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pyrroloquinoline quinone glucose dehydrogenase by biased mutation assembling with
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10.1007/s00253-006-0521-4
180. Tsujimura S, Kojima S, Kano K et al (2006) Novel FAD-dependent glucose dehydrogenase
for a dioxygen-insensitive glucose biosensor. Biosci Biotechnol Biochem 70:654–659.
https://doi.org/10.1271/bbb.70.654
181. Okuda-Shimazaki J, Yoshida H, Sode K (2020) FAD dependent glucose dehydrogenases –
Discovery and engineering of representative glucose sensing enzymes -. Bioelectrochemistry
132:107414. https://doi.org/10.1016/j.bioelechem.2019.107414
182. Ludwig R, Harreither W, Tasca F, Gorton L (2010) Cellobiose Dehydrogenase: A Versatile
Catalyst for Electrochemical Applications. ChemPhysChem 11:2674–2697. https://doi.org/
10.1002/cphc.201000216
183. Ikeda T, Fushimi F, Miki K, Senda M (1988) Direct Bioelectrocatalysis at Electrodes
Modified with D-Gluconate Dehydrogenase. Agric Biol Chem 52:2655–2658. https://doi.
org/10.1080/00021369.1988.10869104
184. Ikeda T, Matsushita F, Senda M (1991) Amperometric fructose sensor based on direct
bioelectrocatalysis. Biosens Bioelectron 6:299–304. https://doi.org/10.1016/0956-5663(91)
85015-O
185. Ikeda T, Miyaoka S, Matsushita F et al (1992) Direct Bioelectrocatalysis at Metal and
Carbon Electrodes Modified with Adsorbed D-Gluconate Dehydrogenase or Adsorbed
Alcohol Dehydrogenase from Bacterial Membranes. Chem Lett 21:847–850. https://doi.org/
10.1246/cl.1992.847
186. Ikeda T, Kobayashi D, Matsushita F et al (1993) Bioelectrocatalysis at electrodes coated
with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator.
J Electroanal Chem 361:221–228. https://doi.org/10.1016/0022-0728(93)87058-4
187. Gorton L, Lindgren A, Larsson T et al (1999) Direct electron transfer between
heme-containing enzymes and electrodes as basis for third generation biosensors. Anal
Chim Acta 400:91–108. https://doi.org/10.1016/S0003-2670(99)00610-8
188. Lindgren A, Larsson T, Ruzgas T, Gorton L (2000) Direct electron transfer between the
heme of cellobiose dehydrogenase and thiol modified gold electrodes. J Electroanal Chem
494:105–113. https://doi.org/10.1016/S0022-0728(00)00326-0
189. Samejima M, Phillips RS, Eriksson K-EL (1992) Cellobiose oxidase from Phanerochaete
chrysosporium Stopped-flow spectrophotometric analysis of pH-dependent reduction. FEBS
Lett 306:165–168. https://doi.org/10.1016/0014-5793(92)80991-O
190. Hyde SM, Wood PM (1996) Kinetic and antigenic similarities for cellobiose dehydrogenase
from the brown rot fungus Coniophora puteana and the white rot fungus Phanerochaete
chrysosporium. FEMS Microbiol Lett 145:439–444. https://doi.org/10.1016/S0378-1097
(96)00448-X
191. Šakinytė I, Barkauskas J, Gaidukevič J, Razumienė J (2015) Thermally reduced graphene
oxide: The study and use for reagentless amperometric d-fructose biosensors. Talanta
144:1096–1103. https://doi.org/10.1016/j.talanta.2015.07.072
192. Tsujimura S, Nishina A, Kamitaka Y, Kano K (2009) Coulometric d-Fructose Biosensor
Based on Direct Electron Transfer Using d-Fructose Dehydrogenase. Anal Chem 81:9383–
9387. https://doi.org/10.1021/ac901771t
193. Ramanavicius A, Habermüller K, Csöregi E et al (1999) Polypyrrole-Entrapped Quinohemoprotein Alcohol Dehydrogenase. Evidence for Direct Electron Transfer via
Conducting-Polymer Chains. Anal Chem 71:3581–3586. https://doi.org/10.1021/
ac981201c
194. Treu BL, Sokic-Lazic D, Minteer S (2010) Bioelectrocatalysis of pyruvate with
PQQ-dependent pyruvate dehydrogenase. pp 1–11
Selective Enzymes at the Core of Advanced Electroanalytical …
355
pyrroloquinoline quinone glucose dehydrogenase by biased mutation assembling with
optimized amino acid substitution. Appl Microbiol Biotechnol 73:607–617. https://doi.org/
10.1007/s00253-006-0521-4
180. Tsujimura S, Kojima S, Kano K et al (2006) Novel FAD-dependent glucose dehydrogenase
for a dioxygen-insensitive glucose biosensor. Biosci Biotechnol Biochem 70:654–659.
https://doi.org/10.1271/bbb.70.654
181. Okuda-Shimazaki J, Yoshida H, Sode K (2020) FAD dependent glucose dehydrogenases –
Discovery and engineering of representative glucose sensing enzymes -. Bioelectrochemistry
132:107414. https://doi.org/10.1016/j.bioelechem.2019.107414
182. Ludwig R, Harreither W, Tasca F, Gorton L (2010) Cellobiose Dehydrogenase: A Versatile
Catalyst for Electrochemical Applications. ChemPhysChem 11:2674–2697. https://doi.org/
10.1002/cphc.201000216
183. Ikeda T, Fushimi F, Miki K, Senda M (1988) Direct Bioelectrocatalysis at Electrodes
Modified with D-Gluconate Dehydrogenase. Agric Biol Chem 52:2655–2658. https://doi.
org/10.1080/00021369.1988.10869104
184. Ikeda T, Matsushita F, Senda M (1991) Amperometric fructose sensor based on direct
bioelectrocatalysis. Biosens Bioelectron 6:299–304. https://doi.org/10.1016/0956-5663(91)
85015-O
185. Ikeda T, Miyaoka S, Matsushita F et al (1992) Direct Bioelectrocatalysis at Metal and
Carbon Electrodes Modified with Adsorbed D-Gluconate Dehydrogenase or Adsorbed
Alcohol Dehydrogenase from Bacterial Membranes. Chem Lett 21:847–850. https://doi.org/
10.1246/cl.1992.847
186. Ikeda T, Kobayashi D, Matsushita F et al (1993) Bioelectrocatalysis at electrodes coated
with alcohol dehydrogenase, a quinohemoprotein with heme c serving as a built-in mediator.
J Electroanal Chem 361:221–228. https://doi.org/10.1016/0022-0728(93)87058-4
187. Gorton L, Lindgren A, Larsson T et al (1999) Direct electron transfer between
heme-containing enzymes and electrodes as basis for third generation biosensors. Anal
Chim Acta 400:91–108. https://doi.org/10.1016/S0003-2670(99)00610-8
188. Lindgren A, Larsson T, Ruzgas T, Gorton L (2000) Direct electron transfer between the
heme of cellobiose dehydrogenase and thiol modified gold electrodes. J Electroanal Chem
494:105–113. https://doi.org/10.1016/S0022-0728(00)00326-0
189. Samejima M, Phillips RS, Eriksson K-EL (1992) Cellobiose oxidase from Phanerochaete
chrysosporium Stopped-flow spectrophotometric analysis of pH-dependent reduction. FEBS
Lett 306:165–168. https://doi.org/10.1016/0014-5793(92)80991-O
190. Hyde SM, Wood PM (1996) Kinetic and antigenic similarities for cellobiose dehydrogenase
from the brown rot fungus Coniophora puteana and the white rot fungus Phanerochaete
chrysosporium. FEMS Microbiol Lett 145:439–444. https://doi.org/10.1016/S0378-1097
(96)00448-X
191. Šakinytė I, Barkauskas J, Gaidukevič J, Razumienė J (2015) Thermally reduced graphene
oxide: The study and use for reagentless amperometric d-fructose biosensors. Talanta
144:1096–1103. https://doi.org/10.1016/j.talanta.2015.07.072
192. Tsujimura S, Nishina A, Kamitaka Y, Kano K (2009) Coulometric d-Fructose Biosensor
Based on Direct Electron Transfer Using d-Fructose Dehydrogenase. Anal Chem 81:9383–
9387. https://doi.org/10.1021/ac901771t
193. Ramanavicius A, Habermüller K, Csöregi E et al (1999) Polypyrrole-Entrapped Quinohemoprotein Alcohol Dehydrogenase. Evidence for Direct Electron Transfer via
Conducting-Polymer Chains. Anal Chem 71:3581–3586. https://doi.org/10.1021/
ac981201c
194. Treu BL, Sokic-Lazic D, Minteer S (2010) Bioelectrocatalysis of pyruvate with
PQQ-dependent pyruvate dehydrogenase. pp 1–11
Selective Enzymes at the Core of Advanced Electroanalytical …
355