54. Scheller FW, Lisdat F, Wollenberger U (2005) Application of electrically contacted enzymes
for biosensors. In: Willner I, Katz E (eds) Bioelectronics. Wiley-VCH Verlag GmbH & Co,
KGaA, Weinheim, FRG, pp 99–126
55. Jiang L, McNeil CJ, Cooper JM (1995) Direct electron transfer reactions of glucose oxidase
immobilised at a self-assembled monolayer. J Chem Soc, Chem Commun 12:1293–1295.
https://doi.org/10.1039/c39950001293
56. Courjean O, Gao F, Mano N (2009) Deglycosylation of glucose oxidase for direct and
efficient glucose electrooxidation on a glassy carbon electrode. Angew Chemie - Int Ed
48:5897–5899. https://doi.org/10.1002/anie.200902191
57. Sajjadi S, Ghourchian H, Rahimi P (2011) Different behaviors of single and multi wall
carbon nanotubes for studying electrochemistry and electrocatalysis of choline oxidase.
Electrochim Acta 56:9542–9548. https://doi.org/10.1016/j.electacta.2011.04.039
58. Wu S, Chen J, Liu D et al (2016) A biocompatible cerasome based platform for direct
electrochemistry of cholesterol oxidase and cholesterol sensing. RSC Adv 6:70781–70790.
https://doi.org/10.1039/C6RA06368C
59. Gao Y, Shen C, Di J, Tu Y (2009) Fabrication of amperometric xanthine biosensors based
on direct chemistry of xanthine oxidase. Mater Sci Eng, C 29:2213–2216. https://doi.org/10.
1016/j.msec.2009.05.004
60. Wilson GS (2016) Native glucose oxidase does not undergo direct electron transfer. Biosens
Bioelectron 82:7–8. https://doi.org/10.1016/j.bios.2016.04.083
61. Milton RD, Minteer SD (2017) Direct enzymatic bioelectrocatalysis: differentiating between
myth and reality. J R Soc Interface 14:20170253. https://doi.org/10.1098/rsif.2017.0253
62. Vogt S, Schneider M, Schäfer-Eberwein H, Nöll G (2014) Determination of the pH
dependent redox potential of glucose oxidase by spectroelectrochemistry. Anal Chem
86:7530–7535. https://doi.org/10.1021/ac501289x
63. Abbasi S, Gharaghani S, Benvidi A et al (2018) An in-depth view of potential dual effect of
thymol in inhibiting xanthine oxidase activity: Electrochemical measurements in combination with four way PARAFAC analysis and molecular docking insights. Int J Biol Macromol
119:1298–1310. https://doi.org/10.1016/j.ijbiomac.2018.08.018
64. Gadda G, Wels G, Pollegioni L et al (1997) Characterization of cholesterol oxidase from
Streptomyces hygroscopicus and Brevibacterium sterolicum. Eur J Biochem 250:369–376.
https://doi.org/10.1111/j.1432-1033.1997.0369a.x
65. Yorita K, Matsuoka T, Misaki H, Massey V (2000) Interaction of two arginine residues in
lactate oxidase with the enzyme flavin: conversion of FMN to 8-formyl-FMN. Proc Natl
Acad Sci 97:13039–13044. https://doi.org/10.1073/pnas.250472297
66. Ivnitski DM, Khripin C, Luckarift HR et al (2010) Surface characterization and direct
bioelectrocatalysis of multicopper oxidases. Electrochim Acta 55:7385–7393. https://doi.
org/10.1016/j.electacta.2010.07.026
67. Ludwig R, Ortiz R, Schulz C et al (2013) Cellobiose dehydrogenase modified electrodes:
advances by materials science and biochemical engineering. Anal Bioanal Chem 405:3637–
3658. https://doi.org/10.1007/s00216-012-6627-x
68. Torimura M, Kano K, Ikeda T, Ueda T (1997) Spectroelectrochemical characterization of
quinohemoprotein alcohol dehydrogenase from gluconobacter suboxydans. Chem Lett
26:525–526. https://doi.org/10.1246/cl.1997.525
69. Tkac J, Svitel J, Vostiar I, et al (2009) Membrane-bound dehydrogenases from
Gluconobacter sp.: Interfacial electrochemistry and direct bioelectrocatalysis. Bioelectrochemistry 76:53–62. https://doi.org/10.1016/j.bioelechem.2009.02.013
70. Tanne C, Göbel G, Lisdat F (2010) Development of a (PQQ)-GDH-anode based on
MWCNT-modified gold and its application in a glucose/O 2 -biofuel cell. Biosens Bioelectron
26:530–535. https://doi.org/10.1016/j.bios.2010.07.052
71. Takeda K, Matsumura H, Ishida T et al (2015) Characterization of a novel PQQ-dependent
quinohemoprotein pyranose dehydrogenase from Coprinopsis cinerea classified into
348
T. Monteiro et al.
for biosensors. In: Willner I, Katz E (eds) Bioelectronics. Wiley-VCH Verlag GmbH & Co,
KGaA, Weinheim, FRG, pp 99–126
55. Jiang L, McNeil CJ, Cooper JM (1995) Direct electron transfer reactions of glucose oxidase
immobilised at a self-assembled monolayer. J Chem Soc, Chem Commun 12:1293–1295.
https://doi.org/10.1039/c39950001293
56. Courjean O, Gao F, Mano N (2009) Deglycosylation of glucose oxidase for direct and
efficient glucose electrooxidation on a glassy carbon electrode. Angew Chemie - Int Ed
48:5897–5899. https://doi.org/10.1002/anie.200902191
57. Sajjadi S, Ghourchian H, Rahimi P (2011) Different behaviors of single and multi wall
carbon nanotubes for studying electrochemistry and electrocatalysis of choline oxidase.
Electrochim Acta 56:9542–9548. https://doi.org/10.1016/j.electacta.2011.04.039
58. Wu S, Chen J, Liu D et al (2016) A biocompatible cerasome based platform for direct
electrochemistry of cholesterol oxidase and cholesterol sensing. RSC Adv 6:70781–70790.
https://doi.org/10.1039/C6RA06368C
59. Gao Y, Shen C, Di J, Tu Y (2009) Fabrication of amperometric xanthine biosensors based
on direct chemistry of xanthine oxidase. Mater Sci Eng, C 29:2213–2216. https://doi.org/10.
1016/j.msec.2009.05.004
60. Wilson GS (2016) Native glucose oxidase does not undergo direct electron transfer. Biosens
Bioelectron 82:7–8. https://doi.org/10.1016/j.bios.2016.04.083
61. Milton RD, Minteer SD (2017) Direct enzymatic bioelectrocatalysis: differentiating between
myth and reality. J R Soc Interface 14:20170253. https://doi.org/10.1098/rsif.2017.0253
62. Vogt S, Schneider M, Schäfer-Eberwein H, Nöll G (2014) Determination of the pH
dependent redox potential of glucose oxidase by spectroelectrochemistry. Anal Chem
86:7530–7535. https://doi.org/10.1021/ac501289x
63. Abbasi S, Gharaghani S, Benvidi A et al (2018) An in-depth view of potential dual effect of
thymol in inhibiting xanthine oxidase activity: Electrochemical measurements in combination with four way PARAFAC analysis and molecular docking insights. Int J Biol Macromol
119:1298–1310. https://doi.org/10.1016/j.ijbiomac.2018.08.018
64. Gadda G, Wels G, Pollegioni L et al (1997) Characterization of cholesterol oxidase from
Streptomyces hygroscopicus and Brevibacterium sterolicum. Eur J Biochem 250:369–376.
https://doi.org/10.1111/j.1432-1033.1997.0369a.x
65. Yorita K, Matsuoka T, Misaki H, Massey V (2000) Interaction of two arginine residues in
lactate oxidase with the enzyme flavin: conversion of FMN to 8-formyl-FMN. Proc Natl
Acad Sci 97:13039–13044. https://doi.org/10.1073/pnas.250472297
66. Ivnitski DM, Khripin C, Luckarift HR et al (2010) Surface characterization and direct
bioelectrocatalysis of multicopper oxidases. Electrochim Acta 55:7385–7393. https://doi.
org/10.1016/j.electacta.2010.07.026
67. Ludwig R, Ortiz R, Schulz C et al (2013) Cellobiose dehydrogenase modified electrodes:
advances by materials science and biochemical engineering. Anal Bioanal Chem 405:3637–
3658. https://doi.org/10.1007/s00216-012-6627-x
68. Torimura M, Kano K, Ikeda T, Ueda T (1997) Spectroelectrochemical characterization of
quinohemoprotein alcohol dehydrogenase from gluconobacter suboxydans. Chem Lett
26:525–526. https://doi.org/10.1246/cl.1997.525
69. Tkac J, Svitel J, Vostiar I, et al (2009) Membrane-bound dehydrogenases from
Gluconobacter sp.: Interfacial electrochemistry and direct bioelectrocatalysis. Bioelectrochemistry 76:53–62. https://doi.org/10.1016/j.bioelechem.2009.02.013
70. Tanne C, Göbel G, Lisdat F (2010) Development of a (PQQ)-GDH-anode based on
MWCNT-modified gold and its application in a glucose/O 2 -biofuel cell. Biosens Bioelectron
26:530–535. https://doi.org/10.1016/j.bios.2010.07.052
71. Takeda K, Matsumura H, Ishida T et al (2015) Characterization of a novel PQQ-dependent
quinohemoprotein pyranose dehydrogenase from Coprinopsis cinerea classified into
348
T. Monteiro et al.