메뉴 건너뛰기




Volumn 90, Issue 9, 2015, Pages 1570-1578

A strategy for improving peroxidase stability via immobilization on surface modified multi-walled carbon nanotubes

Author keywords

Carbon nanotubes; Characterization; Immobilization; Peroxidase; Stability

Indexed keywords

CARBON; CARBON NANOTUBES; CATALYST ACTIVITY; CHARACTERIZATION; CONVERGENCE OF NUMERICAL METHODS; ENZYME ACTIVITY; ENZYME IMMOBILIZATION; ENZYMES; FUNCTIONAL GROUPS; HYDROGEN BONDS; HYDROPHOBICITY; NANOTECHNOLOGY; RADIOACTIVE WASTE VITRIFICATION; STABILITY; THERMODYNAMIC STABILITY; YARN;

EID: 84937817763     PISSN: 02682575     EISSN: 10974660     Source Type: Journal    
DOI: 10.1002/jctb.4698     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 63049107078 scopus 로고    scopus 로고
    • Potential applications of peroxidases
    • Hamid M and Rehman K, Potential applications of peroxidases. Food Chem 115:1177-1186 (2009).
    • (2009) Food Chem , vol.115 , pp. 1177-1186
    • Hamid, M.1    Rehman, K.2
  • 3
    • 33846259719 scopus 로고    scopus 로고
    • Treatment of phenolic wastewater by horseradish peroxidase immobilized by bioaffinity layering
    • Dalal S and Gupta MN, Treatment of phenolic wastewater by horseradish peroxidase immobilized by bioaffinity layering. Chemosphere 67:741-747 (2007).
    • (2007) Chemosphere , vol.67 , pp. 741-747
    • Dalal, S.1    Gupta, M.N.2
  • 4
    • 33748517080 scopus 로고    scopus 로고
    • Decolorization of melanin by lignin peroxidase from Phanerochaete chrysosporium
    • Woo S, Cho J, Lee B and Kim E, Decolorization of melanin by lignin peroxidase from Phanerochaete chrysosporium. Biotechnol Bioprocess E 9:256-260 (2004).
    • (2004) Biotechnol Bioprocess E , vol.9 , pp. 256-260
    • Woo, S.1    Cho, J.2    Lee, B.3    Kim, E.4
  • 5
    • 0343397716 scopus 로고    scopus 로고
    • Highly sensitive determination of hydrogen peroxide and peroxidase with tetrathiafulvalene-based electrodes and the application in immunosensing
    • Wendzinski F, Gründig B, Renneberg R and Spener F, Highly sensitive determination of hydrogen peroxide and peroxidase with tetrathiafulvalene-based electrodes and the application in immunosensing. Biosens Bioelectron 12:43-52 (1997).
    • (1997) Biosens Bioelectron , vol.12 , pp. 43-52
    • Wendzinski, F.1    Gründig, B.2    Renneberg, R.3    Spener, F.4
  • 6
    • 0036210356 scopus 로고    scopus 로고
    • Microfluidic chips for clinical and forensic analysis
    • Verpoorte E, Microfluidic chips for clinical and forensic analysis. Electrophoresis 23:677-712 (2002).
    • (2002) Electrophoresis , vol.23 , pp. 677-712
    • Verpoorte, E.1
  • 7
    • 80053439206 scopus 로고    scopus 로고
    • Enzymes immobilized on carbon nanotubes
    • Feng W and Ji P, Enzymes immobilized on carbon nanotubes. Biotechnol Adv 29:889-895 (2011).
    • (2011) Biotechnol Adv , vol.29 , pp. 889-895
    • Feng, W.1    Ji, P.2
  • 8
    • 84867753849 scopus 로고    scopus 로고
    • Carbon nanotubes: a review on structure and their interaction with proteins
    • Saifuddin N, Raziah AZ and Junizah AR, Carbon nanotubes: a review on structure and their interaction with proteins. J Chem 2013:18 (2013).
    • (2013) J Chem , vol.2013 , pp. 18
    • Saifuddin, N.1    Raziah, A.Z.2    Junizah, A.R.3
  • 9
    • 11144230048 scopus 로고    scopus 로고
    • Structure and function of enzymes adsorbed onto single-walled carbon nanotubes
    • Karajanagi SS, Vertegel AA, Kane RS and Dordick JS, Structure and function of enzymes adsorbed onto single-walled carbon nanotubes. Langmuir 20:11594-11599 (2004).
    • (2004) Langmuir , vol.20 , pp. 11594-11599
    • Karajanagi, S.S.1    Vertegel, A.A.2    Kane, R.S.3    Dordick, J.S.4
  • 10
    • 36649017886 scopus 로고    scopus 로고
    • Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes
    • Asuri P, Bale SS, Pangule RC, Shah DA, Kane RS and Dordick JS, Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes. Langmuir 23:12318-12321 (2007).
    • (2007) Langmuir , vol.23 , 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
  • 11
    • 0141924291 scopus 로고    scopus 로고
    • Carbon nanotubes produced by fluidized bed catalytic CVD: first approach of the process
    • Corrias M, Caussat B, Ayral A, Durand J, Kihn Y, Kalck P et al., Carbon nanotubes produced by fluidized bed catalytic CVD: first approach of the process. Chem Eng Sci 58:4475-4482 (2003).
    • (2003) Chem Eng Sci , vol.58 , pp. 4475-4482
    • Corrias, M.1    Caussat, B.2    Ayral, A.3    Durand, J.4    Kihn, Y.5    Kalck, P.6
  • 13
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC and von Hippel PH, Calculation of protein extinction coefficients from amino acid sequence data. Analyt Biochem 182:319-326 (1989).
    • (1989) Analyt Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 14
    • 84905991979 scopus 로고    scopus 로고
    • Controlling the surface chemistry of multiwalled carbon nanotubes for the production of highly efficient and stable laccase-based biocatalysts
    • Silva CG, Tavares APM, Dražić G, Silva AMT, Loureiro JM and Faria JL, Controlling the surface chemistry of multiwalled carbon nanotubes for the production of highly efficient and stable laccase-based biocatalysts. Chem Plus Chem 79:1116-1122 (2014).
    • (2014) Chem Plus Chem , vol.79 , pp. 1116-1122
    • Silva, C.G.1    Tavares, A.P.M.2    Dražić, G.3    Silva, A.M.T.4    Loureiro, J.M.5    Faria, J.L.6
  • 15
    • 0345516025 scopus 로고    scopus 로고
    • Sánchez-Montero JMa and Sinisterra JV, Thermal stabilization of immobilized lipase B from Candida antarctica on different supports: effect of water activity on enzymatic activity in organic media
    • Arroyo M, Sánchez-Montero JMa and Sinisterra JV, Thermal stabilization of immobilized lipase B from Candida antarctica on different supports: effect of water activity on enzymatic activity in organic media. Enzyme Microbiol Technol 24:3-12 (1999).
    • (1999) Enzyme Microbiol Technol , vol.24 , pp. 3-12
    • Arroyo, M.1
  • 16
    • 0022013872 scopus 로고
    • Categorization of enzyme deactivations using a series-type mechanism
    • Henley JP and Sadana A, Categorization of enzyme deactivations using a series-type mechanism. Enzyme Microbiol Technol 7:50-60 (1985).
    • (1985) Enzyme Microbiol Technol , vol.7 , pp. 50-60
    • Henley, J.P.1    Sadana, A.2
  • 17
    • 21044432132 scopus 로고    scopus 로고
    • Immobilization of β-glucosidase on carbon nanotubes
    • Gómez JM, Romero MD and Fernández TM, Immobilization of β-glucosidase on carbon nanotubes. Catal Lett 101:275-278 (2005).
    • (2005) Catal Lett , vol.101 , pp. 275-278
    • Gómez, J.M.1    Romero, M.D.2    Fernández, T.M.3
  • 18
    • 76549135118 scopus 로고    scopus 로고
    • The role of surface chemistry in catalysis with carbons
    • Figueiredo JL and Pereira MFR, The role of surface chemistry in catalysis with carbons. Catal Today 150:2-7 (2010).
    • (2010) Catal Today , vol.150 , pp. 2-7
    • Figueiredo, J.L.1    Pereira, M.F.R.2
  • 22
    • 0142106510 scopus 로고    scopus 로고
    • Direct electrochemistry of heme proteins in their layer-by-layer films with clay nanoparticles
    • Li Z and Hu N, Direct electrochemistry of heme proteins in their layer-by-layer films with clay nanoparticles. J Electroanal Chem 558:155-165 (2003).
    • (2003) J Electroanal Chem , vol.558 , pp. 155-165
    • Li, Z.1    Hu, N.2
  • 24
    • 0034717010 scopus 로고    scopus 로고
    • Enzymatic peptide synthesis in organic solvent with different zeolites as immobilization matrixes
    • Xing G-W, Li X-W, Tian G-L and Ye Y-H, Enzymatic peptide synthesis in organic solvent with different zeolites as immobilization matrixes. Tetrahedron 56:3517-3522 (2000).
    • (2000) Tetrahedron , vol.56 , pp. 3517-3522
    • Xing, G.-W.1    Li, X.-W.2    Tian, G.-L.3    Ye, Y.-H.4
  • 25
    • 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 and Kyratzis I, Covalent immobilization of proteins on carbon nanotubes using the cross-linker 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide - a critical assessment. Bioconjugate Chem 19:1945-1950 (2008).
    • (2008) Bioconjugate Chem , vol.19 , pp. 1945-1950
    • Gao, Y.1    Kyratzis, I.2
  • 27
    • 56849099090 scopus 로고    scopus 로고
    • Effect of calcium on immobilization of rice (Oryza sativa L.) peroxidase for bioassays in sodium alginate and Agarose gel
    • Nahakpam S, Singh P and Shah K, Effect of calcium on immobilization of rice (Oryza sativa L.) peroxidase for bioassays in sodium alginate and Agarose gel. Biotechnol Bioprocess E 13:632-638 (2008).
    • (2008) Biotechnol Bioprocess E , vol.13 , pp. 632-638
    • Nahakpam, S.1    Singh, P.2    Shah, K.3
  • 28
    • 0031804721 scopus 로고    scopus 로고
    • Characterization of laccases and peroxidases from wood-rotting fungi (family coprinaceae)
    • Heinzkill M, Bech L, Halkier T, Schneider P and Anke T, Characterization of laccases and peroxidases from wood-rotting fungi (family coprinaceae). Appl Environ Microbiol 64:1601-1606 (1998).
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1601-1606
    • Heinzkill, M.1    Bech, L.2    Halkier, T.3    Schneider, P.4    Anke, T.5
  • 29
    • 84884187444 scopus 로고    scopus 로고
    • Enzyme immobilisation on amino-functionalised multi-walled carbon nanotubes: structural and biocatalytic characterisation
    • Verma ML, Naebe M, Barrow CJ and Puri M, Enzyme immobilisation on amino-functionalised multi-walled carbon nanotubes: structural and biocatalytic characterisation. PLoS ONE 8:e73642 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e73642
    • Verma, M.L.1    Naebe, M.2    Barrow, C.J.3    Puri, M.4
  • 31
    • 80052989429 scopus 로고    scopus 로고
    • Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp
    • Aguiar-Oliveira E and Maugeri F, Thermal stability of the immobilized fructosyltransferase from Rhodotorula sp. Braz J Chem Eng 28:363-372 (2011).
    • (2011) Braz J Chem Eng , vol.28 , pp. 363-372
    • Aguiar-Oliveira, E.1    Maugeri, F.2
  • 32
    • 0026544585 scopus 로고
    • Heat inactivation of lipase from psychrotrophic Pseudomonas fluorescens P38: activation parameters and enzyme stability at low or ultra-high temperatures
    • Owusu RK, Makhzoum A and Knapp JS, Heat inactivation of lipase from psychrotrophic Pseudomonas fluorescens P38: activation parameters and enzyme stability at low or ultra-high temperatures. Food Chem 44:261-268 (1992).
    • (1992) Food Chem , vol.44 , pp. 261-268
    • Owusu, R.K.1    Makhzoum, A.2    Knapp, J.S.3
  • 33
    • 33644751068 scopus 로고    scopus 로고
    • What is the role of thermodynamics on protein stability?
    • Gummadi S, What is the role of thermodynamics on protein stability? Biotechnol Bioprocess E 8:9-18 (2003).
    • (2003) Biotechnol Bioprocess E , vol.8 , pp. 9-18
    • Gummadi, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.