JPS58152498A - 低分子ペプチド混合物の製造方法 - Google Patents
低分子ペプチド混合物の製造方法Info
- Publication number
- JPS58152498A JPS58152498A JP57035485A JP3548582A JPS58152498A JP S58152498 A JPS58152498 A JP S58152498A JP 57035485 A JP57035485 A JP 57035485A JP 3548582 A JP3548582 A JP 3548582A JP S58152498 A JPS58152498 A JP S58152498A
- Authority
- JP
- Japan
- Prior art keywords
- protein
- molecular
- low
- reaction
- amino acid
- 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.)
- Granted
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 60
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 56
- 238000004519 manufacturing process Methods 0.000 title claims description 11
- 150000001413 amino acids Chemical class 0.000 claims abstract description 104
- 238000006243 chemical reaction Methods 0.000 claims abstract description 62
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 44
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 44
- 239000000126 substance Substances 0.000 claims abstract description 34
- 102000004190 Enzymes Human genes 0.000 claims abstract description 23
- 108090000790 Enzymes Proteins 0.000 claims abstract description 23
- 229940088598 enzyme Drugs 0.000 claims abstract description 23
- -1 aminoacid ester Chemical class 0.000 claims abstract description 21
- 239000004365 Protease Substances 0.000 claims abstract description 20
- 108091005804 Peptidases Proteins 0.000 claims abstract description 18
- 102000035195 Peptidases Human genes 0.000 claims abstract description 15
- 238000006911 enzymatic reaction Methods 0.000 claims abstract description 13
- 238000006460 hydrolysis reaction Methods 0.000 claims abstract description 12
- 102000057297 Pepsin A Human genes 0.000 claims abstract description 7
- 108090000284 Pepsin A Proteins 0.000 claims abstract description 7
- 229940111202 pepsin Drugs 0.000 claims abstract description 7
- 238000002523 gelfiltration Methods 0.000 claims abstract description 3
- 239000000243 solution Substances 0.000 claims abstract 5
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 20
- 238000000034 method Methods 0.000 claims description 15
- 108090000526 Papain Proteins 0.000 claims description 11
- 239000012528 membrane Substances 0.000 claims description 11
- 235000019834 papain Nutrition 0.000 claims description 11
- 229940055729 papain Drugs 0.000 claims description 11
- 239000002994 raw material Substances 0.000 claims description 11
- 150000003839 salts Chemical class 0.000 claims description 11
- 238000000354 decomposition reaction Methods 0.000 claims description 10
- 238000001223 reverse osmosis Methods 0.000 claims description 7
- 239000012535 impurity Substances 0.000 claims description 5
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 claims description 5
- 108090000270 Ficain Proteins 0.000 claims description 4
- 235000019836 ficin Nutrition 0.000 claims description 4
- POTUGHMKJGOKRI-UHFFFAOYSA-N ficin Chemical compound FI=CI=N POTUGHMKJGOKRI-UHFFFAOYSA-N 0.000 claims description 4
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 claims description 2
- 229920000642 polymer Polymers 0.000 claims description 2
- 235000019419 proteases Nutrition 0.000 claims description 2
- 239000007864 aqueous solution Substances 0.000 claims 1
- 235000001014 amino acid Nutrition 0.000 abstract description 110
- 235000018102 proteins Nutrition 0.000 abstract description 39
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 abstract description 9
- 230000000694 effects Effects 0.000 abstract description 7
- 230000007062 hydrolysis Effects 0.000 abstract description 7
- 239000007853 buffer solution Substances 0.000 abstract 1
- 229940024606 amino acid Drugs 0.000 description 105
- 102000004196 processed proteins & peptides Human genes 0.000 description 16
- 229960004452 methionine Drugs 0.000 description 15
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 14
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 14
- FFEARJCKVFRZRR-UHFFFAOYSA-N L-Methionine Natural products CSCCC(N)C(O)=O FFEARJCKVFRZRR-UHFFFAOYSA-N 0.000 description 12
- 229930195722 L-methionine Natural products 0.000 description 12
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 12
- 108010016626 Dipeptides Proteins 0.000 description 11
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 11
- 235000019441 ethanol Nutrition 0.000 description 11
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 10
- 238000010521 absorption reaction Methods 0.000 description 10
- 239000000047 product Substances 0.000 description 10
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 8
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 8
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 7
- 238000005886 esterification reaction Methods 0.000 description 7
- 150000002148 esters Chemical class 0.000 description 7
- 229910052757 nitrogen Inorganic materials 0.000 description 7
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 6
- 235000016709 nutrition Nutrition 0.000 description 6
- 229960004295 valine Drugs 0.000 description 6
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 5
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 5
- 229960003136 leucine Drugs 0.000 description 5
- 239000007788 liquid Substances 0.000 description 5
- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical compound [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 4
- 235000010469 Glycine max Nutrition 0.000 description 4
- 244000068988 Glycine max Species 0.000 description 4
- 235000019454 L-leucine Nutrition 0.000 description 4
- 239000004395 L-leucine Substances 0.000 description 4
- 230000032050 esterification Effects 0.000 description 4
- ARJXIGOIOGJAKR-LURJTMIESA-N ethyl L-methioninate Chemical compound CCOC(=O)[C@@H](N)CCSC ARJXIGOIOGJAKR-LURJTMIESA-N 0.000 description 4
- 229910000029 sodium carbonate Inorganic materials 0.000 description 4
- 108010068370 Glutens Proteins 0.000 description 3
- 239000004472 Lysine Substances 0.000 description 3
- 241000209140 Triticum Species 0.000 description 3
- 235000021307 Triticum Nutrition 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 230000008485 antagonism Effects 0.000 description 3
- 150000005693 branched-chain amino acids Chemical class 0.000 description 3
- 239000003054 catalyst Substances 0.000 description 3
- 235000021312 gluten Nutrition 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 230000003301 hydrolyzing effect Effects 0.000 description 3
- 229930192033 plastin Natural products 0.000 description 3
- 108010049148 plastin Proteins 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 235000019766 L-Lysine Nutrition 0.000 description 2
- 239000004201 L-cysteine Substances 0.000 description 2
- 235000013878 L-cysteine Nutrition 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- 229930182844 L-isoleucine Natural products 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- UIIMBOGNXHQVGW-DEQYMQKBSA-M Sodium bicarbonate-14C Chemical compound [Na+].O[14C]([O-])=O UIIMBOGNXHQVGW-DEQYMQKBSA-M 0.000 description 2
- 108010073771 Soybean Proteins Proteins 0.000 description 2
- 230000003042 antagnostic effect Effects 0.000 description 2
- 229910000019 calcium carbonate Inorganic materials 0.000 description 2
- 159000000007 calcium salts Chemical class 0.000 description 2
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
- 239000000470 constituent Substances 0.000 description 2
- CZEPJJXZASVXQF-ZETCQYMHSA-N ethyl (2s)-2,6-diaminohexanoate Chemical compound CCOC(=O)[C@@H](N)CCCCN CZEPJJXZASVXQF-ZETCQYMHSA-N 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 210000001035 gastrointestinal tract Anatomy 0.000 description 2
- IXCSERBJSXMMFS-UHFFFAOYSA-N hydrogen chloride Substances Cl.Cl IXCSERBJSXMMFS-UHFFFAOYSA-N 0.000 description 2
- 229910000041 hydrogen chloride Inorganic materials 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 150000007524 organic acids Chemical class 0.000 description 2
- 239000000843 powder Substances 0.000 description 2
- 238000010992 reflux Methods 0.000 description 2
- 235000019710 soybean protein Nutrition 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- FYSNRJHAOHDILO-UHFFFAOYSA-N thionyl chloride Chemical compound ClS(Cl)=O FYSNRJHAOHDILO-UHFFFAOYSA-N 0.000 description 2
- 108091005508 Acid proteases Proteins 0.000 description 1
- 241001385733 Aesculus indica Species 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 102000005367 Carboxypeptidases Human genes 0.000 description 1
- 108010006303 Carboxypeptidases Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 235000002918 Fraxinus excelsior Nutrition 0.000 description 1
- 206010019663 Hepatic failure Diseases 0.000 description 1
- 102000004157 Hydrolases Human genes 0.000 description 1
- 108090000604 Hydrolases Proteins 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 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
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 206010067125 Liver injury Diseases 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 108090000787 Subtilisin Proteins 0.000 description 1
- 101710097834 Thiol protease Proteins 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 235000010724 Wisteria floribunda Nutrition 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 239000002956 ash Substances 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000010612 desalination reaction Methods 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 235000012888 dietary physiology Nutrition 0.000 description 1
- 229940079919 digestives enzyme preparation Drugs 0.000 description 1
- 238000004821 distillation Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 125000004494 ethyl ester group Chemical group 0.000 description 1
- 231100000234 hepatic damage Toxicity 0.000 description 1
- 208000007386 hepatic encephalopathy Diseases 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 231100000568 intoxicate Toxicity 0.000 description 1
- 230000008818 liver damage Effects 0.000 description 1
- 208000019423 liver disease Diseases 0.000 description 1
- 208000007903 liver failure Diseases 0.000 description 1
- 231100000835 liver failure Toxicity 0.000 description 1
- 235000018977 lysine Nutrition 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 235000010755 mineral Nutrition 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 235000016236 parenteral nutrition Nutrition 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 239000003531 protein hydrolysate Substances 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 238000005057 refrigeration Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000009469 supplementation Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- 230000004614 tumor growth Effects 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
- 239000004474 valine Substances 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
- C07K1/12—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by hydrolysis, i.e. solvolysis in general
- C07K1/126—Aminolysis
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
Landscapes
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Microbiology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biotechnology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Analytical Chemistry (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Priority Applications (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP57035485A JPS58152498A (ja) | 1982-03-06 | 1982-03-06 | 低分子ペプチド混合物の製造方法 |
| DE8383102142T DE3365962D1 (en) | 1982-03-06 | 1983-03-04 | Low-molecular weight peptide mixture and method of producing same |
| EP83102142A EP0088398B1 (en) | 1982-03-06 | 1983-03-04 | Low-molecular weight peptide mixture and method of producing same |
| US06/794,322 US4940662A (en) | 1982-03-06 | 1985-11-01 | Low-molecular weight peptide mixture and method of producing same |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP57035485A JPS58152498A (ja) | 1982-03-06 | 1982-03-06 | 低分子ペプチド混合物の製造方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS58152498A true JPS58152498A (ja) | 1983-09-10 |
| JPS6217520B2 JPS6217520B2 (enExample) | 1987-04-17 |
Family
ID=12443045
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP57035485A Granted JPS58152498A (ja) | 1982-03-06 | 1982-03-06 | 低分子ペプチド混合物の製造方法 |
Country Status (4)
| Country | Link |
|---|---|
| US (1) | US4940662A (enExample) |
| EP (1) | EP0088398B1 (enExample) |
| JP (1) | JPS58152498A (enExample) |
| DE (1) | DE3365962D1 (enExample) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6098994A (ja) * | 1983-11-04 | 1985-06-01 | Fuji Oil Co Ltd | オリゴペプチド混合物の製造法 |
| JPH01132339A (ja) * | 1987-11-16 | 1989-05-24 | Fuji Oil Co Ltd | 蛋白含有食品の製造方法 |
| JP2003092996A (ja) * | 2001-09-25 | 2003-04-02 | Yaizu Suisankagaku Industry Co Ltd | イミダゾールジペプチド類含有組成物の製造方法 |
| WO2006134752A1 (ja) * | 2005-06-15 | 2006-12-21 | Fuji Oil Company, Limited | 大豆ペプチド組成物 |
| JP2012249597A (ja) * | 2011-06-03 | 2012-12-20 | Kaneka Corp | リン脂質の製造方法 |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| BE1003298A3 (nl) * | 1990-01-12 | 1992-02-18 | Tessenderlo Chem Nv | Werkwijze voor het bereiden van een enzymatisch hydrolysaat. |
| WO1991012331A1 (en) * | 1990-02-14 | 1991-08-22 | Receptor Laboratories, Inc. | Method for generating and screening useful peptides |
| US5366862A (en) * | 1990-02-14 | 1994-11-22 | Receptor Laboratories, Inc. | Method for generating and screening useful peptides |
| DK19991D0 (da) * | 1991-02-06 | 1991-02-06 | Novo Nordisk As | Proteinpraeparationer |
| EP0499306B1 (en) * | 1991-02-11 | 1995-09-27 | Unilever N.V. | Starches with an improved flavour |
| FR2714390B1 (fr) * | 1993-12-23 | 1996-03-08 | Agronomique Inst Nat Rech | Procédé d'obtention de produits peptidiques et produits obtenus. |
| US5750360A (en) * | 1995-06-07 | 1998-05-12 | Lxr Biotechnology Inc. | Method for quantitatively measuring apoptosis |
| US20030138402A1 (en) * | 1995-12-25 | 2003-07-24 | Otsuka Pharmaceutical Co., Ltd. | Dry compositions |
| US6221423B1 (en) | 1998-04-13 | 2001-04-24 | Protein Technologies Int'l Inc. | Short-chained peptide material |
| US6939693B2 (en) * | 1999-10-29 | 2005-09-06 | Novus International, Inc. | Enantioselective oligomerization of α-hydroxy carboxylic acids and α-amino acids |
| WO2001032906A2 (en) * | 1999-10-29 | 2001-05-10 | Novus International, Inc. | Oligomers and oligomeric segments of alpha-hydroxy carboxylic acids and alpha-amino acids |
| EG24184A (en) * | 2001-06-15 | 2008-10-08 | Otsuka Pharma Co Ltd | Dry powder inhalation system for transpulmonary |
| US6973759B2 (en) * | 2001-08-28 | 2005-12-13 | Cardinal Ig Company | Methods and apparatus for providing information at the point of use for an insulating glass unit |
| NL1029059C2 (nl) * | 2005-05-17 | 2006-11-20 | Noord Nl Oliemolen Holding B V | Peptidenpreparaat voor het groeien en/of kweken van micro-organismen en/of cellen. |
| AU2009228250B2 (en) * | 2008-03-26 | 2015-03-19 | Glanbia Nutritionals (Ireland) Ltd. | Leucine-rich peptide compositions and methods for isolation |
| NO20100359A1 (no) | 2010-03-08 | 2011-09-09 | Marine Bioproducts As | Peptidmateriale og preparater og anvendelser derav. |
| NO20100369A1 (no) | 2010-03-08 | 2011-09-09 | Marine Bioproducts As | Peptidmateriale, fôrsammensetning og preparater og anvendelser derav. |
| NO20100370A1 (no) | 2010-03-08 | 2011-09-09 | Marine Bioproducts As | Peptidmateriale, fôrsammensetninger og preparater, og anvendelser derav. |
| CN111088310A (zh) * | 2019-12-27 | 2020-05-01 | 广州合诚实业有限公司 | 具有抑制α-葡萄糖苷酶活性的大豆肽及制备方法与应用 |
| EP4149277A4 (en) | 2021-05-21 | 2024-11-20 | Cambridge Crops, Inc. d/b/a Mori | SYSTEMS AND METHODS FOR MANUFACTURING SILK FIBROIN SOLUTION AND POWDERS CONTAINING SILK FIBROIN |
| US11864569B2 (en) | 2021-08-16 | 2024-01-09 | Cambridge Crops, Inc. | Systems and methods for improving the performance of cereal using a silk fibroin solution and powders containing silk fibroin |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS50123889A (enExample) * | 1974-03-06 | 1975-09-29 | ||
| JPS5182791A (enExample) * | 1975-01-16 | 1976-07-20 | Fuji Oil Co Ltd | |
| JPS54163894A (en) * | 1978-03-23 | 1979-12-26 | Miles Lab | Production and utilizaton of llamino acid substituted polypeptide |
| JPS5718995A (en) * | 1980-07-10 | 1982-01-30 | Terumo Corp | Production of low-molecular-weight peptide composition |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3803327A (en) * | 1970-11-24 | 1974-04-09 | Idemitsu Petrochemical Co | Process for producing plastein |
| US3904519A (en) * | 1971-10-19 | 1975-09-09 | Us Interior | Reverse osmosis process using crosslinked aromatic polyamide membranes |
| JPS5926636B2 (ja) * | 1975-04-04 | 1984-06-29 | フジセイユ カブシキガイシヤ | 蛋白質の改質方法 |
| US4087388A (en) * | 1976-10-21 | 1978-05-02 | E. I. Du Pont De Nemours And Company | Process of preparing a permselective membrane |
| JPS5718623A (en) * | 1980-07-10 | 1982-01-30 | Terumo Corp | Nutrition supplement containing peptide oligomer |
| US4452888A (en) * | 1980-07-10 | 1984-06-05 | Terumo Corporation | Process for producing a low-molecular weight peptide composition and nutrient agent containing the same |
| JPS5750900A (en) * | 1980-09-11 | 1982-03-25 | Terumo Corp | Preparation of modified protein-like composition |
-
1982
- 1982-03-06 JP JP57035485A patent/JPS58152498A/ja active Granted
-
1983
- 1983-03-04 EP EP83102142A patent/EP0088398B1/en not_active Expired
- 1983-03-04 DE DE8383102142T patent/DE3365962D1/de not_active Expired
-
1985
- 1985-11-01 US US06/794,322 patent/US4940662A/en not_active Expired - Fee Related
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS50123889A (enExample) * | 1974-03-06 | 1975-09-29 | ||
| JPS5182791A (enExample) * | 1975-01-16 | 1976-07-20 | Fuji Oil Co Ltd | |
| JPS54163894A (en) * | 1978-03-23 | 1979-12-26 | Miles Lab | Production and utilizaton of llamino acid substituted polypeptide |
| JPS5718995A (en) * | 1980-07-10 | 1982-01-30 | Terumo Corp | Production of low-molecular-weight peptide composition |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6098994A (ja) * | 1983-11-04 | 1985-06-01 | Fuji Oil Co Ltd | オリゴペプチド混合物の製造法 |
| JPH01132339A (ja) * | 1987-11-16 | 1989-05-24 | Fuji Oil Co Ltd | 蛋白含有食品の製造方法 |
| JP2003092996A (ja) * | 2001-09-25 | 2003-04-02 | Yaizu Suisankagaku Industry Co Ltd | イミダゾールジペプチド類含有組成物の製造方法 |
| WO2006134752A1 (ja) * | 2005-06-15 | 2006-12-21 | Fuji Oil Company, Limited | 大豆ペプチド組成物 |
| JP2012249597A (ja) * | 2011-06-03 | 2012-12-20 | Kaneka Corp | リン脂質の製造方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| EP0088398A1 (en) | 1983-09-14 |
| EP0088398B1 (en) | 1986-09-10 |
| JPS6217520B2 (enExample) | 1987-04-17 |
| DE3365962D1 (en) | 1986-10-16 |
| US4940662A (en) | 1990-07-10 |
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