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Volumn 136, Issue , 2014, Pages 537-541

Glucose oxidation catalyzed by FAD-dependent glucose dehydrogenase within Os complex-tethered redox polymer hydrogel

Author keywords

Biofuel cell; Blood glucose sensor; Glucose dehydrogenase; Os complex; Wiring

Indexed keywords

ASPERGILLUS; BIOLOGICAL FUEL CELLS; CATALYTIC OXIDATION; CHLORINE COMPOUNDS; ELECTRIC WIRING; ELECTRODES; ENZYME ELECTRODES; GLUCOSE SENSORS; HYDROGELS; OSMIUM;

EID: 84902653068     PISSN: 00134686     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.electacta.2014.05.088     Document Type: Article
Times cited : (49)

References (22)
  • 1
    • 49049113124 scopus 로고    scopus 로고
    • Electrochemical glucose sensors and their applications in diabetes management
    • A. Heller, and B. Feldman Electrochemical glucose sensors and their applications in diabetes management Chem. Rev. 108 2008 2482
    • (2008) Chem. Rev. , vol.108 , pp. 2482
    • Heller, A.1    Feldman, B.2
  • 2
    • 7544227821 scopus 로고    scopus 로고
    • Enzymatic biofuel cells for implantable and microscale devices
    • S. Calabrese Barton, J. Gallaway, and P. Atanassov Enzymatic biofuel cells for implantable and microscale devices Chem. Rev. 104 2004 4867
    • (2004) Chem. Rev. , vol.104 , pp. 4867
    • Calabrese Barton, S.1    Gallaway, J.2    Atanassov, P.3
  • 7
    • 33748990573 scopus 로고    scopus 로고
    • Potential-step coulometry of d-glucose using a novel FAD-dependent glucose dehydrogenase
    • S. Tsujimura, S. Kojima, T. Ikeda, and K. Kano Potential-step coulometry of d-glucose using a novel FAD-dependent glucose dehydrogenase Anal. Bioanal. Chem. 386 2006 645
    • (2006) Anal. Bioanal. Chem. , vol.386 , pp. 645
    • Tsujimura, S.1    Kojima, S.2    Ikeda, T.3    Kano, K.4
  • 8
    • 80053179412 scopus 로고    scopus 로고
    • Screening of Aspergillus-derived FAD-glucose dehydrogenases from fungal genome database
    • K. Mori, M. Nakajima, K. Kojima, K. Murakami, S. Ferri, and K. Sode Screening of Aspergillus-derived FAD-glucose dehydrogenases from fungal genome database Biotech. Lett. 33 2011 2255
    • (2011) Biotech. Lett. , vol.33 , pp. 2255
    • Mori, K.1    Nakajima, M.2    Kojima, K.3    Murakami, K.4    Ferri, S.5    Sode, K.6
  • 9
    • 84858706476 scopus 로고    scopus 로고
    • Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells
    • M.N. Zafar, N. Beden, D. Leech, C. Sygmund, R. Ludwig, and L. Gorton Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells Anal. Bioanal. Chem. 402 2012 2069
    • (2012) Anal. Bioanal. Chem. , vol.402 , pp. 2069
    • Zafar, M.N.1    Beden, N.2    Leech, D.3    Sygmund, C.4    Ludwig, R.5    Gorton, L.6
  • 11
    • 77956801249 scopus 로고    scopus 로고
    • Effect of degree of glycosylation on charge of glucose oxidase and redox hydrogel catalytic efficiency
    • O. Courjean, V. Flexer, A. Prévoteau, E. Suraniti, and N. Mano Effect of degree of glycosylation on charge of glucose oxidase and redox hydrogel catalytic efficiency ChemPhysChem. 11 2010 2795
    • (2010) ChemPhysChem. , vol.11 , pp. 2795
    • Courjean, O.1    Flexer, V.2    Prévoteau, A.3    Suraniti, E.4    Mano, N.5
  • 12
    • 74149094985 scopus 로고    scopus 로고
    • Deglycosylation of glucose oxidase to improve biosensors and biofuel cells
    • A. Prévoteau, O. Courjean, and N. Mano Deglycosylation of glucose oxidase to improve biosensors and biofuel cells Electrochem. Commun. 12 2010 213
    • (2010) Electrochem. Commun. , vol.12 , pp. 213
    • Prévoteau, A.1    Courjean, O.2    Mano, N.3
  • 13
    • 0037462122 scopus 로고    scopus 로고
    • Long tethers binding redox centers to polymer backbones enhance electron transport in enzyme wiring hydrogels
    • F. Mao, N. Mano, and A. Heller Long tethers binding redox centers to polymer backbones enhance electron transport in enzyme wiring hydrogels J. Amer. Chem. Soc. 125 2003 4951
    • (2003) J. Amer. Chem. Soc. , vol.125 , pp. 4951
    • Mao, F.1    Mano, N.2    Heller, A.3
  • 14
    • 81155152401 scopus 로고    scopus 로고
    • Carbon fiber microelectrodes modified with carbon nanotubes as a new support for immobilization of glucose oxidase
    • H. Wen, V. Nallathambi, D. Chakraborty, and S. Calabrese Barton Carbon fiber microelectrodes modified with carbon nanotubes as a new support for immobilization of glucose oxidase Microchim. Acta 175 2011 283
    • (2011) Microchim. Acta , vol.175 , pp. 283
    • Wen, H.1    Nallathambi, V.2    Chakraborty, D.3    Calabrese Barton, S.4
  • 15
  • 16
    • 85032612943 scopus 로고    scopus 로고
    • Mediatorless high-power glucose biofuel cells based on compressed carbon nanotube-enzyme electrodes
    • F. Gao, L. Viry, M. Maugey, P. Poulin, and N. Mano Mediatorless high-power glucose biofuel cells based on compressed carbon nanotube-enzyme electrodes Nature Com. 1 2010 2
    • (2010) Nature Com. , vol.1 , pp. 2
    • Gao, F.1    Viry, L.2    Maugey, M.3    Poulin, P.4    Mano, N.5
  • 18
    • 84875666171 scopus 로고    scopus 로고
    • Designing thin films of redox hydrogel for highly efficient enzymatic anodes
    • E. Suraniti, S. Vives, S. Tsujimura, and N. Mano Designing thin films of redox hydrogel for highly efficient enzymatic anodes J. Electrochem. Soc. 160 2013 G79
    • (2013) J. Electrochem. Soc. , vol.160 , pp. 79
    • Suraniti, E.1    Vives, S.2    Tsujimura, S.3    Mano, N.4
  • 19
    • 84867374212 scopus 로고    scopus 로고
    • Crosslinked redox polymer enzyme electrodes containing carbon nanotubes for high and stable glucose oxidation current
    • D. MacAodha, M.L. Ferrer, P. Ó Conghaile, P. Kavanagh, and D. Leech Crosslinked redox polymer enzyme electrodes containing carbon nanotubes for high and stable glucose oxidation current Phys. Chem. Chem. Phys. 14 2012 14667
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 14667
    • Macaodha, D.1    Ferrer, M.L.2    Conghaile, O.C.P.3    Kavanagh, P.4    Leech, D.5
  • 20
    • 77951879080 scopus 로고    scopus 로고
    • Dependence of catalytic activity and long-term stability of enzyme hydrogel films on curing time
    • J. Lehr, B.E. Williamson, F. Barrière, and A.J. Downard Dependence of catalytic activity and long-term stability of enzyme hydrogel films on curing time Bioelectrochemistry 79 2010 142
    • (2010) Bioelectrochemistry , vol.79 , pp. 142
    • Lehr, J.1    Williamson, B.E.2    Barrière, F.3    Downard, A.J.4
  • 21
    • 84855365640 scopus 로고    scopus 로고
    • Electron-transfer studies with a new flavin adenine dinucleotide dependent glucose dehydrogenase and osmium polymers of different redox potentials
    • M.N. Zafar, X. Wang, C. Sygmund, R. Ludwig, D. Leech, and L. Gorton Electron-transfer studies with a new flavin adenine dinucleotide dependent glucose dehydrogenase and osmium polymers of different redox potentials Anal. Chem. 84 2012 334
    • (2012) Anal. Chem. , vol.84 , pp. 334
    • Zafar, M.N.1    Wang, X.2    Sygmund, C.3    Ludwig, R.4    Leech, D.5    Gorton, L.6
  • 22
    • 84872543951 scopus 로고    scopus 로고
    • Comparison of glucose oxidation by crosslinked redox polymer enzyme electrodes containing carbon nanotubes and a range of glucose oxidising enzymes
    • D. MacAodha, P.Ó. Conghaile, B. Egan, P. Kavanagh, C. Sygmund, R. Ludwig, and D. Leech Comparison of glucose oxidation by crosslinked redox polymer enzyme electrodes containing carbon nanotubes and a range of glucose oxidising enzymes Electroanal 25 2013 94.
    • (2013) Electroanal , vol.25 , pp. 94
    • Macaodha, D.1    Conghaile, P.Ó.2    Egan, B.3    Kavanagh, P.4    Sygmund, C.5    Ludwig, R.6    Leech, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.