Premium
Immobilisation of Flavin‐Adenine‐Dinucleotide‐Dependent Glucose Dehydrogenase α Subunit in Free‐Standing Graphitised Carbon Nanofiber Paper Using a Bifunctional Cross‐Linker for an Enzymatic Biofuel Cell
Author(s) -
Fapyane Deby,
Lee Yooseok,
Lim Chyi Yan,
Ahn JouHyeon,
Kim SeonWon,
Chang In Seop
Publication year - 2014
Publication title -
chemelectrochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.182
H-Index - 59
ISSN - 2196-0216
DOI - 10.1002/celc.201402035
Subject(s) - bifunctional , cellobiose dehydrogenase , glucose oxidase , chemistry , flavin group , electrode , chemical engineering , nicotinamide adenine dinucleotide , biosensor , materials science , organic chemistry , catalysis , biochemistry , enzyme , nad+ kinase , engineering , cellobiose , cellulase
Free‐standing graphitised carbon nanofiber paper (GCNFp) is fabricated using a dispersion–filtration method and modified by non‐covalent functionalisation with 1‐pyrenebutyric acid N ‐hydroxysuccinimide ester—a bifunctional linker reagent—through π–π stacking. This modified GCNFp is then used to immobilise enzymes, and together they form an electrode for enzymatic biofuel cell (EBFC) applications. This fabrication method is shown to be capable of providing a practical platform for enzyme–electrode electrical communication that is faster than comparable systems based on other carbon materials, as calculated from the heterogeneous electron‐transfer rate constant. The GCNFp‐based EBFC reaches a maximum power density at a glucose concentration of 100 m M , yielding 834.9±200, 262.9±15.6 and 147.2±4.70 μW cm −2 for flavin‐adenine‐dinucleotide‐dependent glucose dehydrogenase (FADGDH)–menadione, glucose oxidase (GOX)–menadione, and GOX‐only systems (as the anode), respectively, with laccase as the cathode.