CA2511549A1 - Agents de reticulation hydrophiles s'utilisant dans des capteurs enzymatiques - Google Patents
Agents de reticulation hydrophiles s'utilisant dans des capteurs enzymatiques Download PDFInfo
- Publication number
- CA2511549A1 CA2511549A1 CA002511549A CA2511549A CA2511549A1 CA 2511549 A1 CA2511549 A1 CA 2511549A1 CA 002511549 A CA002511549 A CA 002511549A CA 2511549 A CA2511549 A CA 2511549A CA 2511549 A1 CA2511549 A1 CA 2511549A1
- Authority
- CA
- Canada
- Prior art keywords
- membrane
- enzyme
- oxidase
- cross
- glucose
- 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.)
- Abandoned
Links
- 239000003431 cross linking reagent Substances 0.000 title claims abstract description 39
- 230000002255 enzymatic effect Effects 0.000 title claims abstract description 19
- 102000004190 Enzymes Human genes 0.000 claims abstract description 38
- 108090000790 Enzymes Proteins 0.000 claims abstract description 38
- 239000012528 membrane Substances 0.000 claims abstract description 33
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims abstract description 31
- 239000008103 glucose Substances 0.000 claims abstract description 31
- 239000012491 analyte Substances 0.000 claims abstract description 29
- 238000000034 method Methods 0.000 claims abstract description 15
- 239000000758 substrate Substances 0.000 claims abstract description 12
- 229940088598 enzyme Drugs 0.000 claims description 35
- 108010015776 Glucose oxidase Proteins 0.000 claims description 16
- 239000004366 Glucose oxidase Substances 0.000 claims description 15
- 229940116332 glucose oxidase Drugs 0.000 claims description 15
- 235000019420 glucose oxidase Nutrition 0.000 claims description 15
- 229920001223 polyethylene glycol Polymers 0.000 claims description 15
- XLJMAIOERFSOGZ-UHFFFAOYSA-M cyanate Chemical compound [O-]C#N XLJMAIOERFSOGZ-UHFFFAOYSA-M 0.000 claims description 8
- 239000012948 isocyanate Substances 0.000 claims description 8
- 150000002513 isocyanates Chemical class 0.000 claims description 8
- 125000005442 diisocyanate group Chemical group 0.000 claims description 7
- 239000002202 Polyethylene glycol Substances 0.000 claims description 6
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 claims description 6
- 229920001451 polypropylene glycol Polymers 0.000 claims description 6
- 101710088194 Dehydrogenase Proteins 0.000 claims description 4
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 claims description 4
- 229930091371 Fructose Natural products 0.000 claims description 4
- 239000005715 Fructose Substances 0.000 claims description 4
- 108010073450 Lactate 2-monooxygenase Proteins 0.000 claims description 4
- 108030001003 Long-chain-alcohol oxidases Proteins 0.000 claims description 4
- 108090000854 Oxidoreductases Proteins 0.000 claims description 4
- 102000004316 Oxidoreductases Human genes 0.000 claims description 4
- 108010060059 Sarcosine Oxidase Proteins 0.000 claims description 4
- 102000008118 Sarcosine oxidase Human genes 0.000 claims description 4
- 108090000531 Amidohydrolases Proteins 0.000 claims description 3
- 102000004092 Amidohydrolases Human genes 0.000 claims description 3
- 101000950981 Bacillus subtilis (strain 168) Catabolic NAD-specific glutamate dehydrogenase RocG Proteins 0.000 claims description 3
- 102000016901 Glutamate dehydrogenase Human genes 0.000 claims description 3
- 102000003855 L-lactate dehydrogenase Human genes 0.000 claims description 3
- 108700023483 L-lactate dehydrogenases Proteins 0.000 claims description 3
- 102000013009 Pyruvate Kinase Human genes 0.000 claims description 3
- 108020005115 Pyruvate Kinase Proteins 0.000 claims description 3
- 229920005862 polyol Polymers 0.000 claims description 3
- 150000003077 polyols Chemical class 0.000 claims description 3
- 229920001577 copolymer Polymers 0.000 claims description 2
- 239000011159 matrix material Substances 0.000 claims description 2
- 229920000642 polymer Polymers 0.000 claims description 2
- 125000002485 formyl group Chemical class [H]C(*)=O 0.000 claims 4
- 108010046334 Urease Proteins 0.000 claims 2
- 238000009792 diffusion process Methods 0.000 abstract description 5
- 230000036571 hydration Effects 0.000 abstract description 4
- 238000006703 hydration reaction Methods 0.000 abstract description 4
- 230000035945 sensitivity Effects 0.000 abstract description 4
- 238000010348 incorporation Methods 0.000 abstract description 3
- 230000037361 pathway Effects 0.000 abstract description 3
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 10
- 239000001301 oxygen Substances 0.000 description 10
- 229910052760 oxygen Inorganic materials 0.000 description 10
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 4
- 150000001299 aldehydes Chemical class 0.000 description 4
- CVSVTCORWBXHQV-UHFFFAOYSA-N creatine Chemical compound NC(=[NH2+])N(C)CC([O-])=O CVSVTCORWBXHQV-UHFFFAOYSA-N 0.000 description 4
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 3
- 238000006243 chemical reaction Methods 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- PHOQVHQSTUBQQK-SQOUGZDYSA-N D-glucono-1,5-lactone Chemical compound OC[C@H]1OC(=O)[C@H](O)[C@@H](O)[C@@H]1O PHOQVHQSTUBQQK-SQOUGZDYSA-N 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 229960003624 creatine Drugs 0.000 description 2
- 239000006046 creatine Substances 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- 235000012209 glucono delta-lactone Nutrition 0.000 description 2
- 229960003681 gluconolactone Drugs 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- 238000007747 plating Methods 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 230000001954 sterilising effect Effects 0.000 description 2
- 238000004659 sterilization and disinfection Methods 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 108010077078 Creatinase Proteins 0.000 description 1
- RGHNJXZEOKUKBD-UHFFFAOYSA-N D-gluconic acid Natural products OCC(O)C(O)C(O)C(O)C(O)=O RGHNJXZEOKUKBD-UHFFFAOYSA-N 0.000 description 1
- 241001633942 Dais Species 0.000 description 1
- RGHNJXZEOKUKBD-SQOUGZDYSA-N Gluconic acid Natural products OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C(O)=O RGHNJXZEOKUKBD-SQOUGZDYSA-N 0.000 description 1
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 1
- 206010041235 Snoring Diseases 0.000 description 1
- 239000000090 biomarker Substances 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 150000001913 cyanates Chemical class 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000000151 deposition Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- -1 diimm_ides Chemical class 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 235000012208 gluconic acid Nutrition 0.000 description 1
- 239000000174 gluconic acid Substances 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 238000007654 immersion Methods 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- RGXCTRIQQODGIZ-UHFFFAOYSA-O isodesmosine Chemical compound OC(=O)C(N)CCCC[N+]1=CC(CCC(N)C(O)=O)=CC(CCC(N)C(O)=O)=C1CCCC(N)C(O)=O RGXCTRIQQODGIZ-UHFFFAOYSA-O 0.000 description 1
- 150000002596 lactones Chemical group 0.000 description 1
- 239000012035 limiting reagent Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 229920005606 polypropylene copolymer Polymers 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- 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
- C12Q1/005—Enzyme electrodes involving specific analytes or enzymes
- C12Q1/006—Enzyme electrodes involving specific analytes or enzymes for glucose
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
- C12N11/02—Enzymes or microbial cells immobilised on or in an organic carrier
- C12N11/06—Enzymes or microbial cells immobilised on or in an organic carrier attached to the carrier via a bridging agent
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- General Health & Medical Sciences (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Analytical Chemistry (AREA)
- Physics & Mathematics (AREA)
- Emergency Medicine (AREA)
- Biomedical Technology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Abstract
L'invention concerne un capteur enzymatique qui comprend une enzyme produisant un signal lorsqu'elle entre en contact avec un analyte ; un substrat ; et un agent de réticulation qui comprend une ou plusieurs fractions hydrophiles. L'enzyme est immobilisée dans le substrat au moyen de l'agent de réticulation hydrophile. On applique une membrane biocompatible qui comprend l'enzyme, le substrat et l'agent de réticulation hydrophile sur un capteur afin de former un capteur enzymatique. Le capteur enzymatique présente des fonctions de détection renforcées en ce qu'il améliore la diffusion des espèces réactives, ce qui accroît la sensibilité générale et la durée de vie du capteur. L'incorporation de fractions hydrophiles dans l'agent de réticulation permet d'optimiser l'hydratation du capteur et de former des canaux ou voies hydrophiles pour les espèces réactives, telles que H¿2?0¿2? et l'analyte étudié. La membrane et le capteur enzymatique peuvent être utilisés dans un procédé de détection d'un analyte tel que le glucose.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US33550602A | 2002-12-31 | 2002-12-31 | |
| US10/335,506 | 2002-12-31 | ||
| PCT/US2003/041060 WO2004060297A2 (fr) | 2002-12-31 | 2003-12-19 | Agents de reticulation hydrophiles s'utilisant dans des capteurs enzymatiques |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2511549A1 true CA2511549A1 (fr) | 2004-07-22 |
Family
ID=32710917
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002511549A Abandoned CA2511549A1 (fr) | 2002-12-31 | 2003-12-19 | Agents de reticulation hydrophiles s'utilisant dans des capteurs enzymatiques |
Country Status (4)
| Country | Link |
|---|---|
| EP (1) | EP1587546A4 (fr) |
| AU (1) | AU2003297503A1 (fr) |
| CA (1) | CA2511549A1 (fr) |
| WO (1) | WO2004060297A2 (fr) |
Families Citing this family (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US9493806B2 (en) | 2001-06-01 | 2016-11-15 | Colorado State University Research Foundation | Enzymatic biosensing systems |
| US9493805B2 (en) | 2001-06-01 | 2016-11-15 | Colorado State University Research Foundation | Enzymatic biosensors with enhanced activity retention for detection of organic compounds |
| US9796998B2 (en) | 2007-04-09 | 2017-10-24 | Colorado State University Research Foundation | Oxygenase-based biosensing systems for measurement of halogenated alkene concentrations |
| US20110082356A1 (en) * | 2009-10-01 | 2011-04-07 | Medtronic Minimed, Inc. | Analyte sensor apparatuses having interference rejection membranes and methods for making and using them |
| WO2012071471A2 (fr) | 2010-11-22 | 2012-05-31 | Colorado State University Research Foundation | Systèmes de biodétection pour une mesure de lactose |
| US9499853B2 (en) | 2011-08-02 | 2016-11-22 | Colorado State University Research Foundation | Biosensing system with extended lifetime via cofactor recycling |
| US10669153B2 (en) | 2017-05-23 | 2020-06-02 | International Business Machines Corporation | Neuro-chemical sensor with selectively permeable membrane on nano-electrode |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3106456A1 (de) * | 1981-02-21 | 1982-10-07 | Röhm GmbH, 6100 Darmstadt | Verfahren zur herstellung von perlfoermigen, hydrophilen, gegenueber proteinen bindungsaktiven traegerpolymeren |
| US5786439A (en) * | 1996-10-24 | 1998-07-28 | Minimed Inc. | Hydrophilic, swellable coatings for biosensors |
| US5874165A (en) * | 1996-06-03 | 1999-02-23 | Gore Enterprise Holdings, Inc. | Materials and method for the immobilization of bioactive species onto polymeric subtrates |
| US6485703B1 (en) * | 1998-07-31 | 2002-11-26 | The Texas A&M University System | Compositions and methods for analyte detection |
| WO2001022820A1 (fr) * | 1999-09-30 | 2001-04-05 | The General Hospital Corporation | Utilisation de pramipexole pour traiter l'etat de besoin de cocaine |
| WO2001048052A1 (fr) * | 1999-12-24 | 2001-07-05 | Kyowa Hakko Kogyo Co., Ltd. | Glycols de polyalkylene ramifies |
-
2003
- 2003-12-19 EP EP03814924A patent/EP1587546A4/fr not_active Withdrawn
- 2003-12-19 CA CA002511549A patent/CA2511549A1/fr not_active Abandoned
- 2003-12-19 WO PCT/US2003/041060 patent/WO2004060297A2/fr not_active Application Discontinuation
- 2003-12-19 AU AU2003297503A patent/AU2003297503A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| WO2004060297A2 (fr) | 2004-07-22 |
| WO2004060297A3 (fr) | 2005-05-06 |
| AU2003297503A1 (en) | 2004-07-29 |
| EP1587546A4 (fr) | 2007-02-14 |
| EP1587546A2 (fr) | 2005-10-26 |
| AU2003297503A8 (en) | 2004-07-29 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Discontinued | ||
| FZDE | Discontinued |
Effective date: 20120925 |
|
| FZDE | Discontinued |
Effective date: 20120925 |