JP2011116761A - Antioxidative peptide derived from royal jelly - Google Patents
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本発明は、抗酸化作用を有するペプチドに関し、詳しくはローヤルゼリーに含まれる蛋白質を加水分解して得られる抗酸化ペプチドに関する。 The present invention relates to a peptide having an antioxidant action, and more particularly to an antioxidant peptide obtained by hydrolyzing a protein contained in royal jelly.
現在ローヤルゼリーは健康食品、医薬品、化粧品など世界中で広く利用されており、血管拡張、血圧降下、抗菌作用など種々の薬理作用および栄養生理的作用が報告されている。ローヤルゼリーは蜜蜂の唾液腺で合成され、頭部にあるマンデブラー腺から分泌されるミルク状の物質で、女王蜂幼虫用の巣房に入れられた幼虫蜂に対して働き蜂が女王蜂を作るために与えるものである。ローヤルゼリーはタンパク質やビタミン、ミネラルをバランスよく含んでおり、これを一生食べ続ける女王蜂は、働き蜂の４０倍の寿命と、１日２０００個の産卵能力を持つ。このローヤルゼリーの有効成分の研究は、10-ヒドロキシ-2-デセン酸を代表とする脂肪酸、アミノ酸、ビタミンなどの低分子化合物を中心になされてきた。 Currently, royal jelly is widely used around the world, such as health foods, pharmaceuticals, and cosmetics, and various pharmacological and nutritional physiological effects such as vasodilation, blood pressure lowering, and antibacterial effects have been reported. Royal jelly is a milky substance that is synthesized in the salivary glands of bees and secreted from the mandible glands on the head, and is given to the larvae bees placed in the nests for the queen bee larvae to make the queen bee. is there. Royal jelly contains protein, vitamins, and minerals in a well-balanced manner, and the queen bee that keeps eating this throughout its life is 40 times the life of a worker bee and has the ability to spawn 2000 eggs a day. Research on the active ingredients of this royal jelly has been focused on low molecular weight compounds such as fatty acids, amino acids, vitamins such as 10-hydroxy-2-decenoic acid.
一方、ローヤルゼリーには通常１０％以上のタンパク質が含まれているが、このタンパク質の分子構造や生理作用に関する研究は遅れている。また、ローヤルゼリー配合の化粧品、ドリンク剤などの製造時には、アルコール抽出が行われ、タンパク質は沈殿物として分離されるが、このタンパク質の有効利用は図られていないのが現状である。 On the other hand, royal jelly usually contains 10% or more protein, but research on the molecular structure and physiological function of this protein has been delayed. In addition, when manufacturing cosmetics, drinks and the like containing royal jelly, alcohol extraction is performed and the protein is separated as a precipitate, but at present, the protein is not effectively used.
ローヤルゼリータンパク質のプロテアーゼ処理物については、カルシウム吸収促進作用（非特許文献１）、血糖値低下作用（非特許文献２）が知られ、抗酸化作用についても報告されているが（非特許文献３）、その効果はビタミンＥよりも弱いものであった。 Regarding the protease-treated products of royal jelly protein, calcium absorption promoting action (Non-patent Document 1) and blood glucose level-lowering action (Non-Patent Document 2) are known, and the antioxidant action has also been reported (Non-Patent Document 3). The effect was weaker than vitamin E.
本発明は、強力な抗酸化作用を有する天然由来の物質を提供することを目的とする。 An object of the present invention is to provide a naturally occurring substance having a strong antioxidant action.
上記課題に鑑み検討を重ねた結果、ローヤルゼリーをトリプシン・キモトリプシンで酵素処理することにより、ビタミンＥと同等程度の抗酸化力を有する強力な抗酸化ペプチドが得られることを見出した。 As a result of repeated studies in view of the above problems, it has been found that a powerful antioxidant peptide having an antioxidant power comparable to that of vitamin E can be obtained by enzymatic treatment of royal jelly with trypsin / chymotrypsin.
即ち、本発明は以下の発明に関する。
１． 以下の(1)〜(3)のいずれかのアミノ酸配列を有する抗酸化ペプチド：
(1) Tyr-Tyr-Ser-Pro-Leu；
(2) Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln；
(3) Ser-Leu-Pro-Ile-Leu-His-Glu-Trp。
２． 上記１．に記載の抗酸化ペプチドを有効成分とする抗酸化剤。
３． 上記１．に記載の抗酸化ペプチドを含む食品。
４． ローヤルゼリー由来の蛋白質をプロテアーゼで加水分解することを特徴とする、以下の(1)〜(3)のいずれかのアミノ酸配列を有する抗酸化ペプチドの製造方法：
(1) Tyr-Tyr-Ser-Pro-Leu；
(2) Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln；
(3) Ser-Leu-Pro-Ile-Leu-His-Glu-Trp。
５． 上記１．に記載の抗酸化ペプチドを含む化粧料。
That is, the present invention relates to the following inventions.
1. Antioxidant peptide having any one of the following amino acid sequences (1) to (3):
(1) Tyr-Tyr-Ser-Pro-Leu;
(2) Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln;
(3) Ser-Leu-Pro-Ile-Leu-His-Glu-Trp.
2. Above 1. An antioxidant comprising the antioxidant peptide described in 1 as an active ingredient.
3. Above 1. A food comprising the antioxidant peptide according to 1.
4). A method for producing an antioxidant peptide having any one of the following amino acid sequences (1) to (3), wherein a protein derived from royal jelly is hydrolyzed with a protease:
(1) Tyr-Tyr-Ser-Pro-Leu;
(2) Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln;
(3) Ser-Leu-Pro-Ile-Leu-His-Glu-Trp.
5. Above 1. A cosmetic comprising the antioxidant peptide according to 1.
本発明によれば、天然物に由来する極めて安全性の高い抗酸化ペプチドを得ることができ、食品、化粧料などに広く応用することができる。 According to the present invention, an extremely safe antioxidant peptide derived from a natural product can be obtained, and can be widely applied to foods, cosmetics and the like.
本発明の抗酸化ペプチドは、以下のアミノ酸配列を有する。
・Tyr-Tyr-Ser-Pro-Leu（以下、「ペプチド１」と略すことがある）
・Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln（以下、「ペプチド２」と略すことがある）
・Ser-Leu-Pro-Ile-Leu-His-Glu-Trp（以下、「ペプチド３」と略すことがある）
ペプチド１〜ペプチド３は新規なペプチドであり、その抗酸化作用が本発明により初めて明らかにされた。
The antioxidant peptide of the present invention has the following amino acid sequence.
・ Tyr-Tyr-Ser-Pro-Leu (hereinafter sometimes abbreviated as “peptide 1”)
Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln (hereinafter sometimes abbreviated as “peptide 2”)
Ser-Leu-Pro-Ile-Leu-His-Glu-Trp (hereinafter sometimes abbreviated as “peptide 3”)
Peptide 1 to Peptide 3 are novel peptides, and their antioxidant activity was revealed for the first time by the present invention.
本発明の抗酸化ペプチドは、遺伝子組換えや化学合成により得ることもでき、また、ローヤルゼリー自体（生ローヤルゼリー、乾燥ローヤルゼリーなど）またはローヤルゼリー由来のタンパク質画分をペプシン、トリプシン、キモトリプシン、豚由来小腸酵素を、作用させて得ることもできる。また、ペプチド１〜ペプチド３を得られる限りにおいて、ローヤルゼリー以外のタンパク質原料をペプシン、トリプシン、キモトリプシン、豚由来小腸酵素などの加水分解酵素で加水分解したものを使用することもできる。 The antioxidant peptide of the present invention can also be obtained by gene recombination or chemical synthesis. Moreover, royal jelly itself (raw royal jelly, dried royal jelly, etc.) or a royal jelly-derived protein fraction is converted into pepsin, trypsin, chymotrypsin, pig-derived small intestine enzyme Can also be obtained by acting. In addition, as long as peptides 1 to 3 can be obtained, a protein raw material other than royal jelly hydrolyzed with a hydrolase such as pepsin, trypsin, chymotrypsin, or porcine-derived small intestine enzyme can also be used.
タンパク質の酵素分解により本発明の抗酸化ペプチドを製造するための酵素としては、ペプシン、トリプシン、キモトリプシン、小腸酵素、などが挙げられ、これらは、微生物、哺乳動物を含む動物、植物、酵母、真菌などの任意の生物由来のペプチド結合を加水分解し得る酵素が例示され、好ましくはペプシン、トリプシン、キモトリプシン、豚由来小腸酵素を作用させる。例えばローヤルゼリー由来のタンパク質を３７℃程度の温度下に各種生物由来のペプシン、トリプシン、キモトリプシン、小腸酵素とともに、１〜４８時間程度処理することにより、本発明のいずれかの抗酸化ペプチドを得ることができる。 Examples of the enzyme for producing the antioxidant peptide of the present invention by enzymatic degradation of protein include pepsin, trypsin, chymotrypsin, small intestine enzyme, etc., and these include microorganisms, animals including mammals, plants, yeasts, fungi Examples include enzymes capable of hydrolyzing peptide bonds derived from any organism such as pepsin, trypsin, chymotrypsin, and porcine small intestine enzymes. For example, by treating a protein derived from royal jelly with pepsin, trypsin, chymotrypsin and small intestine enzymes derived from various organisms at a temperature of about 37 ° C. for about 1 to 48 hours, any of the antioxidant peptides of the present invention can be obtained. it can.
本発明のペプチドは、ローヤルゼリーに由来するタンパク質の酵素分解物から分離・精製して使用してもよく、本発明の抗酸化ペプチドとともに多数の他のペプチドを含む蛋白分解物組成物（必要に応じて塩類、糖類あるいは高分子タンパク質などを除去処理したもの）を抗酸化ペプチドとして食品、化粧品などの各種用途に使用してもよい。 The peptide of the present invention may be used after being separated and purified from the enzymatic degradation product of a protein derived from royal jelly, and a proteolysate composition containing a large number of other peptides together with the antioxidant peptide of the present invention (if necessary) In addition, salts obtained by removing salts, saccharides, polymer proteins, etc.) may be used as antioxidant peptides for various applications such as foods and cosmetics.
例えば、ローヤルゼリーを配合したドリンク剤は、ローヤルゼリーに７０〜９５％ｖ／ｖ程度のアルコール、好ましくはエタノールを添加して沈殿するタンパク質を除去して製造されているが、この含水アルコールに不溶性のローヤルゼリー由来のタンパク質を酵素処理の原料タンパク質として用いることができる。化学合成法としては、ペプチドシンセサイザーにより合成することもでき、固相合成または液相合成により段階的にアミノ酸をペプチド結合を介して伸長して製造することもできる。 For example, a drink containing royal jelly is manufactured by adding about 70 to 95% v / v alcohol, preferably ethanol, to the precipitated protein to remove the precipitated protein. The royal jelly is insoluble in this hydrous alcohol. The derived protein can be used as a raw material protein for enzyme treatment. As a chemical synthesis method, it can also synthesize | combine with a peptide synthesizer and can also manufacture by extending | stretching an amino acid stepwise through a peptide bond by solid phase synthesis or liquid phase synthesis.
本発明の抗酸化ペプチドは、抗酸化作用に基づき、活性酸素に起因する各種疾患の予防ないし治療用食品に好適に配合することができる。本発明の抗酸化ペプチドは、ビタミンEと同等程度の抗酸化力を有し、食品として１日に１μｇ〜１０００ｍｇ程度摂取することにより、活性酸素に起因する各種疾患の予防ないし治療作用を有し得る。食品としては、飲料、ドリンク剤などの液状食品、ゼリー状食品（栄養補助食品、燕下困難者用の食品を含む）中に配合してもよいし、サプリメント、機能性食品などとしてタブレット、顆粒などの固形食品形態で摂取してもよい。また、医薬部外品（口中清涼剤、デンタルケア、スキンケア、毛髪用剤、浴用剤、てんか粉類、ドリンク剤、健胃清涼剤など）、動物用食品（ペットフードなど）、動物用飼料、植物用肥料などにも使用できる。 The antioxidant peptide of the present invention can be suitably blended in foods for preventing or treating various diseases caused by active oxygen based on the antioxidant action. The antioxidant peptide of the present invention has an antioxidant power equivalent to that of vitamin E, and has a preventive or therapeutic action for various diseases caused by active oxygen by ingesting about 1 μg to 1000 mg per day as food. obtain. As food, it may be blended in liquid foods such as beverages and drinks, jelly-like foods (including dietary supplements and foods for those with difficulty in swallowing), and tablets and granules as supplements and functional foods. You may ingest in solid food form. In addition, quasi-drugs (in-mouth refreshers, dental care, skin care, hair preparations, bath preparations, powdered meals, drinks, healthy stomach fresheners, etc.), animal foods (pet foods, etc.), animal feeds, It can also be used for plant fertilizers.
本発明の抗酸化ペプチドは、酸化に不安定な食品に配合することにより、安定化剤として使用することもできる。 The antioxidant peptide of this invention can also be used as a stabilizer by mix | blending with the food unstable to oxidation.
また、本発明の抗酸化ペプチドは化粧料に配合することができる。化粧料としては、例えばローション、化粧水、乳液、口紅、クリーム、ゼリー、パック、ファンデーション等の主として皮膚や粘膜などに適用されるものに用いるのが好適である。 Moreover, the antioxidant peptide of this invention can be mix | blended with cosmetics. As the cosmetic, for example, it is suitable to be used mainly for skin, mucous membrane and the like such as lotion, lotion, milky lotion, lipstick, cream, jelly, pack, foundation and the like.
以下、本発明を実施例を用いてより詳細に説明する Hereinafter, the present invention will be described in more detail with reference to examples.
実施例１
（１）抗酸化ペプチド画分の調製
アルコール変性ローヤルゼリータンパク質を凍結乾燥した後、５倍量の蒸留水に溶解した。透析を行うことで低分子の糖、不純物を取り除き、より純度の高いアルコール変性ローヤルゼリータンパク質を得た。そのタンパク質溶液を１ＮＨＣｌでｐＨ２．８に調整し、最初に、1/500重量比のペプシンを作用させた。その分解物をトリプシン、キモトリプシン（シグマ社製）、豚由来小腸酵素で順次処理した。ペプシン、トリプシン、キモトリプシンについては添加後３７℃で２４時間、小腸酵素については添加後３７℃で１時間インキュベートした。反応停止には、ペプシンの場合、１ＮＮａＯＨでｐＨ８．０に調整することで酵素を失活させ、トリプシン、キモトリプシン、小腸酵素の場合は４倍量の９９．７％エタノールを添加し、３，０００×ｇで２０分遠心分離して未反応のタンパク質および酵素を除去した。小腸酵素処理で得られた上清をエバボレーターで濃縮乾固後、蒸留水に溶解し、アルコール変性ローヤルゼリータンパク質のプロテアーゼ分解物とした。このようにして得られたペプシン／トリプシン／キモトリプシン分解物（Ｃｈｙｍｏ画分）、ペプシン／トリプシン／キモトリプシン／小腸酵素分解物（Ｓ.I 画分）をサンプルとして用いた。ベプチドの濃度測定はＬｏｗｒｙ法により行われた。標準タンパク質として牛血清アルブミンを用いた。
Example 1
(1) Preparation of Antioxidant Peptide Fraction Alcohol-denatured royal jelly protein was lyophilized and then dissolved in 5 volumes of distilled water. By dialysis, low-molecular sugars and impurities were removed, and a higher-purity alcohol-denatured royal jelly protein was obtained. The protein solution was adjusted to pH 2.8 with 1N HCl and first a 1/500 weight ratio of pepsin was applied. The degradation product was sequentially treated with trypsin, chymotrypsin (manufactured by Sigma), and porcine-derived small intestine enzyme. Pepsin, trypsin, and chymotrypsin were incubated at 37 ° C. for 24 hours after addition, and small intestine enzymes were incubated at 37 ° C. for 1 hour after addition. For stopping the reaction, in the case of pepsin, the enzyme was inactivated by adjusting the pH to 8.0 with 1N NaOH, and in the case of trypsin, chymotrypsin and small intestine enzyme, 4 times the amount of 99.7% ethanol was added, and 3,000. Unreacted proteins and enzymes were removed by centrifugation at xg for 20 minutes. The supernatant obtained by the small intestine enzyme treatment was concentrated to dryness with an evaporator and then dissolved in distilled water to obtain a protease degradation product of alcohol-denatured royal jelly protein. The thus obtained pepsin / trypsin / chymotrypsin degradation product (Chymo fraction) and pepsin / trypsin / chymotrypsin / small intestine enzyme degradation product (S.I fraction) were used as samples. The peptide concentration was measured by the Lowry method. Bovine serum albumin was used as a standard protein.
なお、「アルコール変性ローヤルゼリータンパク質」として、ローヤルゼリーをアルコール（本実施例では70％ｖ／ｖ含水エタノール）沈殿処理し、得られたローヤルゼリータンパク質を凍結乾燥したものを使用した。 In addition, as “alcohol-denatured royal jelly protein”, royal jelly was precipitated by alcohol (70% v / v water-containing ethanol in this example), and the resulting royal jelly protein was lyophilized.
（２）抗酸化作用の測定
（２−１）酸化モデル系
酸化モデル系は、Ｃｈｅｎらの方法（14）に改良を加えて行った。バイアル瓶に ５ｍｇリノレン酸、および１ｍｌの0.2M K-phosphate buffer(ｐＨ７．０；１％TritonX-100)を加え、酸化促進剤として０．０５ｍＭ塩化鉄（II）と蒸留水を添加し、４０℃で４分間超音波処理を行い、エマルションを作成した。最終容量が１ｍｌとなるようにサンプル（0.2％） と蒸留水を加え、４０℃の恒温槽で６０分間加熱、振とうした。加熱前および加熱後の反応液の過酸化脂質量を、直ちにロダン鉄法で測定した。抗酸化作用の評価は、加熱前後における過酸化脂質の増加量を比較することにより行った。
(2) Measurement of antioxidant action (2-1) Oxidation model system The oxidation model system was performed by modifying the method (14) of Chen et al. Add 5 mg linolenic acid and 1 ml of 0.2 M K-phosphate buffer (pH 7.0; 1% TritonX-100) to the vial, add 0.05 mM iron (II) chloride and distilled water as an oxidation promoter, Sonication was carried out at 4 ° C. for 4 minutes to prepare an emulsion. A sample (0.2%) and distilled water were added to a final volume of 1 ml, and the mixture was heated and shaken in a 40 ° C. constant temperature bath for 60 minutes. The amount of lipid peroxide in the reaction solution before and after heating was immediately measured by the rodan iron method. The antioxidant action was evaluated by comparing the increased amount of lipid peroxide before and after heating.
（２−２）ロダン鉄法
大澤らの方法（２３）に準じて行った。０．０５ｍｌの反応液に２．２５ｍ1の99.5％エタノール、０．０５ｍ１の３０％チオシアン酸アンモニウム水溶液、0.1ｍｌのｌＮ ＨＣｌおよび０．１ｍ1の0.02ＭＦｅＣｌ２／3.5％ＨＣｌを加え、よく攪拌後、500nｍでの吸光度を測定した。測定には、Jasco、V-530UVsectrophotometerを用いた。S.I画分、Chymo画分、ビタミンE（VE）及びタンパク質のないコントロール（none）を比較した結果を図１に示す。なお、各ペプチドは０．２％の濃度で添加した。これは通常、食品添加物が使用される濃度が０．１％程度なので、その濃度に近い値を用いたものである。Ｓ.Ｉサンプルはα‐トコフェロールと同等の抗酸化作用を示すことが明らかとなった。
(2-2) Rodan iron method It was performed according to the method (23) of Osawa et al. 2.25 ml of 99.5% ethanol, 0.05 ml of 30% aqueous ammonium thiocyanate, 0.1 ml of 1N HCl and 0.1 ml of 0.02 M FeCl 2 /3.5% HCl were added to 0.05 ml of the reaction solution, and after stirring well, Absorbance at 500 nm was measured. For the measurement, Jasco, V-530 UV sectrophotometer was used. The results of comparing the SI fraction, the Chymo fraction, vitamin E (VE) and the control without protein (none) are shown in FIG. Each peptide was added at a concentration of 0.2%. Since the concentration at which food additives are used is usually about 0.1%, a value close to that concentration is used. It was revealed that the S.I sample showed an antioxidant effect equivalent to that of α-tocopherol.
（３）抗酸化ペプチドの単離・同定
（３−１）陽イオン交換クロマトグラフィー
Ｓ．Ｉ画分は、０．０５Ｍ 酢酸アンモニウム緩衝液（ｐＨ６．０）に溶解させ、同緩衝液で平衡化したＡＧ５０ＷＸ２(Ｈ+form，50-100mesh，ＢｉｏＲａｄ)カラムに吸着させた。非吸着物質を同じ緩衝液で洗浄した後、吸着画分を0.2Ｍ の ＮＨ４ＯＨで溶出させた。溶出した吸着画分を凍結乾燥し、塩基性ベプチド画分を得た。陽イオン交換クロマトグラフィーのクロマトグラム、および各フラクションの抗酸化試験の結果を、図２に示した。図２で最も高い抗酸化活性を示した画分ＶをさらにＨＰＬＣで精製した。
(3) Isolation and identification of antioxidant peptides (3-1) Cation exchange chromatography The I fraction was dissolved in 0.05 M ammonium acetate buffer (pH 6.0) and adsorbed onto an AG50WX2 (H + form, 50-100 mesh, BioRad) column equilibrated with the same buffer. After washing the non-adsorbed material with the same buffer, the adsorbed fraction was eluted with 0.2 M NH 4 OH. The eluted adsorbed fraction was lyophilized to obtain a basic peptide fraction. The chromatogram of cation exchange chromatography and the result of the antioxidant test of each fraction are shown in FIG. Fraction V showing the highest antioxidant activity in FIG. 2 was further purified by HPLC.
（３−２）ＨＰＬＣ
画分Ｖに存在する抗酸化ペプチドを単難するため、逆相カラムを用いた高速液体クロマトグラフィー（ＨＰＬＣ）を行った。カラムとしてＯＤＳカラム（Pegasil-3000DS，Senshu Scientific Co.）を用い、溶離には0.1％ ＴＦＡ水溶液から0.085％ＴＦＡを含む６０％アセトニトリル溶液への６０分間での濃度勾配法（１％／ｍｉｎ）を用いた。ベプチドの溶出位置は220nｍでの吸光度で確認した。また、再ＨＰＬＣを行った場合は、０．１％TFAを含む２０％アセトニトリル溶液から0.085％ＴＦＡを含む４０％アセトニトリル溶液への４０分間での濃度勾配法(０．５％／ｍｉｎ)を用いた。逆相カラムを用いたＨＰＬＣで単離した抗酸化ベプチドのアミノ酸配列を、プロテインシークエンサーG-1005A（ヒューレット・パッカード社）を用いて分析した。その結果、ペプチド１（配列番号１）、ペプチド２（配列番号２）、ペプチド３（配列番号３）が得られた。これらペプチドのマススペクトルの結果を以下の表１に示す。
(3-2) HPLC
High-performance liquid chromatography (HPLC) using a reverse phase column was performed in order to make it difficult for the antioxidant peptide present in fraction V. An ODS column (Pegasil-3000DS, Senshu Scientific Co.) was used as the column, and a concentration gradient method (1% / min) over 60 minutes from 0.1% TFA aqueous solution to 60% acetonitrile solution containing 0.085% TFA was used for elution. Using. The elution position of the peptide was confirmed by absorbance at 220 nm. When re-HPLC was performed, a concentration gradient method (0.5% / min) over 40 minutes from a 20% acetonitrile solution containing 0.1% TFA to a 40% acetonitrile solution containing 0.085% TFA was used. It was. The amino acid sequence of the antioxidant peptide isolated by HPLC using a reverse phase column was analyzed using a protein sequencer G-1005A (Hewlett Packard). As a result, peptide 1 (SEQ ID NO: 1), peptide 2 (SEQ ID NO: 2), and peptide 3 (SEQ ID NO: 3) were obtained. The results of mass spectra of these peptides are shown in Table 1 below.
表１のマススペクトルの結果は、プロテインシークエンサーの結果と一致しており、本発明のペプチドの配列が同定された。 The mass spectrum results in Table 1 are consistent with the protein sequencer results, and the sequence of the peptide of the present invention was identified.
製剤例１：化粧水
以下の各成分を配合し、常法に従い化粧水を調製した。
エタノール ５重量％
グリセリン ４重量％
ＢＧ（１，３−ブチレングリコール） ４重量％
実施例１で得られたローヤルゼリータンパク質酵素分解物 ０．５重量％
クエン酸 適量
クエン酸ナトリウム 適量
精製水 残余
Formulation Example 1: Toner lotion was prepared according to a conventional method by blending the following components.
Glycerin 4% by weight
BG (1,3-butylene glycol) 4% by weight
Royal jelly protein enzyme degradation product obtained in Example 1 0.5% by weight
Citric acid Suitable amount Sodium citrate Suitable amount Purified water Residual
製剤例２：ドリンク剤
以下の各成分を配合し、常法に従いドリンク剤を調製した。
水 ８８重量％
ブドウ糖 １０重量％
アスコルビン酸ナトリウム ４重量％
実施例１で得られたローヤルゼリータンパク質酵素分解物 １重量％
ＥＤＴＡ２Ｎａ ０．５重量％
Formulation Example 2: Drinks The following components were blended, and drinks were prepared according to conventional methods.
88% by weight of water
Glucose 10% by weight
Sodium ascorbate 4% by weight
1% by weight of royal jelly protein enzyme degradation product obtained in Example 1
EDTA2Na 0.5% by weight
製剤例３：健康食品（錠剤）
以下の各成分を配合し、常法に従い錠剤を調製した。
デンプン １５重量％
乳糖 ２５重量％
ヒドロキシプロピルセルロース ４重量％
ステアリン酸マグネシウム １重量％
シェラック ５重量％
グラニュー糖 ４５重量％
実施例１で得られたローヤルゼリータンパク質酵素分解物 ５重量％
Formulation Example 3: Health food (tablets)
The following components were blended, and tablets were prepared according to a conventional method.
15% by weight starch
Hydroxypropylcellulose 4% by weight
Magnesium stearate 1% by weight
5% by weight of royal jelly protein enzyme degradation product obtained in Example 1
Claims (5)
Ser-Leu-Pro-Ile-Leu-His-Glu-Trp。 Antioxidant peptides consisting of the following amino acid sequences:
Ser-Leu-Pro-Ile-Leu-His-Glu-Trp.
Ser-Leu-Pro-Ile-Leu-His-Glu-Trp。 A method for producing an antioxidant peptide having the following amino acid sequence, characterized by hydrolyzing a protein derived from royal jelly with a protease:
Ser-Leu-Pro-Ile-Leu-His-Glu-Trp.
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103819541A (en) * | 2014-03-06 | 2014-05-28 | 福州大学 | Microalgae oxidation prevention polypeptide |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN101824077A (en) * | 2010-03-12 | 2010-09-08 | 中国科学院昆明动物研究所 | Large green frog antioxidant peptide (antioxidin-RL) as well as gene and application thereof |
| CN108283617A (en) * | 2018-04-24 | 2018-07-17 | 上海上水和肌化妆品有限公司 | A kind of composition and forming method of skin basement membrane maintenance |
| CN110951811B (en) * | 2019-12-30 | 2021-08-31 | 云南天卉蜂业科技有限公司 | Glycosylated royal jelly antioxidant peptide and preparation method thereof |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH04279597A (en) * | 1991-03-07 | 1992-10-05 | Gifu Youhou Kk | New peptide, angiotensinase inhibitory peptide and per oral composition containing the same peptide |
| JP2002193997A (en) * | 2000-10-03 | 2002-07-10 | Yamada Bee Farm | Decomposed composition of royal jelly by protease and food composition containing the same |
-
2005
- 2005-02-16 CN CNA2008100852627A patent/CN101284866A/en active Pending
- 2005-02-16 CN CNA2008100852631A patent/CN101284867A/en active Pending
- 2005-02-16 CN CN 200510009423 patent/CN1680429A/en active Pending
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH04279597A (en) * | 1991-03-07 | 1992-10-05 | Gifu Youhou Kk | New peptide, angiotensinase inhibitory peptide and per oral composition containing the same peptide |
| JP2002193997A (en) * | 2000-10-03 | 2002-07-10 | Yamada Bee Farm | Decomposed composition of royal jelly by protease and food composition containing the same |
Non-Patent Citations (1)
| Title |
|---|
| JPN6013005779; 日本農芸化学会大会講演要旨集， ２００２， Ｖｏｌ．２００２， ｐ．１１１ * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN103819541A (en) * | 2014-03-06 | 2014-05-28 | 福州大学 | Microalgae oxidation prevention polypeptide |
Also Published As
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| CN1680429A (en) | 2005-10-12 |
| CN101284866A (en) | 2008-10-15 |
| CN101284867A (en) | 2008-10-15 |
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