EA028228B1 - Гидролизующая глютеновые олигопептиды эндопептидазная композиция, способ ее получения и применение - Google Patents
Гидролизующая глютеновые олигопептиды эндопептидазная композиция, способ ее получения и применение Download PDFInfo
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- EA028228B1 EA028228B1 EA201491117A EA201491117A EA028228B1 EA 028228 B1 EA028228 B1 EA 028228B1 EA 201491117 A EA201491117 A EA 201491117A EA 201491117 A EA201491117 A EA 201491117A EA 028228 B1 EA028228 B1 EA 028228B1
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- Eurasian Patent Office
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- endopeptidase
- sequence
- enzyme composition
- endopep
- tht
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- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
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- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
- A61K38/482—Serine endopeptidases (3.4.21)
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
- A23J3/00—Working-up of proteins for foodstuffs
- A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
- A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
- A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
- A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L2/00—Non-alcoholic beverages; Dry compositions or concentrates therefor; Preparation or treatment thereof
- A23L2/52—Adding ingredients
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES, NOT OTHERWISE PROVIDED FOR; PREPARATION OR TREATMENT THEREOF
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
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- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
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- A—HUMAN NECESSITIES
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- A61P37/02—Immunomodulators
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- C—CHEMISTRY; METALLURGY
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- 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
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
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- C—CHEMISTRY; METALLURGY
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- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21026—Prolyl oligopeptidase (3.4.21.26), i.e. proline-specific endopeptidase
Landscapes
- Health & Medical Sciences (AREA)
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- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
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- Molecular Biology (AREA)
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- Dermatology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP11425291 | 2011-12-06 | ||
| PCT/EP2012/071816 WO2013083338A1 (en) | 2011-12-06 | 2012-11-05 | New proteases able to hydrolyze gluten peptides and proteins at acidic ph, from the actinomycete actinoallomurus |
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| EA201491117A1 EA201491117A1 (ru) | 2014-09-30 |
| EA028228B1 true EA028228B1 (ru) | 2017-10-31 |
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| EA201491117A EA028228B1 (ru) | 2011-12-06 | 2012-11-05 | Гидролизующая глютеновые олигопептиды эндопептидазная композиция, способ ее получения и применение |
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| US (2) | US20140356345A1 (enExample) |
| EP (1) | EP2788018B1 (enExample) |
| JP (1) | JP6203743B2 (enExample) |
| CN (1) | CN104039345B (enExample) |
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| BR (1) | BR112014012100B1 (enExample) |
| CA (1) | CA2852365C (enExample) |
| EA (1) | EA028228B1 (enExample) |
| ES (1) | ES2595500T3 (enExample) |
| IN (1) | IN2014CN04131A (enExample) |
| WO (1) | WO2013083338A1 (enExample) |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| LT2718434T (lt) | 2011-08-10 | 2018-08-10 | University Of Washington Through Its Center For Commercialization | Kompozicijos ir būdai, skirti celiakijos gydymui |
| US10266815B2 (en) * | 2013-08-14 | 2019-04-23 | University Of Washington Through Its Center For Commercialization | Compositions and methods for treating celiac sprue disease |
| US9867872B2 (en) | 2013-09-05 | 2018-01-16 | Dsm Ip Assets B.V. | Use of an acidic soft drink to enhance the efficacy of a gluten-digesting enzyme |
| WO2015078372A1 (en) * | 2013-11-26 | 2015-06-04 | Novozymes A/S | Milling process |
| CN107105707B (zh) * | 2014-10-24 | 2022-07-22 | 杜邦营养生物科学有限公司 | 脯氨酸耐受性三肽基肽酶及其用途 |
| TN2017000520A1 (en) | 2015-06-08 | 2019-04-12 | Univ California | Compositions and methods for treating celiac sprue disease |
| WO2017139659A1 (en) | 2016-02-11 | 2017-08-17 | Trustees Of Boston University | Rothia subtilisins, s8a family proteases, as therapeutic enzymes for application in gluten-intolerance disorders |
| IT201900012942A1 (it) | 2019-07-25 | 2021-01-25 | Nemysis Ltd | Metodo per la produzione di una composizione enzimatica comprendente una endopeptidasi ricombinante |
| AU2020318422B2 (en) * | 2019-07-25 | 2026-03-19 | Nemysis Limited | Method for the production of an enzymatic composition comprising a recombinant endopeptidase |
| CN111172138B (zh) * | 2020-02-14 | 2022-03-25 | 江南大学 | 一种蛋白水解酶及其在蛋白肽生产中的应用 |
| CA3186744A1 (en) | 2020-06-09 | 2021-12-16 | Dr. Schar S.P.A. | Method to prepare a mixture and food products deriving therefrom |
| IT202100018254A1 (it) | 2021-07-12 | 2023-01-12 | Nemysis Ltd | New systems for producing recombinant proteins/ nuovi sistemi di produzione di proteine ricombinanti |
| CN114438044B (zh) * | 2022-01-14 | 2024-03-29 | 南昌大学 | 一种高效降解麸质蛋白的多酶复合体及其应用 |
| TWI864494B (zh) | 2022-11-17 | 2024-12-01 | 國立中興大學 | 天冬胺酸蛋白酶於水解麩質蛋白之用途、編碼該天冬胺酸蛋白酶之核酸分子、生產該天冬胺酸蛋白酶之方法及其應用 |
| AU2024269012A1 (en) * | 2023-05-11 | 2026-01-08 | Amplifye, Inc. | Wine dehazing methods and compositions |
| WO2025067635A1 (en) * | 2023-09-26 | 2025-04-03 | Amyra Biotech Ag | Pharmaceutical compositions comprising exopeptidases and uses thereof |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003068170A2 (en) * | 2002-02-14 | 2003-08-21 | The Board Of Trustees Of The Leland Stanford Junior University | Enzyme treatment of foodstuffs for celiac sprue |
| WO2005107786A1 (en) * | 2004-04-26 | 2005-11-17 | Celiac Sprue Research Foundation | Therapeutic enzyme formulations and uses thereof |
| WO2011077359A2 (en) * | 2009-12-21 | 2011-06-30 | Centre Hospitalier Universitaire Vaudois (Chuv) | Synergic action of a prolyl protease and tripeptidyl proteases |
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| JP3104935B2 (ja) | 1992-05-28 | 2000-10-30 | 株式会社ブリヂストン | 空気入りタイヤ |
| US7265093B2 (en) * | 2002-05-14 | 2007-09-04 | The Board Of Trustees Of The Leland Stanford Junior University | Drug therapy for Celiac Sprue |
| DK1673457T3 (da) | 2003-08-25 | 2011-09-05 | Funzyme Biotechnologies Sa | Nye svampeproteiner og nukleinsyrer, der koder for disse |
| US8524225B2 (en) | 2003-09-23 | 2013-09-03 | Dsm Ip Assets B.V. | Use of proline specific endoproteases to hydrolyse peptides and proteins |
| NL1027650C1 (nl) | 2004-12-03 | 2006-06-07 | Leonardus Antonius Luttikhold | Transporthulpmiddel voor deuren en panelen. |
| EP1985698A1 (en) * | 2007-04-25 | 2008-10-29 | Nestec S.A. | Peptidases from basidiomycetes |
| EP2531521B1 (en) * | 2010-02-02 | 2017-09-06 | Amano Enzyme USA., Ltd. | Use of proteases for gluten intolerance |
| JP2013523133A (ja) * | 2010-03-30 | 2013-06-17 | アルヴィン ファーマシューティカルズ インコーポレーティッド | グルテンを分解するためのプロテアーゼ |
| JP2011211997A (ja) * | 2010-04-02 | 2011-10-27 | Astellas Pharma Inc | アントラサイクリン化合物を生産する微生物 |
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- 2012-11-05 BR BR112014012100-1A patent/BR112014012100B1/pt active IP Right Grant
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- 2012-11-05 AU AU2012348782A patent/AU2012348782B2/en active Active
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Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003068170A2 (en) * | 2002-02-14 | 2003-08-21 | The Board Of Trustees Of The Leland Stanford Junior University | Enzyme treatment of foodstuffs for celiac sprue |
| WO2005107786A1 (en) * | 2004-04-26 | 2005-11-17 | Celiac Sprue Research Foundation | Therapeutic enzyme formulations and uses thereof |
| WO2011077359A2 (en) * | 2009-12-21 | 2011-06-30 | Centre Hospitalier Universitaire Vaudois (Chuv) | Synergic action of a prolyl protease and tripeptidyl proteases |
Non-Patent Citations (1)
| Title |
|---|
| ROBERTA POZZI, MATTEO SIMONE, CARLO MAZZETTI, SONIA MAFFIOLI, PAOLO MONCIARDINI, LINDA CAVALETTI, RUGGIERO BAMONTE, MARGHERITA SOS: "The genus Actinoallomurus and some of its metabolites", THE JOURNAL OF ANTIBIOTICS, NATURE PUBLISHING GROUP, GB, vol. 64, no. 1, 1 January 2011 (2011-01-01), GB, pages 133 - 139, XP002673610, ISSN: 0021-8820, DOI: 10.1038/ja.2010.149 * |
Also Published As
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|---|---|
| US20140356345A1 (en) | 2014-12-04 |
| ES2595500T3 (es) | 2016-12-30 |
| IN2014CN04131A (enExample) | 2015-07-17 |
| CA2852365A1 (en) | 2013-06-13 |
| US20160114009A1 (en) | 2016-04-28 |
| CA2852365C (en) | 2021-01-26 |
| US10201593B2 (en) | 2019-02-12 |
| EP2788018B1 (en) | 2016-06-29 |
| AU2012348782A1 (en) | 2014-05-15 |
| HK1198244A1 (en) | 2015-03-20 |
| WO2013083338A1 (en) | 2013-06-13 |
| JP2015500641A (ja) | 2015-01-08 |
| JP6203743B2 (ja) | 2017-09-27 |
| CN104039345B (zh) | 2016-11-09 |
| CN104039345A (zh) | 2014-09-10 |
| BR112014012100A2 (pt) | 2020-10-27 |
| EA201491117A1 (ru) | 2014-09-30 |
| EP2788018A1 (en) | 2014-10-15 |
| BR112014012100B1 (pt) | 2023-04-18 |
| AU2012348782B2 (en) | 2017-10-26 |
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