NL9001731A - Werkwijze voor het bereiden van stabiele enzymdispersies. - Google Patents
Werkwijze voor het bereiden van stabiele enzymdispersies. Download PDFInfo
- Publication number
- NL9001731A NL9001731A NL9001731A NL9001731A NL9001731A NL 9001731 A NL9001731 A NL 9001731A NL 9001731 A NL9001731 A NL 9001731A NL 9001731 A NL9001731 A NL 9001731A NL 9001731 A NL9001731 A NL 9001731A
- Authority
- NL
- Netherlands
- Prior art keywords
- enzymes
- enzyme
- activity
- aqueous medium
- process according
- Prior art date
Links
- 102000004190 Enzymes Human genes 0.000 title claims description 93
- 108090000790 Enzymes Proteins 0.000 title claims description 93
- 238000000034 method Methods 0.000 title claims description 35
- 239000006185 dispersion Substances 0.000 title description 6
- 229940088598 enzyme Drugs 0.000 claims description 92
- 102000035195 Peptidases Human genes 0.000 claims description 42
- 108091005804 Peptidases Proteins 0.000 claims description 42
- 239000004365 Protease Substances 0.000 claims description 35
- 239000000203 mixture Substances 0.000 claims description 23
- 238000002360 preparation method Methods 0.000 claims description 21
- 239000000725 suspension Substances 0.000 claims description 21
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 16
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 16
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 16
- 102000013142 Amylases Human genes 0.000 claims description 14
- 108010065511 Amylases Proteins 0.000 claims description 14
- 238000001556 precipitation Methods 0.000 claims description 14
- 150000003839 salts Chemical class 0.000 claims description 14
- 235000019418 amylase Nutrition 0.000 claims description 13
- 239000004367 Lipase Substances 0.000 claims description 12
- 108090001060 Lipase Proteins 0.000 claims description 11
- 102000004882 Lipase Human genes 0.000 claims description 11
- 235000019421 lipase Nutrition 0.000 claims description 11
- 230000002797 proteolythic effect Effects 0.000 claims description 11
- GJCOSYZMQJWQCA-UHFFFAOYSA-N 9H-xanthene Chemical compound C1=CC=C2CC3=CC=CC=C3OC2=C1 GJCOSYZMQJWQCA-UHFFFAOYSA-N 0.000 claims description 10
- 239000012736 aqueous medium Substances 0.000 claims description 10
- 229920001285 xanthan gum Polymers 0.000 claims description 10
- 229940025131 amylases Drugs 0.000 claims description 9
- 230000008569 process Effects 0.000 claims description 9
- 238000003756 stirring Methods 0.000 claims description 8
- 239000002562 thickening agent Substances 0.000 claims description 8
- 230000002906 microbiologic effect Effects 0.000 claims description 5
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 claims description 4
- 238000009826 distribution Methods 0.000 claims description 4
- 229910052938 sodium sulfate Inorganic materials 0.000 claims description 3
- 235000011152 sodium sulphate Nutrition 0.000 claims description 3
- 230000006641 stabilisation Effects 0.000 claims description 3
- 238000011105 stabilization Methods 0.000 claims description 3
- 238000000605 extraction Methods 0.000 claims description 2
- 102000004157 Hydrolases Human genes 0.000 claims 1
- 108090000604 Hydrolases Proteins 0.000 claims 1
- 230000006978 adaptation Effects 0.000 claims 1
- 239000001166 ammonium sulphate Substances 0.000 claims 1
- 239000000284 extract Substances 0.000 claims 1
- 238000010008 shearing Methods 0.000 claims 1
- 230000000694 effects Effects 0.000 description 51
- 239000007788 liquid Substances 0.000 description 17
- 230000002538 fungal effect Effects 0.000 description 15
- 239000000243 solution Substances 0.000 description 13
- 210000004907 gland Anatomy 0.000 description 9
- 235000019833 protease Nutrition 0.000 description 9
- 230000001580 bacterial effect Effects 0.000 description 8
- 235000019419 proteases Nutrition 0.000 description 8
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
- 235000011389 fruit/vegetable juice Nutrition 0.000 description 7
- 229940079919 digestives enzyme preparation Drugs 0.000 description 6
- 102000004139 alpha-Amylases Human genes 0.000 description 5
- 108090000637 alpha-Amylases Proteins 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 238000002955 isolation Methods 0.000 description 5
- 239000010985 leather Substances 0.000 description 5
- 210000001819 pancreatic juice Anatomy 0.000 description 5
- 239000012266 salt solution Substances 0.000 description 5
- 239000007787 solid Substances 0.000 description 5
- 239000004382 Amylase Substances 0.000 description 4
- 241000228212 Aspergillus Species 0.000 description 4
- 210000000496 pancreas Anatomy 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 230000008719 thickening Effects 0.000 description 4
- 241000193830 Bacillus <bacterium> Species 0.000 description 3
- 241000194108 Bacillus licheniformis Species 0.000 description 3
- 108090000317 Chymotrypsin Proteins 0.000 description 3
- 241000235395 Mucor Species 0.000 description 3
- 108010019160 Pancreatin Proteins 0.000 description 3
- 241000235527 Rhizopus Species 0.000 description 3
- 240000005384 Rhizopus oryzae Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 229920002472 Starch Polymers 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 229960002376 chymotrypsin Drugs 0.000 description 3
- 238000011109 contamination Methods 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 229940055695 pancreatin Drugs 0.000 description 3
- 238000011084 recovery Methods 0.000 description 3
- 238000004062 sedimentation Methods 0.000 description 3
- 235000019698 starch Nutrition 0.000 description 3
- 239000008107 starch Substances 0.000 description 3
- 241000228245 Aspergillus niger Species 0.000 description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- 102000001554 Hemoglobins Human genes 0.000 description 2
- 108010054147 Hemoglobins Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- GXCLVBGFBYZDAG-UHFFFAOYSA-N N-[2-(1H-indol-3-yl)ethyl]-N-methylprop-2-en-1-amine Chemical compound CN(CCC1=CNC2=C1C=CC=C2)CC=C GXCLVBGFBYZDAG-UHFFFAOYSA-N 0.000 description 2
- 241000589516 Pseudomonas Species 0.000 description 2
- 241000235525 Rhizomucor pusillus Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 241000187747 Streptomyces Species 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108010027252 Trypsinogen Proteins 0.000 description 2
- 102000018690 Trypsinogen Human genes 0.000 description 2
- 229940024171 alpha-amylase Drugs 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
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000000287 crude extract Substances 0.000 description 2
- 238000005238 degreasing Methods 0.000 description 2
- 239000003792 electrolyte Substances 0.000 description 2
- 239000000706 filtrate Substances 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 235000013372 meat Nutrition 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 230000000813 microbial effect Effects 0.000 description 2
- 235000008390 olive oil Nutrition 0.000 description 2
- 239000004006 olive oil Substances 0.000 description 2
- 239000003755 preservative agent Substances 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 238000003307 slaughter Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- URAYPUMNDPQOKB-UHFFFAOYSA-N triacetin Chemical compound CC(=O)OCC(OC(C)=O)COC(C)=O URAYPUMNDPQOKB-UHFFFAOYSA-N 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 235000013311 vegetables Nutrition 0.000 description 2
- 108091005508 Acid proteases Proteins 0.000 description 1
- 229920000945 Amylopectin Polymers 0.000 description 1
- 229920000856 Amylose Polymers 0.000 description 1
- 241001513093 Aspergillus awamori Species 0.000 description 1
- 241000228197 Aspergillus flavus Species 0.000 description 1
- 241000459887 Aspergillus luchuensis Species 0.000 description 1
- 240000006439 Aspergillus oryzae Species 0.000 description 1
- 241000228230 Aspergillus parasiticus Species 0.000 description 1
- 241000228251 Aspergillus phoenicis Species 0.000 description 1
- 241000228257 Aspergillus sp. Species 0.000 description 1
- 241001112078 Aspergillus usamii Species 0.000 description 1
- 208000035404 Autolysis Diseases 0.000 description 1
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 1
- 241000194106 Bacillus mycoides Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000606215 Bacteroides vulgatus Species 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 108010004032 Bromelains Proteins 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- 240000001817 Cereus hexagonus Species 0.000 description 1
- 108010038061 Chymotrypsinogen Proteins 0.000 description 1
- 102100039501 Chymotrypsinogen B Human genes 0.000 description 1
- 101710147853 Chymotrypsinogen B Proteins 0.000 description 1
- 241000221756 Cryphonectria parasitica Species 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 241000178951 Endomyces Species 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 241001246273 Endothia Species 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 108090000270 Ficain Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 244000168141 Geotrichum candidum Species 0.000 description 1
- 235000017388 Geotrichum candidum Nutrition 0.000 description 1
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerol Natural products OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 1
- 241000223198 Humicola Species 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 108010093096 Immobilized Enzymes Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 108091005507 Neutral proteases Proteins 0.000 description 1
- 102000035092 Neutral proteases Human genes 0.000 description 1
- 102000019280 Pancreatic lipases Human genes 0.000 description 1
- 108050006759 Pancreatic lipases Proteins 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 241000228143 Penicillium Species 0.000 description 1
- 241000228150 Penicillium chrysogenum Species 0.000 description 1
- 241000985513 Penicillium oxalicum Species 0.000 description 1
- 241000228168 Penicillium sp. Species 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 241000303962 Rhizopus delemar Species 0.000 description 1
- 241000952054 Rhizopus sp. Species 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 241000235004 Saccharomycopsis fibuligera Species 0.000 description 1
- 241000015473 Schizothorax griseus Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 241000187438 Streptomyces fradiae Species 0.000 description 1
- 241000938061 Streptomyces thermophilus Species 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 241000222354 Trametes Species 0.000 description 1
- 241000042002 Trametes sanguinea Species 0.000 description 1
- 241000179532 [Candida] cylindracea Species 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 150000003863 ammonium salts Chemical class 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 235000013405 beer Nutrition 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 235000019835 bromelain Nutrition 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 235000013351 cheese Nutrition 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 229920006037 cross link polymer Polymers 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000018044 dehydration Effects 0.000 description 1
- 238000006297 dehydration reaction Methods 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 230000006866 deterioration Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 229940066758 endopeptidases Drugs 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 235000013861 fat-free Nutrition 0.000 description 1
- 239000000835 fiber 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
- 239000000499 gel Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- -1 glycerine ester Chemical class 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 239000001087 glyceryl triacetate Substances 0.000 description 1
- 235000013773 glyceryl triacetate Nutrition 0.000 description 1
- 229930182470 glycoside Natural products 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 239000000644 isotonic solution Substances 0.000 description 1
- 239000012669 liquid formulation Substances 0.000 description 1
- 238000011169 microbiological contamination Methods 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- RUOJZAUFBMNUDX-UHFFFAOYSA-N propylene carbonate Chemical compound CC1COC(=O)O1 RUOJZAUFBMNUDX-UHFFFAOYSA-N 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 230000007281 self degradation Effects 0.000 description 1
- 230000028043 self proteolysis Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000009923 sugaring Methods 0.000 description 1
- 239000008399 tap water Substances 0.000 description 1
- 235000020679 tap water Nutrition 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 229960002622 triacetin Drugs 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 238000005303 weighing Methods 0.000 description 1
- 238000010626 work up procedure Methods 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)
-
- 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)
-
- 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)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE3927286A DE3927286C2 (de) | 1989-08-18 | 1989-08-18 | Wäßrige Enzym-Flüssigformulierungen |
| DE3927286 | 1989-08-18 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NL9001731A true NL9001731A (nl) | 1991-03-18 |
Family
ID=6387365
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NL9001731A NL9001731A (nl) | 1989-08-18 | 1990-07-31 | Werkwijze voor het bereiden van stabiele enzymdispersies. |
Country Status (14)
Families Citing this family (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR101670016B1 (ko) | 2007-02-20 | 2016-10-27 | 앨러간 파마슈티컬스 인터내셔널 리미티드 | 안정한 소화 효소 조성물 |
| DK2621476T4 (da) | 2010-10-01 | 2020-10-26 | Nestle Sa | Enterisk overtrukne pancrelipaseformuleringer med lav styrke |
| AU2012293325B2 (en) | 2011-08-08 | 2015-05-07 | Allergan Pharmaceuticals International Limited | Method for dissolution testing of solid compositions containing digestive enzymes |
| MX2016001593A (es) | 2013-08-09 | 2016-09-29 | Allergan Pharmaceuticals Int Ltd | Composicion de enzima digestiva adecuada para administracion enterica. |
| CA2915671A1 (en) * | 2013-11-05 | 2015-05-14 | Aptalis Pharma Ltd. | High potency pancreatin pharmaceutical compositions |
| CA2947998A1 (en) | 2014-06-19 | 2015-12-23 | Aptalis Pharma Ltd. | Methods for removing viral contaminants from pancreatic extracts |
| KR20170045408A (ko) * | 2015-10-16 | 2017-04-27 | 대한민국(농촌진흥청장) | 산 생성능이 우수한 토착 종균, 아스퍼질러스 루추엔시스 74-5를 이용한 탁주용 고체종국 제조방법 |
| CN118903386A (zh) | 2017-08-24 | 2024-11-08 | 诺和诺德股份有限公司 | Glp-1组合物及其用途 |
| CN115135304A (zh) | 2020-02-18 | 2022-09-30 | 诺和诺德股份有限公司 | Glp-1组合物及其用途 |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| FR2001M (fr) * | 1961-11-06 | 1963-09-09 | Felix Amour | Nouveau procédé de préparation de solutions aqueuses stables d'enzymes et cristallisation. solution-type : solution isotonique stable de papaine. |
| US3557002A (en) * | 1967-11-15 | 1971-01-19 | Procter & Gamble | Stabilized aqueous enzyme preparation |
| US3741902A (en) * | 1971-05-24 | 1973-06-26 | Purex Corp | Laundry prespotter composition |
| DE2234412B2 (de) * | 1972-07-13 | 1980-07-03 | Henkel Kgaa, 4000 Duesseldorf | Verfahren zur Stabilisierung und Fällung konzentrierter Protease-Lösungen |
| SU659613A1 (ru) * | 1976-09-24 | 1979-04-30 | Всесоюзный Научно-Исследовательский Биотехнический Институт | Способ получени комплекса пектолитических ферментов |
| US4923981A (en) * | 1982-09-03 | 1990-05-08 | Sbp, Inc. | Use of parenchymal cell cellulose to improve comestibles |
| US4540506A (en) * | 1983-04-15 | 1985-09-10 | Genex Corporation | Composition for cleaning drains clogged with deposits containing hair |
| US4517101A (en) * | 1983-08-22 | 1985-05-14 | David Williams | Reduced biodegradability in a polymer flood process |
| US4806479A (en) * | 1985-05-13 | 1989-02-21 | Miles Inc. | Use of stabilizing agents in culture media for growing acid producing bacteria |
| DE3704465C2 (de) * | 1987-02-13 | 1995-11-02 | Roehm Gmbh | Flüssig-Formulierungen von Enzymen |
| JPH01104171A (ja) * | 1987-10-16 | 1989-04-21 | Agency Of Ind Science & Technol | α−１・６−グルコシダーゼの安定化法 |
| JPH01104170A (ja) * | 1987-10-16 | 1989-04-21 | Agency Of Ind Science & Technol | 安定なα−１，６−グルコシダーゼ組成物 |
| JPH01104173A (ja) * | 1987-10-16 | 1989-04-21 | Agency Of Ind Science & Technol | アミラーゼの安定化法 |
-
1989
- 1989-08-18 DE DE3927286A patent/DE3927286C2/de not_active Expired - Fee Related
-
1990
- 1990-07-10 ES ES9001884A patent/ES2020889A6/es not_active Expired - Lifetime
- 1990-07-17 FR FR9009093A patent/FR2651006B1/fr not_active Expired - Fee Related
- 1990-07-31 NL NL9001731A patent/NL9001731A/nl not_active Application Discontinuation
- 1990-08-10 SE SE9002623A patent/SE9002623L/ not_active Application Discontinuation
- 1990-08-15 US US07/568,468 patent/US5169771A/en not_active Expired - Lifetime
- 1990-08-16 BR BR909004059A patent/BR9004059A/pt not_active IP Right Cessation
- 1990-08-17 JP JP2215961A patent/JP3004327B2/ja not_active Expired - Lifetime
- 1990-08-17 GB GB9018065A patent/GB2234973B/en not_active Expired - Fee Related
- 1990-08-17 AR AR90317621A patent/AR243602A1/es active
- 1990-08-17 CH CH2689/90A patent/CH681809A5/de not_active IP Right Cessation
- 1990-08-17 DK DK197190A patent/DK197190A/da not_active Application Discontinuation
- 1990-08-17 IT IT67649A patent/IT1240976B/it active IP Right Grant
- 1990-08-18 KR KR1019900012715A patent/KR0174263B1/ko not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| KR910004798A (ko) | 1991-03-29 |
| IT9067649A1 (it) | 1992-02-17 |
| JPH0398580A (ja) | 1991-04-24 |
| SE9002623D0 (sv) | 1990-08-10 |
| GB2234973A (en) | 1991-02-20 |
| BR9004059A (pt) | 1991-09-03 |
| AR243602A1 (es) | 1993-08-31 |
| IT1240976B (it) | 1993-12-27 |
| US5169771A (en) | 1992-12-08 |
| SE9002623L (sv) | 1991-02-19 |
| DK197190D0 (da) | 1990-08-17 |
| CH681809A5 (GUID-C5D7CC26-194C-43D0-91A1-9AE8C70A9BFF.html) | 1993-05-28 |
| GB2234973B (en) | 1993-05-19 |
| GB9018065D0 (en) | 1990-10-03 |
| DE3927286C2 (de) | 1997-07-24 |
| DK197190A (da) | 1991-02-19 |
| FR2651006A1 (fr) | 1991-02-22 |
| KR0174263B1 (ko) | 1999-02-01 |
| IT9067649A0 (it) | 1990-08-17 |
| DE3927286A1 (de) | 1991-02-21 |
| FR2651006B1 (fr) | 1993-03-26 |
| JP3004327B2 (ja) | 2000-01-31 |
| ES2020889A6 (es) | 1991-10-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| B� ckle et al. | Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530 | |
| DE3704465C2 (de) | Flüssig-Formulierungen von Enzymen | |
| Aunstrup | Production, isolation and economics of extracellular enzymes | |
| DE3779753T2 (de) | Bei niedriger temperatur aktive alkalische protease aus nocardiopsis dassonvillei und deren herstellung. | |
| CA1320164C (en) | Separation process | |
| Chakrabarti et al. | Purification and characterization of an extracellular alkaline serine protease from Aspergillus terreus (IJIRA 6.2) | |
| Ali et al. | PRODUCTION, PURIFICATION AND SOME PROPERTIES OF EXTRACELLULAR KERATINASE FROM FEATHERS-DEGRADATION BY ASPERGILLUS ORYZAE NRRL-447. | |
| Coral et al. | Thermostable alkaline protease produced by an Aspergillus niger strain | |
| US5891708A (en) | Nutrient composition resulting from maize steeping | |
| NL9001731A (nl) | Werkwijze voor het bereiden van stabiele enzymdispersies. | |
| RU2104300C1 (ru) | Способ получения белкового гидролизата дрожжевой биомассы | |
| US5192677A (en) | Alkali and heat stable protease from thermomonospora fusca | |
| US20130115671A1 (en) | Enzymes from conidiobolus brefeldianus and process for preparation thereof | |
| Korkmaz et al. | Keratinolytic activity of Streptomyces strain BA7, a new isolate from Turkey | |
| EP0458644A1 (en) | A micro-organism and proteases therefrom | |
| US2979440A (en) | Stabilized diastatic enzyme compositions | |
| US5395613A (en) | Process for degradation of keratin, keratinaceous material, collagen and collagenaceous material with enzyme material, cell-free culture or cell culture from micrococcus sedentarius | |
| US4904586A (en) | Enzymatic process for treating xanthan gums in order to improve the filterability of their aqueous solutions | |
| Triveni et al. | Clarification of xanthan gum with extracellular enzymes secreted by Trichoderma koningii | |
| Ogundero et al. | The purification and activities of an alkaline protease of Aspergillus clavatus from Nigerian poultry feeds | |
| US2547429A (en) | Isolation of enzymes from aqueous solutions with lignin and gelatin and product obtained thereby | |
| NL9101869A (nl) | Protease als taminecomplex bevattende enzympreparaten, de toepassing hiervan alsmede leder, bereid met behulp van deze preparaten. | |
| US6451586B1 (en) | Enzyme preparation containing protease | |
| EP0127938A1 (en) | Whey derivatives | |
| Lee et al. | Purification and characterization of an alkaline protease produced by a Xanthomonas sp. YL-37 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| BA | A request for search or an international-type search has been filed | ||
| BC | A request for examination has been filed | ||
| BV | The patent application has lapsed |