NO126375B - - Google Patents
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- Publication number
- NO126375B NO126375B NO00413/69*[A NO41369A NO126375B NO 126375 B NO126375 B NO 126375B NO 41369 A NO41369 A NO 41369A NO 126375 B NO126375 B NO 126375B
- Authority
- NO
- Norway
- Prior art keywords
- enzyme
- glass
- carrier
- molar
- water
- Prior art date
Links
- 102000004190 Enzymes Human genes 0.000 claims description 131
- 108090000790 Enzymes Proteins 0.000 claims description 131
- 230000000694 effects Effects 0.000 claims description 41
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 31
- 239000000243 solution Substances 0.000 claims description 30
- 239000005373 porous glass Substances 0.000 claims description 20
- 238000002360 preparation method Methods 0.000 claims description 13
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 claims description 11
- 238000000034 method Methods 0.000 claims description 10
- 125000005372 silanol group Chemical group 0.000 claims description 9
- 239000010456 wollastonite Substances 0.000 claims description 9
- 229910052882 wollastonite Inorganic materials 0.000 claims description 9
- 238000006243 chemical reaction Methods 0.000 claims description 8
- 239000007853 buffer solution Substances 0.000 claims description 7
- 229910052739 hydrogen Inorganic materials 0.000 claims description 5
- 239000001257 hydrogen Substances 0.000 claims description 5
- 238000004140 cleaning Methods 0.000 claims description 3
- 229940075614 colloidal silicon dioxide Drugs 0.000 claims description 3
- 125000000524 functional group Chemical group 0.000 claims description 3
- 238000004925 denaturation Methods 0.000 claims description 2
- 230000036425 denaturation Effects 0.000 claims description 2
- 239000000377 silicon dioxide Substances 0.000 claims description 2
- 235000012239 silicon dioxide Nutrition 0.000 claims description 2
- 238000002203 pretreatment Methods 0.000 claims 1
- 229940088598 enzyme Drugs 0.000 description 124
- 239000011521 glass Substances 0.000 description 55
- 108090000526 Papain Proteins 0.000 description 37
- 239000004365 Protease Substances 0.000 description 32
- 229940055729 papain Drugs 0.000 description 30
- 235000019834 papain Nutrition 0.000 description 30
- 239000008363 phosphate buffer Substances 0.000 description 26
- 239000011148 porous material Substances 0.000 description 21
- 238000004458 analytical method Methods 0.000 description 18
- 239000000872 buffer Substances 0.000 description 16
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 15
- 235000018417 cysteine Nutrition 0.000 description 15
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 15
- 238000002386 leaching Methods 0.000 description 15
- 238000003860 storage Methods 0.000 description 15
- 238000012360 testing method Methods 0.000 description 13
- 235000019420 glucose oxidase Nutrition 0.000 description 11
- 239000002245 particle Substances 0.000 description 11
- 239000004366 Glucose oxidase Substances 0.000 description 10
- 108010015776 Glucose oxidase Proteins 0.000 description 10
- 229940116332 glucose oxidase Drugs 0.000 description 10
- 239000000758 substrate Substances 0.000 description 9
- 238000002474 experimental method Methods 0.000 description 8
- 238000011534 incubation Methods 0.000 description 8
- 241001122767 Theaceae Species 0.000 description 7
- 235000018102 proteins Nutrition 0.000 description 7
- 102000004169 proteins and genes Human genes 0.000 description 7
- 108090000623 proteins and genes Proteins 0.000 description 7
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 6
- 229910052760 oxygen Inorganic materials 0.000 description 6
- 239000001301 oxygen Substances 0.000 description 6
- 238000004519 manufacturing process Methods 0.000 description 5
- 239000008351 acetate buffer Substances 0.000 description 4
- 125000003277 amino group Chemical group 0.000 description 4
- 239000000969 carrier Substances 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 238000002604 ultrasonography Methods 0.000 description 4
- 108010093096 Immobilized Enzymes Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 102000003992 Peroxidases Human genes 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 230000003287 optical effect Effects 0.000 description 3
- 108040007629 peroxidase activity proteins Proteins 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 239000000741 silica gel Substances 0.000 description 3
- 229910002027 silica gel Inorganic materials 0.000 description 3
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 2
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 2
- 101710163270 Nuclease Proteins 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 102000004357 Transferases Human genes 0.000 description 2
- 108090000992 Transferases Proteins 0.000 description 2
- 239000012190 activator Substances 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 230000003301 hydrolyzing effect Effects 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 239000011368 organic material Substances 0.000 description 2
- 230000003647 oxidation Effects 0.000 description 2
- 238000007254 oxidation reaction Methods 0.000 description 2
- VLTRZXGMWDSKGL-UHFFFAOYSA-N perchloric acid Chemical compound OCl(=O)(=O)=O VLTRZXGMWDSKGL-UHFFFAOYSA-N 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- WZIMSXIXZTUBSO-UHFFFAOYSA-N 2-[[bis(carboxymethyl)amino]methyl-(carboxymethyl)amino]acetic acid Chemical compound OC(=O)CN(CC(O)=O)CN(CC(O)=O)CC(O)=O WZIMSXIXZTUBSO-UHFFFAOYSA-N 0.000 description 1
- JRBJSXQPQWSCCF-UHFFFAOYSA-N 3,3'-Dimethoxybenzidine Chemical compound C1=C(N)C(OC)=CC(C=2C=C(OC)C(N)=CC=2)=C1 JRBJSXQPQWSCCF-UHFFFAOYSA-N 0.000 description 1
- 108700023418 Amidases Proteins 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 102000004452 Arginase Human genes 0.000 description 1
- 108700024123 Arginases Proteins 0.000 description 1
- 108010004032 Bromelains Proteins 0.000 description 1
- 102100035882 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- 108010059892 Cellulase Proteins 0.000 description 1
- 108010022172 Chitinases Proteins 0.000 description 1
- 102000012286 Chitinases Human genes 0.000 description 1
- 102000003914 Cholinesterases Human genes 0.000 description 1
- 108090000322 Cholinesterases Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 102000018832 Cytochromes Human genes 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 108090000270 Ficain Proteins 0.000 description 1
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 1
- 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 description 1
- 108010073324 Glutaminase Proteins 0.000 description 1
- 102000009127 Glutaminase Human genes 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 102000003820 Lipoxygenases Human genes 0.000 description 1
- 108090000128 Lipoxygenases Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical group 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
- GRYLNZFGIOXLOG-UHFFFAOYSA-N Nitric acid Chemical compound O[N+]([O-])=O GRYLNZFGIOXLOG-UHFFFAOYSA-N 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 108010059820 Polygalacturonase Proteins 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 102000003929 Transaminases Human genes 0.000 description 1
- 108090000340 Transaminases Proteins 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- COQLPRJCUIATTQ-UHFFFAOYSA-N Uranyl acetate Chemical compound O.O.O=[U]=O.CC(O)=O.CC(O)=O COQLPRJCUIATTQ-UHFFFAOYSA-N 0.000 description 1
- 108010046334 Urease Proteins 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000001133 acceleration Effects 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 108010028144 alpha-Glucosidases Proteins 0.000 description 1
- 102000016679 alpha-Glucosidases Human genes 0.000 description 1
- 102000005922 amidase Human genes 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 235000001014 amino acid Nutrition 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- -1 arginase Chemical class 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 239000005388 borosilicate glass Substances 0.000 description 1
- 235000019835 bromelain Nutrition 0.000 description 1
- 108010089934 carbohydrase Proteins 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 125000004432 carbon atom Chemical group C* 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 229940048961 cholinesterase Drugs 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 239000004927 clay Substances 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 238000011067 equilibration Methods 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 108010093305 exopolygalacturonase Proteins 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 235000019836 ficin Nutrition 0.000 description 1
- POTUGHMKJGOKRI-UHFFFAOYSA-N ficin Chemical compound FI=CI=N POTUGHMKJGOKRI-UHFFFAOYSA-N 0.000 description 1
- VWWQXMAJTJZDQX-UYBVJOGSSA-N flavin adenine dinucleotide Chemical group C1=NC2=C(N)N=CN=C2N1[C@@H]([C@H](O)[C@@H]1O)O[C@@H]1CO[P@](O)(=O)O[P@@](O)(=O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C2=NC(=O)NC(=O)C2=NC2=C1C=C(C)C(C)=C2 VWWQXMAJTJZDQX-UYBVJOGSSA-N 0.000 description 1
- 235000019162 flavin adenine dinucleotide Nutrition 0.000 description 1
- 239000011714 flavin adenine dinucleotide Substances 0.000 description 1
- 229940093632 flavin-adenine dinucleotide Drugs 0.000 description 1
- 239000008098 formaldehyde solution Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- GPRLSGONYQIRFK-UHFFFAOYSA-N hydron Chemical class [H+] GPRLSGONYQIRFK-UHFFFAOYSA-N 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 230000001788 irregular Effects 0.000 description 1
- 108010059345 keratinase Proteins 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 229910017604 nitric acid Inorganic materials 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 229920000620 organic polymer Polymers 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- DTBNBXWJWCWCIK-UHFFFAOYSA-N phosphoenolpyruvic acid Chemical compound OC(=O)C(=C)OP(O)(O)=O DTBNBXWJWCWCIK-UHFFFAOYSA-N 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000005295 porous vycor glass Substances 0.000 description 1
- 150000004032 porphyrins Chemical group 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 229940107700 pyruvic acid Drugs 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000006722 reduction reaction Methods 0.000 description 1
- 229920002477 rna polymer Polymers 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000002943 spectrophotometric absorbance Methods 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229960001322 trypsin Drugs 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
Classifications
-
- 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
- C12N11/14—Enzymes or microbial cells immobilised on or in an inorganic carrier
-
- 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
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/81—Carrier - bound or immobilized peptides or proteins and the preparation thereof, e.g. biological cell or cell fragment as carrier
- Y10S530/811—Peptides or proteins is immobilized on, or in, an inorganic carrier
Landscapes
- Chemical & Material Sciences (AREA)
- Genetics & Genomics (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Inorganic Chemistry (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US70282968A | 1968-02-05 | 1968-02-05 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NO126375B true NO126375B (fr) | 1973-01-29 |
Family
ID=24822771
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO00413/69*[A NO126375B (fr) | 1968-02-05 | 1969-02-04 |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US3556945A (fr) |
| JP (1) | JPS5532356B1 (fr) |
| BE (1) | BE727912A (fr) |
| DE (1) | DE1905681C3 (fr) |
| DK (1) | DK120692B (fr) |
| FR (1) | FR2001336A1 (fr) |
| GB (1) | GB1259321A (fr) |
| NL (1) | NL6901742A (fr) |
| NO (1) | NO126375B (fr) |
| SE (1) | SE348740B (fr) |
Families Citing this family (28)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1224181A (en) * | 1968-02-29 | 1971-03-03 | Beecham Group Ltd | Penicillins |
| US3957748A (en) * | 1971-07-30 | 1976-05-18 | Corning Glass Works | Nicotinamide-adenine-dinucleotide chemically coupled to water-insoluble carriers |
| PT64790B (en) * | 1975-02-18 | 1977-07-07 | Uop Inc | Immobilized enzyme conjugates |
| JPS5218892A (en) * | 1975-08-04 | 1977-02-12 | Kyowa Hakko Kogyo Co Ltd | Process for preparing 5'-ribonucleotides |
| US4072566A (en) * | 1976-09-27 | 1978-02-07 | Corning Glass Works | Immobilized biologically active proteins |
| US4202939A (en) * | 1977-09-01 | 1980-05-13 | Cpc International Inc. | Glucoamylase immobilized on cationic colloidal silica |
| US4340448A (en) * | 1978-08-28 | 1982-07-20 | University Of Pittsburgh | Potentiometric detection of hydrogen peroxide and apparatus therefor |
| US4218363A (en) * | 1978-10-16 | 1980-08-19 | Uop Inc. | Preparation of support matrices for immobilized enzymes |
| US4506015A (en) * | 1980-05-08 | 1985-03-19 | Borden Company Limited | Multi-layer immobilized enzyme compositions |
| CA1130228A (fr) * | 1980-05-21 | 1982-08-24 | Chiang-Chang Liao | Matrice de soutien pour substances ayant des proprietes biologiques et contenant des radicaux amino |
| US4530963A (en) * | 1982-08-20 | 1985-07-23 | Devoe-Holbein International, N.V. | Insoluble chelating compositions |
| US4679562A (en) * | 1983-02-16 | 1987-07-14 | Cardiac Pacemakers, Inc. | Glucose sensor |
| US4748121A (en) * | 1984-11-30 | 1988-05-31 | Ppg Industries, Inc. | Porous glass fibers with immobilized biochemically active material |
| US5205929A (en) * | 1988-02-03 | 1993-04-27 | Regents Of The University Of Minnesota | High stability porous zirconium oxide spherules |
| US5015373A (en) * | 1988-02-03 | 1991-05-14 | Regents Of The University Of Minnesota | High stability porous zirconium oxide spherules |
| US5141634A (en) * | 1988-02-03 | 1992-08-25 | Regents Of The University Of Minnesota | High stability porous zirconium oxide spherules |
| US5043288A (en) * | 1988-06-20 | 1991-08-27 | Motsenbocker Marvin A | Immobilize molecular binding partners to contact activating supports |
| CA2028593C (fr) * | 1989-10-31 | 2007-08-21 | Douglas R. Brandt | Compositions d'enzymes stabilises |
| US5443975A (en) * | 1990-06-13 | 1995-08-22 | Ente Per Le Nuove Technologie, L'energia E L'ambiente (Enea) | Method of binding enzymes to sintered expanded clays |
| US5985328A (en) * | 1994-03-07 | 1999-11-16 | Regents Of The University Of California | Micromachined porous membranes with bulk support |
| US5798042A (en) * | 1994-03-07 | 1998-08-25 | Regents Of The University Of California | Microfabricated filter with specially constructed channel walls, and containment well and capsule constructed with such filters |
| US5985164A (en) * | 1994-03-07 | 1999-11-16 | Regents Of The University Of California | Method for forming a filter |
| US5893974A (en) * | 1994-03-07 | 1999-04-13 | Regents Of University Of California | Microfabricated capsules for immunological isolation of cell transplants |
| US5770076A (en) * | 1994-03-07 | 1998-06-23 | The Regents Of The University Of California | Micromachined capsules having porous membranes and bulk supports |
| EP0937776A3 (fr) * | 1998-02-18 | 2002-06-12 | Kabushiki Kaisha Toyota Chuo Kenkyusho | Enzymes immobilisées |
| CA2243230A1 (fr) * | 1998-07-15 | 2000-01-15 | Aled Edwards | Dispositif et methode pour la determination des limites du domaine des proteines |
| US20080102497A1 (en) * | 2006-10-31 | 2008-05-01 | Dominic Wong | Enzymatic hydrolysis of starch |
| CN113151241B (zh) * | 2021-04-09 | 2024-02-09 | 东南大学 | 一种二维纳米片固定化纤维素酶的方法 |
-
1968
- 1968-02-05 US US702829A patent/US3556945A/en not_active Expired - Lifetime
-
1969
- 1969-01-29 SE SE01210/69A patent/SE348740B/xx unknown
- 1969-02-04 NO NO00413/69*[A patent/NO126375B/no unknown
- 1969-02-04 JP JP787669A patent/JPS5532356B1/ja active Pending
- 1969-02-04 DK DK60669AA patent/DK120692B/da unknown
- 1969-02-04 NL NL6901742A patent/NL6901742A/xx unknown
- 1969-02-04 FR FR6902432A patent/FR2001336A1/fr not_active Withdrawn
- 1969-02-04 BE BE727912D patent/BE727912A/xx not_active IP Right Cessation
- 1969-02-05 DE DE1905681A patent/DE1905681C3/de not_active Expired
- 1969-02-05 GB GB1259321D patent/GB1259321A/en not_active Expired
Also Published As
| Publication number | Publication date |
|---|---|
| JPS5532356B1 (fr) | 1980-08-25 |
| SE348740B (fr) | 1972-09-11 |
| DE1905681A1 (de) | 1970-05-21 |
| DE1905681B2 (de) | 1977-12-01 |
| DE1905681C3 (de) | 1978-08-10 |
| DK120692B (da) | 1971-07-05 |
| BE727912A (fr) | 1969-08-04 |
| US3556945A (en) | 1971-01-19 |
| NL6901742A (fr) | 1969-08-07 |
| FR2001336A1 (fr) | 1969-09-26 |
| GB1259321A (fr) | 1972-01-05 |
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