Hokkaido University · Energy
Professor Masaru Kato's research lab specializes in bio-hybrid materials and sustainable energy conversion, focusing on integrating biological components such as Photosystem II and enzymes with functional materials for applications in renewable energy and analytical chemistry. Key research directions include protein film photoelectrochemistry, bio-inspired water oxidation, and the development of sol-gel-encapsulated enzyme systems for miniaturized bioreactors and chiral separations. The lab pioneers innovative immobilization strategies using nanostructured electrodes and sol-gel matrices to enhance electron transfer efficiency and enzyme stability.
Figures are computed from collected data and may differ slightly.
We report on a hybrid photoanode for water oxidation consisting of a cyanobacterial photosystem II (PSII) from Thermosynechococcus elongatus on a mesoporous indium-tin oxide (mesoITO) electrode. The three-dimensional metal oxide environment allows for high protein coverage (26 times an ideal monolayer coverage) and direct (mediator-free) electron transfer from PSII to mesoITO. The oxidation of water occurs with 1.6 ± 0.3 μA cm(-2) and a corresponding turnover frequency of approximately 0.18 ± 0.
A novel protein-encapsulation technique using sol-gels was developed for the preparation of monolithic capillary columns for capillary electrochromatography. Two chiral compounds, bovine serum albumin (BSA) and ovomucoid (OVM) from chicken egg white, were encapsulated in tetramethoxysilane-based hydrogel and their chiral selectivity was evaluated for the separation of some selected enantiomers (tryptophan, benzoin, eperisone, chlorpheniramine). The protein encapsulation was carried out within a
Photosynthesis is responsible for the sunlight-powered conversion of carbon dioxide and water into chemical energy in the form of carbohydrates and the release of O2 as a by-product. Although many proteins are involved in photosynthesis, the fascinating machinery of Photosystem II (PSII) is at the heart of this process. This tutorial review describes an emerging technique named protein film photoelectrochemistry (PF-PEC), which allows for the light-dependent activity of PSII adsorbed onto an ele
Photosystem II (PSII) offers a biological and sustainable route of photochemical water oxidation to O2 and can provide protons and electrons for the generation of solar fuels, such as H2. We present a rational strategy to electrostatically improve the orientation of PSII from a thermophilic cyanobacterium, Thermosynechococcus elongatus , on a nanostructured indium tin oxide (ITO) electrode and to covalently immobilize PSII on the electrode. The ITO electrode was modified with a self-assembled mo
A miniaturized pepsin reactor was prepared inside a fused-silica capillary (i.d. 75 microm) by coating a pepsin-containing gel on a photopolymerized porous silica monolith. The pepsin-encapsulated film was prepared by a sol-gel method. The sol-gel reaction was optimized so that the sol solution containing pepsin forms a thin film on the photopolymerized sol-gel (PSG) monolith that was initially fabricated at the inlet of the capillary. Pepsin was encapsulated into the gel matrix without losing i
Abstract Sol‐gel technology was first discovered in the late 1800s, but it was not until the early 1970s that renewed interest in the technique was generated, when monolithic inorganic gels were formed at low temperature. In this review, we introduce the sol‐gel reaction and the properties of the gel matrix in the first half and the applications of the matrix in the latter half.
A miniaturized trypsin reactor was prepared by coating a trypsin-containing gel on a porous silica monolith. The trypsin-encapsulated gel was prepared by the sol-gel method. The sol-gel reaction was optimized so that the sol solution containing trypsin forms a thin film on the sol-gel monolith. The trypsin was encapsulated into the gel matrix without losing its activity. The silica monolith was fabricated to fit into a 96-well microtiter plate well and could then be easily removed. The trypsin-i
A solution is prepared of 5 microm silica particles modified with (S)-N-3,5-dinitrobenzoyl-1-naphthylglycine (particle 1) or (S)-N-3,5-dinitrophenylaminocarbonyl-valine (particle 2) suspended in liquid tetraethylorthosilicate, ethanol, and aqueous hydrochloric acid. This solution is injected under pressure into a 30 cm long, 75 microm inner diameter capillary column and heated for 1 h at 120 degrees C after which the modified particles are embedded in a monolithic column of sol gel. The packed c
A liquid chromatography system, comprising a separation column with a width and depth of a few hundred nanometers, was fabricated on a glass microchip (femto liquid chromatography, fLC). The size of this system was approximately 10(11) times smaller than that of a conventional LC system, the flow rate was subpicoliter/minute, and the injection volume was a few hundred attoliters. The fLC system did not require packing stationary phase and was capable of separating solutes with different molecula
A water-soluble phospholipid polymer having an active ester group in the side chain, poly[2-methacryloyloxyethyl phosphorylcholine (MPC)-co-n-butyl methacrylate (BMA)-co-p-nitrophenyloxycarbonyl polyethyleneglycol methacrylate (MEONP)(PMBN), was used for the immobilization of an enzyme on a plastic microchip. The MPC polymers with BMA units were adsorbed onto the poly(methyl methacrylate)(PMMA) microchip, and the active ester group in the MEONP unit reacted with the amino groups of the proteolyt
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