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Updated: Feb 4, 2026

Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
An enzyme-modified capillary as a platform for simultaneous fluorometric detection of d-glucose and l- lactate
Atsushi Shoji1, Yusuke Takahashi2, Saki Osato2
1Department of Chemistry, College of Humanities and Sciences, Nihon University, Sakurajousui, Setagaya, Tokyo, 156-8550, Japan; School of Pharmacy, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo, 192-0392, Japan.
Abstract:
The preparation of a glass capillary pattered with lipid layers on which lactate dehydrogenase (LDH) and glucose dehydrogenase (GDH) were regionally adsorbed and its application for simultaneous detection of d-glucose and l-lactate in human serum is described. A lipid layer was formed on the surface of BSA-unabsorbed octadecyltrichlorosilane (OTS) inner wall of a glass capillary. The electrostatic charge of the lipid layer was a key factor for adsorbing the enzymes on the lipid layer. The fluorescence intensities were observed at each enzyme site in the presence of diaphorase (DIA), β-nicotinamide-adenine dinucleotide oxidized (NAD), resazurin, d-glucose and l-lactate. The fluorescence intensities at each enzyme site increased with an increase in the concentration of d-glucose and l-lactate=with the detection limits of 32 μM and 4.9 μM, respectively.
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