US20120000788A1 - Electrolytic method of fuel - Google Patents

Electrolytic method of fuel Download PDF

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Publication number
US20120000788A1
US20120000788A1 US13/254,518 US201013254518A US2012000788A1 US 20120000788 A1 US20120000788 A1 US 20120000788A1 US 201013254518 A US201013254518 A US 201013254518A US 2012000788 A1 US2012000788 A1 US 2012000788A1
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Prior art keywords
enzyme
electrode
fuel
immobilized
reaction
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Abandoned
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US13/254,518
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Inventor
Ryuhei Matsumoto
Yoshio Goto
Hideki Sakai
Yuichi Tokita
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Sony Corp
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Sony Corp
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Assigned to SONY CORPORATION reassignment SONY CORPORATION ASSIGNMENT OF ASSIGNORS INTEREST (SEE DOCUMENT FOR DETAILS). Assignors: TOKITA, YUICHI, GOTO, YOSHIO, MATSUMOTO, RYUHEI, SAKAI, HIDEKI
Publication of US20120000788A1 publication Critical patent/US20120000788A1/en
Abandoned legal-status Critical Current

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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

Definitions

  • the present invention relates to an electrolytic method of a fuel in a fuel cell. More specifically, the present invention relates to a method of electrolyzing a fuel such as glucose by an electrode onto which an enzyme is immobilized in a bio-fuel cell.
  • a bio-fuel cell in which an enzyme as a catalyst is immobilized onto at least one of an anode and a cathode is able to efficiently extract electrons from a fuel such as glucose and ethanol incapable of being used with the use of a general industrial catalyst.
  • a fuel such as glucose and ethanol incapable of being used with the use of a general industrial catalyst.
  • the bio-fuel cell attracts attentions as a next generation fuel cell having high capacity and high safety (for example, see Patent documents 1 to 3).
  • FIG. 8 is a diagram illustrating reaction of an enzyme battery that includes a carbon electrode onto which an enzyme and an electron mediator are immobilized and that uses glucose as a fuel.
  • oxidation reaction of glucose proceeds in an anode
  • reduction reaction of oxygen (O 2 ) in the air proceeds in a cathode.
  • electrons are transferred in the order of glucose, glucose dehydrogenase, nicotinamide adenine dinucleotide (NAD+), diaphorase, the electron mediator, and the electrode (carbon).
  • the existing bio-fuel cell has a problem described below. That is, the enzymes used in the bio-fuel cell include an enzyme that initiates original reaction and reverse reaction concurrently. Thus, in the case where the enzyme initiating the reverse reaction is used, electrolytic time of the fuel is increased and power generation efficiency is lowered. Thus, in the past, an enzyme not initiating the reverse reaction has been developed by inheritable genetic modification or the like. If the enzyme not initiating the reverse reaction is used, electrolytic time of the fuel is able to be decreased and power generation efficiency is able to be improved. However, labor and cost are necessitated in order to realize practical use of such an enzyme.
  • electrolytic reaction is generated only in an electrode in electrolyzing the fuel by the electrode onto which an enzyme is immobilized.
  • an enzyme initiating reverse reaction is able to be used as the enzyme immobilized onto the electrode.
  • an electron mediator may be immobilized onto the electrode together with the enzyme, and ratio between an oxidant and a reductant of the electron mediator may be controlled by changing electric potential applied between electrodes.
  • examples of the enzyme initiating reverse reaction include gluconate-5-dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase.
  • FIG. 1 is a diagram illustrating reaction in which glucose is oxidized by an enzyme and four electrons are extracted.
  • FIG. 2 is a diagram schematically illustrating a method of in-electrode electrolysis according to Example of the present invention.
  • FIG. 3 is a diagram schematically illustrating a method of out-of-electrode electrolysis according to Comparative example.
  • FIGS. 4( a ) and 4 ( b ) are diagrams illustrating results of chronoamperometry performed by the method of Comparative example illustrated in FIG. 3 .
  • FIG. 4( a ) illustrates a result of a case using a GDH immobilized electrode
  • FIG. 4( b ) illustrates a result of a case using a Gn5DH immobilized electrode.
  • FIGS. 5( a ) and 5 ( b ) are diagrams illustrating reaction rate of GHD.
  • FIG. 5( a ) illustrates forward reaction
  • FIG. 5( b ) illustrates reverse reaction.
  • FIGS. 6( a ) and 6 ( b ) are diagrams illustrating reaction rate of Gn5DH.
  • FIG. 6( a ) illustrates forward reaction
  • FIG. 6( b ) illustrates reverse reaction.
  • FIGS. 7( a ) and 7 ( b ) are diagrams illustrating results of chronoamperometry performed by the method of Example illustrated in FIG. 2 .
  • FIG. 7( a ) illustrates a result of a case using the GDH immobilized electrode
  • FIG. 7( b ) illustrates a result of a case using the Gn5DH immobilized electrode.
  • FIG. 8 is a diagram illustrating reaction of an enzyme battery that includes a carbon electrode onto which an enzyme and an electron mediator are immobilized and that uses glucose as a fuel.
  • FIG. 1 is a diagram illustrating reaction in which glucose is oxidized by an enzyme and four electrons are extracted.
  • glucose is oxidized by glucose dehydrogenase (GDH) to obtain gluconolactone, and thereby two electrons are obtained with this reaction.
  • GDH glucose dehydrogenase
  • the generated gluconolactone is degraded into 5-dehydrogluconate by gluconolactonase and gluconate-5-dehydrogenase (Gn5DH).
  • Gn5DH glucose dehydrogenase
  • electrolytic rate of the entire cell is decreased by rate limitation in the reaction contributed by the enzyme.
  • the inventors examined in-electrode electrolysis instead of the existing out-of-electrode electrolysis.
  • electrolytic rate by the enzyme was improved in the in-electrode electrolysis, leading to the present invention. That is, in the electrolytic method of the present invention, in a bio-fuel cell including an electrode onto which an enzyme is immobilized, electrolytic reaction of a fuel is generated only in the electrode.
  • the fuel is degraded by the enzyme immobilized onto the electrode to extract electrons, and protons (H + ) is generated.
  • an electrode made of a carbon material having internal voids and having a large surface area such as porous carbon, carbon pellet, carbon felt, and carbon paper is preferable. It is to be noted that the electrode material is not limited to the carbon material, and a metal material such as titanium, gold, copper, and nickel is able to be used.
  • the above-mentioned enzyme immobilized onto the electrode is able to be selected as appropriate according to the fuel used.
  • glucose used as a fuel
  • glucose dehydrogenase (GDH) that oxidizes and degrades glucose is able to be used.
  • GDH glucose dehydrogenase
  • a coenzyme oxidase and an electron mediator are desirably immobilized together with an oxidase contributing to degradation of the fuel such as glucose dehydrogenase (GDH).
  • the coenzyme oxidase oxidizes a coenzyme reduced by the oxidase (for example, NAD+, NADP+ or the like) and a reductant of the coenzyme (for example, NADH, NADPH or the like).
  • oxidase for example, NAD+, NADP+ or the like
  • reductant of the coenzyme for example, NADH, NADPH or the like.
  • DI diaphorase
  • polysaccharide in addition to the oxidase, the coenzyme oxidase, and the electron mediator, a degrading enzyme that encourages degradation such as hydrolysis of the polysaccharide to generate a monomeric sugar such as glucose is desirably immobilized.
  • a degrading enzyme that encourages degradation such as hydrolysis of the polysaccharide to generate a monomeric sugar such as glucose is desirably immobilized.
  • polysaccharide is polysaccharide in the broad sense of the term, means all carbohydrates from which a monomeric sugar with two or more molecules is generated by hydrolysis, and includes an oligosaccharide such as a disaccharide, a trisaccharide, and a tetrasaccharide.
  • polysaccharide examples include starch, amylose, amylopectin, glycogen, cellulose, maltose, sucrose, and lactose. In such a polysaccharide, two or more monomeric sugars are bound. In any polysaccharide, glucose is contained as a monomeric sugar as a binding unit.
  • amylose and amylopectin are components contained in starch.
  • Starch is a mixture of amylose and amylopectin.
  • glucoamylase is used as a degradation enzyme of a polysaccharide
  • glucose dehydrogenase GDH
  • a polysaccharide capable of being degraded to glucose by glucoamylase is able to be used.
  • Specific examples of such a polysaccharide include starch, amylose, amylopectin, glycogen, and maltose.
  • Glucoamylase is a degradation enzyme that hydrolyzes ⁇ -glucan such as starch to generate glucose.
  • Glucose dehydrogenase is an oxidase that oxidizes ⁇ -D-glucose to D-glucono- ⁇ -lactone.
  • the electrolytic method of the present invention is in particular suitably applied to a system using an enzyme initiating reverse reaction such as gluconate-5-dehydrogenase (Gn5DH), alcohol dehydrogenase, and malate dehydrogenase.
  • an enzyme initiating reverse reaction such as gluconate-5-dehydrogenase (Gn5DH), alcohol dehydrogenase, and malate dehydrogenase.
  • a compound having a quinone skeleton is preferably used, and specially a compound having a naphthoquinone skeleton is suitably used.
  • Specific examples thereof include 2-amino-1,4-naphthoquinone (ANQ), 2-amino-3-methyl-1,4-naphthoquinone (AMNQ), 2-methyl-1,4-naphthoquinone (VK3), and 2-amino-3-carboxy-1,4-naphthoquinone (ACNQ).
  • the compound having a quinone skeleton in addition to the compound having a naphthoquinone skeleton, for example, anthraquinone and a derivative thereof are able to be used. Furthermore, according to needs, in addition to the compound having a quinone skeleton, one or more kinds of other compounds working as an electron mediator may be immobilized.
  • electrolytic reaction is generated only in the electrode onto which an enzyme is immobilized.
  • the method is not particularly limited, and examples thereof include a method of supplying an electrode surface with a fuel solution with a quantity corresponding to the surface area and a method of forming a micro flow path on the electrode surface and conducting a fuel solution through the flow path.
  • a pump including feedback function in which a vaporized solution amount is calculated by using a mass sensor, and a vaporization portion of solution is refilled.
  • electrolytic reaction as electric potential applied between electrodes, electric potential higher than half wave potential of the electron mediator is desirably applied. Thereby, inside of the electrode is able to be in the environment with high oxidant/reductant ratio of the electron mediator, and entire reaction is able to be shifted in desirable direction.
  • electrolytic reaction is generated only in the electrode.
  • dissolution of the electron mediator is able to be prevented.
  • ratio between the oxidant and the reductant of the electron mediator is able to be easily controlled by set electric potential.
  • FIG. 2 schematically illustrates a method of in-electrode electrolysis according to Example of the present invention.
  • FIG. 3 schematically illustrates a method of out-of-electrode electrolysis according to Comparative example.
  • the in-electrode electrolysis (Example) illustrated in FIG. 2 and the out-of-electrode electrolysis (Comparative example) illustrated in FIG. 3 were performed by using an electrode onto which gluconate-5-dehydrogenase (Gn5DH) was immobilized, and fuel electrolytic time was measured. Further, for comparison, similar measurement was performed for an electrode onto which glucose dehydrogenase (GDH) was immobilized.
  • each electrode onto which each enzyme was immobilized first, the following respective solutions (1) to (7) were prepared.
  • a buffer solution 100 mM of sodium dihydrogen phosphate (NaH 2 PO 4 ) buffer solution (I.S.: 0.3, pH: 7.0) was used.
  • the buffer solution in which each enzyme is dissolved is desirably kept in cold storage until just before usage.
  • the prepared enzyme buffer solution is also desirably kept in cold storage as much as possible.
  • DI diaphorase
  • GDH glucose dehydrogenase
  • Gn5DH gluconate-5-dehydrogenase
  • NADH manufactured by Sigma-Aldrich Corporation, N-8129
  • ANQ 2-amino-1,4-naphthoquinone
  • PLL poly-L-lysine hydrobromate
  • PAAcNa sodium polyacrylate
  • each given amount of the foregoing respective solutions was prepared and mixed to obtain a mixed solution.
  • a porous carbon electrode was coated with the mixed solution, was subsequently dried, and an enzyme/electron-mediator-coated electrode was formed.
  • Each blending quantity of each solution in the mixed solution with which the porous electrode was coated is shown in the following Table 1.
  • the enzyme/electron-mediator-coated electrode was further coated with 50 ⁇ L of (6) PLL aqueous solution (corresponding to 0.2 ⁇ g of PLL) and 50 ⁇ L of (7) PAAcNa aqueous solution (corresponding to 0.003 ⁇ g of PAAcNa), is subsequently dried, and an enzyme/electron mediator immobilized electrode was formed.
  • an electrode coated with a mixed solution containing the GDH enzyme buffer solution will be hereinafter referred to as “GDH immobilized electrode,” and an electrode coated with a mixed solution containing the Gn5DH enzyme buffer solution will be hereinafter referred to as “Gn5DH immobilized electrode.”
  • 0.1 V as electric potential sufficiently higher than half wave electric potential of the electron mediator was set with respect to a reference electrode 2 (Ag
  • a fuel solution a solution obtained by dissolving glucose or gluconic acid as a fuel in 2 M imidazole buffer solution (pH: 7.0) so that the concentration became 0.4 M was used.
  • 0.4 M glucose fuel solution and “0.4 M gluconic acid fuel solution,” respectively.
  • out-of-electrode electrolysis of glucose or gluconic acid was performed by the electrochemical measurement method based on three-electrode method illustrated in FIG. 3 .
  • electrolysis was performed while 2 ml (0.8 mmol) of the 0.4 M glucose fuel solution or the 0.4 M gluconic acid fuel solution was thrown in and the solution was stirred by a stirrer 5 .
  • the enzyme/electron mediator immobilized electrode 1 was used as an anode (work electrode), and a platinum wire 3 was used as a counter electrode.
  • FIGS. 4( a ) and 4 ( b ) are diagrams illustrating results of chronoamperometry performed by the method of Comparative example illustrated in FIG. 3 .
  • FIG. 4( a ) illustrates a result of a case using the GDH immobilized electrode
  • FIG. 4( b ) illustrates a result of a case using the Gn5DH immobilized electrode.
  • FIGS. 4( a ) and 4 ( b ) illustrates a result of a case using the Gn5DH immobilized electrode.
  • the out-of electrode electrolysis was performed by using the Gn5DH immobilized electrode, it took about 20 times as many as in the case of using the GDH immobilized electrode to complete all electrolysis. Thereby, it was found that the electrolysis rate of the Gn5DH immobilized electrode was significantly slow.
  • oxygen activity measurement of respective forward reactions and reverse reactions in GDH and Gn5DH was performed by using ultraviolet light (UV).
  • the detection wavelength was 340 nm, and the spectroscopic measurement cell having a light path length of 1 cm was used.
  • As a measurement solution a phosphate buffer solution (pH: 7.0) containing 10 mM of glucose or gluconic acid was used. Each NAD+ concentration of each measurement solution was adjusted to obtain the entire amount of 3 ml. Further, reaction was started by adding the enzyme to the prepared measurement solution. A rate at which NADH was generated from NAD+ ( ⁇ ABS/min) was regarded as reaction rate of each enzyme.
  • FIGS. 5( a ) and 5 ( b ) are diagrams illustrating reaction rate of GHD.
  • FIG. 5( a ) illustrates forward reaction
  • FIG. 5( b ) illustrates reverse reaction
  • FIGS. 6( a ) and 6 ( b ) are diagrams illustrating reaction rate of Gn5DH.
  • FIG. 6( a ) illustrates forward reaction
  • FIG. 6( b ) illustrates reverse reaction.
  • FIGS. 5( a ) and 5 ( b ) and FIGS. 6( a ) and 6 ( b ) it was confirmed that reverse reaction rate of Gn5DH was significantly higher than that of GDH.
  • Example of the present invention in-electrode electrolysis of glucose or gluconic acid was performed by the electrochemical measurement method based on three-electrode method illustrated in FIG. 2 .
  • electrolysis was performed by dropping 2 ⁇ L of the 0.4 M glucose fuel solution or the 0.4 M gluconic acid fuel solution onto the surface of the enzyme/electron mediator immobilized electrode 1 (the GDH immobilized electrode or the Gn5DH immobilized electrode).
  • the enzyme/electron mediator immobilized electrode 1 was used as an anode (work electrode), a platinum mesh 6 was used as a counter electrode, and an insulator (paper) 7 was provided between the enzyme/electron mediator immobilized electrode 1 and the platinum mesh 6 .
  • FIGS. 7( a ) and 7 ( b ) are diagrams illustrating results of chronoamperometry performed by the method of Example illustrated in FIG. 2 .
  • FIG. 7( a ) illustrates a result of a case using the GDH immobilized electrode
  • FIG. 7( b ) illustrates a result of a case using the Gn5DH immobilized electrode.
  • electrolysis was completed within from 2000 to 3000 seconds both inclusive, showing almost no difference in electrolysis time.

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JP2009054493A JP2010209375A (ja) 2009-03-09 2009-03-09 電解方法
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PCT/JP2010/053286 WO2010103954A1 (ja) 2009-03-09 2010-03-02 燃料の電解方法

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Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP1531512A1 (en) * 2002-07-26 2005-05-18 Sony Corporation Fuel battery
US20070062821A1 (en) * 2005-07-27 2007-03-22 Sony Corporation Porous electroconductive material and process for production thereof; electrode and process for production thereof; fuel cell and process for production thereof; and electronic instrument, mobile machine, electric power generating system, cogeneration system, and electrode reaction-based apparatus
WO2007088975A1 (ja) * 2006-02-02 2007-08-09 Ube Industries, Ltd. 生体分子固定化炭素膜

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US8415059B2 (en) * 2005-11-02 2013-04-09 St. Louis University 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

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP1531512A1 (en) * 2002-07-26 2005-05-18 Sony Corporation Fuel battery
US20070062821A1 (en) * 2005-07-27 2007-03-22 Sony Corporation Porous electroconductive material and process for production thereof; electrode and process for production thereof; fuel cell and process for production thereof; and electronic instrument, mobile machine, electric power generating system, cogeneration system, and electrode reaction-based apparatus
WO2007088975A1 (ja) * 2006-02-02 2007-08-09 Ube Industries, Ltd. 生体分子固定化炭素膜
US20090192297A1 (en) * 2006-02-02 2009-07-30 Ube Industries, Ltd. Carbon membrane having biological molecule immobilized thereon

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