DE2234412B2 - Verfahren zur Stabilisierung und Fällung konzentrierter Protease-Lösungen - Google Patents
Verfahren zur Stabilisierung und Fällung konzentrierter Protease-LösungenInfo
- Publication number
- DE2234412B2 DE2234412B2 DE2234412A DE2234412A DE2234412B2 DE 2234412 B2 DE2234412 B2 DE 2234412B2 DE 2234412 A DE2234412 A DE 2234412A DE 2234412 A DE2234412 A DE 2234412A DE 2234412 B2 DE2234412 B2 DE 2234412B2
- Authority
- DE
- Germany
- Prior art keywords
- protease
- solutions
- concentrated
- activity
- precipitation
- 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.)
- Withdrawn
Links
- 108091005804 Peptidases Proteins 0.000 title claims description 53
- 239000004365 Protease Substances 0.000 title claims description 47
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 title claims description 43
- 238000000034 method Methods 0.000 title claims description 23
- 238000001556 precipitation Methods 0.000 title description 23
- 230000006641 stabilisation Effects 0.000 title description 14
- 238000011105 stabilization Methods 0.000 title description 14
- 102000004190 Enzymes Human genes 0.000 claims description 26
- 108090000790 Enzymes Proteins 0.000 claims description 26
- 239000003381 stabilizer Substances 0.000 claims description 12
- 102000004407 Lactalbumin Human genes 0.000 claims description 11
- 108090000942 Lactalbumin Proteins 0.000 claims description 11
- 235000020183 skimmed milk Nutrition 0.000 claims description 10
- 239000000843 powder Substances 0.000 claims description 9
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 claims description 8
- 230000000087 stabilizing effect Effects 0.000 claims description 8
- 150000002500 ions Chemical class 0.000 claims description 7
- 229910052938 sodium sulfate Inorganic materials 0.000 claims description 7
- 235000011152 sodium sulphate Nutrition 0.000 claims description 7
- 150000003839 salts Chemical class 0.000 claims description 4
- 108091005658 Basic proteases Proteins 0.000 claims description 3
- 230000001376 precipitating effect Effects 0.000 claims description 3
- 241000194108 Bacillus licheniformis Species 0.000 claims description 2
- 244000063299 Bacillus subtilis Species 0.000 claims description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 claims description 2
- 239000000243 solution Substances 0.000 description 40
- 230000000694 effects Effects 0.000 description 33
- MTHSVFCYNBDYFN-UHFFFAOYSA-N diethylene glycol Chemical compound OCCOCCO MTHSVFCYNBDYFN-UHFFFAOYSA-N 0.000 description 27
- 229940088598 enzyme Drugs 0.000 description 25
- 102000035195 Peptidases Human genes 0.000 description 10
- 238000007792 addition Methods 0.000 description 10
- 241000193830 Bacillus <bacterium> Species 0.000 description 7
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 7
- 230000000977 initiatory effect Effects 0.000 description 6
- 238000002360 preparation method Methods 0.000 description 5
- -1 Ether alcohols Chemical class 0.000 description 4
- 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 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 4
- 230000008033 biological extinction Effects 0.000 description 4
- 235000010633 broth Nutrition 0.000 description 4
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 3
- OSGAYBCDTDRGGQ-UHFFFAOYSA-L calcium sulfate Chemical compound [Ca+2].[O-]S([O-])(=O)=O OSGAYBCDTDRGGQ-UHFFFAOYSA-L 0.000 description 3
- 239000005018 casein Substances 0.000 description 3
- 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 3
- 235000021240 caseins Nutrition 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 238000000855 fermentation Methods 0.000 description 3
- 230000004151 fermentation Effects 0.000 description 3
- 230000002779 inactivation Effects 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 238000010626 work up procedure Methods 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 230000000996 additive effect Effects 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 239000012496 blank sample Substances 0.000 description 2
- 238000009395 breeding Methods 0.000 description 2
- 230000001488 breeding effect Effects 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 235000011187 glycerol Nutrition 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 239000012266 salt solution Substances 0.000 description 2
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 1
- 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
- NIXOWILDQLNWCW-UHFFFAOYSA-M Acrylate Chemical compound [O-]C(=O)C=C NIXOWILDQLNWCW-UHFFFAOYSA-M 0.000 description 1
- 102000004400 Aminopeptidases Human genes 0.000 description 1
- 108090000915 Aminopeptidases Proteins 0.000 description 1
- 241000186063 Arthrobacter Species 0.000 description 1
- 241000228212 Aspergillus Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 229920002785 Croscarmellose sodium Polymers 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- CERQOIWHTDAKMF-UHFFFAOYSA-M Methacrylate Chemical compound CC(=C)C([O-])=O CERQOIWHTDAKMF-UHFFFAOYSA-M 0.000 description 1
- 102000016387 Pancreatic elastase Human genes 0.000 description 1
- 108010067372 Pancreatic elastase Proteins 0.000 description 1
- 241000228143 Penicillium Species 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 241000607720 Serratia Species 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 108090000787 Subtilisin Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000000378 dietary effect Effects 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- RTZKZFJDLAIYFH-UHFFFAOYSA-N ether Substances CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000005189 flocculation Methods 0.000 description 1
- 230000016615 flocculation Effects 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 108010059345 keratinase Proteins 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- VYQNWZOUAUKGHI-UHFFFAOYSA-N monobenzone Chemical compound C1=CC(O)=CC=C1OCC1=CC=CC=C1 VYQNWZOUAUKGHI-UHFFFAOYSA-N 0.000 description 1
- 239000012452 mother liquor Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 125000000542 sulfonic acid group Chemical group 0.000 description 1
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
-
- 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
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Enzymes And Modification Thereof (AREA)
- Detergent Compositions (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Priority Applications (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE2234412A DE2234412B2 (de) | 1972-07-13 | 1972-07-13 | Verfahren zur Stabilisierung und Fällung konzentrierter Protease-Lösungen |
| DK364773AA DK131346B (da) | 1972-07-13 | 1973-07-02 | Fremgangsmåde til udvinding af proteaser fra koncentrerede vandige proteaseopløsninger. |
| NL7309196A NL7309196A (cg-RX-API-DMAC7.html) | 1972-07-13 | 1973-07-02 | |
| IT26460/73A IT1001518B (it) | 1972-07-13 | 1973-07-11 | Procedimento per la stibilizzazione e la precipitazione di soluzioni comcentrate in protbasi |
| ES416813A ES416813A1 (es) | 1972-07-13 | 1973-07-12 | Procedimiento para estabilizar y precipitar soluciones acuosas concentradas de proteasa. |
| FR7325899A FR2193029A1 (en) | 1972-07-13 | 1973-07-13 | Protease pptn - with lactalbumin or skim milk powder as stabilising agent |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE2234412A DE2234412B2 (de) | 1972-07-13 | 1972-07-13 | Verfahren zur Stabilisierung und Fällung konzentrierter Protease-Lösungen |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| DE2234412A1 DE2234412A1 (de) | 1974-01-24 |
| DE2234412B2 true DE2234412B2 (de) | 1980-07-03 |
Family
ID=5850531
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DE2234412A Withdrawn DE2234412B2 (de) | 1972-07-13 | 1972-07-13 | Verfahren zur Stabilisierung und Fällung konzentrierter Protease-Lösungen |
Country Status (6)
| Country | Link |
|---|---|
| DE (1) | DE2234412B2 (cg-RX-API-DMAC7.html) |
| DK (1) | DK131346B (cg-RX-API-DMAC7.html) |
| ES (1) | ES416813A1 (cg-RX-API-DMAC7.html) |
| FR (1) | FR2193029A1 (cg-RX-API-DMAC7.html) |
| IT (1) | IT1001518B (cg-RX-API-DMAC7.html) |
| NL (1) | NL7309196A (cg-RX-API-DMAC7.html) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3225250A1 (de) * | 1981-07-06 | 1983-01-20 | Toyo Boseki K.K., Osaka | Stabile enzymzubereitung |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3019612A1 (de) * | 1980-05-22 | 1981-11-26 | Boehringer Mannheim Gmbh, 6800 Mannheim | Stabilisiertes thrombinpraeparat |
| DE3927286C2 (de) * | 1989-08-18 | 1997-07-24 | Roehm Gmbh | Wäßrige Enzym-Flüssigformulierungen |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB1156900A (en) * | 1968-06-14 | 1969-07-02 | Dresden Arzneimittel | Process for the Isolation of Enzymes |
-
1972
- 1972-07-13 DE DE2234412A patent/DE2234412B2/de not_active Withdrawn
-
1973
- 1973-07-02 DK DK364773AA patent/DK131346B/da unknown
- 1973-07-02 NL NL7309196A patent/NL7309196A/xx not_active Application Discontinuation
- 1973-07-11 IT IT26460/73A patent/IT1001518B/it active
- 1973-07-12 ES ES416813A patent/ES416813A1/es not_active Expired
- 1973-07-13 FR FR7325899A patent/FR2193029A1/fr active Granted
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3225250A1 (de) * | 1981-07-06 | 1983-01-20 | Toyo Boseki K.K., Osaka | Stabile enzymzubereitung |
Also Published As
| Publication number | Publication date |
|---|---|
| DK131346C (cg-RX-API-DMAC7.html) | 1975-11-24 |
| FR2193029B1 (cg-RX-API-DMAC7.html) | 1976-04-30 |
| DE2234412A1 (de) | 1974-01-24 |
| FR2193029A1 (en) | 1974-02-15 |
| DK131346B (da) | 1975-06-30 |
| NL7309196A (cg-RX-API-DMAC7.html) | 1974-01-15 |
| ES416813A1 (es) | 1976-02-16 |
| IT1001518B (it) | 1976-04-30 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DE69024812T2 (de) | Verfahren zur hydrolyse von hemizellulose durch immobilisierte enzyme und ein produkt bestehend aus einem immobilisierten hemizellulytischen enzym | |
| DE2551742C3 (de) | Proteasepräparat und seine Verwendung in Waschmitteln | |
| DE2149653A1 (de) | Synthese-Verfahren fuer die Herstellung von Ascorbinsaeureglukoside | |
| DE1807185A1 (de) | Verfahren zur Herstellung von proteolytische Enzyme enthaltenden Aufbereitungen | |
| DE69116192T2 (de) | Für die Polysaccharidhydrolyse aus einem lignozellulosehaltigen Substrat geeignete Enzymzusammensetzung, ihre Herstellung und Verwendung | |
| DE2234412B2 (de) | Verfahren zur Stabilisierung und Fällung konzentrierter Protease-Lösungen | |
| EP0215306B1 (de) | Bierherstellungsverfahren | |
| DE3636825C2 (de) | Verfahren zur Herstellung von lösungsmittelstabiler alpha-Amylase | |
| CH643261A5 (de) | Verfahren zur gewinnung von riboflavin. | |
| DE2143816A1 (de) | Verfahren zur Gewinnung von Urokinase | |
| DE2143945C3 (cg-RX-API-DMAC7.html) | ||
| DE3013627A1 (de) | Verfahren zur gewinnung von cellulaseenzymen aus thielavia terrestris | |
| DE2925427C2 (de) | Verfahren zur Herstellung von Protease | |
| DE1518382B2 (de) | Verfahren zur herstellung von l- alanin | |
| DE1294307B (de) | Verfahren zur Reinigung eines durch Zuechten von Schimmelpilzen, wie Schimmelpilzen der Gattung Aspergillus niger, erhaltenen Glucamylase enthaltenden Enzympraeparates von Transglucosidase | |
| DE2301031A1 (de) | Verfahren zur reinigung eines auf mikroorganismenzellen lytisch wirkenden enzyms | |
| CH628682A5 (de) | Diagnostisches mittel zum testen der suszeptibilitaet von bakterien gegenueber die bildung von folsaeure hemmenden mitteln. | |
| DE2239210C3 (de) | Verfahren zur Herstellung von a- Galactosidase, die eine starke a- Galactosidase-Aktivität und eine äußerst geringe Invertase-Aktivität aufweist, und deren Verwendung zur Zerlegung von Raffinose | |
| CH510700A (de) | Verfahren zur Herstellung einer von Transglucosidase freien Lösung von Amyloglucosidase und so erhaltenes Amyloglucosidase enthaltendes Enzympräparat | |
| DE1916723C3 (de) | Verfahren zur Reinigung von L-Asparaginase | |
| DE2120438A1 (de) | Verfahren zur Verbesserung'der Eigenschaften von Isoamylasen (Alpha-1,6glukosidasen) | |
| DE4035839A1 (de) | Protease als wirkenzym enthaltende, tensidfreie feste enzympraeparate | |
| AT309661B (de) | Verfahren zum enzymatischen Enthaaren von geweichten Häuten mit proteolytischen Enzymen in alkalischer Flotte | |
| DE833894C (de) | Verfahren zur Entfernung organischer Basen aus Eiweisshydrolysaten | |
| DE1936437A1 (de) | Verfahren zur Herstellung von Proteasen und die dadurch hergestellten Proteasen |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| OD | Request for examination | ||
| 8239 | Disposal/non-payment of the annual fee |