CN1680429A - Anti-oxidation peptide from bee milk - Google Patents
Anti-oxidation peptide from bee milk Download PDFInfo
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- CN1680429A CN1680429A CN 200510009423 CN200510009423A CN1680429A CN 1680429 A CN1680429 A CN 1680429A CN 200510009423 CN200510009423 CN 200510009423 CN 200510009423 A CN200510009423 A CN 200510009423A CN 1680429 A CN1680429 A CN 1680429A
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- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
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Abstract
The antioxidative peptide has an amino acid sequence described in either one of the formulas (1) to (3). (1) Tyr-Tyr-Ser-Pro-Leu; (2) Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln; and (3) Ser-Leu-Pro-Ile-Leu-His-Glu-Trp.
Description
Technical field
The present invention relates to have the peptide of antioxygenation, in particular to the anti-oxidation peptide that proteolysis obtained by containing in the royal jelly.
Background technology
Now, royal jelly is widely used in fields such as protective foods, pharmaceuticals, makeup, and report shows that it has vasodilation, brings high blood pressure down, various pharmacological actions and nutritional-physiological effect such as antibiotic.
Royal jelly be synthetic by the sialisterium of honeybee, by the milky substance of the big jaw glandular secretion that is positioned at head, be the material of worker bee young honeybee in the feeding queen bee nit nest in order to cultivate queen bee.Royal jelly is rich in proteins, VITAMIN, mineral substance balancedly, and the life-span that all eat the queen bee of royal jelly all one's life is 40 times of worker bee, and has 2000 the ability of laying eggs in a day.To the research of the effective constituent of royal jelly, be that the low molecular compound such as lipid acid, amino acid, VITAMIN of representative is that carry out at the center with 10-hydroxyl-2-decylenic acid (acid of デ セ Application) always.
On the other hand, though royal jelly generally contains the protein more than 10%, to relatively backward always with this protein molecular structure, research that physiological action is relevant.And, make the makeup contain royal jelly, when health care liquid medicine (De リ Application Network drug) waits, carry out ethanol-extracted, protein is separated as throw out, but present stage not realization to this proteinic effective utilization.
About the proteinic protease treatment thing of royal jelly, known is that it has calcium absorption promoter action (Zhong Zuo Hui, food と development, 34,5 (1999)), lowering blood glucose value effect (is gone up Tian Xiuyi youth, Food Style, 21,6,5 (2002)), and also relevant for the report of its antioxygenation ((society) Japanese national royal jelly fair trade board of management (national ロ one ャ Le ゼ リ one just Qu Yin Association Meetings meeting) " ロ one ャ Le ゼ リ one (research of Royal Jelly) に Seki The Ru " puts down into 13 years research Reported and accuses Books), but its effect is not as vitamin-E.
The object of the present invention is to provide crude substance with strong antioxidant action.
Summary of the invention
At above-mentioned problem, through research repeatedly, the inventor finds by royal jelly is carried out the enzyme processing with trypsinase, Quimotrase as a result, can obtain to have the anti-oxidation peptide with the strong anti-oxidation ability of vitamin-E equal extent.
That is, the present invention relates to invention as follows:
1. the anti-oxidation peptide that has any one aminoacid sequence of following (1)～(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. with the antioxidant of above-mentioned 1 described anti-oxidation peptide as effective constituent.
3. the food that contains above-mentioned 1 described anti-oxidation peptide.
4. the manufacture method of anti-oxidation peptide that has any one aminoacid sequence of following (1)～(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，
It is characterized in that, with the proteolysis of proteolytic enzyme derived from bee milk.
5. the makeup that contain above-mentioned 1 described anti-oxidation peptide.
Description of drawings
Fig. 1: the measurement result of the antioxygenation that expression is undertaken by thiocyanate-ferric.Among Fig. 1, " none " expression does not have proteinic contrast, the resolvent (Chymo fraction) that is obtained is handled in " Chymom " expression with stomach en-, trypsinase and Quimotrase, " S.I " expression expression is handled the resolvent (S.I fraction) that is obtained with stomach en-, trypsinase, Quimotrase and intestinal enzymes, and " V.E " represents vitamin-E.
Fig. 2: the color atlas of expression cation-exchange chromatography analytical method, and the result of the anti-oxidant test of each fraction.
Embodiment
Anti-oxidation peptide of the present invention has following aminoacid sequence.
Tyr-Tyr-Ser-Pro-Leu (being designated hereinafter simply as " peptide 1 ")
Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln (being designated hereinafter simply as " peptide 2 ")
Ser-Leu-Pro-Ile-Leu-His-Glu-Trp (being designated hereinafter simply as " peptide 3 ")
Peptide 1～peptide 3 is new peptides, and its antioxygenation obtains clearly first by the present invention.
Anti-oxidation peptide of the present invention also can obtain by gene recombination or chemosynthesis, and the protein level that also can act on royal jelly itself (raw royal jelly, dried royal jelly etc.) or derived from bee milk by the intestinal enzymes that makes stomach en-, trypsinase, Quimotrase, is derived from pig assigns to obtain.And,, also can use the material that the protein raw material hydrolysis beyond the royal jelly is obtained by stomach en-, trypsinase, Quimotrase, the lytic enzymes such as intestinal enzymes that are derived from pig as long as can obtain peptide 1～peptide 3.
Can enumerate stomach en-, trypsinase, Quimotrase, intestinal enzymes etc. as being used for decomposing the enzyme of making anti-oxidation peptide of the present invention by proteinic enzyme, these enzymes are can be with the animal, plant, yeast, fungi etc. that are derived from microorganism, the comprise Mammals example of the enzyme of biological peptide bond hydrolysis arbitrarily, preferred stomach en-, trypsinase, Quimotrase, are derived from the intestinal enzymes of pig.For example, under the temperature about 37 ℃, carry out about 1～about 48 hours processing simultaneously by protein, can obtain any one anti-oxidation peptide of the present invention with the stomach en-, trypsinase, Quimotrase, the intestinal enzymes that are derived from various biologies with derived from bee milk.
Peptide of the present invention uses after can separating from the proteinic enzyme resolvent of derived from bee milk, purifying, and also the proteolysis compositions (removing the material of salt, carbohydrate or hmw protein etc. as required) that comprises anti-oxidation peptide of the present invention and other multiple peptides can be used for various uses such as food, makeup as anti-oxidation peptide.
For example, the health care liquid medicine that contains royal jelly is to make by the protein that adds about alcohol of 70～about 95% (v/v), preferred alcohol postprecipitation to royal jelly is removed, and the protein of insoluble derived from bee milk can be used as the material protein use that enzyme is handled in this aqueous alcohol.As chemical synthesis, can synthesize by peptide synthesizer, also can be synthetic by solid phase synthesis or liquid phase, interim ground prolongs amino acid by peptide bond to be made.
Anti-oxidation peptide of the present invention can be fit to add the prevention of the various diseases that is caused by active oxygen to and treat in the food of usefulness based on its antioxygenation.Anti-oxidation peptide of the present invention has the resistance of oxidation with the vitamin-E equal extent, by absorbing about 1 μ g～about 1000mg every day as food, can prevent or treat the various diseases that is caused by active oxygen.As food, can add aqueous food, gel-like foodstuffs (food of comprise dietary supplement, the difficult person that swallows using) such as beverage, health care liquid medicine to, also can be used as the form picked-up with solid shape food such as tablet, particle such as subsidiary, functional foodstuff.And, also can be used for accurate pharmaceuticals (mouthful freshener, protect tooth, skin care, hair with agent, wash baths, toilet powder shui class (て ん か powder Class), the liquid medicine that keeps healthy, freshener etc. is good for the stomach), animal usefulness food (pet food etc.), animal feed, plant is with fertilizer etc.
Anti-oxidation peptide of the present invention can be used as stablizer and uses by adding in the unsettled food of oxidation.
And anti-oxidation peptide of the present invention also can add in the makeup.As makeup, for example be applicable to that lotion, astringent, milk sap, lipstick, creme, gel, facial mask (パ ッ Network), foundation cream etc. are mainly used in the material of skin or mucous membrane etc.
Below the present invention is elaborated by embodiment.
Embodiment 1
(1) modulation of anti-oxidation peptide fraction
After the freeze-drying of pure sex change royal jelly protein, be dissolved in the distilled water of 5 times of amounts.Remove low molecular sugar, impurity by dialysing, obtain the higher pure sex change royal jelly protein of purity.This protein soln is adjusted to pH2.8 with 1N HCl, handling with the stomach en-of 1/500 weight ratio at first.With its resolvent use trypsinase, Quimotrase (manufacturing of シ グ マ company) successively, the intestinal enzymes that is derived from pig handles.For stomach en-, trypsinase, Quimotrase, add the back and under 37 ℃, carry out 24 hours incubations, for intestinal enzymes, add the back and under 37 ℃, carry out 1 hour incubation.When reaction stops, if stomach en-is adjusted to pH8.0 so that enzyme deactivation with 1N NaOH, if when trypsinase, Quimotrase, intestinal enzymes, add 99.7% ethanol of 4 times of amounts, with 3,000 * g carries out 20 minutes centrifugation, removes unreacted protein and enzyme.To handle the supernatant liquor that obtained by intestinal enzymes carries out being dissolved in the distilled water, as the proteinic proteolytic enzyme resolvent of pure sex change royal jelly after concentrate drying solidifies with vaporizer.Such stomach en-/trypsinase that obtains/Quimotrase resolvent (Chymo fraction), stomach en-/trypsinase/Quimotrase resolvent/intestinal enzymes resolvent (S.I fraction) are used as sample.The concentration determination of peptide is undertaken by the Lowry method.Standard protein uses bovine serum albumin.
In addition, as " pure sex change royal jelly protein " use by with royal jelly with alcohol (being the 70%v/v aqueous ethanol in the present embodiment) precipitation process, the material that the royal jelly protein freeze-drying that obtained is obtained.
(2) mensuration of antioxygenation
(2-1) model of oxidation system
The model of oxidation system is to carry out after the method (14) with Chen etc. is improved.0.2M potassium phosphate buffer (the K-phosphatebuffer) (pH7.0 that in phial, adds 5mg linolenic acid, 1ml; 1%TritonX-100), add 0.05mM iron(ic) chloride (II) and distilled water, under 40 ℃, carry out 4 minutes ultrasonic treatment, make emulsion as oxidation promotor.It is 1ml that adding sample (0.2%) and distilled water make termination capacity,, heating is 60 minutes in 40 ℃ thermostatic bath, and vibration.Measure by the thiocyanation iron processes as soon as possible for the amount that reaches the lipid peroxide of the reaction solution after heating before the heating.For the evaluation of antioxygenation, by relatively the carrying out of increasing amount to the lipid peroxide before and after the heating.
(2-2) thiocyanate-ferric
Method (23) according to big pool etc. is carried out.Ethanol 2.25ml, 30% ammonium thiocyanate aqueous solution 0.05ml, the 1N HCl of 0.1ml and the 0.02MFeCl of 0.1ml of adding 99.5% in the reaction solution of 0.05ml
2/ 3.5%HCl after fully stirring, measures the absorbancy under the 500nm.Use Jasco, V-530UV spectrophotometer during mensuration.S.I fraction, Chymo fraction, vitamin-E (VE) and the comparative result that do not have a protein contrast (none) are as shown in Figure 1.In addition, each peptide adds with 0.2% concentration.This is because the working concentration of food additives is about 0.1% generally speaking, so use the value close with this concentration.As can be seen, the S.I sample demonstrates and the equal antioxygenation of alpha-tocopherol (vitamin-E).
(3) separation of anti-oxidation peptide, evaluation
(3-1) cation-exchange chromatography analytical method
The S.I fraction is dissolved in the ammonium acetate buffer (pH6.0) of 0.05M, and (the H+ type, the 50-100 order is BioRad) on the post to make it be adsorbed onto AG50WX2 with this damping fluid equilibration.With non-adsorbent with same buffer solution for cleaning after, with the fraction of absorption with the NH of 0.2M
4The OH wash-out.With the absorption fraction freeze-drying of wash-out, obtain the basic peptide fraction.The anti-oxidant test-results of the color atlas of cation-exchange chromatography analytical method and each fraction as shown in Figure 2.Having the active fraction V of high anti-oxidation among Fig. 2 further purifies with HPLC.
(3-2)HPLC
In order to separate the anti-oxidation peptide that exists among the fraction V, use the high efficiency liquid chromatography analytical method (HPLC) of reversed-phase column.Its center pillar uses ODS post (Pegasil-3000DS, SenshuScientific Co.), uses 60 minutes E-test (1%/min) from the 0.1%TFA aqueous solution to 60% acetonitrile solution that contains 0.085%TFA during wash-out.The wash-out position of peptide is confirmed with the absorbancy under the 220nm.And, when carrying out HPLC once more, use 40 minutes E-test (0.5%/min) from 20% acetonitrile solution that contains 0.1%TFA to 40% acetonitrile solution that contains 0.085%TFA.For the aminoacid sequence that passes through with the isolating anti-oxidation peptide of HPLC of reversed-phase column, use protein sequencing instrument (プ ロ テ ィ Application シ one Network ェ Application サ one) G-1005A (ヒ ュ one レ ッ ト パ ッ カ one De society) to analyze.Peptide 1 (sequence number 1), peptide 2 (sequence number 2), peptide 3 (sequence number 3) have consequently been obtained.The result of the mass spectroscopy of these peptides is as shown in table 1 below.
Table 1
| Peptide | Chemical formula | Mass spectrum [M+H] + | |
| Calculated value | Measured value | ||
| ??Tyr-Tyr-Ser-Pro-Leu | ????C 32H 42N 5O 9 | ????642.3 | ??642.2 |
| ??Asn-Tyr-Pro-Phe-Asp-Val-Asp-Gln | ????C 45H 60N 10O 16 | ????997.4 | ??997.4 |
| ??Ser-Leu-Pro-Ile-Leu-His-Glu-Trp | ????C 48H 71N 11O 12 | ????994.5 | ??994.5 |
The result of the mass spectroscopy of table 1 is consistent with the result of protein sequencing instrument, thereby has identified the sequence of peptide of the present invention.
Formulation example 1: astringent
Cooperate following each composition, be modulated into astringent according to usual method.
Ethanol 5 weight %
Glycerine 4 weight %
BG (1,3 butylene glycol) 4 weight %
The royal jelly protein enzyme resolvent 0.5 weight % that embodiment 1 is obtained
Citric acid is an amount of
Trisodium Citrate is an amount of
Remnants purify waste water
Formulation example 2: health care liquid medicine
Cooperate following each composition, be modulated into health care liquid medicine according to usual method.
Water 88 weight %
Glucose 10 weight %
Sodium ascorbate 4 weight %
The royal jelly protein enzyme resolvent 1 weight % that embodiment 1 is obtained
Citric acid is an amount of
EDTA2Na 0.5 weight %
Formulation example 3: heath food (tablet)
Cooperate following each composition, be modulated into tablet according to usual method.
Starch 15 weight %
Hydroxypropylcellulose 4 weight %
Magnesium Stearate 1 weight %
Shellac (シ ェ ラ ッ Network) 5 weight %
The royal jelly protein enzyme resolvent 5 weight % that embodiment 1 is obtained
According to the present invention, can obtain to be derived from anti-oxidation peptide crude substance, safe, and can be widely used in fields such as food, makeup.
Sequence table
＜110〉Yamada Bee-yard Co., Ltd (YAMADA APICULTURE CENTER, INC.)
＜120〉anti-oxidation peptide of derived from bee milk
<130>SPI050357-25
<160>3
<170>PatentIn?version?3.1
<210>1
<211>5
<212>PRT
＜213〉royal jelly
<400>1
Tyr?Tyr?Ser?Pro?Leu
5
<210>2
<211>8
<212>PRT
＜213〉royal jelly
<400>2
Asn?Tyr?Pro?Phe?Asp?Val?Asp?Gln
5????????????8
<210>3
<211>8
<212>PRT
＜213〉royal jelly
<400>3
Ser?Leu?Pro?Ile?Leu?His?Glu?Trp
5????????????8
Claims (5)
1. the anti-oxidation peptide that has any one aminoacid sequence of following (1)～(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. with any one antioxidant of the described anti-oxidation peptide of claim 1 as effective constituent.
3. any one the food that contains the described anti-oxidation peptide of claim 1.
4. the manufacture method of anti-oxidation peptide that has any one aminoacid sequence of following (1)～(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，
It is characterized in that, with the proteolysis of proteolytic enzyme derived from bee milk.
5. the makeup that contain the described anti-oxidation peptide of claim 1.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP200437954 | 2004-02-16 | ||
| JP2004037954 | 2004-02-16 |
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CNA2008100852627A Division CN101284866A (en) | 2004-02-16 | 2005-02-16 | Anti-oxidation peptide from bee milk |
| CNA2008100852631A Division CN101284867A (en) | 2004-02-16 | 2005-02-16 | Anti-oxidation peptide from bee milk |
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| Publication Number | Publication Date |
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| CN1680429A true CN1680429A (en) | 2005-10-12 |
Family
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| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN 200510009423 Pending CN1680429A (en) | 2004-02-16 | 2005-02-16 | Anti-oxidation peptide from bee milk |
| CNA2008100852631A Pending CN101284867A (en) | 2004-02-16 | 2005-02-16 | Anti-oxidation peptide from bee milk |
| CNA2008100852627A Pending CN101284866A (en) | 2004-02-16 | 2005-02-16 | Anti-oxidation peptide from bee milk |
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| Application Number | Title | Priority Date | Filing Date |
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| CNA2008100852631A Pending CN101284867A (en) | 2004-02-16 | 2005-02-16 | Anti-oxidation peptide from bee milk |
| CNA2008100852627A Pending CN101284866A (en) | 2004-02-16 | 2005-02-16 | Anti-oxidation peptide from bee milk |
Country Status (2)
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| JP (1) | JP2011116761A (en) |
| CN (3) | CN1680429A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| CN110951811A (en) * | 2019-12-30 | 2020-04-03 | 云南天卉蜂业科技有限公司 | Glycosylated royal jelly antioxidant peptide and preparation method thereof |
Families Citing this family (2)
| 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 |
| CN103819541B (en) * | 2014-03-06 | 2016-01-06 | 福州大学 | A kind of micro-algae antioxidation polypeptide |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP3068656B2 (en) * | 1991-03-07 | 2000-07-24 | アピ株式会社 | Novel peptide and angiotensin converting enzyme inhibitory peptide and oral feeding composition containing them |
| JP4045401B2 (en) * | 2000-10-03 | 2008-02-13 | 株式会社山田養蜂場本社 | Degradation composition of royal jelly by proteolytic enzyme and food composition containing the same |
-
2005
- 2005-02-16 CN CN 200510009423 patent/CN1680429A/en active Pending
- 2005-02-16 CN CNA2008100852631A patent/CN101284867A/en active Pending
- 2005-02-16 CN CNA2008100852627A patent/CN101284866A/en active Pending
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2011
- 2011-01-25 JP JP2011012488A patent/JP2011116761A/en active Pending
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| CN110951811A (en) * | 2019-12-30 | 2020-04-03 | 云南天卉蜂业科技有限公司 | Glycosylated royal jelly antioxidant peptide and preparation method thereof |
| 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 |
Also Published As
| Publication number | Publication date |
|---|---|
| CN101284866A (en) | 2008-10-15 |
| CN101284867A (en) | 2008-10-15 |
| JP2011116761A (en) | 2011-06-16 |
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