ZA200601739B - Casein hydrolyzate, process for producing the same and use thereof - Google Patents
Casein hydrolyzate, process for producing the same and use thereof Download PDFInfo
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- ZA200601739B ZA200601739B ZA200601739A ZA200601739A ZA200601739B ZA 200601739 B ZA200601739 B ZA 200601739B ZA 200601739 A ZA200601739 A ZA 200601739A ZA 200601739 A ZA200601739 A ZA 200601739A ZA 200601739 B ZA200601739 B ZA 200601739B
- Authority
- ZA
- South Africa
- Prior art keywords
- pro
- casein
- enzymes
- hydrolysate
- peptides
- Prior art date
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- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 238000012921 fluorescence analysis Methods 0.000 description 1
- 235000013355 food flavoring agent Nutrition 0.000 description 1
- 235000003599 food sweetener Nutrition 0.000 description 1
- -1 for example Chemical class 0.000 description 1
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- 238000002523 gelfiltration Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 235000020251 goat milk Nutrition 0.000 description 1
- 230000007407 health benefit Effects 0.000 description 1
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- 230000000415 inactivating effect Effects 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
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- 238000002347 injection Methods 0.000 description 1
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- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 230000000968 intestinal effect Effects 0.000 description 1
- 235000015110 jellies Nutrition 0.000 description 1
- 239000008274 jelly Substances 0.000 description 1
- 238000004895 liquid chromatography mass spectrometry Methods 0.000 description 1
- 235000021056 liquid food Nutrition 0.000 description 1
- 239000012263 liquid product Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
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- 239000003475 metalloproteinase inhibitor Substances 0.000 description 1
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- 210000003240 portal vein Anatomy 0.000 description 1
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- 230000002265 prevention Effects 0.000 description 1
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- 239000003001 serine protease inhibitor Substances 0.000 description 1
- 235000020254 sheep milk Nutrition 0.000 description 1
- 239000004328 sodium tetraborate Substances 0.000 description 1
- 235000010339 sodium tetraborate Nutrition 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 235000012461 sponges Nutrition 0.000 description 1
- 239000003765 sweetening agent Substances 0.000 description 1
- JREYOWJEWZVAOR-UHFFFAOYSA-N triazanium;[3-methylbut-3-enoxy(oxido)phosphoryl] phosphate Chemical compound [NH4+].[NH4+].[NH4+].CC(=C)CCOP([O-])(=O)OP([O-])([O-])=O JREYOWJEWZVAOR-UHFFFAOYSA-N 0.000 description 1
- 229940066528 trichloroacetate Drugs 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/06—Dipeptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/06—Dipeptides
- C07K5/06104—Dipeptides with the first amino acid being acidic
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- 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
- A23L33/17—Amino acids, peptides or proteins
- A23L33/18—Peptides; Protein hydrolysates
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/12—Antihypertensives
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/06—Dipeptides
- C07K5/06008—Dipeptides with the first amino acid being neutral
- C07K5/06017—Dipeptides with the first amino acid being neutral and aliphatic
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/06—Dipeptides
- C07K5/06008—Dipeptides with the first amino acid being neutral
- C07K5/06017—Dipeptides with the first amino acid being neutral and aliphatic
- C07K5/06034—Dipeptides with the first amino acid being neutral and aliphatic the side chain containing 2 to 4 carbon atoms
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/06—Dipeptides
- C07K5/06086—Dipeptides with the first amino acid being basic
- C07K5/06095—Arg-amino acid
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/08—Tripeptides
- C07K5/0802—Tripeptides with the first amino acid being neutral
- C07K5/0804—Tripeptides with the first amino acid being neutral and aliphatic
- C07K5/081—Tripeptides with the first amino acid being neutral and aliphatic the side chain containing O or S as heteroatoms, e.g. Cys, Ser
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2003285007 | 2003-08-01 |
Publications (1)
Publication Number | Publication Date |
---|---|
ZA200601739B true ZA200601739B (en) | 2007-05-30 |
Family
ID=34113859
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ZA200601739A ZA200601739B (en) | 2003-08-01 | 2006-02-28 | Casein hydrolyzate, process for producing the same and use thereof |
ZA200601746A ZA200601746B (en) | 2003-08-01 | 2006-02-28 | Biologically non-degradable peptide, angiotensin converting enzyme inhibitor, drug and functional food |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ZA200601746A ZA200601746B (en) | 2003-08-01 | 2006-02-28 | Biologically non-degradable peptide, angiotensin converting enzyme inhibitor, drug and functional food |
Country Status (23)
Country | Link |
---|---|
US (3) | US20070299014A1 (de) |
EP (2) | EP1661909B1 (de) |
JP (3) | JP4669396B2 (de) |
KR (3) | KR101115557B1 (de) |
CN (3) | CN101381401A (de) |
AT (2) | ATE442855T1 (de) |
AU (2) | AU2004261522B2 (de) |
BR (2) | BRPI0413238A (de) |
CA (2) | CA2546497A1 (de) |
DE (2) | DE602004023210D1 (de) |
DK (2) | DK1669463T3 (de) |
EA (2) | EA010098B1 (de) |
ES (2) | ES2313067T3 (de) |
HK (2) | HK1093991A1 (de) |
MX (2) | MXPA06000879A (de) |
NO (2) | NO20060995L (de) |
NZ (2) | NZ545341A (de) |
PL (1) | PL1669463T3 (de) |
PT (2) | PT1669463E (de) |
TW (2) | TWI349676B (de) |
UA (2) | UA87278C2 (de) |
WO (2) | WO2005012542A1 (de) |
ZA (2) | ZA200601739B (de) |
Families Citing this family (36)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EA016396B1 (ru) * | 2005-02-24 | 2012-04-30 | ДСМ АйПи АССЕТС Б.В. | Способ получения пептидного гидролизата, содержащего ipp, и применение указанного гидролизата для производства функционального пищевого продукта, предназначенного для поддержания здоровья сердечно-сосудистой системы |
US20090304869A1 (en) * | 2005-04-28 | 2009-12-10 | Christianus Jacobus Van Platerink | Peptides Having an Ace Inhibiting Effect |
BRPI0612923A2 (pt) * | 2005-04-28 | 2010-12-07 | Unilever Nv | uso do tripeptìdeo map, uso do tripeptìdeo map em combinação com o tripeptìdeo itp e produto alimentìcio |
US20090325888A1 (en) * | 2005-04-28 | 2009-12-31 | Luppo Edens | Peptides having a health benefit and compositions comprising them |
KR20080040683A (ko) | 2005-07-26 | 2008-05-08 | 칼피스가부시키가이샤 | 발효유의 제조 방법 및 발효유 음식품 |
AU2006309040B2 (en) | 2005-10-28 | 2011-10-06 | Nestec S.A. | Methods for the use of branched chain amino acids |
JP5096173B2 (ja) * | 2006-02-09 | 2012-12-12 | カルピス株式会社 | 経口摂取用関節リウマチ抑制剤 |
JP4956164B2 (ja) * | 2006-12-06 | 2012-06-20 | 味の素株式会社 | メラニン輸送及び/又は放出抑制剤 |
BRPI0809319A2 (pt) * | 2007-03-27 | 2014-09-23 | Calpis Co Ltd | Agente para suprimir espessamento de parede de coração, agente profilático para hipertrofia cardíaca, agente profilático para insuficiência cardíaca, e, alimento funcional |
CN101095457B (zh) * | 2007-06-23 | 2010-04-07 | 临夏州华安生物制品有限责任公司 | 酸水解酪蛋白的生产方法 |
CA2719857C (en) * | 2008-03-26 | 2019-08-06 | Glanbia Nutritionals (Ireland) Ltd. | Leucine-rich peptide compositions and methods for isolation |
CN101768209B (zh) * | 2009-01-05 | 2011-08-31 | 北京林业大学 | 具有高体内活性的降血压肽及其制备和纯化方法 |
CN101570568B (zh) * | 2009-06-15 | 2012-05-30 | 东北农业大学 | 一种发酵乳中的ace抑制肽及其制备方法 |
CN102187935B (zh) * | 2010-03-19 | 2012-12-19 | 江南大学 | 一种制备酪蛋白磷酸肽与ace抑制肽的方法 |
CN102399261B (zh) * | 2010-09-07 | 2014-06-25 | 任发政 | 具有血管紧张素转化酶c-端选择性抑制活性的三肽及其应用和组合物 |
US20120115786A1 (en) * | 2010-11-09 | 2012-05-10 | Calpis Co., Ltd. | Agent for reducing risk in onset of disease ascribable to non-dipper circadian rhythm of blood pressure |
US9523109B2 (en) | 2011-06-24 | 2016-12-20 | Calpis Co., Ltd. | Method for enzymatically preparing peptides for use in improvement of brain function |
JP5718741B2 (ja) * | 2011-06-24 | 2015-05-13 | カルピス株式会社 | 脳機能改善用ペプチドの酵素的製造方法 |
BR112014009000A2 (pt) * | 2011-10-14 | 2017-05-02 | Abbott Lab | suplemento proteico líquido esterilizado |
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 |
JP6306197B2 (ja) | 2013-10-04 | 2018-04-04 | イノウェイ・カンパニー・リミテッド | 動物性タンパク加水分解物、その製造方法及びその用途 |
FR3017536B1 (fr) * | 2014-02-18 | 2017-05-26 | Univ La Rochelle | Compositions pour la prevention et/ou le traitement de pathologies liees a l'alpha-glucosidase |
ES2544153B1 (es) * | 2014-02-24 | 2016-06-06 | Ntd Labs, S.L. | Uso de un hidrolizado de caseína como agente antiviral |
JP6251667B2 (ja) | 2014-06-03 | 2017-12-20 | アサヒカルピスウェルネス株式会社 | 錠剤型即放性製剤及びその製造方法 |
CN105693817B (zh) | 2014-11-27 | 2020-06-05 | 西北大学 | 一类三肽化合物及其制备方法与应用 |
JP6005202B2 (ja) * | 2015-03-19 | 2016-10-12 | アサヒグループホールディングス株式会社 | 脳機能改善用ペプチドの酵素的製造方法 |
JP6625366B2 (ja) * | 2015-08-05 | 2019-12-25 | 学校法人北里研究所 | 豚肉の熟成中に生成する生理活性ペプチドを含む血圧降下剤及び食品、並びにペプチドを指標とする豚肉の熟成評価法 |
CN106119325A (zh) * | 2016-06-23 | 2016-11-16 | 哈尔滨商业大学 | 一种具有增加肌肉含量和力量作用的酪蛋白水解物的制备方法 |
CN107375897A (zh) * | 2017-08-15 | 2017-11-24 | 普维食品发展(上海)有限公司 | 一种辅助降血压的组合物及其用途 |
CN107348511B (zh) * | 2017-08-21 | 2018-04-06 | 东方红(通化)生物医药股份有限公司 | 一种具有辅助降血压作用的西洋参/人参提取物的发酵提取方法 |
CN108003231A (zh) * | 2017-11-13 | 2018-05-08 | 江苏大学 | 一种降低小分子肽中游离氨基酸含量的方法 |
CN108588156A (zh) * | 2018-04-24 | 2018-09-28 | 浙江大学 | 一种水牛乳酪蛋白抗氧化活性肽的制备方法 |
CN112041328A (zh) * | 2018-04-26 | 2020-12-04 | 志瑞亚新药工业株式会社 | 二肽和含有该二肽的药物组合物 |
CN110467649A (zh) * | 2019-09-12 | 2019-11-19 | 浙江省农业科学院 | 一种抑制血管紧张素转换酶活性的多肽qeip及其应用 |
CN113321719B (zh) * | 2021-05-20 | 2022-03-18 | 澳优乳业(中国)有限公司 | 一种寡肽及其制备方法与应用 |
CN114656521B (zh) * | 2022-04-01 | 2023-08-18 | 广西大学 | 抑制新型冠状病毒刺突蛋白与ace2结合的化合物及其应用 |
Family Cites Families (21)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS6023087B2 (ja) * | 1982-09-04 | 1985-06-05 | 工業技術院長 | アンジオテンシン転換酵素阻害剤 |
FR2608051B1 (fr) * | 1986-12-15 | 1989-04-07 | Bellon Labor Sa Roger | Procede de fabrication d'un hydrolysat enzymatique de proteines riche en di- et tri-peptides, utilisable notamment en nutrition artificielle et en dietetique |
JPH0630615B2 (ja) * | 1988-07-27 | 1994-04-27 | 江崎グリコ株式会社 | 低分子ペプチド組成物及びその製造方法 |
JPH0262828A (ja) | 1988-08-26 | 1990-03-02 | Ajinomoto Co Inc | 新規ベプチドおよびこれを含有する降圧剤 |
JPH03120225A (ja) | 1989-10-04 | 1991-05-22 | Ajinomoto Co Inc | 新規ペプチドおよびこれを含有する降圧剤 |
EP0457565B1 (de) * | 1990-05-18 | 1997-07-30 | Morinaga Milk Industry Co., Ltd. | Milchproteinhydrolysate und Zusammensetzungen zur Verwendung als Haar- und Hautbehandlungsmittel |
JP3010795B2 (ja) * | 1991-07-04 | 2000-02-21 | 不二製油株式会社 | ペプチドの苦味除去方法 |
JP3378279B2 (ja) | 1991-11-07 | 2003-02-17 | 株式会社日清製粉グループ本社 | ペプチドおよびその製造方法 |
JPH05252979A (ja) * | 1992-02-28 | 1993-10-05 | Nippon Steel Corp | 低分子ペプチドの製造方法 |
JP2782142B2 (ja) | 1992-07-23 | 1998-07-30 | カルピス株式会社 | アンジオテンシン変換酵素阻害剤及びその製造法 |
DK46793D0 (da) * | 1993-04-26 | 1993-04-26 | Novo Nordisk As | Enzym |
AU7381098A (en) * | 1997-05-16 | 1998-12-08 | Novo Nordisk Biotech, Inc. | Polypeptides having prolyl pipeptidyl aminopeptidase activity and nucleic acids encoding same |
JP2873327B2 (ja) * | 1998-01-23 | 1999-03-24 | 工業技術院長 | アンジオテンシン変換酵素阻害剤 |
JP4633876B2 (ja) * | 1999-11-11 | 2011-02-16 | カルピス株式会社 | トリペプチドの製造方法 |
CN1140190C (zh) * | 1999-11-29 | 2004-03-03 | 协和发酵工业株式会社 | 食盐味增强方法、食盐味增强剂、食盐味调料以及食盐味增强食品 |
JP4490547B2 (ja) * | 2000-03-30 | 2010-06-30 | 株式会社 レオロジー機能食品研究所 | 新規ペプチド、その製造法及び用途 |
JP4436961B2 (ja) * | 2000-07-25 | 2010-03-24 | 森永乳業株式会社 | 蛋白質加水分解物の製造方法 |
JP2003024012A (ja) * | 2001-07-18 | 2003-01-28 | National Institute Of Advanced Industrial & Technology | アンジオテンシンi変換酵素阻害剤及び血圧降下性機能食品 |
DK1457498T3 (da) * | 2001-11-21 | 2007-06-04 | Morinaga Milk Industry Co Ltd | Hidtil ukendt peptid med angiotensinkonvertaseinhibitorisk virkning |
JP2003210138A (ja) | 2002-01-24 | 2003-07-29 | Yoko Takenaka | 機能性食品、その製造方法及び医薬 |
US7900438B2 (en) * | 2006-07-28 | 2011-03-08 | General Electric Company | Heat transfer system and method for turbine engine using heat pipes |
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2004
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- 2004-07-30 DK DK04771089.2T patent/DK1661909T3/da active
- 2004-07-30 NZ NZ545341A patent/NZ545341A/en not_active IP Right Cessation
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- 2004-07-30 CN CNB2004800223447A patent/CN100439393C/zh not_active Expired - Fee Related
- 2004-07-30 TW TW093123003A patent/TWI341866B/zh active
- 2004-07-30 AT AT04771089T patent/ATE442855T1/de not_active IP Right Cessation
- 2004-07-30 UA UAA200602131A patent/UA89616C2/ru unknown
- 2004-07-30 AU AU2004261855A patent/AU2004261855B2/en not_active Ceased
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- 2004-07-30 PT PT04771089T patent/PT1661909E/pt unknown
- 2004-07-30 NZ NZ545340A patent/NZ545340A/en unknown
- 2004-07-30 CN CNB2004800222139A patent/CN100398661C/zh active Active
- 2004-07-30 US US10/566,057 patent/US20070122451A1/en not_active Abandoned
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2006
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2007
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2010
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2011
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