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Updated: Apr 11, 2026
Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Surface modifications for enhanced enzyme immobilization and improved electron transfer of PQQ-dependent glucose
Ryan J Lopez1, Sofia Babanova1, Kateryna Artyushkova1
1Department of Chemical and Biological Engineering University of New Mexico, 1 University of New Mexico, Albuquerque, NM 87131, USA.
Abstract:
Pyrroloquinoline quinone dependent soluble glucose dehydrogenase (PQQ-sGDH) enzymatic MWCNT electrodes were p roduced using 1-pyrenecarboxylic acid (PCA) activated through carbodiimide functionalization and 1-Pyrenebutyric acid N-hydroxysuccinimide ester (PBSE) as tethering agents. At 600 mV potential, the current density generated by the activated-PCA tethered PQQ-sGDH anode was significantly greater than the current density generated by the untethered PQQ-sGDH and PBSE tethered anodes, and performance was nearly identical to the performance of a covalently bound PQQ-sGDH anode. A technique for covalently bonding heme-b (hemin), a natural quinohemoprotein porphyrin redox cofactor, to carbon nanotubes modified with arylamine groups is reported. The resulting performance of the covalently bound hemin PQQ-sGDH anode is considerably higher than that of any other PQQ-sGDH anodes tested.
