CN110128523A - 一种具有调节b淋巴细胞活性的羊乳酪蛋白水解肽及其制备方法 - Google Patents
一种具有调节b淋巴细胞活性的羊乳酪蛋白水解肽及其制备方法 Download PDFInfo
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- CN110128523A CN110128523A CN201910479554.7A CN201910479554A CN110128523A CN 110128523 A CN110128523 A CN 110128523A CN 201910479554 A CN201910479554 A CN 201910479554A CN 110128523 A CN110128523 A CN 110128523A
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- A—HUMAN NECESSITIES
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- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
- C07K14/4701—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals not used
- C07K14/4732—Casein
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- 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
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- G—PHYSICS
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- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
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- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
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- G—PHYSICS
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- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6848—Methods of protein analysis involving mass spectrometry
Landscapes
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- Molecular Biology (AREA)
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- Bioinformatics & Cheminformatics (AREA)
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- General Chemical & Material Sciences (AREA)
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- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Priority Applications (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201910479554.7A CN110128523A (zh) | 2019-06-04 | 2019-06-04 | 一种具有调节b淋巴细胞活性的羊乳酪蛋白水解肽及其制备方法 |
| PCT/CN2020/088606 WO2020244351A1 (fr) | 2019-06-04 | 2020-05-06 | Peptide protéolytique pour la caséine dans le lait de chèvre qui régule l'activité des lymphocytes b, et procédé de préparation associé |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| CN201910479554.7A CN110128523A (zh) | 2019-06-04 | 2019-06-04 | 一种具有调节b淋巴细胞活性的羊乳酪蛋白水解肽及其制备方法 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CN110128523A true CN110128523A (zh) | 2019-08-16 |
Family
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Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN201910479554.7A Pending CN110128523A (zh) | 2019-06-04 | 2019-06-04 | 一种具有调节b淋巴细胞活性的羊乳酪蛋白水解肽及其制备方法 |
Country Status (2)
| Country | Link |
|---|---|
| CN (1) | CN110128523A (fr) |
| WO (1) | WO2020244351A1 (fr) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2020244351A1 (fr) * | 2019-06-04 | 2020-12-10 | 海普诺凯营养品有限公司 | Peptide protéolytique pour la caséine dans le lait de chèvre qui régule l'activité des lymphocytes b, et procédé de préparation associé |
Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005082927A2 (fr) * | 2004-02-26 | 2005-09-09 | Puleva Biotech, S.A. | Peptides utilises contre l'hypertension |
| CN103215332A (zh) * | 2013-04-16 | 2013-07-24 | 陕西科技大学 | 一种分步酶解羊乳酪蛋白制备ace抑制肽的方法 |
| CN103483418A (zh) * | 2013-09-12 | 2014-01-01 | 陈尚武 | 一种dpp-ⅳ抑制多肽及其应用 |
| CN104031965A (zh) * | 2014-06-05 | 2014-09-10 | 西北农林科技大学 | 一种山羊乳酪蛋白源抗菌肽的制备方法 |
| CN108314704A (zh) * | 2018-01-25 | 2018-07-24 | 海普诺凯营养品有限公司 | 一种羊乳清蛋白免疫调节肽、其制备方法及其应用 |
| WO2019091472A1 (fr) * | 2017-11-13 | 2019-05-16 | 江苏大学 | Procédé de digestion simulée assisté par ultrasons de peptide actif de protéine de lait et son application dans les aliments diététiques |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TW201716581A (zh) * | 2015-11-12 | 2017-05-16 | 首都國際商業有限公司 | 羊乳胜肽之製備方法、其產物及其用於製備保養品之用途 |
| CN110128523A (zh) * | 2019-06-04 | 2019-08-16 | 海普诺凯营养品有限公司 | 一种具有调节b淋巴细胞活性的羊乳酪蛋白水解肽及其制备方法 |
-
2019
- 2019-06-04 CN CN201910479554.7A patent/CN110128523A/zh active Pending
-
2020
- 2020-05-06 WO PCT/CN2020/088606 patent/WO2020244351A1/fr active Application Filing
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2005082927A2 (fr) * | 2004-02-26 | 2005-09-09 | Puleva Biotech, S.A. | Peptides utilises contre l'hypertension |
| CN103215332A (zh) * | 2013-04-16 | 2013-07-24 | 陕西科技大学 | 一种分步酶解羊乳酪蛋白制备ace抑制肽的方法 |
| CN103483418A (zh) * | 2013-09-12 | 2014-01-01 | 陈尚武 | 一种dpp-ⅳ抑制多肽及其应用 |
| CN104031965A (zh) * | 2014-06-05 | 2014-09-10 | 西北农林科技大学 | 一种山羊乳酪蛋白源抗菌肽的制备方法 |
| WO2019091472A1 (fr) * | 2017-11-13 | 2019-05-16 | 江苏大学 | Procédé de digestion simulée assisté par ultrasons de peptide actif de protéine de lait et son application dans les aliments diététiques |
| CN108314704A (zh) * | 2018-01-25 | 2018-07-24 | 海普诺凯营养品有限公司 | 一种羊乳清蛋白免疫调节肽、其制备方法及其应用 |
Non-Patent Citations (1)
| Title |
|---|
| FATIMA ZOHRA BOUNOUALA等: "Casein Hydrolysates by Lactobacillus brevis and Lactococcus lactis Proteases: Peptide Profile Discriminates Strain-Dependent Enzyme Specificity", 《JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY》 * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2020244351A1 (fr) * | 2019-06-04 | 2020-12-10 | 海普诺凯营养品有限公司 | Peptide protéolytique pour la caséine dans le lait de chèvre qui régule l'activité des lymphocytes b, et procédé de préparation associé |
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| WO2020244351A1 (fr) | 2020-12-10 |
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