CN1049009C - Organic phase biosensor prepared from low-temperature hydrogel immobilized enzyme - Google Patents
Organic phase biosensor prepared from low-temperature hydrogel immobilized enzyme Download PDFInfo
- Publication number
- CN1049009C CN1049009C CN 94108666 CN94108666A CN1049009C CN 1049009 C CN1049009 C CN 1049009C CN 94108666 CN94108666 CN 94108666 CN 94108666 A CN94108666 A CN 94108666A CN 1049009 C CN1049009 C CN 1049009C
- Authority
- CN
- China
- Prior art keywords
- organic phase
- low temperature
- enzyme
- enzymes
- temperature hydrogel
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Fee Related
Links
- 239000000017 hydrogel Substances 0.000 title claims abstract description 16
- 239000012074 organic phase Substances 0.000 title claims abstract description 16
- 108010093096 Immobilized Enzymes Proteins 0.000 title abstract description 3
- 102000004190 Enzymes Human genes 0.000 claims abstract description 27
- 108090000790 Enzymes Proteins 0.000 claims abstract description 27
- 239000004372 Polyvinyl alcohol Substances 0.000 claims abstract description 13
- 229920002451 polyvinyl alcohol Polymers 0.000 claims abstract description 13
- 239000001913 cellulose Substances 0.000 claims abstract description 12
- 229920002678 cellulose Polymers 0.000 claims abstract description 12
- 238000007710 freezing Methods 0.000 claims description 17
- 230000008014 freezing Effects 0.000 claims description 16
- 238000000034 method Methods 0.000 claims description 12
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 10
- 108010001336 Horseradish Peroxidase Proteins 0.000 claims description 6
- XOGGUFAVLNCTRS-UHFFFAOYSA-N tetrapotassium;iron(2+);hexacyanide Chemical compound [K+].[K+].[K+].[K+].[Fe+2].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-] XOGGUFAVLNCTRS-UHFFFAOYSA-N 0.000 claims description 5
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 4
- 101710088194 Dehydrogenase Proteins 0.000 claims description 3
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 3
- 238000002156 mixing Methods 0.000 claims description 3
- 238000003756 stirring Methods 0.000 claims description 3
- 239000007864 aqueous solution Substances 0.000 abstract description 12
- 230000004044 response Effects 0.000 abstract description 10
- 238000002360 preparation method Methods 0.000 abstract description 9
- 239000000203 mixture Substances 0.000 abstract description 4
- 229940088598 enzyme Drugs 0.000 description 15
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 14
- MVPPADPHJFYWMZ-UHFFFAOYSA-N chlorobenzene Chemical compound ClC1=CC=CC=C1 MVPPADPHJFYWMZ-UHFFFAOYSA-N 0.000 description 12
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 9
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 7
- 239000003960 organic solvent Substances 0.000 description 5
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 3
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 229910002804 graphite Inorganic materials 0.000 description 3
- 239000010439 graphite Substances 0.000 description 3
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 239000011149 active material Substances 0.000 description 2
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 150000002978 peroxides Chemical class 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 2
- WSLDOOZREJYCGB-UHFFFAOYSA-N 1,2-Dichloroethane Chemical compound ClCCCl WSLDOOZREJYCGB-UHFFFAOYSA-N 0.000 description 1
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- 108010025188 Alcohol oxidase Proteins 0.000 description 1
- 102000003914 Cholinesterases Human genes 0.000 description 1
- 108090000322 Cholinesterases Proteins 0.000 description 1
- 108020005199 Dehydrogenases Proteins 0.000 description 1
- 101000892220 Geobacillus thermodenitrificans (strain NG80-2) Long-chain-alcohol dehydrogenase 1 Proteins 0.000 description 1
- 108010029541 Laccase Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 239000012620 biological material Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- 229940048961 cholinesterase Drugs 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- JHIVVAPYMSGYDF-UHFFFAOYSA-N cyclohexanone Chemical compound O=C1CCCCC1 JHIVVAPYMSGYDF-UHFFFAOYSA-N 0.000 description 1
- 238000000280 densification Methods 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 229920001971 elastomer Polymers 0.000 description 1
- 239000000806 elastomer Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- KTWOOEGAPBSYNW-UHFFFAOYSA-N ferrocene Chemical compound [Fe+2].C=1C=C[CH-]C=1.C=1C=C[CH-]C=1 KTWOOEGAPBSYNW-UHFFFAOYSA-N 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- HZVOZRGWRWCICA-UHFFFAOYSA-N methanediyl Chemical compound [CH2] HZVOZRGWRWCICA-UHFFFAOYSA-N 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 229950006238 nadide Drugs 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 150000002989 phenols Chemical class 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 150000004053 quinones Chemical class 0.000 description 1
- 238000005096 rolling process Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 230000008961 swelling Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- BYGOPQKDHGXNCD-UHFFFAOYSA-N tripotassium;iron(3+);hexacyanide Chemical compound [K+].[K+].[K+].[Fe+3].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-].N#[C-] BYGOPQKDHGXNCD-UHFFFAOYSA-N 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- 230000003245 working effect Effects 0.000 description 1
Landscapes
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Abstract
The invention belongs to an organic phase biosensor prepared by low-temperature hydrogel immobilized enzyme.
The invention adopts the mixed aqueous solution of soluble cellulose and polyvinyl alcohol to be frozen at the temperature of-4 to-10 ℃ to prepare low-temperature hydrogel; the preparation of the organic phase biosensor is to uniformly mix enzyme, a mediator and the like with a mixed aqueous solution of soluble cellulose and polyvinyl alcohol and then freeze the mixture into a film. The biosensor has short balance time, fast response and long service life when applied.
Description
The invention belongs to the method for organic phase biologic sensor prepared from low temperature hydrogel enzymes.
Organic biosensor (especially enzyme telegram) has a wide range of applications in fields such as organic synthesis, biotechnology, environmental monitoring, medicine analysis, 1988, people's reported first such as Hall organic phase enzyme electrodes [G.F.Hall, D.J.Best and A.P.F.Turner, Enzyme Microb.Technol., 10 (1988) 543].Thenceforth so far.Reported the organic phase enzyme telegram of many kinds, but all be to adopt absorption method immobilized enzyme (the easy desorption of this kind of enzyme, electrode life is short).And in organic solvent, must add a certain amount of water, to guarantee the catalytic activity of enzyme.For example, horseradish peroxidase electrode [F.Schurbert, the S.Saini of the mensuration organic phase hydrogen peroxide of report such as F.Schurbert, A.P.F.Turnar, Anal.Chim.Acta, 245 (1991) 188], its telegram performance is: reached starting time 1～1.5 hour; 2～5 minutes time of response; Stablize the life-span: sensitivity reduces by 60% in two weeks; Adapting to solvent is in advance with the satisfied chloroform of 5～20% aqueous solution, chlorobenzene, dioxan.
The south is prosperous give birth to wait the people to obtain the high aqueous polyvinyl alcohol elastomer of higher-strength with freezing repeatedly-melt and dissolved method and vacuum-freezing process first (during preparation, elder generation thawed 200 hours-20～-30 ℃ of freezing and room temperatures; Freezing 5 hours at-50 ℃ then), and as material [southern prosperous life, Process Technology of Polymer (Japan), 32 (1983) 523 such as wrapping, freezing, biomaterial are fixing; Masao, Nambu, Eur.Pat.Appl.EP 58,497].
The objective of the invention is mixed aqueous solution with soluble cellulose and polyvinyl alcohol-4～-10 ℃ of freezing treatment, prepare low temperature hydrogel.Preparation is during Organic biosensor, and the mixed aqueous solution of enzyme, mediator and Mierocrystalline cellulose and polyvinyl alcohol is mixed freezing film forming afterwards.The biosensor of preparing reaches starting time weak point, fast, the long service life of response.
The present invention-4～-10 ℃ of freezing treatment 10～20 hours, prepares low temperature hydrogel with the mixed aqueous solution of soluble cellulose 0.1～10% and polyvinyl alcohol 5～25%; During the preparation biosensor, with enzyme, comprise peroxidase, rCO, tyrosine oxydase, alcohol oxidase, alcoholdehydrogenase, laccase, serum lactic dehydrogenase, glycerol dehydrogenase, cholinesterase, lipase, phospholipase, also can be with mediator, mix as the mixed aqueous solution with Mierocrystalline cellulose and polyvinyl alcohol such as the Tripotassium iron hexacyanide, ferrocene and derivative thereof, quinones, organic dye, direct freezing film forming is fixed to film on the substrate telegram then; Also this mixture can be dripped and be coated onto the basal electrode surface, freezing then.This class transmitter can drying be deposited or is soaked and deposit, and can freezingly deposit or room temperature is deposited.This biosensor at chloroform, ethylene dichloride, chlorobenzene, dioxan, acetonitrile, acetone, methyl alcohol, ethanol, pimelinketone, tetrahydrofuran (THF), N, in the organic solvents such as dinethylformamide, all has biocatalysis.
Because the swelling behavior effect of the present invention's preparation is little, and the physical strength height, has Semi-IPN cross-linked network structure, the hole densification, can introduce carboxyl, amino etc. has more bonding action with the enzyme molecule, and just electrode response is stable.
The biosensor of the present invention preparation is compared with absorption method in the past, and wide adaptability both can be in water or organic water phase, also can be in absolute organic phase work; Because this hydrogel itself can be for biological active materials provides little water surrounding, thereby realized anhydrous organic phase enzyme electrodes test.This sensor performance is stable, and its biological active materials both had been difficult for leaking out, and can also keep stable, higher activity simultaneously.
Embodiment provided by the invention is as follows:
Embodiment 1. is a mediator with the yellow prussiate of potash, preparation horseradish peroxidase electrode.In the soluble cellulose 5% that 5 milligrams of horseradish peroxidases is dissolved in 200 microlitres and the mixed aqueous solution of polyvinyl alcohol 15%, wherein contain the yellow prussiate of potash of 0.01mol/L, after stirring.This is mixed drop be coated in graphite electrode surface, freezing 20 hours at-4 ℃.This electrode has excellent response performance: it is short to reach starting time, within 10 minutes; Time of response is fast, 0.5～2 minute; Useful range is wide, 0～7.5mmol/L long service life, 2 months. and this electrode is used for chloroform, chlorobenzene, acetonitrile, acetone and other organic solvent determination of peroxide.
Embodiment 2. is a mediator with the yellow prussiate of potash, preparation horseradish peroxidase electrode.In the soluble cellulose 5% that 5 milligrams of horseradish peroxidases is dissolved in 200 microlitres and the mixed aqueous solution of polyvinyl alcohol 5%, wherein contain the yellow prussiate of potash of 0.01mol/L, after stirring.This is mixed drop be coated in graphite electrode surface, freezing 20 hours at-4 ℃.This electrode has excellent response performance: it is short to reach starting time, within 10 minutes; Time of response is fast, 0.5～2 minute; Useful range is wide, 0～7.5mmol/L long service life, 2 months. and this electrode is used for chloroform, chlorobenzene, acetonitrile, acetone and other organic solvent determination of peroxide.
Embodiment 3. tyrosine oxidase electrodes.In the soluble cellulose 0.5% that 3 milligrams of tyrosine oxydase is dissolved in 100 microlitres and mixing of polyvinyl alcohol 10% water-soluble the rolling, then with this drop-coated on the glass-carbon electrode surface, freezing 12 hours at-10 ℃.This electrode performance: starting time, within 5 minutes; Time of response, 1 minute; Work-ing life, 1 month.This enzyme electrodes is determined at the phenolic compound in chloroform, the chlorobenzene equal solvent.
Embodiment 4. rCO electrodes.In the soluble cellulose 6% that 1 milligram of rCO is dissolved in 100 microlitres and the mixed aqueous solution of polyvinyl alcohol 20%, then this liquid is coated on the nylon wire, freezing 12 hours at-10 ℃.With this enzyme membrane and oxygen electrode coupling, measure content of cholesterol in chloroform, the dioxan.Electrode performance: reach starting time, within 30 minutes; Time of response is within 10 minutes.
Embodiment 5. media build ethanol dehydrogenase electrodes, in the soluble cellulose 2% that 2 milligrams of ethanol dehydrogenases and 1 milligram of nadide is dissolved in 300 microlitres and the aqueous solution of polyvinyl alcohol 12%, then this drop is coated onto the graphite electrode surface of the green modification of methylene radical,-4 ℃ freezing 15 hours, prepare the enzyme electrodes of ethanol content in the organic solvents such as measuring chloroform, chlorobenzene.
Embodiment 6. preparation low temperature hydrogels.The mixed aqueous solution of soluble fiber 1% and polyvinyl alcohol 5%-4 ℃ of freezing treatment 10 hours, is formed low temperature hydrogel.
Claims (6)
1. the method for an organic phase biologic sensor prepared from low temperature hydrogel enzymes, it is characterized in that enzyme is dissolved in the mixing solutions of soluble cellulose 0.5-6% (W/W) and polyvinyl alcohol 10-15% (W/W), after stirring, this mixing solutions dripped be coated in electrode surface, at-4--10 ℃ freezing treatment 10-20 hour, obtain Organic biosensor.
2. the method for organic phase biologic sensor prepared from low temperature hydrogel enzymes as claimed in claim 1 is characterized in that described enzyme is a horseradish peroxidase.
3. the method for organic phase biologic sensor prepared from low temperature hydrogel enzymes as claimed in claim 2 is characterized in that adding the mediator yellow prussiate of potash in addition.
4. the method for organic phase biologic sensor prepared from low temperature hydrogel enzymes as claimed in claim 1 is characterized in that described enzyme is a rCO.
5. the method for organic phase biologic sensor prepared from low temperature hydrogel enzymes as claimed in claim 1 is characterized in that described enzyme is the tyrosine oxydase.
6. the method for organic phase biologic sensor prepared from low temperature hydrogel enzymes as claimed in claim 1 is characterized in that described enzyme is an ethanol dehydrogenase.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN 94108666 CN1049009C (en) | 1994-09-06 | 1994-09-06 | Organic phase biosensor prepared from low-temperature hydrogel immobilized enzyme |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN 94108666 CN1049009C (en) | 1994-09-06 | 1994-09-06 | Organic phase biosensor prepared from low-temperature hydrogel immobilized enzyme |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN1118376A CN1118376A (en) | 1996-03-13 |
| CN1049009C true CN1049009C (en) | 2000-02-02 |
Family
ID=5033568
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN 94108666 Expired - Fee Related CN1049009C (en) | 1994-09-06 | 1994-09-06 | Organic phase biosensor prepared from low-temperature hydrogel immobilized enzyme |
Country Status (1)
| Country | Link |
|---|---|
| CN (1) | CN1049009C (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN100368072C (en) * | 2005-09-16 | 2008-02-13 | 东南大学 | Visualized aquogel, and its preparing method |
-
1994
- 1994-09-06 CN CN 94108666 patent/CN1049009C/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| CN1118376A (en) | 1996-03-13 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| AU621913B2 (en) | Enzyme electrodes and improvements in the manufacture thereof | |
| Arya et al. | Recent advances in cholesterol biosensor | |
| Xu et al. | Direct electrochemistry of horseradish peroxidase based on biocompatible carboxymethyl chitosan–gold nanoparticle nanocomposite | |
| Cosnier et al. | Electrogeneration of biotinylated functionalized polypyrroles for the simple immobilization of enzymes | |
| EP0125137B1 (en) | Measurement of enzyme-catalysed reactions | |
| Cosnier et al. | Amperometric detection of nitrate via a nitrate reductase immobilized and electrically wired at the electrode surface | |
| Iwuoha et al. | Organic phase enzyme electrodes: kinetics and analytical applications | |
| Gregg et al. | Cross-linked redox gels containing glucose oxidase for amperometric biosensor applications | |
| Bartlett et al. | Strategies for the development of amperometric enzyme electrodes | |
| Abasıyanık et al. | Immobilization of glucose oxidase on reagentless ferrocene-containing polythiophene derivative and its glucose sensing application | |
| US20110229916A1 (en) | Nanofibers with high enzyme loading for highly sensitive biosensors | |
| Liu et al. | Heme protein-gluten films: voltammetric studies and their electrocatalytic properties | |
| Du et al. | Development of an amperometric biosensor for glucose based on electrocatalytic reduction of hydrogen peroxide at the single-walled carbon nanotube/nile blue A nanocomposite modified electrode | |
| Chawla et al. | Preparation of cholesterol oxidase nanoparticles and their application in amperometric determination of cholesterol | |
| Qian et al. | An amperometric new methylene blue N-mediating sensor for hydrogen peroxide based on regenerated silk fibroin as an immobilization matrix for peroxidase | |
| He et al. | α-Amylase immobilized on bulk acoustic-wave sensor by UV-curing coating | |
| CN1049009C (en) | Organic phase biosensor prepared from low-temperature hydrogel immobilized enzyme | |
| CN101196487A (en) | Method for producing modified electrode by electro-deposition chitosan-ionic liquid-enzyme compound film | |
| Espinosa et al. | Development of a disposable organophosphate biosensor | |
| Zen et al. | Electrocatalytic Oxidation of Hypoxanthine on a Nafion/Lead‐Ruthenium Oxide Pyrochlore Modified Electrode | |
| Holt et al. | An amperometric opiate assay | |
| Laurinavičius et al. | Reagentless biosensor based on PQQ-depended glucose dehydrogenase and partially hydrolyzed polyarbutin | |
| CN115236158A (en) | Glucose biosensor, MXene nanosheet and preparation method thereof | |
| Yapar et al. | Immobilizing cholesterol oxidase in chitosan–alginic acid network | |
| JPS5816693B2 (en) | electrode |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| C06 | Publication | ||
| PB01 | Publication | ||
| C14 | Grant of patent or utility model | ||
| GR01 | Patent grant | ||
| C19 | Lapse of patent right due to non-payment of the annual fee | ||
| CF01 | Termination of patent right due to non-payment of annual fee |