2020
DOI: 10.1016/j.bioelechem.2020.107496
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PQQ-GDH – Structure, function and application in bioelectrochemistry

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Cited by 27 publications
(21 citation statements)
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“…However, GDH presents several limitations. PQQGDH suffers from low selectivity and requires suitable solubilisation detergents and purification to allow membrane binding, while water-soluble PQQGDH suffers from poor thermal stability [ 38 ]. NAD-dependent GDH biosensors require the addition of NAD cofactor which leads to complications (e.g., not always stable, contamination) in the analysis [ 37 , 39 ].…”
Section: Introductionmentioning
confidence: 99%
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“…However, GDH presents several limitations. PQQGDH suffers from low selectivity and requires suitable solubilisation detergents and purification to allow membrane binding, while water-soluble PQQGDH suffers from poor thermal stability [ 38 ]. NAD-dependent GDH biosensors require the addition of NAD cofactor which leads to complications (e.g., not always stable, contamination) in the analysis [ 37 , 39 ].…”
Section: Introductionmentioning
confidence: 99%
“…Furthermore, the electrochemistry of the oxidised form (NAD + ) and reduced form (NADH) of NAD cofactor is irreversible. Direct oxidation of NADH at an unmodified electrode requires high overpotential due to its slow electron-transfer kinetics [ 37 , 38 ]. Moreover, for electrochemical measurements, GDH requires the use of artificial electron acceptors [ 40 ].…”
Section: Introductionmentioning
confidence: 99%
“…GOx has a high temperature and pH stability along with excellent glucose substrate selectivity [ 13 , 14 , 15 ]; however, GOx uses O 2 as an external electron acceptor in the oxidation reaction so device performance is sensitive to and variable depending on the atmospheric oxygen level [ 16 , 17 , 18 ]. To overcome this challenge and improve sensing reliability, glucose dehydrogenase (GDH) does not require O 2 and is hence being used in various types of glucose sensors together with pyrroloquinoline (PQQ), nicotinamide adenine dinucleotide (NAD), and flavin adenine dinucleotide (FAD) redox cofactors [ 19 , 20 , 21 ]. Among them, FAD–GDH has excellent thermal stability and substrate selectivity and does not require additional cofactors or active catalysts [ 21 , 22 , 23 ].…”
Section: Introductionmentioning
confidence: 99%
“…[20,21] However, an efficient electron transfer between the prosthetic group of the enzyme and the electrode surface might be achieved through the electrical wiring of redox enzymes, by using a flexible redox polymer as electron shuttle [22,23] or nanomaterials (e. g., gold nanoparticles, carbon nanotubes etc.). [24][25][26][27] In particular, several sugar oxidizing enzymes (e. g., fructose dehydrogenase (FDH), [28,29] pyranose dehydrogenase, [30] cellobiose dehydrogenase, [31][32][33] FAD-dependent glucose dehydrogenase, [34][35][36][37] PQQ-dependent glucose dehydrogenase [38][39][40][41] etc.) as well as oxidant reducing enzymes (e. g., multicopper oxidases, [42][43][44] plant peroxidases [45][46][47][48] etc.)…”
Section: Introductionmentioning
confidence: 99%