JP2005220091A - Angiotensin-converting enzyme-inhibiting peptide - Google Patents
Angiotensin-converting enzyme-inhibiting peptide Download PDFInfo
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- JP2005220091A JP2005220091A JP2004030816A JP2004030816A JP2005220091A JP 2005220091 A JP2005220091 A JP 2005220091A JP 2004030816 A JP2004030816 A JP 2004030816A JP 2004030816 A JP2004030816 A JP 2004030816A JP 2005220091 A JP2005220091 A JP 2005220091A
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- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02P—CLIMATE CHANGE MITIGATION TECHNOLOGIES IN THE PRODUCTION OR PROCESSING OF GOODS
- Y02P20/00—Technologies relating to chemical industry
- Y02P20/50—Improvements relating to the production of bulk chemicals
- Y02P20/52—Improvements relating to the production of bulk chemicals using catalysts, e.g. selective catalysts
Abstract
Description
本発明は、アンギオテンシン変換酵素阻害剤等として有用なペプチド、さらに該ペプチドを含む高血圧予防用食品および降圧剤に関する。 The present invention relates to a peptide useful as an angiotensin converting enzyme inhibitor and the like, a food for preventing hypertension and a hypotensive agent containing the peptide.
アンギオテンシン変換酵素（ＡＣＥ）は主にヒトの血管の内皮細胞、肺、腎臓及び脳に存在する。この酵素は、血管の収縮を引き起こし、血圧を上昇させるために、Ｃ末端から２つのアミノ酸（Ｈｉｓ−Ｌｅｕ）を切断することにより、不活性なアンギオテンシンＩを活性なアンギオテンシンIIに変換し得る。したがって、ＡＣＥは血圧を上昇させることができる。 Angiotensin converting enzyme (ACE) is mainly present in human vascular endothelial cells, lung, kidney and brain. This enzyme can convert inactive angiotensin I into active angiotensin II by cleaving two amino acids (His-Leu) from the C-terminus to cause vasoconstriction and increase blood pressure. Thus, ACE can increase blood pressure.
アンギオテンシン変換酵素阻害剤（ＡＣＥＩ）のＡＣＥへの結合はアンギオテンシンIIの生成を減少し得る。ＡＣＥＩを食品に加えると、高血圧症状を減少させるのにプラスの効果を引き起こすであろう。現在のところ、多くのペプチドがＡＣＥの阻害についての効果を有することが知られている（特許文献１〜６）。それらは異なったアミノ酸配列と長さを有する。
従って、本発明は、食肉（特に豚肉）由来の機能性成分として、高血圧予防効果が期待されるアンギオテンシン変換酵素（ＡＣＥ）阻害ペプチドを提供することを主な課題とする。 Therefore, the main object of the present invention is to provide an angiotensin converting enzyme (ACE) inhibitory peptide that is expected to have an effect of preventing hypertension as a functional component derived from meat (particularly pork).
本発明は、食肉由来の新規なアンギオテンシン変換酵素（ＡＣＥ）阻害ペプチドを見出した。 The present invention has found a novel angiotensin converting enzyme (ACE) inhibitory peptide derived from meat.
本発明は、以下の項１〜６の活性ペプチド、アンギオテンシン変換酵素阻害剤ならびにその製造法、高血圧予防用食品および降圧剤に関する。
項１． 下記式で示されるポリペプチド：
Ｌｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ。
項２． 以下の４種のペプチドのいずれかからなるアンギオテンシン変換酵素阻害剤：
Ｌｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；及び
Ｇｌｎ−Ｔｙｒ。
項３． 食肉由来のミオシンＢ素材をペプシンで加水分解することを特徴とするアンギオテンシン変換酵素阻害剤の製造法。
項４． アンギオテンシン変換酵素阻害剤がＬｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒである項３の製造法。
項５． Ｌｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；及び
Ｇｌｎ−Ｔｙｒ
からなる群より選択される少なくとも１種のペプチドを含む高血圧予防用食品。
項６． Ｌｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；及び
Ｇｌｎ−Ｔｙｒ
からなる群より選択される少なくとも１種のペプチドを含む降圧剤。
The present invention relates to the following active peptide, angiotensin converting enzyme inhibitor and method for producing the same, food for hypertension and antihypertensive agent.
Item 1. A polypeptide represented by the following formula:
Lys-Arg-Val-Ile-Gln-Tyr.
Item 2. Angiotensin converting enzyme inhibitor comprising any of the following four peptides:
Lys-Arg-Val-Ile-Gln-Tyr;
Val-Ile-Gln-Tyr;
Ile-Gln-Tyr; and Gln-Tyr.
Item 3. A method for producing an angiotensin converting enzyme inhibitor comprising hydrolyzing meat-derived myosin B material with pepsin.
Item 4. Item 4. The method according to Item 3, wherein the angiotensin converting enzyme inhibitor is Lys-Arg-Val-Ile-Gln-Tyr.
Item 5. Lys-Arg-Val-Ile-Gln-Tyr;
Val-Ile-Gln-Tyr;
Ile-Gln-Tyr; and Gln-Tyr
A food for preventing hypertension, comprising at least one peptide selected from the group consisting of:
Item 6. Lys-Arg-Val-Ile-Gln-Tyr;
Val-Ile-Gln-Tyr;
Ile-Gln-Tyr; and Gln-Tyr
An antihypertensive agent comprising at least one peptide selected from the group consisting of:
本発明のペプチドは、食肉由来の安全なタンパク質（ミオシンＢ）をペプシンで分解したペプチドなので、長期摂取しても安定性の高いものである。 Since the peptide of the present invention is a peptide obtained by degrading a safe protein derived from meat (myosin B) with pepsin, it is highly stable even when ingested for a long time.
本発明のペプチドＬｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ（KRVIQY）は、食肉由来のタンパク質から抽出したミオシンＢをペプシンで加水分解することによって得られる。また、ペプチドKRVIQYの部分構造ペプチドは、Fmoc固相合成などの公知の方法に従い合成できる。 The peptide Lys-Arg-Val-Ile-Gln-Tyr (KRVIQY) of the present invention can be obtained by hydrolyzing myosin B extracted from meat-derived protein with pepsin. Moreover, the partial structure peptide of peptide KRVIQY can be synthesized according to a known method such as Fmoc solid phase synthesis.
以下、食肉として豚肉を例にとり説明するが、豚肉以外の食肉（牛肉、馬肉、魚肉、鶏肉など）についても同様に実施することができる。 Hereinafter, pork will be described as an example of meat, but meat (beef, horse meat, fish, chicken, etc.) other than pork can be similarly applied.
本発明のペプチドKRVIQYは、ミオシンＢのペプシン加水分解生成物を、イオン交換クロマトグラフィー、ゲルろ過クロマトグラフィー、逆相HPLCなどを組み合わせて精製することにより得られる。 The peptide KRVIQY of the present invention can be obtained by purifying the myosin B pepsin hydrolysis product by combining ion exchange chromatography, gel filtration chromatography, reverse phase HPLC and the like.
本発明のペプチドとしては、ブタミオシンＢのペプシン分解物またはその分画もしくは濃縮分画が使用され得る。 As the peptide of the present invention, a pepsin degradation product of porcine myosin B or a fraction or concentrated fraction thereof can be used.
本発明の製造法において、豚肉由来のタンパク質から抽出することができるミオシンＢをペプシンで加水分解すると、ACE阻害活性を有するペプチドＬｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ（KRVIQY）が生成することが見出された。このペプチドは、骨格筋ミオシン重鎖の190-195位由来と認められた。 In the production method of the present invention, when myosin B that can be extracted from pork-derived protein is hydrolyzed with pepsin, a peptide Lys-Arg-Val-Ile-Gln-Tyr (KRVIQY) having ACE inhibitory activity is produced. Was found. This peptide was found to be derived from positions 190-195 of the skeletal muscle myosin heavy chain.
本発明の製造法において、ミオシンＢは、肉の３倍量の高濃度塩溶液（０．６Ｍ ＫＣｌなど）で豚肉由来のタンパク質から０〜２０℃で抽出され得る。また、ミオシンＢの抽出時間は、５分〜１２０時間であり得る。ミオシンＢは、ミオシン、アクチン、トロポミオシン、トロポニンの複合体であり得る。 In the production method of the present invention, myosin B can be extracted at 0-20 ° C. from pork-derived protein with a high-concentration salt solution (0.6 M KCl, etc.) three times the amount of meat. In addition, the extraction time of myosin B can be 5 minutes to 120 hours. Myosin B can be a complex of myosin, actin, tropomyosin, troponin.
本発明の製造法において、本発明のペプチドは、ペプシンを用いて、ミオシンＢをｐＨ１〜４で２５〜４５℃で５分〜７２時間加水分解することによって生成され得る。使用されるペプシンとしては、ブタペプシン、ウシペプシン、ヒトペプシンなどが挙げられ得る。 In the production method of the present invention, the peptide of the present invention can be produced by hydrolyzing myosin B at pH 1 to 4 at 25 to 45 ° C. for 5 minutes to 72 hours using pepsin. The pepsin used may include porcine pepsin, bovine pepsin, human pepsin and the like.
本発明の製造法において、ペプシンによるミオシンＢのタンパク分解混合物を使用可能とするために、脱塩処理が行われ得る。脱塩処理は、ゲルろ過クロマトグラフィーまたは逆相クロマトグラフィーなどによって行われ得る。 In the production method of the present invention, desalting treatment can be performed in order to make it possible to use a proteolytic mixture of myosin B with pepsin. The desalting treatment can be performed by gel filtration chromatography or reverse phase chromatography.
本発明のペプチドは、高血圧予防用食品または降圧剤中に含まれ得る。 The peptide of the present invention can be contained in a food for preventing hypertension or an antihypertensive agent.
本発明のペプチドを含む高血圧予防用食品または降圧剤は、高血圧を予防するために投与され得る。 The food for preventing hypertension or the antihypertensive agent containing the peptide of the present invention can be administered to prevent hypertension.
本発明のペプチドを含む高血圧予防用食品または降圧剤は、投与される場合、血圧を穏やかに低下させ得る。 When administered, the antihypertensive food or antihypertensive agent containing the peptide of the present invention can gently lower blood pressure.
本発明のペプチドを含む高血圧予防用食品または降圧剤は、投与される場合、血圧の低下を長期間、好ましくは４８時間、維持し得る。 When administered, the antihypertensive food or antihypertensive agent comprising the peptide of the present invention can maintain a decrease in blood pressure for a long period, preferably 48 hours.
本発明のペプチドを含む高血圧予防用食品または降圧剤は、投与される場合、乾咳などの副作用が実質的にないことが期待される。 When administered, the antihypertensive food or antihypertensive agent containing the peptide of the present invention is expected to have substantially no side effects such as dry cough.
本発明の降圧剤の形態としては、経口製剤、例えば錠剤、カプセル剤、顆粒剤、細粒剤、散剤、丸剤等が挙げられるが、これらに限定されない。これらの製剤には、有効成分（ブタミオシンＢのペプシン分解物またはその分画もしくは濃縮分画）の他に医薬の分野で通常使用される賦形剤、希釈剤、担体などが適宜含まれ得る。 Examples of the antihypertensive agent of the present invention include, but are not limited to, oral preparations such as tablets, capsules, granules, fine granules, powders, pills and the like. These preparations may appropriately contain excipients, diluents, carriers and the like that are commonly used in the pharmaceutical field in addition to the active ingredient (pepsin degradation product of porcine myosin B or a fraction or concentrated fraction thereof).
本発明の降圧剤の用法用量は、患者の症状、年齢、体重などによって異なるが、例えばポリペプチドとして成人１日当たり乾燥重量で０．１ｍｇ〜１０ｇ、好ましくは１ｍｇ〜１００ｍｇを１回もしくは２回以上に分けて投与する。 The dosage of the antihypertensive agent of the present invention varies depending on the symptoms, age, body weight, etc. of the patient, but for example, 0.1 mg to 10 g, preferably 1 mg to 100 mg, in dry weight per day for an adult as a polypeptide, once or twice or more Divide into two doses.
本発明の高血圧予防用食品は、固形または半固形状であってもよいし、液状（飲料）であってもよい。該食品には、上記有効成分（ブタミオシンＢのペプシン分解物またはその分画もしくは濃縮分画）が配合される。高血圧予防用食品に対する本発明のペプチドの配合割合は、高血圧予防用食品の形態、素材によって異なり、通常０．０００１〜５０重量％程度を含有する。本発明のペプチドの１日の摂取量としてトータルで、成人１日当たり、乾燥重量で０．１ｍｇ〜１０ｇ、好ましくは１ｍｇ〜１００ｍｇである。 The food for preventing hypertension of the present invention may be solid or semi-solid, or liquid (beverage). The active ingredient (pepsin degradation product of porcine myosin B or a fraction or concentrated fraction thereof) is blended in the food. The blending ratio of the peptide of the present invention to the food for preventing hypertension varies depending on the form and material of the food for preventing hypertension, and usually contains about 0.0001 to 50% by weight. The total daily intake of the peptide of the present invention is 0.1 mg to 10 g, preferably 1 mg to 100 mg, in dry weight per adult day.
本発明の高血圧予防用食品は、本発明のペプチドのみから構成されていてもよいが、通常は他の食品とともに既存の食品の形態で製造される。具体的な食品としては、ハム、ウインナー、惣菜、粉末飲料、キャンディー、老人用食品等が挙げられる。 Although the food for preventing hypertension of the present invention may be composed of only the peptide of the present invention, it is usually produced in the form of an existing food together with other foods. Specific foods include hams, wieners, side dishes, powdered drinks, candy, foods for the elderly, and the like.
本発明の高血圧予防用食品は、正常高値（収縮期血圧１３０〜１３９ｍｍＨｇ、拡張期血圧８５〜８９ｍｍＨｇ）、軽症高血圧（収縮期血圧１４０〜１５９ｍｍＨｇ、拡張期血圧９０〜９９ｍｍＨｇ）のヒトに投与したときに、有効に血圧を低下させることができる。 When the food for preventing hypertension of the present invention is administered to a human having a normal high level (systolic blood pressure 130 to 139 mmHg, diastolic blood pressure 85 to 89 mmHg) or mild hypertension (systolic blood pressure 140 to 159 mmHg, diastolic blood pressure 90 to 99 mmHg). In addition, blood pressure can be effectively reduced.
本発明により、豚肉タンパク質由来の新規なアンギオテンシン変換酵素（ＡＣＥ）阻害ペプチドを提供することができる。 According to the present invention, a novel angiotensin converting enzyme (ACE) inhibitory peptide derived from pork protein can be provided.
KRVIQYは有原らが報告したミオシン由来ペプチド（Meat Science, 57: 319-324, 2001）よりも強いACE阻害活性を示し、これまでに報告されている動物筋肉食品由来のACE阻害ペプチドの中で最も強い活性を示した。 KRVIQY has a stronger ACE inhibitory activity than the myosin-derived peptide reported by Arihara et al. (Meat Science, 57: 319-324, 2001). Among ACE inhibitory peptides derived from animal muscle foods, It showed the strongest activity.
一般的にジペプチドもしくはトリペプチドなどの小さなペプチドのみが、腸管から吸収される(Adibi et al. Clinical research, 17: 376, 1969) とされているが、一方では、Pappenheimer et al. (Proceedings of the National Academy of Sciences of the United States of America, 91: 1942-1945, 1994) はオクタペプチドが細胞間隙経路で腸管から吸収されることを示している。Shimizu et al. (Peptides, 18: 681-687, 1997) は疎水性ノナペプチドが経細胞輸送により上皮細胞を通過することを明らかにしている。さらにSatake et al. (Bioscience, Biotechnology, and Biochemistry, 66: 378-384, 2002)は消化酵素に対する耐性が高く腸管内に長時間滞留するペプチドの場合は、なんらかのトランスポート機能を利用して吸収される可能性を示唆している。これらのことから、本発明による新規ACE阻害ペプチドKRVIQYも腸管から吸収される可能性があると考えられる。すなわち、KRVIQYが腸管から吸収されて、ACE阻害剤として有効に機能する可能性が期待される。 In general, only small peptides such as dipeptides or tripeptides are absorbed from the intestinal tract (Adibi et al. Clinical research, 17: 376, 1969), while Pappenheimer et al. (Proceedings of the The National Academy of Sciences of the United States of America, 91: 1942-1945, 1994) shows that octapeptides are absorbed from the intestinal tract via the intercellular pathway. Shimizu et al. (Peptides, 18: 681-687, 1997) have shown that hydrophobic nonapeptides pass through epithelial cells by transcellular transport. In addition, Satake et al. (Bioscience, Biotechnology, and Biochemistry, 66: 378-384, 2002) is a peptide that is highly resistant to digestive enzymes and stays in the intestine for a long time. This suggests the possibility. From these facts, it is considered that the novel ACE inhibitory peptide KRVIQY according to the present invention may also be absorbed from the intestinal tract. That is, it is expected that KRVIQY is absorbed from the intestinal tract and functions effectively as an ACE inhibitor.
下記実施例において、より具体的に本発明を説明する。 The present invention will be described more specifically in the following examples.
以下実施例において測定されたACEに対する５０％阻害活性（IC50）は、ウサギ肺由来のACEに対するもので、Cushman -Cheungの方法（Biochemical Pharmacology, 20: 1637-1648, 1971）で測定した。 The 50% inhibitory activity (IC 50 ) for ACE measured in the following examples was for rabbit lung-derived ACE and was measured by the Cushman-Cheung method (Biochemical Pharmacology, 20: 1637-1648, 1971).
実施例１
国産の豚ロース肉からWeber-Edsall溶液（０．６Ｍ ＫＣｌ、０．０４Ｍ 炭酸水素ナトリウム、０．０１Ｍ 炭酸ナトリウム）で抽出したミオシンＢをブタペプシンで、ｐＨ２で３７℃で６時間加水分解した。このミオシンＢのペプシン加水分解物のウサギ肺由来のACEに対するIC50は19.3 μg/mlであった。未加水分解ミオシンＢにはACE阻害活性が認められなかったことから、活性の発現はペプシン分解で生じたペプチドに由来することが分かった。そこで、この加水分解物からのACE阻害ペプチドの単離を検討した。
Example 1
Myosin B extracted from domestic pork loin with a Weber-Edsall solution (0.6 M KCl, 0.04 M sodium bicarbonate, 0.01 M sodium carbonate) was hydrolyzed with porcine pepsin at pH 2 for 6 hours. The IC 50 of this myosin B pepsin hydrolyzate for rabbit lung-derived ACE was 19.3 μg / ml. Since ACE inhibitory activity was not observed in unhydrolyzed myosin B, it was found that the expression of the activity was derived from a peptide produced by pepsin degradation. Therefore, isolation of the ACE inhibitory peptide from this hydrolyzate was examined.
該加水分解物をまず、Superdex30 prep grade（アマシャムバイオサイエンス社製）を用いるゲル濾過クロマトグラフィーに供した。すなわち、バッファー（20 mM 酢酸ナトリウム、150 mM 塩化ナトリウム、pH６）で該加水分解物をアプライし、同バッファーで溶出した（図１）。流速は0.45 ml/分とし、６分毎(2.7 ml)に分画した。得られた画分をそれぞれ濃縮して、その活性を測定した。ここで得られた最も活性の高い画分（画分No.56）をInertsil ODS-2（ジーエルサイエンス社製）を用いる逆相HPLCに供し、0.1%トリフルオロ酢酸(TFA)を含むアセトニトリルの0-50%のグラジェント溶出(流速0.5 ml/分)で分画した。これ以降のHPLCでは225 nmの吸光度をモニターした。活性画分はさらに、同じカラムで0.1%TFAを含むアセトニトリルの10-24%のグラジェント溶出(流速0.5 ml/分)で分画した。ここで得られた活性画分をCOSMOSIL 5PE-MS（ナカライテスク社製） を用いる逆相HPLCに供して、精製を数回行った。溶出は、まず0.1%TFAを含むアセトニトリル濃度13％のイソクラティック溶出（流速0.1 ml/min）で行った（図２）。ここで得られた活性の高い画分をさらに、アセトニトリル濃度10％（流速0.1 ml/min）、8％(流速0.3 ml/min)、7％(流速0.5 ml/min)、6％(流速0.5 ml/min)と段階的に低い濃度でイソクラティック溶出を行い、単一と思われる画分を得た。 The hydrolyzate was first subjected to gel filtration chromatography using Superdex30 prep grade (Amersham Biosciences). That is, the hydrolyzate was applied with a buffer (20 mM sodium acetate, 150 mM sodium chloride, pH 6) and eluted with the same buffer (FIG. 1). The flow rate was 0.45 ml / min, and fractionation was performed every 6 minutes (2.7 ml). Each of the obtained fractions was concentrated and its activity was measured. The most active fraction obtained here (fraction No. 56) was subjected to reverse phase HPLC using Inertsil ODS-2 (manufactured by GL Sciences), and 0% acetonitrile containing 0.1% trifluoroacetic acid (TFA) was obtained. Fractionation was performed with -50% gradient elution (flow rate 0.5 ml / min). In the subsequent HPLC, the absorbance at 225 nm was monitored. The active fraction was further fractionated by 10-24% gradient elution of acetonitrile containing 0.1% TFA (flow rate 0.5 ml / min) on the same column. The active fraction obtained here was subjected to reverse phase HPLC using COSMOSIL 5PE-MS (manufactured by Nacalai Tesque) and purified several times. Elution was first performed by isocratic elution (flow rate: 0.1 ml / min) containing 0.1% TFA and having an acetonitrile concentration of 13% (FIG. 2). The highly active fractions obtained here were further divided into 10% acetonitrile concentration (flow rate 0.1 ml / min), 8% (flow rate 0.3 ml / min), 7% (flow rate 0.5 ml / min), 6% (flow rate 0.5). Isocratic elution was carried out at a stepwise lower concentration (ml / min) to obtain a fraction that appeared to be single.
精製で得られた画分のアミノ酸配列を、G1000A型プロテインシーケンサー（Hewlett Packard社製）でシーケンス解析した。得られたペプチドは骨格筋ミオシン重鎖の190位から195位にあたるKRVIQYであると認められた。これはこれまでに報告のない、新規なACE阻害ペプチドであった。KRVIQYのACE阻害活性は6.1 μMであり、これまでに報告されている豚肉タンパク質由来ペプチドの中で最も強いACE阻害活性を示した。 The amino acid sequences of the fractions obtained by purification were sequence-analyzed with a G1000A type protein sequencer (manufactured by Hewlett Packard). The obtained peptide was recognized as KRVIQY corresponding to positions 190 to 195 of the skeletal muscle myosin heavy chain. This was a novel ACE-inhibiting peptide that has never been reported. The ACE inhibitory activity of KRVIQY was 6.1 μM, indicating the strongest ACE inhibitory activity among pork protein-derived peptides reported so far.
Claims (6)
Ｌｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ。 A polypeptide represented by the following formula:
Lys-Arg-Val-Ile-Gln-Tyr.
Ｌｙｓ−Ａｒｇ−Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；及び
Ｇｌｎ−Ｔｙｒ。 Angiotensin converting enzyme inhibitor comprising any of the following four peptides:
Lys-Arg-Val-Ile-Gln-Tyr;
Val-Ile-Gln-Tyr;
Ile-Gln-Tyr; and Gln-Tyr.
Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；及び
Ｇｌｎ−Ｔｙｒ
からなる群より選択される少なくとも１種のペプチドを含む高血圧予防用食品。 Lys-Arg-Val-Ile-Gln-Tyr;
Val-Ile-Gln-Tyr;
Ile-Gln-Tyr; and Gln-Tyr
A food for preventing hypertension, comprising at least one peptide selected from the group consisting of:
Ｖａｌ−Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；
Ｉｌｅ−Ｇｌｎ−Ｔｙｒ；及び
Ｇｌｎ−Ｔｙｒ
からなる群より選択される少なくとも１種のペプチドを含む降圧剤。 Lys-Arg-Val-Ile-Gln-Tyr;
Val-Ile-Gln-Tyr;
Ile-Gln-Tyr; and Gln-Tyr
An antihypertensive agent comprising at least one peptide selected from the group consisting of:
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Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
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| JP2016531951A (en) * | 2013-10-04 | 2016-10-13 | イノウェイ・カンパニー・リミテッド | Animal protein hydrolyzate, production method thereof and use thereof |
| US10676505B2 (en) | 2016-06-16 | 2020-06-09 | Sunstar Inc. | Tripeptides having angiotensin converting enzyme inhibitory activity and uses thereof |
| CN114591397A (en) * | 2021-12-08 | 2022-06-07 | 河北东康乳业有限公司 | Polypeptide with function of reducing blood pressure and preparation method thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| JP2016531951A (en) * | 2013-10-04 | 2016-10-13 | イノウェイ・カンパニー・リミテッド | Animal protein hydrolyzate, production method thereof and use thereof |
| US10676505B2 (en) | 2016-06-16 | 2020-06-09 | Sunstar Inc. | Tripeptides having angiotensin converting enzyme inhibitory activity and uses thereof |
| CN114591397A (en) * | 2021-12-08 | 2022-06-07 | 河北东康乳业有限公司 | Polypeptide with function of reducing blood pressure and preparation method thereof |
| CN114591397B (en) * | 2021-12-08 | 2023-06-20 | 新东康营养科技有限公司 | Polypeptide with blood pressure reducing function and preparation method thereof |
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