Kyoto University · Engineering
Professor Kenji Kano's research lab specializes in bioelectrochemistry and bioenergy, focusing on the development of high-performance, sustainable biofuel cells. The lab pioneers direct electron transfer (DET)-type bioelectrocatalysis using enzymes such as fructose dehydrogenase (FDH) and laccase or bilirubin oxidase (BOD) for efficient oxidation and reduction reactions. Key research directions include enzyme immobilization strategies on carbon-based electrodes, optimization of biocathode performance through surface modification, and enhancing power density in passive, mediator-free biofuel cells operating under physiological conditions. The lab also investigates the structure-function relationships of multi-subunit redox enzymes to improve electron transfer efficiency.
Figures are computed from collected data and may differ slightly.
One-compartment biofuel cells without separators have been constructed, in which d-fructose dehydrogenase (FDH) from Gluconobacter sp. and laccase from Trametes sp. (TsLAC) work as catalysts of direct electron transfer (DET)-type bioelectrocatalysis in the two-electron oxidation of d-fructose and four-electron reduction of dioxygen as fuels, respectively. FDH adsorbs strongly and stably on Ketjen black (KB) particles that have been modified on carbon papers (CP) and produces the catalytic curren
Biofuel cells are a next-generation energy device because they use renewable fuels with high energy density and safety. We have developed passive-type biofuel cell units, which generate a power over 100 mW (80 cm3, 39.7 g). Our biofuel cell, in which two-electron oxidation of glucose and four-electron reduction of O2 occurs at pH 7 in mediated bioelectrochemical processes under quiescent conditions, accomplished the maximum power density of 1.45 ± 0.24 mW cm−2 at 0.3 V. This performance was achi
The fructose/dioxygen biofuel cell, one of the direct electron transfer (DET)-type bioelectrochemical devices, utilizes fructose dehydrogenase (FDH) on the anode and multi-copper oxidase such as bilirubin oxidase (BOD) on the cathode as catalysts. The power density in the literature is limited by the biocathode performance. We show that the DET-type biocathode performance is greatly improved, when bilirubin or some related substances are adsorbed on electrodes before the BOD adsorption. Several
A heterotrimeric membrane-bound fructose dehydrogenase (FDH) complex from Gluconobacter japonicus NBRC3260 catalyzes oxidation of d-fructose into 2-keto-d-fructose and is one of typical enzymes allowing a direct electron transfer (DET)-type bioelectrocatalysis. Subunits I and II have a covalently bound flavin adenine dinucleotide and three heme C moieties, respectively. We have constructed subunit I/III subcomplex (ΔcFDH) lacking of the heme C subunit. ΔcFDH catalyzes the oxidation of d-fructose
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