WO2005093400A1 - Capteur d’enzyme sans fil de type cellule electrochimique - Google Patents

Capteur d’enzyme sans fil de type cellule electrochimique Download PDF

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Publication number
WO2005093400A1
WO2005093400A1 PCT/JP2005/003108 JP2005003108W WO2005093400A1 WO 2005093400 A1 WO2005093400 A1 WO 2005093400A1 JP 2005003108 W JP2005003108 W JP 2005003108W WO 2005093400 A1 WO2005093400 A1 WO 2005093400A1
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Prior art keywords
enzyme
enzyme sensor
change
concentration
anode
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PCT/JP2005/003108
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English (en)
Japanese (ja)
Inventor
Koji Sode
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Ultizyme International Ltd.
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Publication date
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Priority to JP2006511403A priority Critical patent/JPWO2005093400A1/ja
Publication of WO2005093400A1 publication Critical patent/WO2005093400A1/fr

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Classifications

    • G—PHYSICS
    • G01—MEASURING; TESTING
    • G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
    • G01N27/00—Investigating or analysing materials by the use of electric, electrochemical, or magnetic means
    • G01N27/26—Investigating or analysing materials by the use of electric, electrochemical, or magnetic means by investigating electrochemical variables; by using electrolysis or electrophoresis
    • G01N27/28—Electrolytic cell components
    • G01N27/30—Electrodes, e.g. test electrodes; Half-cells
    • G01N27/327—Biochemical electrodes, e.g. electrical or mechanical details for in vitro measurements
    • G01N27/3271—Amperometric enzyme electrodes for analytes in body fluids, e.g. glucose in blood
    • 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

Definitions

  • the present invention relates to an enzyme sensor.
  • An enzyme sensor is a sensor in which an enzyme is immobilized on an electrode surface such as an oxygen electrode or a hydrogen peroxide electrode, and the enzyme reaction detects the concentration of a compound used as a substrate by the enzyme as a signal of the electrode.
  • an enzyme is immobilized on an electrode surface such as an oxygen electrode or a hydrogen peroxide electrode, and the enzyme reaction detects the concentration of a compound used as a substrate by the enzyme as a signal of the electrode.
  • a glucose sensor that can easily and quickly measure a blood glucose level has been developed.
  • the number of diabetic patients tends to increase year by year, and diagnosis of diabetes and home management of patients are very important. Therefore, glucose sensors that can easily and quickly measure blood glucose levels have been developed.
  • Darcos oxidase (GOD) is most often used as a glucose sensor element.
  • GOD glucose detection an oxygen electrode type that detects oxygen consumed during the oxidation reaction of GOD glucose or a hydrogen peroxide electrode type that detects generated hydrogen peroxide has been developed.
  • glucose dehydrogenase has been attracting attention as an ideal mediator-type sensor element that is not affected by the concentration of dissolved oxygen.
  • the enzyme-linked PQQ glucose dehydrogenase PQQGDH
  • PQQGDH enzyme-linked PQQ glucose dehydrogenase
  • the response current value is high. High response time no longer. That is, accurate and quick measurement is possible.
  • it since it is a coenzyme-bound type, it is not necessary to add an expensive coenzyme to the reaction solution.
  • QQGDH PQQGDH-B
  • QQGDH-B is very ideal as an element of a glucose sensor. In any case, continuous and reliable development of a blood glucose measurement device is desired.
  • An object of the present invention is to provide a new principle of an enzyme sensor that can continuously measure the concentration of a substrate wirelessly and does not include a power source. Means for solving the problem
  • the present invention includes a circuit that resonates by radio waves supplied wirelessly from the outside, and an enzyme fuel cell that applies a potential to the circuit.
  • a fuel cell is an enzyme fuel cell that uses an enzyme for the anode, where the potential (electromotive force) changes depending on the concentration of the substrate to be measured.
  • a disposable sensor chip consisting of a resonance circuit that converts the change in electromotive force of the enzyme fuel cell into a change in resonance frequency is used, and this is used for external force control, display, and radio wave transmission. It is an enzyme sensor system that also comprises the power of an external controller for receiving.
  • the capacitor is constituted by a resonance circuit using a varicap diode.
  • the enzyme used for the anode is acid oxidase, particularly when glucose is to be measured, glucose oxidase or glucose dehydrogenase.
  • glucose dehydrogenase is an enzyme containing pyro-mouth quinolinine quinone (PQQ) or flavin adenine dinucleotide (FAD) as a coenzyme.
  • the present invention relates to an enzyme sensor characterized in that the concentration of a substrate is measured by an electromotive force generated by passing electrons generated by an enzyme reaction at an anode to an electron acceptor at a cathode. It is.
  • the present invention is the above-described enzyme sensor, further comprising an oscillation circuit, wherein a resonance frequency in the oscillation circuit changes based on the electromotive force, and the resonance frequency is detected to detect a substrate.
  • An enzyme sensor characterized by measuring a concentration.
  • the present invention is the enzyme sensor described above, wherein the resonance frequency is detected by a radio wave supplied from the outside.
  • the present invention is the enzyme sensor described above, wherein the change in electromotive force depending on the substrate concentration at the anode changes the resonance frequency in the oscillation circuit.
  • the present invention is the enzyme sensor described above, characterized by using a resonance circuit that converts a change in electromotive force into a change in capacitor capacitance.
  • the present invention is the above-mentioned enzyme sensor, characterized by using a barrier diode to convert a change in electromotive force into a change in capacitor capacitance.
  • the present invention relates to an enzyme sensor including a circuit that resonates with a radio wave supplied wirelessly by an external force,
  • the change in the potential is caused by a change in electromotive force of an enzyme fuel cell using an enzyme as an anode
  • the change in the electromotive force depends on the concentration of the substrate to be measured, It is an enzyme sensor.
  • the present invention is the above-mentioned enzyme sensor, characterized by using an enzyme using glucose as a substrate as an anode enzyme.
  • the present invention also provides the enzyme sensor described above, wherein the enzyme is a glucose oxidase.
  • the present invention is the above enzyme sensor, wherein the enzyme is glucose dehydrogenase.
  • the present invention is the above enzyme sensor, wherein the glucose dehydrogenase has pyroquinoline quinone as a coenzyme.
  • the present invention is the above-mentioned enzyme sensor, wherein the glucose dehydrogenase has flavin adenyldinucleotide (FAD) as a coenzyme.
  • FAD flavin adenyldinucleotide
  • FIG. 1 shows a configuration diagram of an enzyme fuel cell of the present invention.
  • FIG. 2 shows a circuit diagram of a fuel cell type wireless enzyme sensor of the present invention.
  • FIG. 3 shows the glucose concentration dependence of the output current of an enzyme fuel cell using the catalytic subunit of glucose dehydrogenase using FAD as a coenzyme of the present invention as an anode enzyme.
  • FIG. 4 shows the glucose concentration dependence of the output voltage of an enzyme fuel cell using the catalytic subunit of glucose dehydrogenase using FAD of the present invention as a coenzyme as an anode enzyme.
  • FIG. 5 shows the glucose concentration dependence of the output of an enzyme fuel cell using the catalytic subunit of glucose dehydrogenase using FAD of the present invention as a coenzyme as an anode enzyme.
  • FIG. 6 shows the glucose concentration dependence of the output current of an enzyme fuel cell using the glucose dehydrogenase complex using FAD of the present invention as a coenzyme as an anodic enzyme.
  • FIG. 7 shows the glucose concentration dependency of the output voltage of an enzyme fuel cell using the glucose dehydrogenase complex using FAD of the present invention as a coenzyme as an anode enzyme.
  • Fig. 8 shows the dependence of the output of an enzyme fuel cell on the dulcose concentration when the glucose dehydrogenase complex of the present invention using FAD as a coenzyme was used as an anodic enzyme.
  • FIG. 9 shows a block diagram of a fuel cell type wireless enzyme sensor of the present invention.
  • FIG. 10 shows a block diagram of a fuel cell type wireless enzyme sensor (including a signal amplifier (amplifier)) of the present invention.
  • various acid reductases can be used.
  • glucose dehydrogenase using glucose oxidase or FAD or PQQ as a coenzyme is desired.
  • This may be a microorganism producing the enzyme, an enzyme isolated and purified from cells, or an enzyme recombinantly produced in E. coli or the like.
  • the fuel cell used in the present invention is an enzyme fuel cell characterized in that an oxidase or a dehydrogenase is fixed to an anode.
  • the force source may be an electrode using an enzyme that reduces oxygen, such as pyrilvin oxidase, or an electrode combining an appropriate electron acceptor.
  • the anode can be configured to include an electron acceptor together with the enzyme. That is, an electron obtained by the enzymatic reaction may be passed to an artificial electron acceptor, and this may be oxidized on an electrode.
  • a dehydrogenase that can transfer electrons directly to an electrode can form an anode without adding an artificial electron acceptor.
  • a carbon electrode, a gold electrode, a platinum electrode, or the like can be used as an electrode material for the anode and the force source.
  • the artificial electron acceptor of the anode is not particularly limited, and examples thereof include an osmium complex, a ruthenium complex, phenazine methosulfate, and derivatives thereof.
  • the enzyme of force sword is not particularly limited, but pyrylvin oxidase and laccase can be applied.
  • the artificial electron acceptor of the force sword is not particularly limited, but potassium ferricyanide, ABTS and the like can be used.
  • various oxidases can be used as the anode enzyme! /, And dehydrogenase can be used.
  • dehydrogenase can be used.
  • P Glucose dehydrogenase using QQ or FAD as a coenzyme can be used.
  • the immobilized enzyme may be prepared and then mounted on an electrode using a general enzyme immobilization method.
  • a di-crosslinking reagent such as daltaraldehyde
  • the mixture is immobilized in a synthetic polymer such as a photo-crosslinkable polymer, a conductive polymer, or an acid-reducing polymer, or a natural polymer matrix.
  • the mixed protein thus prepared is mixed with the carbon paste or mixed with the carbon paste and then subjected to a crosslinking treatment, and the mixture prepared is mounted on an electrode made of carbon, gold, platinum, or the like.
  • the enzyme when the enzyme is mounted on the electrode in this way, the artificial electron acceptor can be immobilized at the same time.
  • glucose dehydrogenase using FAD as a coenzyme, FADGDH, and methoxyphenazine methosulfate (mPMS) are mixed, further mixed with a carbon paste, and then freeze-dried. This is mounted on a carbon electrode, and immersed in an aqueous solution of daltaraldehyde in that state to crosslink the protein and create an enzyme electrode.
  • oxidation or dehydrogenation appeal using the measurement object as a substrate is fixed to the anode electrode.
  • An oxygen reductase is immobilized on the force sword.
  • the electrode thus prepared is used as an anode and an electrode for a force source.
  • m-PMS can be used as a human electron acceptor
  • ABTS can be used as an artificial electron acceptor.
  • a battery is constructed by connecting a variable resistor between the two electrodes, and the resulting current or voltage value is measured by adding a sample containing the substrate to be measured.
  • the addition of a sample changes the voltage value in a substrate concentration-dependent manner, and the voltage value changes the capacitance of the varicap diode constituting the resonance circuit, resulting in a change in the resonance frequency.
  • concentration of the substrate can be measured. That is, the correlation between the resonance frequency and the substrate concentration is recorded in advance, a calibration curve is created based on the correlation, and the substrate concentration of the unknown sample can be measured from the observed resonance frequency.
  • a heat-resistant glucose dehydrogenase catalytic subunit using FAD as a coenzyme was prepared according to a previous report, and the anode electrode was fixed.
  • the enzyme used was recombinantly produced using Escherichia coli.
  • the force source electrode was prepared by mixing Myrothecium sp.-derived bilirubin oxidase (Bilirubin Oxidase; BOD) (provided by Amano Enzym) with 20 mg of carbon paste and freeze-drying. The amount of enzyme used was 50 U according to a previous report. After mixing this well, it was filled only on the surface of the carbon paste electrode already filled with about 40 mg of carbon paste, and polished on filter paper. These electrodes, and stirred at 10mM MOPS buf fer (pH7. 0 ) 30 min in room temperature with 1% glutaraldehyde, further lOmM Tris buffer (pH 7. 0 ) was stirred at 2 0 min at room temperature in.
  • BOD Myrothecium sp.-derived bilirubin Oxidase
  • This electrode is kept in lOmM MOPS buffer (pH 7.0) for 1 hour or less. Stir at room temperature to equilibrate. Except during measurement, the cells were stored at 4 ° C in 10 mM MOPS buffer (pH 7.0).
  • the thus prepared BOD electrode and force sword reaction solution were mixed with 100 mM ppb (pH 7.0) 98001 and 25 mM ABTS 2001 (final concentration; 0.5 mM), and the total amount was used as 10 mM.
  • the electrodes and the reaction solution were set in separate thermostat cells for the anode and the power source, and the cells were connected by a salt bridge (a 2.17M KC1 solution solidified with 30% agarose) to construct a battery.
  • a variable resistor and digital multimeter were connected between each electrode (Fig. 1). The measurement was performed at 25 ° C. The load was changed stepwise from 1 ⁇ to 1 M ⁇ with a variable resistor, and the resulting current and voltage values were measured with a digital multimeter. The anode, force sword and digital multimeter were connected in series for current measurement and connected in parallel for voltage measurement. The power was determined by the product of the current value and the voltage value.
  • Example 2
  • a cell was constructed with an m-PMS concentration of 2 mM in an enzyme fuel cell using an anode electrode on which a 20 U catalytic subunit was fixed.
  • a load of resistance 40 k ⁇ was applied, the glucose concentration of the anode was gradually increased by the OmM force, and the current and voltage values obtained at each glucose concentration were measured with a digital multimeter to calculate the power.
  • the current density and the power density were determined by the quotient of the obtained current value and power value with respect to the electrode surface area (7.1 ⁇ 10 ′′ 2 cm 2 ).
  • Figures 3, 4 and 5 show the glucose concentration dependence of the current, voltage and power of the battery in which the glucose dehydrogenase catalytic subunit 20U using FAD as a coenzyme is immobilized. Electric power was obtained by the addition of glucose, and the electric power increased in a glucose concentration-dependent manner. Thus, the glucose concentration of the unknown sample can be measured from the output of the present enzyme fuel cell.
  • Example 3
  • a fuel cell was constructed in which an electrode on which a glucose dehydrogenase complex having FAD as a coenzyme was immobilized was used as an anode.
  • 20 U (290 ⁇ g) of glucose dehydrogenase complex was mixed with 20 mg of carbon paste and freeze-dried. After mixing well, the surface of the carbon paste electrode previously filled with about 40 mg of carbon paste was filled and polished on filter paper.
  • These electrodes were stirred in lOOmM p.p.b. (pH 7.0) containing 1% glutaraldehyde for 30 minutes at room temperature, and further stirred in lOmM Tris buffer (pH 7.0) for 20 minutes at room temperature.
  • a resistance load of 40k ⁇ is applied, the glucose concentration at the anode is increased stepwise from OmM, and the current and voltage values obtained at each glucose concentration are measured with a digital multimeter to calculate the power.
  • Immobilize glucose dehydrogenase complex 20U with FAD as coenzyme Figures 6, 7, and 8 show the glucose concentration dependence of the battery current, voltage and power. Electric power was obtained by the addition of glucose, and the electric power increased in a glucose concentration-dependent manner. Thus, the glucose concentration of the unknown sample can be measured from the output of the present enzyme fuel cell.
  • the present invention provides a new principle of an enzyme sensor that can continuously measure the concentration of a substrate wirelessly and does not include a power source.

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  • Chemical & Material Sciences (AREA)
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Abstract

[PROBLEMES] Nouveau principe d’un capteur d’enzyme susceptible de mesurer en continu la concentration d’un substrat sans fil, n’incluant aucune alimentation. [MOYENS POUR RESOUDRE LES PROBLEMES] Il est prévu un système capteur d’enzyme comprenant une puce capteur jetable composée d’un circuit résonnant à la réception d’une onde radio sans fil provenant de l’extérieur, une cellule électrochimique d’enzyme appliquant un potentiel au circuit, la cellule électrochimique étant une cellule électrochimique à enzyme sous forme d’anode changeant de potentiel en fonction de la concentration de substrat à mesurer, et un circuit de résonance convertissant un changement de puissance de la cellule électrochimique à enzyme en changement de fréquence de résonance, et un contrôleur externe réalisant le contrôle, l’affichage, la réception et la transmission d’une onde radio sur la puce capteur depuis l’extérieur. On peut mesurer sans fil un substrat cible à l’aide d’un capteur d’enzyme caractérisé par la détection de la concentration du substrat en fonction de la concentration d’un élément de détection et à l’aide d’un changement de force électromotrice comme indice, dans une force électromotrice produite par le transfert d’électrons né d’une réaction d’enzyme d’anode vers un récepteur externe d’électrons au niveau d’une cathode.
PCT/JP2005/003108 2004-03-25 2005-02-25 Capteur d’enzyme sans fil de type cellule electrochimique WO2005093400A1 (fr)

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Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2009037840A1 (fr) * 2007-09-18 2009-03-26 Tokyo University Of Agriculture And Technology Procédé pour mesurer une concentration de substrat et son dispositif
RU2476869C2 (ru) * 2007-09-18 2013-02-27 Алтизайм Интернэшнл Лтд Ферментный электрод
ES2786450A1 (es) * 2019-04-09 2020-10-09 Consejo Superior Investigacion Procedimiento de cuantificacion de la concentracion de analitos en una celda electroquimica
JPWO2019189808A1 (ja) * 2018-03-29 2021-03-18 東洋紡株式会社 ナノカーボンの電子伝達作用

Citations (2)

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Publication number Priority date Publication date Assignee Title
JP2001137207A (ja) * 1999-11-17 2001-05-22 Star Medical Kk 小動物用埋込型医学的計測送信装置
WO2003019170A1 (fr) * 2001-08-29 2003-03-06 Yissum Research Development Company Of The Hebrew University Of Jerusalem Biocapteur autonome

Patent Citations (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2001137207A (ja) * 1999-11-17 2001-05-22 Star Medical Kk 小動物用埋込型医学的計測送信装置
WO2003019170A1 (fr) * 2001-08-29 2003-03-06 Yissum Research Development Company Of The Hebrew University Of Jerusalem Biocapteur autonome

Non-Patent Citations (2)

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Title
SODE K. ET AL: "Tainetsusei Glucose Dassuiso Koso o Mochiita Seibutsu Nenryo Denchi no Kaihatsu.", THE CHEMICAL SOCIETY OF JAPAN KOEN YOKOSHU., vol. 84, no. 2, 11 March 2004 (2004-03-11), pages 1166 - ABSTR.NR. 3 J6-31, XP002996536 *
YUBASHI N. ET AL: "Glucose Dassuiso Koso o Mochiita Koso Denchi no Kaihatsu.", KOSO KOGAKU KENKYUKAI KOENKAI KOEN YOSHITSHU., 24 October 2003 (2003-10-24), pages 68, XP002996535 *

Cited By (16)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US9617576B2 (en) 2007-09-18 2017-04-11 Bioengineering Laboratories, Llc Enzyme electrode
US8641972B2 (en) 2007-09-18 2014-02-04 Bioengineering Laboratories, Llc Device for measuring substrate concentration
US8252236B2 (en) 2007-09-18 2012-08-28 Bioengineering Laboratories, Llc Method for measuring substrate concentration and device for the same
JP5051479B2 (ja) * 2007-09-18 2012-10-17 国立大学法人東京農工大学 基質濃度の測定方法及びその装置
WO2009037840A1 (fr) * 2007-09-18 2009-03-26 Tokyo University Of Agriculture And Technology Procédé pour mesurer une concentration de substrat et son dispositif
RU2476869C2 (ru) * 2007-09-18 2013-02-27 Алтизайм Интернэшнл Лтд Ферментный электрод
CN101802601A (zh) * 2007-09-18 2010-08-11 究极酵素国际股份有限公司 基质浓度的测定方法和其装置
US8642344B2 (en) 2007-09-18 2014-02-04 Bioengineering Laboratories, Llc Method for measuring substrate concentration
JP2012255790A (ja) * 2007-09-18 2012-12-27 Tokyo Univ Of Agriculture & Technology 基質濃度の測定方法及びその装置
US20170191105A1 (en) * 2007-09-18 2017-07-06 Arkray, Inc. Enzyme electrode
JPWO2019189808A1 (ja) * 2018-03-29 2021-03-18 東洋紡株式会社 ナノカーボンの電子伝達作用
JP7398744B2 (ja) 2018-03-29 2023-12-15 東洋紡株式会社 ナノカーボンの電子伝達作用
US11906461B2 (en) 2018-03-29 2024-02-20 Toyobo Co., Ltd. Electron transfer by nanocarbon
ES2786450A1 (es) * 2019-04-09 2020-10-09 Consejo Superior Investigacion Procedimiento de cuantificacion de la concentracion de analitos en una celda electroquimica
WO2020208286A1 (fr) 2019-04-09 2020-10-15 Consejo Superior De Investigaciones Científicas Dispositif et procédé de quantification de la concentration d'analytes dans un échantillon
CN114026412A (zh) * 2019-04-09 2022-02-08 西班牙高等科研理事会 样品中分析物浓度定量的装置和程序

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