CN102341528A - Method for electrolyzing fuel - Google Patents
Method for electrolyzing fuel Download PDFInfo
- Publication number
- CN102341528A CN102341528A CN2010800104848A CN201080010484A CN102341528A CN 102341528 A CN102341528 A CN 102341528A CN 2010800104848 A CN2010800104848 A CN 2010800104848A CN 201080010484 A CN201080010484 A CN 201080010484A CN 102341528 A CN102341528 A CN 102341528A
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- electrode
- enzyme
- fuel
- electrolysis
- reaction
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Classifications
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- H—ELECTRICITY
- H01—ELECTRIC ELEMENTS
- H01M—PROCESSES OR MEANS, e.g. BATTERIES, FOR THE DIRECT CONVERSION OF CHEMICAL ENERGY INTO ELECTRICAL ENERGY
- H01M8/00—Fuel cells; Manufacture thereof
- H01M8/16—Biochemical fuel cells, i.e. cells in which microorganisms function as catalysts
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/001—Enzyme electrodes
- C12Q1/004—Enzyme electrodes mediator-assisted
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/26—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase
- C12Q1/32—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving oxidoreductase involving dehydrogenase
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
- Y02E60/00—Enabling technologies; Technologies with a potential or indirect contribution to GHG emissions mitigation
- Y02E60/30—Hydrogen technology
- Y02E60/50—Fuel cells
Abstract
Provided is a method for electrolyzing a fuel whereby the electrolysis speed can be improved by inhibiting the reverse reaction of an enzyme. In the electrolysis of a fuel such as glucose by using an enzyme/electron mediator in which an enzyme such as gluconate-5-dehydrogenase, alcohol dehydrogenase or malate dehydrogenase and an electron mediator are immobilized on a porous electrode comprising a carbonaceous material or the like, the electrolysis reaction is conducted exclusively within the enzyme/electron mediator electrode.
Description
Technical field
The present invention relates to the fuel electrolysis process in the fuel cell.More specifically, the present invention relates in the biofuel cell to be fixed to the method for electrolysis fuel such as the glucose on it through enzyme.
Background technology
In biofuel cell; Enzyme as catalyzer is fixed at least one in negative pole and the positive pole; Such biofuel cell can be from extracting electronics such as glucose and alcoholic acid fuel-efficient ground, and can not use with the general industrial catalyzer such as glucose and alcoholic acid fuel.Therefore, as the fuel cell of future generation with heavy body and high security, biofuel cell has attracted to note in many ways (for example referring to patent document 1-3).
Fig. 8 shows the view of the reaction of enzymatic battery, and said enzymatic battery comprises enzyme and electron mediator is fixed to the carbon dioxide process carbon electrode on it, and uses glucose to act as a fuel.In enzymatic battery shown in Figure 8, the oxidizing reaction of glucose is carried out in negative pole, airborne oxygen (O
2) reduction reaction carries out at positive pole.In addition, in negative pole, electronics is pressed the sequential transfer of glucose, Hexose phosphate dehydrogenase, Reduced nicotinamide-adenine dinucleotide (NAD+), diaphorase, electron mediator and electrode (carbon).
Reference listing
Patent document
Patent document 1: japanese unexamined patent spy opens the 2007-280944 communique
Patent document 2: japanese unexamined patent spy opens the 2008-177088 communique
Patent document 3: japanese unexamined patent spy opens the 2008-270206 communique
Summary of the invention
Yet the prior biological fuel cell has following problems.In other words, the enzyme that is used for biofuel cell comprises the enzyme that causes this reaction (original reaction) and reversed reaction simultaneously.Therefore, under the situation of using the enzyme that causes reversed reaction, the electrolysis time of fuel increases, and generating efficiency reduces.Therefore, in the past, developed the enzyme that does not cause reversed reaction through gene transformation etc.If use the enzyme that does not cause reversed reaction, can shorten the electrolysis time of fuel, improve generating efficiency.But, for the practical application that realizes such enzyme needs labour and cost.
Therefore, it is a principal object of the present invention to provide a kind of reversed reaction and the fuel electrolysis process that improves electrolysis speed of inhibitory enzyme.
In fuel electrolysis process according to an embodiment of the invention, when the said fuel of electrolysis that is fixed to the upper through enzyme, electrolytic reaction only takes place in electrode.
In the present invention, because fuel electrolysis in electrode, so the reversed reaction of enzyme is suppressed, and electrolysis speed is enhanced.
In this electrolysis process, the endonuclease capable that causes reversed reaction is used as the enzyme that is fixed on the electrode.
In addition, electron mediator can be fixed on the said electrode with said enzyme, and can control the oxygenant of said electron mediator and the ratio between the reductive agent through changing the electromotive force that applies between the electrode.
In the case, the electromotive force that is higher than the half wave potential of said electron mediator is applied in.
In addition, the instance of the enzyme of initiation reversed reaction comprises glucono--5-desaturase, alcoholdehydrogenase and MDH.
According to embodiments of the invention because fuel electrolysis in electrode, so can the inhibitory enzyme reversed reaction, and can obtain to be equal to or greater than use do not cause reversed reaction enzyme situation electrolysis speed and need not carry out that gene are transformed etc.
Description of drawings
Fig. 1 shows wherein the view of the reaction that is extracted through oxydasis glucose and four electronics.
Fig. 2 is the view that schematically shows electrolytic method in the electrode according to an embodiment of the invention.
Fig. 3 is the view that schematically shows according to the outer electrolytic method of electrode of Comparative Examples.
Fig. 4 (a) and 4 (b) show the result's of the chronoamperometry of carrying out through the method for Comparative Examples shown in Figure 3 view.Fig. 4 (a) shows and uses the fixedly result of the example of the electrode of GDH, Fig. 4 (b) to show the fixedly result of the example of the electrode of Gn5DH of use.
Fig. 5 (a) and 5 (b) show the view of the speed of reaction of GDH.Fig. 5 (a) shows positive reaction, and Fig. 5 (b) shows reversed reaction.
Fig. 6 (a) and 6 (b) show the view of the speed of reaction of Gn5DH.Fig. 6 (a) shows positive reaction, and Fig. 6 (b) shows reversed reaction.
Fig. 7 (a) and 7 (b) show the result's of the chronoamperometry of carrying out through the method for embodiment shown in Figure 2 view.Fig. 7 (a) shows and uses the fixedly result of the example of the electrode of GDH, Fig. 7 (b) to show the fixedly result of the example of the electrode of Gn5DH of use.
Fig. 8 shows the view of the reaction of enzymatic battery, and wherein, said enzymatic battery comprises that enzyme and electron mediator are fixed to the carbon dioxide process carbon electrode on it, and uses glucose to act as a fuel.
Embodiment
Will describe embodiments of the invention in detail with reference to accompanying drawing hereinafter.Should be noted that and the invention is not restricted to embodiment described below.
[one-piece construction]
The contriver tested observantly already and checked, to solve the problem in the existing biofuel cell.As a result, the contriver has found the following fact.In other words; As in the described biofuel cell of patent document 1-3 therein solution be present in the system of outside of electrode and carry out under the electrolytic situation, adopt the electrolysis time of the enzyme that causes reversed reaction and adopt the difference between the electrolysis time of the enzyme that does not cause reversed reaction big especially.
Fig. 1 shows the view of the reaction that glucose wherein is extracted by oxydasis and four electronics.In this system, at first, glucose is obtained Gluconolactone by Hexose phosphate dehydrogenase (GDH) oxidation, thereby in this reaction, obtains two electronics.Subsequently, the Gluconolactone that is generated is degraded into the 5-glucono-by gluconolactonase and glucono--5-desaturase (Gn5DH).Be used under the situation of such system at the enzyme with high reversed reaction speed such as glucono--5-desaturase (Gn5DH),, reduced the electrolysis speed of entire cell owing to the rate limiting in the acting reaction of enzyme.
Therefore, the contriver has checked electrolysis in the electrode, replaces the outer electrolysis of existing electrode.As a result, the contriver finds that in electrode the electrolysis speed through enzyme is enhanced in the electrolysis, has obtained the present invention.In other words, in electrolysis process of the present invention, comprising that enzyme is fixed in the biofuel cell of the electrode on it, the electrolytic reaction of fuel only takes place in electrode.
[electrode]
In electrolysis process of the present invention, fuel is fixed to the enzyme liberating on the electrode, with the extraction electronics, and generates proton (H
+).As the electrode in this use, preferably by having inner hole and having the electrode that the carbon material of big surface-area is processed, said carbon material is such as being porous carbon, carbon ball, carbon felt and carbon paper.Should be noted that electrode materials is not limited to carbon material, and can use metallic substance such as titanium, gold, copper and mickel.
[enzyme]
The above-mentioned endonuclease capable that is fixed on the electrode suitably selects according to employed fuel.For example, be used as at glucose under the situation of fuel, can use the Hexose phosphate dehydrogenase (GDH) of oxidation and degraded glucose.In addition, under the situation of using monose such as glucose, preferably, with coenzyme oxydase and electron mediator with the acting oxydase of the degraded of fuel such as Hexose phosphate dehydrogenase (GDH) is fixed.
The reductive agent of oxidized enzyme of coenzyme oxydasis (for example NAD+, NADP+ or analogue) and coenzyme (for example NADH, NADPH or analogue) reductive coenzyme.The example comprises diaphorase (DI).Through the oxidasic effect of coenzyme, when coenzyme is resumed to oxygenant, generate electronics, and electronics is transferred to electrode from the coenzyme oxydase through electron mediator.
In addition, at glycocalix as under the situation of fuel, except oxydase, coenzyme oxydase and electron mediator, fixing degrading enzyme also preferably, said degrading enzyme promotes polysaccharide degradation (such as hydrolysis) with generation monose such as glucose.It should be noted that in specification sheets, " polysaccharide " is the polysaccharide with wide sense of this term, mean through hydrolysis and generate the glucide of two molecules or more polymolecular monose, and comprise oligosaccharides, like disaccharides, trisaccharide and tetrose by it.The specific examples of polysaccharide comprises starch (starch), amylose starch, pulullan, glycogen, Mierocrystalline cellulose, SANMALT-S, sucrose and lactose.In such polysaccharide, two or more monose are combined.In any polysaccharide, the monose of combining unit is served as in the involved conduct of glucose.
And amylose starch and pulullan are the components that comprises in the starch.Starch is the mixture of amylose starch and pulullan.For example, be used as the polysaccharide degradation enzyme, and Hexose phosphate dehydrogenase (GDH) is used as under the oxidasic situation of the monose of degrading, can uses the polysaccharide that can be degraded to glucose by glucoamylase at glucoamylase.The specific examples of such polysaccharide comprises starch, amylose starch, pulullan, glycogen and SANMALT-S.At this, glucoamylase is that hydrolysis alpha-glucan such as starch is with glucogenic degrading enzyme.Hexose phosphate dehydrogenase is that β-D-glucose oxidase is become maltonic acid-delta-lactone.
In addition, electrolysis process of the present invention is specially adapted to use the system of enzyme such as the glucono--5-desaturase (Gn5DH), alcoholdehydrogenase and the MDH that cause reversed reaction.
[electron mediator]
As being fixed to the electron mediator on the electrode surface with aforesaid enzyme, preferred use has the compound of quinone skeleton, and particularly, suitable use has the compound of naphthoquinones skeleton.Its specific examples comprises 2-amino-1,4-naphthoquinones (ANQ), 2-amino-3-methyl isophthalic acid, 4-naphthoquinones (AMNQ), 2-methyl isophthalic acid, 4-naphthoquinones (VK3) and 2-amino-3-carboxyl-1,4-naphthoquinones (ACNQ).In addition, as compound, except compound, can also use for example anthraquinone and verivate thereof with naphthoquinones skeleton with quinone skeleton.In addition, as required,, can also fix other compounds that one or more serve as electron mediator except having the compound of quinone skeleton.
[electrolysis process]
In electrolysis process of the present invention, electrolytic reaction only is fixed in the electrode on it at enzyme and takes place.For the not concrete restriction of this method, and the example comprises to the method for the fuel solution of electrode surface supply and the corresponding amount of surface-area and on electrode surface, forms the microfluidic path and the guiding fuel solution passes through the method for this flow passage.And, in the case,, can obtain very high electrolytic efficiency through sequentially keeping watch on electrolysis amount and fuel metering supply.In addition, other instances can comprise the pump that comprises feedback function, wherein utilize mass sensor to calculate the solution amount of evaporation, and the evaporation section of solution is replenished.
In electrolytic reaction, when between electrode, applying electromotive force, preferably apply the electromotive force of the half wave potential that is higher than electron mediator.Thus, the inside of electrode can be in the environment of the high oxidation agent/reductive agent ratio with electron mediator, and can the direction of W-response towards expectation be moved.
As stated, in electrolysis process of the present invention, electrolytic reaction only takes place in electrode.Therefore, can prevent the dissolving of electron mediator.In addition, can easily control the ratio between the Oxidizing and Reducing Agents of electron mediator through the electromotive force of setting.Thus, can promote the reaction of total system to carry out, and suppress the reversed reaction of enzyme towards the direction of this reaction.Therefore, can improve whole electrolysis speed.As a result, even use the enzyme that causes reversed reaction, also can improve generating efficiency, and need not carry out enzyme transformation etc.
Embodiment
To specifically effect of the present invention be described below with reference to embodiments of the invention and Comparative Examples.Fig. 2 schematically shows according to an embodiment of the invention electrolytic method in the electrode.Fig. 3 schematically shows according to the outer electrolytic method of the electrode of Comparative Examples.In an embodiment, the outer electrolysis (Comparative Examples) of the electrode shown in electrolysis (embodiment) and Fig. 3 utilizes the electrode that glucono--5-desaturase (Gn5DH) is fixed on it to carry out in the electrode shown in Fig. 2, and measures the fuel electrolysis time.In addition, in order to compare, the electrode that is fixed on it for Hexose phosphate dehydrogenase (GDH) has carried out similar measurement.
When the various enzymes of formation are fixed to the electrode on it respectively, at first, various solution (1)-(7) that preparation is following.In addition, as buffered soln, use the SODIUM PHOSPHATE, MONOBASIC (NaH of 100mM
2PO
4) buffered soln (I.S.=0.3, pH=7.0).And the buffered soln that wherein dissolves various enzymes is respectively preferably refrigerated, up to use.The enzyme buffer solution for preparing is also preferably by refrigeration as much as possible.
(1) DI enzyme buffer solution
Weighing, (EC1.6.99 is made by Unitika Ltd., B1D111), and in the buffered soln that is partly dissolved in 1ml with gained for the diaphorase (DI) of 5-50mg.
(2) GDH enzyme buffer solution
Weigh 5-50mg Hexose phosphate dehydrogenase (GDH) (NAD-relies on, EC1.1.1.47, by Toyobo Co., Ltd. (Co., Ltd. is spun by Japan) makes, GLD-311), and in the buffered soln that is partly dissolved in 1ml with gained.
(3) Gn5DH enzyme buffer solution
Weigh glucono--5-desaturase (Gn5DH) (NAD-is dependent, and EC1.1.1.69 is made by Amano Enzyme Inc.) of 5-50mg, and in the buffered soln that is partly dissolved in 1ml with gained.
(4) NADH buffered soln
The NADH of 10-50mg of weighing (is made by Sigma-Aldrich Corporation, N-8129), and in the buffered soln that is partly dissolved in 0.1ml with gained.
(5) ANQ acetone soln
The 2-of 10-50mg of weighing is amino-1,4-naphthoquinones (ANQ) (synthetic compound), and in the acetone that is partly dissolved in 1ml with gained.
(6) the PLL aqueous solution
Weigh the poly-L-Lysine hydrobromate (PLL) of appropriate amount (by Wako Pure Chemical Industries; Ltd. (Wako Pure Chemical Industries, Ltd.) makes; 164-16961), and with being partly dissolved in the water of IX of gained, to obtain the solution of 2wt%.
(7) the PAAcNa aqueous solution
The ZX-I (PAAcNa) of appropriate amount of weighing (is made by Sigma-Aldrich Corporation, 041-00595), and with being partly dissolved in the water of IX of gained, to obtain the solution of 0.22wt%.
Then, prepare and mix aforementioned each solution of specified rate, to obtain mixing solutions.With the applying porous carbon dioxide process carbon electrode of mixing solutions, dried electrode forms the electrode through enzyme/electron mediator coating then.The combined amount of various solution that is used for the mixing solutions of applying porous electrode is shown in the following table 1.
[table 1]
Then; Further be coated with electrode with (6) PLL aqueous solution (corresponding to the PLL of 0.2 μ g) of 50 μ L and (7) PAAcNa aqueous solution (corresponding to the PAAcNa of 0.003 μ g) of 50 μ L through enzyme/electron mediator coating; The subsequent drying electrode forms the electrode that is fixed with enzyme/electron mediator.In the above-mentioned electrode that respectively is fixed with enzyme/electron mediator; After this electrode with the mixing solutions coating that comprises GDH enzyme buffer solution will be called as " the fixedly electrode of GDH ", and after this electrode that is coated with the mixing solutions that comprises Gn5DH enzyme buffer solution will be called as " the fixedly electrode of Gn5DH ".
For the as above formed electrode 1 that is fixed with enzyme/electron mediator; Set the 0.1V electromotive force with respect to reference electrode 2 (Ag|AgCl); As the electromotive force of the half wave potential that fully is higher than electron mediator, and carry out chronoamperometry through Fig. 2 and method shown in Figure 3.At this moment, the solution that acts as a fuel uses the solution that obtains through following: glucose that acts as a fuel or glucono-are dissolved in the imidazole buffer solution (pH=7.0) of 2M, thereby make that concentration is 0.4M.These fuel solutions are after this with being called as " 0.4M glucose fuel solution " and " 0.4M glucono-fuel solution " respectively.
In addition, routine as a comparison, through carry out the outer electrolysis of electrode of glucose or glucono-based on the electrochemical measuring method of the three-electrode method shown in Fig. 3.At this moment, at the 0.4M glucose fuel solution that adds 2ml (0.8mmol) or 0.4M glucono-fuel solution and through in whisking appliance 5 stirred solutions, carry out electrolysis.In the electrolysis, the electrode 1 that is fixed with enzyme/electron mediator is used as anode (working electrode) outside the electrode of Comparative Examples, and platinum line 3 is used as counter electrode.
Fig. 4 (a) and 4 (b) show the result's of the chronoamperometry of carrying out through the method for Comparative Examples shown in Figure 3 view.Fig. 4 (a) shows and uses the fixedly result of the example of the electrode of GDH, Fig. 4 (b) to show the fixedly result of the example of the electrode of Gn5DH of use.Shown in Fig. 4 (a) and 4 (b), through using fixedly the electrode of Gn5DH to carry out outside the electrode under the electrolytic situation, it accomplishes all electrolytic for the situation of using the fixing electrode of GDH about 20 times consuming time.Therefore, find that fixedly the electrolysis speed of the electrode of Gn5DH is very slow.
Therefore, use ultraviolet ray (UV) to carry out among GDH and the Gn5DH separately positive reaction and the oxygen activity measurement of reversed reaction.The detection wavelength is 340nm, and uses the spectral measurement pond of the optical path length with 1cm.Comprise the glucose of 10mM or the phosphate buffer solution of glucono-(pH=7.0) as measuring solution, using.Each NAD+ concentration of measuring solution is conditioned respectively to obtain the total amount of 3ml.In addition, begin reaction through adding enzyme to the measurement solution for preparing.Be used as the speed of reaction of each enzyme by the speed (Δ ABS/min) of NAD+ generation NADH.
Fig. 5 (a) and 5 (b) show the view of the speed of reaction of GDH.Fig. 5 (a) shows positive reaction, and Fig. 5 (b) shows reversed reaction.Fig. 6 (a) and 6 (b) show the view of the speed of reaction of Gn5DH.Fig. 6 (a) shows positive reaction, and Fig. 6 (b) shows reversed reaction.Shown in Fig. 5 (a) and 5 (b) and Fig. 6 (a) and 6 (b), confirmed the reversed reaction speed of the reversed reaction speed of Gn5DH apparently higher than GDH.
Therefore, next, as embodiments of the invention, through electrolysis in the electrode of carrying out glucose or glucono-based on the electrochemical measuring method of the three-electrode method shown in Fig. 2.At this moment, through carrying out electrolysis as follows: 0.4M glucose fuel solution or the 0.4M glucono-fuel solution of 2 μ L are added drop-wise on the surface of the electrode 1 (the fixedly electrode of GDH and the fixedly electrode of Gn5DH) that is fixed with enzyme/electron mediator.In the electrolysis, the electrode 1 that is fixed with enzyme/electron mediator is used as anode (working electrode) in the electrode of embodiment, and platinum guaze 6 is used as counter electrode, and isolator (paper) 7 is set between the electrode 1 and platinum guaze 6 that is fixed with enzyme/electron mediator.
Fig. 7 (a) and 7 (b) show the result's of the chronoamperometry of carrying out through the method for embodiment shown in Figure 2 view.Fig. 7 (a) shows and uses the fixedly result of the example of the electrode of GDH, Fig. 7 (b) to show the fixedly result of the example of the electrode of Gn5DH of use.Shown in Fig. 7 (a) and 7 (b); In electrode in the electrolysis; In the electrode that uses fixing Gn5DH and two kinds of situations using the fixing electrode of GDH, all completion in the time of from 2000 to 3000 seconds (comprising two end points) of electrolysis show the difference that does not almost have electrolysis time.
From the results verification of front, through using electrolysis process of the present invention, can the inhibitory enzyme reversed reaction, and need not carry out that gene are transformed etc.In addition, confirmed,, can obtain to be equal to or greater than the electrolysis speed of situation that use does not cause the enzyme of reversed reaction even use the enzyme that causes reversed reaction through using electrolysis process of the present invention.
Claims (5)
1. fuel electrolysis process, wherein, when the said fuel of electrolysis that is fixed to the upper through enzyme, electrolytic reaction only takes place in electrode.
2. fuel electrolysis process as claimed in claim 1, wherein, the enzyme that causes reversed reaction is used as said enzyme.
3. fuel electrolysis process as claimed in claim 1, wherein, electron mediator is fixed on the said electrode with said enzyme, and
Control the oxygenant of said electron mediator and the ratio between the reductive agent through changing the electromotive force that applies between the electrode.
4. fuel electrolysis process as claimed in claim 3, wherein, the electromotive force that is higher than the half wave potential of said electron mediator is applied in.
5. fuel electrolysis process as claimed in claim 2, wherein, said enzyme is glucono--5-desaturase, alcoholdehydrogenase or MDH.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2009054493A JP2010209375A (en) | 2009-03-09 | 2009-03-09 | Electrolytic process |
| JP2009-054493 | 2009-03-09 | ||
| PCT/JP2010/053286 WO2010103954A1 (en) | 2009-03-09 | 2010-03-02 | Method for electrolyzing fuel |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN102341528A true CN102341528A (en) | 2012-02-01 |
Family
ID=42728244
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN2010800104848A Pending CN102341528A (en) | 2009-03-09 | 2010-03-02 | Method for electrolyzing fuel |
Country Status (4)
| Country | Link |
|---|---|
| US (1) | US20120000788A1 (en) |
| JP (1) | JP2010209375A (en) |
| CN (1) | CN102341528A (en) |
| WO (1) | WO2010103954A1 (en) |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1579033A (en) * | 2002-07-26 | 2005-02-09 | 索尼株式会社 | Fuel battery |
| WO2007088975A1 (en) * | 2006-02-02 | 2007-08-09 | Ube Industries, Ltd. | Carbon membrane having biological molecule immobilized thereon |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007035437A (en) * | 2005-07-27 | 2007-02-08 | Sony Corp | Porous conductive material and its manufacturing method, electrode and its manufacturing method, fuel cell and its manufacturing method, and electronic apparatus, moving object, power generation system, co-generation system, and electrode reaction utilization apparatus |
| KR20080080105A (en) * | 2005-11-02 | 2008-09-02 | 세인트 루이스 유니버시티 | Direct electron transfer using enzymes in bioanodes, biocathodes, and biofuel cells |
| US20090047567A1 (en) * | 2007-08-16 | 2009-02-19 | Sony Corporation | Biofuel cell, method for producing the same, electronic apparatus, enzyme-immobilized electrode, and method for producing the same |
-
2009
- 2009-03-09 JP JP2009054493A patent/JP2010209375A/en not_active Withdrawn
-
2010
- 2010-03-02 CN CN2010800104848A patent/CN102341528A/en active Pending
- 2010-03-02 WO PCT/JP2010/053286 patent/WO2010103954A1/en active Application Filing
- 2010-03-02 US US13/254,518 patent/US20120000788A1/en not_active Abandoned
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN1579033A (en) * | 2002-07-26 | 2005-02-09 | 索尼株式会社 | Fuel battery |
| WO2007088975A1 (en) * | 2006-02-02 | 2007-08-09 | Ube Industries, Ltd. | Carbon membrane having biological molecule immobilized thereon |
Also Published As
| Publication number | Publication date |
|---|---|
| US20120000788A1 (en) | 2012-01-05 |
| JP2010209375A (en) | 2010-09-24 |
| WO2010103954A1 (en) | 2010-09-16 |
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Application publication date: 20120201 |