalized multi-walled carbon nanotubes as affinity ligands. Nanotechnology. 2007;18:115614.
    • (2007) Nanotechnology. , vol.18 , pp. 115614
    • Yu, L.1    Li, C.M.2    Zhou, Q.3    Gan, Y.4    Bao, Q.L.5
  • 27
    • 21344465467 scopus 로고    scopus 로고
    • Efficient probe immobilization on poly(dimethylsiloxane) for sensitive detection of proteins
    • Yu L, Li CM, Zhou Q. Efficient probe immobilization on poly(dimethylsiloxane) for sensitive detection of proteins. Front Biosci. 2005;10:2848-2855.
    • (2005) Front Biosci. , vol.10 , pp. 2848-2855
    • Yu, L.1    Li, C.M.2    Zhou, Q.3
  • 30
    • 0032825993 scopus 로고    scopus 로고
    • Non-conventional hydrolase chemistry: amide and carbamate bond formation catalyzed by lipases
    • Gotor V. Non-conventional hydrolase chemistry: amide and carbamate bond formation catalyzed by lipases. Bioorg Med Chem. 1999;7:2189-2197.
    • (1999) Bioorg Med Chem. , vol.7 , pp. 2189-2197
    • Gotor, V.1
  • 31
    • 0037071912 scopus 로고    scopus 로고
    • Lipases and (R)-oxynitrilases: useful tools in organic synthesis
    • Gotor V. Lipases and (R)-oxynitrilases: useful tools in organic synthesis. J Biotechnol. 2002;96:35-42.
    • (2002) J Biotechnol. , vol.96 , pp. 35-42
    • Gotor, V.1
  • 32
    • 26844576835 scopus 로고    scopus 로고
    • Amide bond formation and peptide coupling
    • Montalbetti CAGN, Falque V. Amide bond formation and peptide coupling. Tetrahedron. 2005;61:10827-10852.
    • (2005) Tetrahedron , vol.61 , pp. 10827-10852
    • Montalbetti, C.A.G.N.1    Falque, V.2
  • 33
    • 76249122876 scopus 로고    scopus 로고
    • Formation and hydrolysis of amide bonds by lipase A from Candida antarctica; exceptional features
    • Liljeblad A, Kallio P, Vainio M, Niemi J, Kanerva LT. Formation and hydrolysis of amide bonds by lipase A from Candida antarctica; exceptional features. Org Biomol Chem. 2010;8:886-895.
    • (2010) Org Biomol Chem. , vol.8 , pp. 886-895
    • Liljeblad, A.1    Kallio, P.2    Vainio, M.3    Niemi, J.4    Kanerva, L.T.5
  • 34
    • 27644440942 scopus 로고    scopus 로고
    • Raman and IR spectroscopy of chemically processed single-walled carbon nanotubes
    • Kim UJ, Furtado CA, Liu C, Chen G, Eklund PC. Raman and IR spectroscopy of chemically processed single-walled carbon nanotubes. J Am Chem Soc. 2005;127:15437-15445.
    • (2005) J Am Chem Soc. , vol.127 , pp. 15437-15445
    • Kim, U.J.1    Furtado, C.A.2    Liu, C.3    Chen, G.4    Eklund, P.C.5
  • 35
    • 44449150180 scopus 로고    scopus 로고
    • IR study on surface chemical properties of catalytic grown carbon nanotubes and nanofibers
    • Teng L-h, Tang T-d. IR study on surface chemical properties of catalytic grown carbon nanotubes and nanofibers. J Zhejiang Univ Sci A. 2008;9:720-726.
    • (2008) J Zhejiang Univ Sci A. , vol.9 , pp. 720-726
    • Teng, L.-H.1    Tang, T.-D.2
  • 37
    • 0028773288 scopus 로고
    • The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica
    • Uppenberg J, Trier Hanse M, Patkar S, Jones TA. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure. 1994;2:293-308.
    • (1994) Structure. , vol.2 , pp. 293-308
    • Uppenberg, J.1    Trier Hanse, M.2    Patkar, S.3    Jones, T.A.4
  • 38
    • 0029148636 scopus 로고
    • On the interfacial activation of Candida antarctica lipase-a and lipase-b as compared with Humicola lanuginosa lipase
    • Martinelle M, Holmquist M, Hult K. On the interfacial activation of Candida antarctica lipase-a and lipase-b as compared with Humicola lanuginosa lipase. Biochim Biophys Acta: Lipid Lipid Metab. 1995;1258:272-276.
    • (1995) Biochim Biophys Acta: Lipid Lipid Metab. , vol.1258 , pp. 272-276
    • Martinelle, M.1    Holmquist, M.2    Hult, K.3
  • 39
    • 0032701223 scopus 로고    scopus 로고
    • Structure and conformational flexibility of Candida rugosa lipase
    • Cygler M, Schrag JD. Structure and conformational flexibility of Candida rugosa lipase. Biochim Biophys Acta. 1999;2-3:205-214.
    • (1999) Biochim Biophys Acta , vol.2-3 , pp. 205-214
    • Cygler, M.1    Schrag, J.D.2
  • 40
    • 84856173455 scopus 로고    scopus 로고
    • Covalently functionalized single-walled carbon nanotubes at reverse micellar interface: a strategy to improve lipase activity
    • Ghosh M, Maiti S, Dutta S, Das D, Das PK. Covalently functionalized single-walled carbon nanotubes at reverse micellar interface: a strategy to improve lipase activity. Langmuir. 2012;28:1715-1724.
    • (2012) Langmuir. , vol.28 , pp. 1715-1724
    • Ghosh, M.1    Maiti, S.2    Dutta, S.3    Das, D.4    Das, P.K.5
  • 41
    • 65249131130 scopus 로고    scopus 로고
    • Superior activity of structurally deprived enzyme-carbon nanotube hybrids in cationic reverse micelles
    • Das D, Das PK. Superior activity of structurally deprived enzyme-carbon nanotube hybrids in cationic reverse micelles. Langmuir. 2009;25:4421-4428.
    • (2009) Langmuir. , vol.25 , pp. 4421-4428
    • Das, D.1    Das, P.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.