JPH11511118A - タンパク質溶液のＡ１／Ｆｅ処理とその後の膜濃縮 - Google Patents
タンパク質溶液のＡ１／Ｆｅ処理とその後の膜濃縮Info
- Publication number
- JPH11511118A JPH11511118A JP8536117A JP53611796A JPH11511118A JP H11511118 A JPH11511118 A JP H11511118A JP 8536117 A JP8536117 A JP 8536117A JP 53611796 A JP53611796 A JP 53611796A JP H11511118 A JPH11511118 A JP H11511118A
- Authority
- JP
- Japan
- Prior art keywords
- protein solution
- protein
- test
- solution
- protease
- 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.)
- Pending
Links
- 239000012460 protein solution Substances 0.000 title claims abstract description 38
- 239000012528 membrane Substances 0.000 title claims abstract description 25
- 238000000034 method Methods 0.000 claims abstract description 41
- 150000001875 compounds Chemical class 0.000 claims abstract description 21
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 19
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 17
- 238000005352 clarification Methods 0.000 claims abstract description 8
- 239000004367 Lipase Substances 0.000 claims description 23
- 108091005804 Peptidases Proteins 0.000 claims description 23
- 238000000855 fermentation Methods 0.000 claims description 23
- 230000004151 fermentation Effects 0.000 claims description 23
- 108090001060 Lipase Proteins 0.000 claims description 22
- 102000004882 Lipase Human genes 0.000 claims description 22
- 239000004365 Protease Substances 0.000 claims description 22
- 235000019421 lipase Nutrition 0.000 claims description 22
- 102000004190 Enzymes Human genes 0.000 claims description 21
- 108090000790 Enzymes Proteins 0.000 claims description 21
- 229940088598 enzyme Drugs 0.000 claims description 21
- 108010065511 Amylases Proteins 0.000 claims description 11
- 102000013142 Amylases Human genes 0.000 claims description 11
- 102000004316 Oxidoreductases Human genes 0.000 claims description 11
- 108090000854 Oxidoreductases Proteins 0.000 claims description 11
- 235000019418 amylase Nutrition 0.000 claims description 11
- 238000000108 ultra-filtration Methods 0.000 claims description 11
- 239000004382 Amylase Substances 0.000 claims description 10
- 150000003839 salts Chemical class 0.000 claims description 9
- 238000001914 filtration Methods 0.000 claims description 8
- 239000008394 flocculating agent Substances 0.000 claims description 7
- 239000000203 mixture Substances 0.000 claims description 7
- VTLYFUHAOXGGBS-UHFFFAOYSA-N Fe3+ Chemical compound [Fe+3] VTLYFUHAOXGGBS-UHFFFAOYSA-N 0.000 claims description 6
- 108010059892 Cellulase Proteins 0.000 claims description 5
- 229940106157 cellulase Drugs 0.000 claims description 5
- 238000005119 centrifugation Methods 0.000 claims description 4
- 238000001471 micro-filtration Methods 0.000 claims description 4
- 229920000642 polymer Polymers 0.000 claims description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- 230000004931 aggregating effect Effects 0.000 abstract 1
- 235000010633 broth Nutrition 0.000 description 42
- XEEYBQQBJWHFJM-UHFFFAOYSA-N iron Substances [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 30
- 102000035195 Peptidases Human genes 0.000 description 22
- 239000000243 solution Substances 0.000 description 18
- 235000018102 proteins Nutrition 0.000 description 14
- 150000004645 aluminates Chemical class 0.000 description 10
- 102000003992 Peroxidases Human genes 0.000 description 9
- 102000016938 Catalase Human genes 0.000 description 6
- 108010053835 Catalase Proteins 0.000 description 6
- DIZPMCHEQGEION-UHFFFAOYSA-H aluminium sulfate (anhydrous) Chemical compound [Al+3].[Al+3].[O-]S([O-])(=O)=O.[O-]S([O-])(=O)=O.[O-]S([O-])(=O)=O DIZPMCHEQGEION-UHFFFAOYSA-H 0.000 description 6
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 6
- 108040007629 peroxidase activity proteins Proteins 0.000 description 6
- 238000001556 precipitation Methods 0.000 description 6
- 238000000746 purification Methods 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 5
- 239000001110 calcium chloride Substances 0.000 description 5
- 229910001628 calcium chloride Inorganic materials 0.000 description 5
- 244000005700 microbiome Species 0.000 description 5
- 241000193830 Bacillus <bacterium> Species 0.000 description 4
- 108010084185 Cellulases Proteins 0.000 description 4
- 102000005575 Cellulases Human genes 0.000 description 4
- 108010056079 Subtilisins Proteins 0.000 description 4
- 102000005158 Subtilisins Human genes 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 239000012141 concentrate Substances 0.000 description 4
- 239000000706 filtrate Substances 0.000 description 4
- 230000002538 fungal effect Effects 0.000 description 4
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 4
- 239000007788 liquid Substances 0.000 description 4
- 238000010979 pH adjustment Methods 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 241000894007 species Species 0.000 description 4
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 241000193422 Bacillus lentus Species 0.000 description 3
- 241000222511 Coprinus Species 0.000 description 3
- 108010029541 Laccase Proteins 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 108700020962 Peroxidase Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 230000001580 bacterial effect Effects 0.000 description 3
- 238000001704 evaporation Methods 0.000 description 3
- 230000008020 evaporation Effects 0.000 description 3
- 235000019253 formic acid Nutrition 0.000 description 3
- 239000012510 hollow fiber Substances 0.000 description 3
- 239000012535 impurity Substances 0.000 description 3
- 229910000358 iron sulfate Inorganic materials 0.000 description 3
- 229920002492 poly(sulfone) Polymers 0.000 description 3
- -1 transhydrogenase Proteins 0.000 description 3
- 241000228212 Aspergillus Species 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 2
- 101001091385 Homo sapiens Kallikrein-6 Proteins 0.000 description 2
- 102100027612 Kallikrein-11 Human genes 0.000 description 2
- 102100034866 Kallikrein-6 Human genes 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 241000589516 Pseudomonas Species 0.000 description 2
- 241000635201 Pumilus Species 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 241000223255 Scytalidium Species 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 101710152431 Trypsin-like protease Proteins 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 239000005018 casein Substances 0.000 description 2
- 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 2
- 235000021240 caseins Nutrition 0.000 description 2
- 125000002091 cationic group Chemical group 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 108010005400 cutinase Proteins 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000005265 energy consumption Methods 0.000 description 2
- 238000005189 flocculation Methods 0.000 description 2
- 230000016615 flocculation Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 108010020132 microbial serine proteinases Proteins 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000011734 sodium Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 238000000967 suction filtration Methods 0.000 description 2
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 241001157813 Cercospora Species 0.000 description 1
- 241000242346 Constrictibacter antarcticus Species 0.000 description 1
- 244000251987 Coprinus macrorhizus Species 0.000 description 1
- 241000223208 Curvularia Species 0.000 description 1
- 241001440269 Cutina Species 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 108010092681 DNA Primase Proteins 0.000 description 1
- 102000016559 DNA Primase Human genes 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 241000255925 Diptera Species 0.000 description 1
- 241001269524 Dura Species 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 241000427940 Fusarium solani Species 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241000223198 Humicola Species 0.000 description 1
- 241001480714 Humicola insolens Species 0.000 description 1
- 241001237944 Hygrophorus Species 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 239000005569 Iron sulphate Substances 0.000 description 1
- 101710098556 Lipase A Proteins 0.000 description 1
- 101710098554 Lipase B Proteins 0.000 description 1
- 241000023320 Luma <angiosperm> Species 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 101710099648 Lysosomal acid lipase/cholesteryl ester hydrolase Proteins 0.000 description 1
- 102100026001 Lysosomal acid lipase/cholesteryl ester hydrolase Human genes 0.000 description 1
- 102000004020 Oxygenases Human genes 0.000 description 1
- 108090000417 Oxygenases Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000228168 Penicillium sp. Species 0.000 description 1
- 241000222640 Polyporus Species 0.000 description 1
- 241000589540 Pseudomonas fluorescens Species 0.000 description 1
- 241000589755 Pseudomonas mendocina Species 0.000 description 1
- 241000589630 Pseudomonas pseudoalcaligenes Species 0.000 description 1
- 101000968491 Pseudomonas sp. (strain 109) Triacylglycerol lipase Proteins 0.000 description 1
- 241000589614 Pseudomonas stutzeri Species 0.000 description 1
- 241001361634 Rhizoctonia Species 0.000 description 1
- 101000968489 Rhizomucor miehei Lipase Proteins 0.000 description 1
- 241000235527 Rhizopus Species 0.000 description 1
- 241000303962 Rhizopus delemar Species 0.000 description 1
- 240000005384 Rhizopus oryzae Species 0.000 description 1
- 244000157378 Rubus niveus Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 108090000787 Subtilisin Proteins 0.000 description 1
- 241000223258 Thermomyces lanuginosus Species 0.000 description 1
- 241000222354 Trametes Species 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 238000010306 acid treatment Methods 0.000 description 1
- YCNZFPXXIWEFCF-UHFFFAOYSA-N alumane;sodium Chemical compound [Na].[AlH3] YCNZFPXXIWEFCF-UHFFFAOYSA-N 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- ANBBXQWFNXMHLD-UHFFFAOYSA-N aluminum;sodium;oxygen(2-) Chemical compound [O-2].[O-2].[Na+].[Al+3] ANBBXQWFNXMHLD-UHFFFAOYSA-N 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 229920006318 anionic polymer Polymers 0.000 description 1
- 229920006317 cationic polymer Polymers 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 150000001805 chlorine compounds Chemical class 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-M hydroxide Chemical compound [OH-] XLYOFNOQVPJJNP-UHFFFAOYSA-M 0.000 description 1
- 150000004679 hydroxides Chemical class 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 229920000592 inorganic polymer Polymers 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 230000002366 lipolytic effect Effects 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 238000005374 membrane filtration Methods 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- OSWPMRLSEDHDFF-UHFFFAOYSA-N methyl salicylate Chemical compound COC(=O)C1=CC=CC=C1O OSWPMRLSEDHDFF-UHFFFAOYSA-N 0.000 description 1
- 229920000620 organic polymer Polymers 0.000 description 1
- 230000033116 oxidation-reduction process Effects 0.000 description 1
- 235000021317 phosphate Nutrition 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 159000000001 potassium salts Chemical class 0.000 description 1
- VJZLQIPZNBPASX-OJJGEMKLSA-L prednisolone sodium phosphate Chemical compound [Na+].[Na+].O=C1C=C[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)COP([O-])([O-])=O)[C@@H]4[C@@H]3CCC2=C1 VJZLQIPZNBPASX-OJJGEMKLSA-L 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 235000015598 salt intake Nutrition 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 229910001388 sodium aluminate Inorganic materials 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 239000008399 tap water Substances 0.000 description 1
- 235000020679 tap water Nutrition 0.000 description 1
- 108010075550 termamyl Proteins 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 238000010977 unit operation Methods 0.000 description 1
- 238000007738 vacuum evaporation Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Wood Science & Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Analytical Chemistry (AREA)
- Biophysics (AREA)
- General Engineering & Computer Science (AREA)
- Enzymes And Modification Thereof (AREA)
- Peptides Or Proteins (AREA)
- Separation Using Semi-Permeable Membranes (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DK0626/95 | 1995-06-02 | ||
| DK62695 | 1995-06-02 | ||
| PCT/DK1996/000229 WO1996038469A1 (en) | 1995-06-02 | 1996-05-31 | Al/Fe-TREATMENT OF A PROTEIN SOLUTION, FOLLOWED BY MEMBRANE CONCENTRATION |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH11511118A true JPH11511118A (ja) | 1999-09-28 |
Family
ID=8095720
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP8536117A Pending JPH11511118A (ja) | 1995-06-02 | 1996-05-31 | タンパク質溶液のＡ１／Ｆｅ処理とその後の膜濃縮 |
Country Status (9)
| Country | Link |
|---|---|
| EP (1) | EP0828753B1 (OSRAM) |
| JP (1) | JPH11511118A (OSRAM) |
| CN (1) | CN1114613C (OSRAM) |
| AT (1) | ATE235506T1 (OSRAM) |
| AU (1) | AU5996996A (OSRAM) |
| DE (1) | DE69626976T2 (OSRAM) |
| DK (1) | DK0828753T3 (OSRAM) |
| IN (1) | IN181859B (OSRAM) |
| WO (1) | WO1996038469A1 (OSRAM) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2009508486A (ja) * | 2005-09-15 | 2009-03-05 | ワイス | 塩を用いた蛋白のフロキュレーション |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2810667B1 (fr) * | 2000-06-23 | 2004-09-03 | Warner Lambert Co | Procede d'isolement et de purification d'une proteine, et proteine obtenue |
| US7659102B2 (en) | 2001-02-21 | 2010-02-09 | Verenium Corporation | Amylases, nucleic acids encoding them and methods for making and using them |
| EP2333098B1 (en) | 2001-02-21 | 2016-08-24 | BASF Enzymes LLC | Enzymes having alpha amylase activity and methods of use thereof |
| US20030013172A1 (en) * | 2001-05-14 | 2003-01-16 | Joel Gerendash | Novel methods of enzyme purification |
| WO2003002136A2 (en) | 2001-06-28 | 2003-01-09 | Novo Nordisk A/S | Stable formulation of modified glp-1 |
| WO2003050274A2 (en) * | 2001-12-11 | 2003-06-19 | Novozymes A/S | Process for harvesting crystalline particles from fermentation broth |
| US7118891B2 (en) | 2001-12-11 | 2006-10-10 | Novozymes A/S | Crystal harvest from fermentation broth |
| MXPA05009566A (es) | 2003-03-06 | 2005-12-14 | Diversa Corp | Amilasas, acidos nucleicos que las codifican, y metodos para hacerlas y usarlas. |
| EP1633391B1 (en) | 2003-06-03 | 2011-10-19 | Novo Nordisk A/S | Stabilized pharmaceutical peptide compositions |
| EP2292254A3 (en) | 2003-06-03 | 2011-12-14 | Novo Nordisk A/S | Stabilized pharmaceutical peptide compositions |
| CN1882356B (zh) | 2003-11-20 | 2015-02-25 | 诺沃挪第克公司 | 对于生产和用于注射装置中是最佳的含有丙二醇的肽制剂 |
| ES2442223T3 (es) | 2004-08-31 | 2014-02-10 | Novo Nordisk A/S | Uso de tris(hidroximetil) aminometano para la estabilización de péptidos, polipéptidos y proteínas |
| CN106137952B (zh) | 2004-11-12 | 2020-11-17 | 诺和诺德公司 | 促胰岛素肽的稳定制剂 |
| ES2575912T3 (es) | 2006-12-21 | 2016-07-04 | Basf Enzymes Llc | Amilasas y glucoamilasas, ácidos nucleicos que las codifican y métodos para formarlas y utilizarlas |
| US20120252066A1 (en) * | 2011-03-29 | 2012-10-04 | Heng Meng H | Methods of foam control |
| CN104797590A (zh) * | 2012-11-01 | 2015-07-22 | 诺维信公司 | 用于去除dna的方法 |
| EP3071589B1 (en) | 2013-11-19 | 2018-03-14 | Kemira OYJ | Method for reducing colour of a biotechnological liquid |
| MX2020001525A (es) | 2017-08-24 | 2020-03-20 | Novo Nordisk As | Composiciones de peptido similar al glucagon tipo 1 (glp-1) y sus usos. |
| CN108949703A (zh) * | 2018-06-28 | 2018-12-07 | 大连理工大学 | 一种半纤维小体类似物粗提纯方法 |
| DK3983425T3 (da) | 2019-06-13 | 2025-12-15 | Basf Se | Fremgangsmåde til udvinding af et protein fra en fermenteringsbouillon ved hjælp af en divalent kation |
| IL294520A (en) | 2020-02-18 | 2022-09-01 | Novo Nordisk As | Pharmaceutical formulations |
| MX2023003276A (es) | 2020-09-22 | 2023-05-03 | Basf Se | Método para recuperar una proteína de un caldo de fermentación que comprende un alto grado de células lisadas. |
| CN112500471B (zh) * | 2020-12-22 | 2022-09-27 | 中美华世通生物医药科技(武汉)股份有限公司 | 一种制备高澄清度蛋白琥珀酸铁的方法 |
| WO2024028338A1 (en) | 2022-08-02 | 2024-02-08 | Basf Se | Stabilized protein production process using bacillus host cells |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3795586A (en) * | 1969-08-11 | 1974-03-05 | Pabst Brewing Co | Recovery of enzymes |
| KR880009044A (ko) * | 1987-01-30 | 1988-09-13 | 원본미기재 | 묽은 수용액으로부터 소마토트로핀의 회수방법 |
| US4894444A (en) * | 1987-07-16 | 1990-01-16 | Merck & Co., Inc. | Recovery and purification of immunogens from immunogen-alum complexes |
| DE3915277A1 (de) * | 1989-05-10 | 1990-11-15 | Henkel Kgaa | Verfahren zur reinigung von enzymfluessigkonzentraten |
| DE4037530A1 (de) * | 1990-11-26 | 1992-05-27 | Henkel Kgaa | Faellungsverfahren fuer exocellulaere proteine |
| DK91092D0 (OSRAM) * | 1992-07-10 | 1992-07-10 | Novo Nordisk As |
-
1996
- 1996-05-31 CN CN96194380.7A patent/CN1114613C/zh not_active Expired - Fee Related
- 1996-05-31 AT AT96917365T patent/ATE235506T1/de not_active IP Right Cessation
- 1996-05-31 DK DK96917365T patent/DK0828753T3/da active
- 1996-05-31 WO PCT/DK1996/000229 patent/WO1996038469A1/en not_active Ceased
- 1996-05-31 AU AU59969/96A patent/AU5996996A/en not_active Abandoned
- 1996-05-31 DE DE69626976T patent/DE69626976T2/de not_active Expired - Lifetime
- 1996-05-31 EP EP96917365A patent/EP0828753B1/en not_active Expired - Lifetime
- 1996-05-31 JP JP8536117A patent/JPH11511118A/ja active Pending
- 1996-06-03 IN IN946MA1996 patent/IN181859B/en unknown
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2009508486A (ja) * | 2005-09-15 | 2009-03-05 | ワイス | 塩を用いた蛋白のフロキュレーション |
| JP2014040449A (ja) * | 2005-09-15 | 2014-03-06 | Wyeth Llc | 塩を用いた蛋白のフロキュレーション |
Also Published As
| Publication number | Publication date |
|---|---|
| CN1186498A (zh) | 1998-07-01 |
| EP0828753A1 (en) | 1998-03-18 |
| DK0828753T3 (da) | 2003-06-30 |
| ATE235506T1 (de) | 2003-04-15 |
| DE69626976D1 (de) | 2003-04-30 |
| CN1114613C (zh) | 2003-07-16 |
| AU5996996A (en) | 1996-12-18 |
| DE69626976T2 (de) | 2004-03-04 |
| EP0828753B1 (en) | 2003-03-26 |
| WO1996038469A1 (en) | 1996-12-05 |
| IN181859B (OSRAM) | 1998-10-03 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JPH11511118A (ja) | タンパク質溶液のＡ１／Ｆｅ処理とその後の膜濃縮 | |
| US5728559A (en) | Separation of proteins | |
| FI111551B (fi) | Menetelmä erittäin puhdistetun emäksisen proteaasin valmistamiseksi ja menetelmällä valmistetun proteaasin käyttö | |
| EP0894091B1 (en) | Method for purification of a protein from a protein containing solution | |
| US6031082A (en) | Increased yields of a crystallized protein by using a solid adsorption material | |
| US5192677A (en) | Alkali and heat stable protease from thermomonospora fusca | |
| US6080564A (en) | Selective inactivation of Aspergillus proteases | |
| US20120122183A1 (en) | Flocculation with divalent salt and phosphate | |
| Dreisbach et al. | Induction of collagenase production in Vibrio B-30 | |
| CA1089384A (en) | Protease inactivated alpha-amylase preparations | |
| US4439522A (en) | Proteolytic enzyme composition | |
| EP0892810B1 (en) | Crystallization of a protein with a sulphur salt | |
| EP0942921B1 (en) | Increased yields of a crystallized protein by using a solid adsorption material | |
| Alekseiva et al. | Enhancement of acid proteinase production by the fungus Humicola lutea 120-5 immobilized in crosslinked poly (vinyl alcohol) mixed with poly (ethylene glycol) | |
| JP2655618B2 (ja) | 微生物凝集剤ｎｏｃ―１の製造方法 | |
| JP2000500983A (ja) | 酵素活性の選択的不活性化 | |
| JPH04354585A (ja) | 発酵液の処理方法 | |
| Nesterova et al. | Properties of proteolytic enzymes isolated from a thermophilic strain of Micromonospora vulgaris 42 | |
| GREEN | Studies of an Extracellular Protease from an Arthrobacter Species | |
| JPH07163338A (ja) | 新規プロテアーゼを産生する新規微生物 |