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Volumn 106, Issue , 2015, Pages 56-63

Employing FAD-dependent glucose dehydrogenase within a glucose/oxygen enzymatic fuel cell operating in human serum

Author keywords

Bilirubin oxidase; FAD dependent glucose dehydrogenase; Glucose; Oxygen; Serum

Indexed keywords

BODY FLUIDS; ENZYMATIC FUEL CELLS; FUEL CELLS; GLUCOSE; GLUCOSE SENSORS; OXYGEN;

EID: 84940796043     PISSN: 15675394     EISSN: 1878562X     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2015.04.005     Document Type: Article
Times cited : (92)

References (43)
  • 3
    • 84876565676 scopus 로고    scopus 로고
    • High power enzymatic biofuel cell based on naphthoquinone-mediated oxidation of glucose by glucose oxidase in a carbon nanotube 3D matrix
    • Reuillard B., Le Goff A., Agnes C., Holzinger M., Zebda A., Gondran C., Elouarzaki K., Cosnier S. High power enzymatic biofuel cell based on naphthoquinone-mediated oxidation of glucose by glucose oxidase in a carbon nanotube 3D matrix. Phys. Chem. Chem. Phys. 2013, 15:4892-4896.
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 4892-4896
    • Reuillard, B.1    Le Goff, A.2    Agnes, C.3    Holzinger, M.4    Zebda, A.5    Gondran, C.6    Elouarzaki, K.7    Cosnier, S.8
  • 5
    • 84870201311 scopus 로고    scopus 로고
    • Direct electron transfer-based bioanodes for ethanol biofuel cells using PQQ-dependent alcohol and aldehyde dehydrogenases
    • Aquino Neto S., Suda E.L., Xu S., Meredith M.T., De Andrade A.R., Minteer S.D. Direct electron transfer-based bioanodes for ethanol biofuel cells using PQQ-dependent alcohol and aldehyde dehydrogenases. Electrochim. Acta 2013, 87:323-329.
    • (2013) Electrochim. Acta , vol.87 , pp. 323-329
    • Aquino Neto, S.1    Suda, E.L.2    Xu, S.3    Meredith, M.T.4    De Andrade, A.R.5    Minteer, S.D.6
  • 6
    • 84855574591 scopus 로고    scopus 로고
    • Enzymatic biofuel cell for oxidation of glucose to CO2
    • Xu S., Minteer S.D. Enzymatic biofuel cell for oxidation of glucose to CO2. ACS Catal. 2012, 2:91-94.
    • (2012) ACS Catal. , vol.2 , pp. 91-94
    • Xu, S.1    Minteer, S.D.2
  • 8
    • 84863317977 scopus 로고    scopus 로고
    • Biofuel cells: enhanced enzymatic bioelectrocatalysis
    • Meredith M.T., Minteer S.D. Biofuel cells: enhanced enzymatic bioelectrocatalysis. Annu. Rev. Anal. Chem. 2012, 5:157-179.
    • (2012) Annu. Rev. Anal. Chem. , vol.5 , pp. 157-179
    • Meredith, M.T.1    Minteer, S.D.2
  • 15
    • 78650284921 scopus 로고    scopus 로고
    • Generating electricity from biofluid with a nanowire-based biofuel cell for self-powered nanodevices
    • Pan C., Fang Y., Wu H., Ahmad M., Luo Z., Li Q., Xie J., Yan X., Wu L., Wang Z.L., Zhu J. Generating electricity from biofluid with a nanowire-based biofuel cell for self-powered nanodevices. Adv. Mater. 2010, 22:5388-5392.
    • (2010) Adv. Mater. , vol.22 , pp. 5388-5392
    • Pan, C.1    Fang, Y.2    Wu, H.3    Ahmad, M.4    Luo, Z.5    Li, Q.6    Xie, J.7    Yan, X.8    Wu, L.9    Wang, Z.L.10    Zhu, J.11
  • 16
    • 84875841606 scopus 로고    scopus 로고
    • A pacemaker powered by an implantable biofuel cell operating under conditions mimicking the human blood circulatory system - battery not included
    • Southcott M., MacVittie K., Halamek J., Halamkova L., Jemison W.D., Lobel R., Katz E. A pacemaker powered by an implantable biofuel cell operating under conditions mimicking the human blood circulatory system - battery not included. Phys. Chem. Chem. Phys. 2013, 15:6278-6283.
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 6278-6283
    • Southcott, M.1    MacVittie, K.2    Halamek, J.3    Halamkova, L.4    Jemison, W.D.5    Lobel, R.6    Katz, E.7
  • 19
    • 0033358042 scopus 로고    scopus 로고
    • A non-compartmentalized glucose vertical bar O-2 biofuel cell by bioengineered electrode surfaces
    • Katz E., Willner I., Kotlyar A.B. A non-compartmentalized glucose vertical bar O-2 biofuel cell by bioengineered electrode surfaces. J. Electroanal. Chem. 1999, 479:64-68.
    • (1999) J. Electroanal. Chem. , vol.479 , pp. 64-68
    • Katz, E.1    Willner, I.2    Kotlyar, A.B.3
  • 20
    • 84886788291 scopus 로고    scopus 로고
    • Hydrogen peroxide produced by glucose oxidase affects the performance of laccase cathodes in glucose/oxygen fuel cells: FAD-dependent glucose dehydrogenase as a replacement
    • Milton R.D., Giroud F., Thumser A.E., Minteer S.D., Slade R.C.T. Hydrogen peroxide produced by glucose oxidase affects the performance of laccase cathodes in glucose/oxygen fuel cells: FAD-dependent glucose dehydrogenase as a replacement. Phys. Chem. Chem. Phys. 2013, 15:19371-19379.
    • (2013) Phys. Chem. Chem. Phys. , vol.15 , pp. 19371-19379
    • Milton, R.D.1    Giroud, F.2    Thumser, A.E.3    Minteer, S.D.4    Slade, R.C.T.5
  • 21
    • 84907600334 scopus 로고    scopus 로고
    • Glucose oxidase progressively lowers bilirubin oxidase bioelectrocatalytic cathode performance in single-compartment glucose/oxygen biological fuel cells
    • Milton R.D., Giroud F., Thumser A.E., Minteer S.D., Slade R.C.T. Glucose oxidase progressively lowers bilirubin oxidase bioelectrocatalytic cathode performance in single-compartment glucose/oxygen biological fuel cells. Electrochim. Acta 2014, 140:59-64.
    • (2014) Electrochim. Acta , vol.140 , pp. 59-64
    • Milton, R.D.1    Giroud, F.2    Thumser, A.E.3    Minteer, S.D.4    Slade, R.C.T.5
  • 22
    • 84858706476 scopus 로고    scopus 로고
    • Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells
    • Zafar M.N., Beden N., Leech D., Sygmund C., Ludwig R., Gorton L. Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells. Anal. Bioanal. Chem. 2012, 402:2069-2077.
    • (2012) Anal. Bioanal. Chem. , vol.402 , pp. 2069-2077
    • Zafar, M.N.1    Beden, N.2    Leech, D.3    Sygmund, C.4    Ludwig, R.5    Gorton, L.6
  • 23
    • 79952958297 scopus 로고    scopus 로고
    • Nano-engineered flavin-dependent glucose dehydrogenase/gold nanoparticle-modified electrodes for glucose sensing and biofuel cell applications
    • Yehezkeli O., Tel-Vered R., Reichlin S., Willner I. Nano-engineered flavin-dependent glucose dehydrogenase/gold nanoparticle-modified electrodes for glucose sensing and biofuel cell applications. ACS Nano 2011, 5:2385-2391.
    • (2011) ACS Nano , vol.5 , pp. 2385-2391
    • Yehezkeli, O.1    Tel-Vered, R.2    Reichlin, S.3    Willner, I.4
  • 25
    • 84888633799 scopus 로고    scopus 로고
    • Bilirubin oxidase bioelectrocatalytic cathodes: the impact of hydrogen peroxide
    • Milton R.D., Giroud F., Thumser A.E., Minteer S.D., Slade R.C.T. Bilirubin oxidase bioelectrocatalytic cathodes: the impact of hydrogen peroxide. Chem. Commun. 2014, 50:94-96.
    • (2014) Chem. Commun. , vol.50 , pp. 94-96
    • Milton, R.D.1    Giroud, F.2    Thumser, A.E.3    Minteer, S.D.4    Slade, R.C.T.5
  • 26
    • 84937128527 scopus 로고    scopus 로고
    • Effect of multi-walled carbon nanotubes on glucose oxidation by glucose oxidase or a flavin-dependent glucose dehydrogenase in redox-polymer-mediated enzymatic fuel cell anodes
    • Osadebe I., Leech D. Effect of multi-walled carbon nanotubes on glucose oxidation by glucose oxidase or a flavin-dependent glucose dehydrogenase in redox-polymer-mediated enzymatic fuel cell anodes. ChemElectroChem 2014, 1:1988-1993.
    • (2014) ChemElectroChem , vol.1 , pp. 1988-1993
    • Osadebe, I.1    Leech, D.2
  • 28
    • 84871806180 scopus 로고    scopus 로고
    • Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes
    • Salaj-Kosla U., Poeller S., Schuhmann W., Shleev S., Magner E. Direct electron transfer of Trametes hirsuta laccase adsorbed at unmodified nanoporous gold electrodes. Bioelectrochemistry 2013, 91:15-20.
    • (2013) Bioelectrochemistry , vol.91 , pp. 15-20
    • Salaj-Kosla, U.1    Poeller, S.2    Schuhmann, W.3    Shleev, S.4    Magner, E.5
  • 32
    • 77958607481 scopus 로고    scopus 로고
    • Mechanistic studies of the 'blue' Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction
    • dos Santos L., Climent V., Blanford C.F., Armstrong F.A. Mechanistic studies of the 'blue' Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction. Phys. Chem. Chem. Phys. 2010, 12:13962-13974.
    • (2010) Phys. Chem. Chem. Phys. , vol.12 , pp. 13962-13974
    • dos Santos, L.1    Climent, V.2    Blanford, C.F.3    Armstrong, F.A.4
  • 33
    • 84881001603 scopus 로고    scopus 로고
    • Bilirubin oxidases in bioelectrochemistry: features and recent findings
    • Mano N., Edembe L. Bilirubin oxidases in bioelectrochemistry: features and recent findings. Biosens. Bioelectron. 2013, 50:478-485.
    • (2013) Biosens. Bioelectron. , vol.50 , pp. 478-485
    • Mano, N.1    Edembe, L.2
  • 34
    • 84866514236 scopus 로고    scopus 로고
    • Features and applications of bilirubin oxidases
    • Mano N. Features and applications of bilirubin oxidases. Appl. Microbiol. Biotechnol. 2012, 96:301-307.
    • (2012) Appl. Microbiol. Biotechnol. , vol.96 , pp. 301-307
    • Mano, N.1
  • 35
    • 0021479012 scopus 로고
    • Catalysis of the reduction of dioxygen at graphite-electrodes coated with fungal laccase-A
    • Lee C.W., Gray H.B., Anson F.C., Malmstrom B.G. Catalysis of the reduction of dioxygen at graphite-electrodes coated with fungal laccase-A. J. Electroanal. Chem. 1984, 172:289-300.
    • (1984) J. Electroanal. Chem. , vol.172 , pp. 289-300
    • Lee, C.W.1    Gray, H.B.2    Anson, F.C.3    Malmstrom, B.G.4
  • 36
    • 55049095938 scopus 로고    scopus 로고
    • Efficient electrocatalytic oxygen reduction by the 'blue' copper oxidase, laccase, directly attached to chemically modified carbons
    • Blanford C.F., Foster C.E., Heath R.S., Armstrong F.A. Efficient electrocatalytic oxygen reduction by the 'blue' copper oxidase, laccase, directly attached to chemically modified carbons. Faraday Discuss. 2008, 140:319-335.
    • (2008) Faraday Discuss. , vol.140 , pp. 319-335
    • Blanford, C.F.1    Foster, C.E.2    Heath, R.S.3    Armstrong, F.A.4
  • 37
    • 82955194837 scopus 로고    scopus 로고
    • Anthracene-modified multi-walled carbon nanotubes as direct electron transfer scaffolds for enzymatic oxygen reduction
    • Meredith M.T., Minson M., Hickey D., Artyushkova K., Glatzhofer D.T., Minteer S.D. Anthracene-modified multi-walled carbon nanotubes as direct electron transfer scaffolds for enzymatic oxygen reduction. ACS Catal. 2011, 1:1683-1690.
    • (2011) ACS Catal. , vol.1 , pp. 1683-1690
    • Meredith, M.T.1    Minson, M.2    Hickey, D.3    Artyushkova, K.4    Glatzhofer, D.T.5    Minteer, S.D.6
  • 38
    • 34247538548 scopus 로고    scopus 로고
    • A stable electrode for high-potential, electrocatalytic O(2) reduction based on rational attachment of a blue copper oxidase to a graphite surface
    • Blanford C.F., Heath R.S., Armstrong F.A. A stable electrode for high-potential, electrocatalytic O(2) reduction based on rational attachment of a blue copper oxidase to a graphite surface. Chem. Commun. 2007, 1710-1712.
    • (2007) Chem. Commun. , pp. 1710-1712
    • Blanford, C.F.1    Heath, R.S.2    Armstrong, F.A.3
  • 40
    • 78650745404 scopus 로고    scopus 로고
    • High current density ferrocene-modified linear poly(ethylenimine) bioanodes and their use in biofuel cells
    • Meredith M.T., Kao D.Y., Hickey D., Schmidtke D.W., Glatzhofer D.T. High current density ferrocene-modified linear poly(ethylenimine) bioanodes and their use in biofuel cells. J. Electrochem. Soc. 2011, 158:B166-B174.
    • (2011) J. Electrochem. Soc. , vol.158 , pp. B166-B174
    • Meredith, M.T.1    Kao, D.Y.2    Hickey, D.3    Schmidtke, D.W.4    Glatzhofer, D.T.5
  • 41
    • 7544225070 scopus 로고    scopus 로고
    • Deactivation of bilirubin oxidase by a product of the reaction of urate and O2
    • Kang C., Shin H., Zhang Y., Heller A. Deactivation of bilirubin oxidase by a product of the reaction of urate and O2. Bioelectrochemistry 2004, 65:83-88.
    • (2004) Bioelectrochemistry , vol.65 , pp. 83-88
    • Kang, C.1    Shin, H.2    Zhang, Y.3    Heller, A.4
  • 42
    • 30144444424 scopus 로고    scopus 로고
    • On the stability of the "wired" bilirubin oxidase oxygen cathode in serum
    • Kang C., Shin H., Heller A. On the stability of the "wired" bilirubin oxidase oxygen cathode in serum. Bioelectrochemistry 2006, 68:22-26.
    • (2006) Bioelectrochemistry , vol.68 , pp. 22-26
    • Kang, C.1    Shin, H.2    Heller, A.3


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