WO2021059840A1 - Inhibiteur d'enzyme de conversion de l'angiotensine - Google Patents

Inhibiteur d'enzyme de conversion de l'angiotensine Download PDF

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Publication number
WO2021059840A1
WO2021059840A1 PCT/JP2020/032271 JP2020032271W WO2021059840A1 WO 2021059840 A1 WO2021059840 A1 WO 2021059840A1 JP 2020032271 W JP2020032271 W JP 2020032271W WO 2021059840 A1 WO2021059840 A1 WO 2021059840A1
Authority
WO
WIPO (PCT)
Prior art keywords
acid
tea
peptide composition
enzyme
phe
Prior art date
Application number
PCT/JP2020/032271
Other languages
English (en)
Japanese (ja)
Inventor
均 山際
一雄 清水
寛央 福原
武嗣 中村
Original Assignee
太陽化学株式会社
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by 太陽化学株式会社 filed Critical 太陽化学株式会社
Priority to JP2021510993A priority Critical patent/JPWO2021059840A1/ja
Publication of WO2021059840A1 publication Critical patent/WO2021059840A1/fr

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Classifications

    • AHUMAN NECESSITIES
    • A23FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23LFOODS, 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
    • A23L33/00Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
    • A23L33/10Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
    • A23L33/17Amino acids, peptides or proteins
    • A23L33/18Peptides; Protein hydrolysates
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K36/00Medicinal preparations of undetermined constitution containing material from algae, lichens, fungi or plants, or derivatives thereof, e.g. traditional herbal medicines
    • A61K36/18Magnoliophyta (angiosperms)
    • A61K36/185Magnoliopsida (dicotyledons)
    • A61K36/82Theaceae (Tea family), e.g. camellia
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00Medicinal preparations containing peptides
    • A61K38/04Peptides having up to 20 amino acids in a fully defined sequence; Derivatives thereof
    • A61K38/05Dipeptides
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61PSPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P43/00Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61PSPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P9/00Drugs for disorders of the cardiovascular system
    • A61P9/12Antihypertensives

Definitions

  • the sweeteners are not particularly limited, and examples thereof include sugars, sugar alcohols, and high-sweetness sweeteners.
  • saccharides include glucose, sucrose, water candy, isomerized sugar, isomalto-oligosaccharide, fructo-oligosaccharide, milk fruit oligosaccharide, xylooligosaccharide, galactooligosaccharide, cellooligosaccharide, fucose (6-deoxy-galactose, methylpentose), dihydroxy.
  • the raw material of the dipeptide mixture of the present invention is not particularly limited as long as it is a peptide or protein having the amino acid sequence of the dipeptide of the present invention, and tea leaves, mulberry leaves, guaba leaves and the like can be used, but the protein content. From the viewpoint of production amount, it is preferable to use tea leaves or tea leaf extraction residue as a raw material.
  • the dipeptide When the dipeptide is obtained as a mixture, it can be prepared as follows, for example, using tea leaves or tea leaf extraction residue as a raw material.
  • the dipeptide is produced by (a) treating the tea leaf or tea leaf extraction residue with hot water at pH 3.0 to 7.0 and 70 ° C. to 95 ° C. for 30 minutes to 12 hours to treat the tea leaf or tea leaf extraction residue hot water.
  • 1 unit in proteolytic power means the amount of enzyme that causes an increase in non-proteinaceous folin test solution colorating substance corresponding to 1 ⁇ g of tyrosine per minute in a reaction at 40 ° C. for 5 minutes using casein as a substrate. ..
  • Formulation Example 2 Instant tea prescription According to the following instant tea prescription, 0.5 mg of any of the dipeptides described in the above ⁇ Synthesis of dipeptides> or the one described in "1. Method for producing a tea peptide composition" is used. It was added so as to be 0 g. This product could be suitably used as a beverage. Camellia extract (manufactured by Taiyo Kagaku Co., Ltd.) was used as the tea extract powder.
  • Instant tea prescription (1) One of the 1.3 dipeptides 0.5 mg 2. Tea extract powder 60.0g 3. 3. Cyclodextrin 15.0g 4. Thaumatin 0.0075g 5. Vitamin C 1.0g 6. Dextrin balance total 100g Instant tea prescription (2) 1. 1. Tea peptide composition 2.0g 2. Tea extract powder 60.0g 3. 3. Cyclodextrin 15.0g 4. Thaumatin 0.0075g 5. Vitamin C 1.0g 6. Dextrin balance total 100g

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Medicinal Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Veterinary Medicine (AREA)
  • Public Health (AREA)
  • Animal Behavior & Ethology (AREA)
  • Natural Medicines & Medicinal Plants (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Organic Chemistry (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Mycology (AREA)
  • General Chemical & Material Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Epidemiology (AREA)
  • Immunology (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Molecular Biology (AREA)
  • Heart & Thoracic Surgery (AREA)
  • Nutrition Science (AREA)
  • Food Science & Technology (AREA)
  • Polymers & Plastics (AREA)
  • Cardiology (AREA)
  • Alternative & Traditional Medicine (AREA)
  • Biotechnology (AREA)
  • Botany (AREA)
  • Medical Informatics (AREA)
  • Microbiology (AREA)
  • Peptides Or Proteins (AREA)
  • Coloring Foods And Improving Nutritive Qualities (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
  • Medicines Containing Plant Substances (AREA)

Abstract

La présente invention a pour but de fournir un dipeptide ayant une activité inhibitrice vis-à-vis d'une enzyme de conversion de l'angiotensine ; entre autres. Selon l'invention, ce but est atteint grâce à un inhibiteur d'enzyme de conversion de l'angiotensine (ACE) comprenant au moins un dipeptide choisi dans le groupe constitué par trois types de dipeptides, à savoir Thr-Arg, Phe-Asp et Phe-Ala. L'inhibiteur d'ACE peut être fourni sous la forme d'un aliment ou d'une boisson ayant un effet hypotensif ou d'un agent hypotenseur.
PCT/JP2020/032271 2019-09-27 2020-08-27 Inhibiteur d'enzyme de conversion de l'angiotensine WO2021059840A1 (fr)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP2021510993A JPWO2021059840A1 (ja) 2019-09-27 2020-08-27 アンジオテンシン変換酵素阻害剤

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
JP2019176532 2019-09-27
JP2019-176532 2019-09-27

Publications (1)

Publication Number Publication Date
WO2021059840A1 true WO2021059840A1 (fr) 2021-04-01

Family

ID=75166077

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/JP2020/032271 WO2021059840A1 (fr) 2019-09-27 2020-08-27 Inhibiteur d'enzyme de conversion de l'angiotensine

Country Status (2)

Country Link
JP (1) JPWO2021059840A1 (fr)
WO (1) WO2021059840A1 (fr)

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2001261698A (ja) * 2000-03-22 2001-09-26 Natl Inst Of Advanced Industrial Science & Technology Meti アンジオテンシンi変換酵素阻害剤およびその製造法
JP2005154326A (ja) * 2003-11-25 2005-06-16 Nichiro Corp アンジオテンシンi変換酵素阻害ペプチド化合物又はそれを含有するペプチド組成物とそれらの製造方法
JP2007217358A (ja) * 2006-02-17 2007-08-30 Nippon Meat Packers Inc 抗酸化性ペプチド
JP2015100276A (ja) * 2013-11-21 2015-06-04 三井農林株式会社 茶葉由来のタンパク質分解物の製造方法

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB201018125D0 (en) * 2010-10-26 2010-12-08 Marealis As Peptide
EP3219324B1 (fr) * 2014-08-11 2020-02-26 Withyou Biotechnology Co., Ltd. Application d'un di-peptide tenant lieu d'inhibiteur de l'enzyme eca
US10676505B2 (en) * 2016-06-16 2020-06-09 Sunstar Inc. Tripeptides having angiotensin converting enzyme inhibitory activity and uses thereof

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2001261698A (ja) * 2000-03-22 2001-09-26 Natl Inst Of Advanced Industrial Science & Technology Meti アンジオテンシンi変換酵素阻害剤およびその製造法
JP2005154326A (ja) * 2003-11-25 2005-06-16 Nichiro Corp アンジオテンシンi変換酵素阻害ペプチド化合物又はそれを含有するペプチド組成物とそれらの製造方法
JP2007217358A (ja) * 2006-02-17 2007-08-30 Nippon Meat Packers Inc 抗酸化性ペプチド
JP2015100276A (ja) * 2013-11-21 2015-06-04 三井農林株式会社 茶葉由来のタンパク質分解物の製造方法

Also Published As

Publication number Publication date
JPWO2021059840A1 (ja) 2021-10-07

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