JP5871330B2 - peptide - Google Patents

Description

The present invention relates to a peptide having an antioxidant action. The present invention also relates to a peptide having an antioxidant action derived from milk protein. Furthermore, this invention relates to the antioxidant which uses this peptide as an active ingredient. Furthermore, this invention relates to the food-drinks or feed which mix | blended this peptide.

Peroxides and free radicals generated by the oxidation of unsaturated fatty acids not only impair the flavor and nutritional value of food and cause quality deterioration, but also in the living body due to its strong oxidizing power, intracellular proteins and genetic DNA It is said that the lipids that make up cell membranes are attacked and lipid peroxides such as highly toxic hydroperoxides are produced, causing cell damage and tissue damage. The accumulation of harmful effects on living bodies due to such active oxygen and free radicals may be related to one of the causes of so-called lifestyle-related diseases such as aging, cancer, arteriosclerosis, and heart disease. It has become clear. Therefore, from the viewpoint of preventing or suppressing oxidative stress due to food components, research on the relationship between the antioxidant properties of foods and food components and the search for components having antioxidant properties are being conducted.

Plant-derived vitamins and polyphenols have been known for antioxidant components. There are many reports on vitamins, especially vitamin C, vitamin E and β
-Antioxidant properties are recognized in carotenes. As for polyphenols, catechins and flavonoids have been shown to have strong antioxidant properties. Furthermore, a wide variety of antioxidant peptides have been separated and identified from protein protease hydrolysates, and there are reports that three types of antioxidant peptides have been separated from the enzyme degradation products of ovalbumin (for example, non-patent literature). 1). There is also a report that six kinds of antioxidant peptides were separated and identified from protease hydrolyzate of β-conglycinin of soybean protein (
For example, see Non-Patent Document 2. ).

On the other hand, many physiological actions such as opioid activity, calcium absorption promoting action, cell proliferation action, antibacterial action, angiotensin I converting enzyme inhibitory action, etc. have been clarified for enzymatic degradation products of milk proteins. A method of suppressing fish oil odor by emulsifying eicosapentaenoic acid-containing fats and oils such as fish oil with a water-soluble protein solution (for example, see Patent Document 1), or emulsifying highly unsaturated fatty acid-containing fats and oils with a partial hydrolyzate of milk. A method for obtaining highly unsaturated fatty acid-containing fats and oils having high oxidation stability (for example, see Patent Document 2) is disclosed. In addition, highly unsaturated fatty acid-containing fats and oils, cheese and water are emulsified to prepare antioxidant emulsions to prevent oxidation of highly unsaturated fatty acid-containing fats and oils. A method (for example, refer to Patent Document 3) of masking the off-flavor of odor is disclosed. However, all of these are highly unsaturated fatty acid-containing fats and oils, each of which is a water-soluble protein solution, a partially hydrolyzed milk product, or an emulsion of highly unsaturated fatty acid-containing fats and oils emulsified with cheese. This prevents the fishy odor of the highly unsaturated fatty acid-containing oil itself and the off-flavor during storage. However, there is no report that a milk protein-derived peptide alone has antioxidant properties without being mixed with a highly unsaturated fatty acid-containing oil and emulsified. In addition, regarding the physiological function of cheese produced from milk, although antitumor action, antimutagenic action, etc. have been reported,
It is not known about having an antioxidant effect. The present inventors have found that the water-soluble peptide fraction of cheese has an antioxidant action, and filed a patent application (see Patent Document 4). However, it has not been found that a peptide having a specific amino acid sequence has an antioxidant effect. Thus, there is no report that the peptide derived from milk protein alone has an antioxidant property.

JP-A-60-102168 JP-A-2-305898 Japanese Patent Laid-Open No. 7-274823 JP 2004-352958 A

Takushoku Nobuaki et al., Japanese Journal of Agricultural Chemistry, 65, p. 1635, 1991 H.M. et al., J. Agric. Food Chem., 43, p.574, 1995

The present invention not only impairs the flavor and nutritional value of food and causes deterioration of quality, but also suppresses oxidative damage of the living body due to active oxygen and free radicals that adversely affect diseases and aging in the living body. It is an object of the present invention to provide a peptide having an effective antioxidative effect.

As a result of intensive studies to solve the above-mentioned problems, the present inventors have an antioxidant effect on peptides consisting of amino acid sequences represented by the following formulas (1) to (7), and are effective at a low dose. As a result, the present invention has been completed.
Phe-Gln-Ser-Glu-Glu-Gln equation (1)
However, serine (Ser) may be phosphorylated.
Phe-Gln-Ser-Glu-Glu formula (2)
However, serine (Ser) may be phosphorylated.
Tyr-Leu-Lys-Thr-Val-Tyr-Gln-His-Gln equation (3)
Met-His-Gln-Pro-His-Gln Formula (4)
Asp-Lys-Ile-His-Pro Formula (5)
Asp-Lys-His-Tyr formula (6)
Ile-His equation (7)
That is, the present invention relates to a peptide having an antioxidant action consisting of the amino acid sequence represented by the above formulas (1) to (7).
The present invention also relates to a peptide having an antioxidative action comprising an amino acid sequence represented by formulas (1) to (7) derived from milk protein.
Furthermore, this invention relates to the antioxidant which uses the peptide represented by Formula (1)-(7) as an active ingredient.
Furthermore, this invention relates to the food-drinks or feed for antioxidants which mix | blended the peptide represented by Formula (1)-(7).

Peptides having an antioxidative action consisting of the amino acid sequences represented by the formulas (1) to (7) of the present invention not only cause deterioration in quality by impairing the flavor and nutritional value of food, but also in the living body It is effective in suppressing oxidative damage of living organisms due to active oxygen and free radicals that adversely affect aging, etc., and as an antioxidant containing this peptide as an active ingredient, and for antioxidants containing this peptide It is useful as a food or drink or feed.

The separation chromatogram of the water-soluble peptide fraction which uses various cheeses as a raw material by a YMC-Pack ODS-A column is shown. C18 column shows the separation chromatogram (Cosmosil 40C ₁₈ -PREP) blue cheese soluble peptide purified fraction by.

Phe-Gln-Ser-Glu-Glu-Gln (however, serine (Ser) may be phosphorylated), Phe-Gln-Ser-Glu-Glu (provided that serine can be used in the present invention) (Ser may be phosphorylated), Tyr-Leu-Lys-Thr-Val-Tyr-Gln-His-Gln, Met-His
-Gln-Pro-His-Gln, Asp-Lys-Ile-His-Pro, Asp-Lys-His-Tyr, or peptide with an anti-oxidant activity consisting of the amino acid sequence represented by Ile-His After suspending in a solvent, insoluble substances can be removed by degreasing and centrifugation. Furthermore, you may remove protein from the obtained fraction. In the present invention, suspending cheese in a solvent means adding a solvent to the cheese to homogenize it or crushing it in the solvent to make it easy to obtain a water-soluble peptide fraction. As the solvent, an aqueous solvent such as water or a phosphate buffer can be used. Thereafter, desalting may be performed with a dialysis membrane, an ion exchange resin, or the like, or powder may be formed by drying by freeze drying or spray drying.

Moreover, as a cheese raw material for obtaining the peptide with the antioxidant effect which consists of an amino acid sequence represented by Formula (1)-(7), Parmesan cheese, Gruyere cheese, Maribo cheese, Gouda cheese, Cheddar cheese, Emmental cheese, Edam cheese , Camembert cheese, Brie cheese, Munster cheese, Pont Levec cheese, Stilton cheese, Dana blue cheese, natural cheese such as blue cheese, and process cheese made from these natural cheeses can be used. It is desirable to use natural cheese having a high degree of ripening, in particular mold-molded natural cheese.

Furthermore, after suspending cheese in a solvent, a fraction containing a peptide consisting of an amino acid sequence represented by formulas (1) to (7) obtained by degreasing, removal of insoluble substances, and removal of protein,
Further purification by reverse phase chromatography using a C18 column is also possible. When the fraction containing this peptide is passed through a C18 column under acidic conditions such as trifluoroacetic acid (TFA) or neutral conditions such as distilled water, the fraction having antioxidant activity is not permeated to the column. And the fraction that is adsorbed on the column and eluted with 10% ethanol. When these fractions were further purified by gel filtration chromatography,
The molecular weight distribution of the active fraction is in the range of 400 to 6,000 for any fraction.
Further, a fraction containing this peptide was dissolved in 0.05% TFA, and then the YMC-Pack ODS-A column (4.
6mm x 150mm) is subjected to reverse phase HPLC to fractionate the peptides. Chromatography is performed using a solvent (liquid A: 0.05% TFA; liquid B: 100% acetonitrile), concentration gradient (0% B⇒45% B, 125 mi
n) It is desirable to carry out under conditions of a flow rate of 0.8 ml / min and a detection wavelength of 220 nm.

A peptide having an antioxidative action comprising the amino acid sequence represented by the formulas (1) to (7) of the present invention and a fraction containing the peptide are used in food and drink and used for preventing quality deterioration of the food and drink. Can do. When blended in food or drink, after the cheese is ground in water, insoluble substances are removed by degreasing and centrifugation, and then the water-soluble peptide of cheese obtained by removing protein can be blended as it is. In addition, those desalted with a dialysis membrane, an ion exchange resin or the like, and further powdered by drying by freeze drying or spray drying can be blended. Moreover, it can utilize also about the peptide obtained by synthesize | combining.

The peptide having an antioxidative action consisting of the amino acid sequence represented by the formulas (1) to (7) of the present invention and a fraction containing the peptide are administered orally or parenterally, and in the living body, active oxygen and free By eliminating radicals and the like, it is possible to prevent progression of illness and aging. When administered orally or parenterally, the dosage form of the peptide having antioxidant activity of the present invention is for oral administration such as tablets, capsules, fine granules, powders, pills, troches, sublingual or liquids. Or preparations for parenteral administration such as injections and suppositories.

The oral dose of the peptide having an antioxidative action consisting of the amino acid sequence represented by the formula (1) to (7) of the present invention is determined in consideration of the purpose of treatment and prevention, symptoms, body weight, age, sex, etc. It can be determined as appropriate, but if it is administered as a peptide consisting of an amino acid sequence having an antioxidative activity represented by the formulas (1) to (7) per day for an adult, administration of 10 μg to 500 mg adversely affects disease or aging. A therapeutic or prophylactic effect can be obtained that suppresses oxidative damage of the living body caused by active oxygen, free radicals, and the like. Thus, the present invention is effective at low doses.

In addition, the peptide having an antioxidative action comprising the amino acid sequences represented by the formulas (1) to (7) of the present invention exhibits an antioxidative action in vivo by ingesting a food or drink or feed containing them. In addition to exerting, it also prevents deterioration of the food or drink blended in the food or drink or feed itself due to oxidation. Examples of the antioxidant food and drink include cheese, butter, milk beverage, juice, yogurt, jelly, bread, ice cream, noodles, sausage, infant formula and baby food.

EXAMPLES The present invention will be described in more detail below with reference to examples and test examples, but these are merely illustrative and the present invention is not limited by these.

(Preparation of blue cheese peptide)
Add 80 ml of distilled water to 20 g of blue cheese, grind with a stomacher (organo) for 15 minutes, and then in water with an ultradisperser (ULTRA-TURRAX, T-25; IKA Japan) 30
Further crushing for 2 seconds. The milk fat produced at the time of crushing was removed, and the resulting cheese slurry was shaken for 30 minutes with a shaker, and then insoluble material was removed by centrifugation (6,000 rpm, 20 min, 4 ° C.), and the supernatant was filtered (No. 113; (Whatman). Ethanol was added to the obtained filtrate to a concentration of 70%, and the mixture was allowed to stand at 4 ° C for 4 hours. Then, insoluble matters were removed by centrifugation (10,000rpm, 20min, 4 ° C), and the ethanol was removed by an evaporator. And then freeze-dried to obtain a water-soluble peptide fraction of blue cheese.
After dissolving this water-soluble peptide fraction with 0.05% TFA, YMC-Pack ODS-A column (4.6 mm x 15
0 mm) was subjected to reverse phase HPLC and fractionated into a water-soluble peptide purified fraction. Chromatography is performed using a solvent (liquid A: 0.05% TFA; liquid B: 100% acetonitrile), concentration gradient (0% B⇒45% B, 125
min), a flow rate of 0.8 ml / min, and a detection wavelength of 220 nm. The results are shown in FIG. 1 (chromatogram indicated as Blue). When the antioxidant activity of these fractions was measured by the method of Test Example 1 shown below, strong antioxidant activity was confirmed in the fraction indicated by the arrow in the chromatogram.
The purified fraction of water-soluble peptide that has been confirmed to have strong antioxidant activity was identified as Cosmosil 5C22-AR-II (4.6
mm × 150 mm), and subjected to reverse phase HPLC, and further fractionated to obtain peptides. Chromatography is solvent (liquid A: 0.1% TFA; liquid B: 80% acetonitrile), concentration gradient (0% B⇒15% B, 40 min)
The measurement was performed under the conditions of a flow rate of 0.8 ml / min and a detection wavelength of 220 nm. The results are shown in FIG. When the antioxidant activity of these fractionated peptides was measured, strong antioxidant activity was confirmed in fractions 5, 6, 8, 9, and 10 of the chromatogram.
The amino acid sequence of the resulting blue cheese peptide was analyzed with a peptide sequencer (Applied Biosystems). As a result, No. 5 shown in FIG. 2 was Asp-Lys-His.
-Tyr and Ile-His, number 6 is Phe-Gln-Ser-Glu-Glu-Gln and Phe-Gln-Ser-Glu-Glu, number 8 is T
yr-Leu-Lys-Thr-Val-Tyr-Gln-His-Gln, No. 9 Asp-Lys-Ile-His-Pro, No. 10 Met-His-Gln
It was confirmed that the sequence was -Pro-His-Gln.
The peptide of the present invention thus obtained can be used as an antioxidant as it is.

(Preparation of various cheese peptides)
Peptides in the same manner as in Example 1 for Bon Reveck cheese and Münster cheese using lactic acid bacteria as starters, Blue cheese and Dana blue cheese using lactic acid bacteria and blue mold, Brie cheese and Camembert cheese using lactic acid bacteria and white mold Was prepared.
That is, 80 ml of distilled water is added to 20 g of the various cheeses described above, and a stomacher (organo) is used.
After grinding for 15 minutes, it was further crushed in water with an ultradisperser (ULTRA-TURRAX, T-25; IKA Japan) for 30 seconds. The milk fat produced at the time of crushing was removed, and the resulting cheese slurry was shaken for 30 minutes with a shaker, and then insoluble material was removed by centrifugation (6,000 rpm, 20 min, 4 ° C.), and the supernatant was filtered (No. 113; (Whatman). Ethanol was added to the obtained filtrate to a concentration of 70%, and the mixture was allowed to stand at 4 ° C. for 4 hours, and then centrifuged (10,000 rpm, 20 min, 4
Insoluble matter was removed by (° C.), ethanol was removed by an evaporator, and freeze-dried to obtain each water-soluble peptide fraction.
Each water-soluble peptide fraction was dissolved in 0.05% TFA, and then YMC-Pack ODS-A column (4.6 mm x
150 mm) was subjected to reverse phase HPLC, and further fractionated into each peptide purified fraction. Chromatography is performed using a solvent (liquid A: 0.05% TFA; liquid B: 100% acetonitrile), concentration gradient (0% B⇒4
5% B, 125 min), flow rate 0.8 ml / min, detection wavelength 220 nm. The results are shown in FIG. When the antioxidant activity of these fractions was measured by the method of Test Example 1 shown below, strong antioxidant activity was confirmed in the fraction indicated by the arrow in the chromatogram.
A purified fraction of water-soluble peptide that has been confirmed to have this strong antioxidant activity was added to Cosmosil 5C22-AR-II (4
.6 mm x 150 mm) was subjected to reverse phase HPLC and further fractionated to obtain peptides. Chromatography is performed using a solvent (liquid A: 0.1% TFA; liquid B: 80% acetonitrile), concentration gradient (0% B⇒15% B, 40 mi).
n) When the flow rate was 0.8 ml / min and the detection wavelength was 220 nm, a chromatogram similar to that of the blue cheese shown in FIG. 2 was obtained, and the fraction for which antioxidant activity was confirmed was the same as in Example 1. When the amino acid sequence was confirmed, it was the same peptide as in the case of Blue Cheese.
The peptide of the present invention thus obtained can be used as an antioxidant as it is.

Test example 1

(Measurement of antioxidant activity of water-soluble peptide purified fractions of various cheeses)
About the water-soluble peptide refined | fractionated fraction and peptide fractionated in Example 1 and Example 2, the antioxidant activity was measured by the method of utilizing the effect | action which the oxide of linoleic acid discolors (beta) -carotene. That is, β-carotene solution (10mg / 10ml chloroform) 0.5ml, linoleic acid solution (1g / 10ml
Chloroform (0.2 ml) and Tween 40 solution (2 g / 10 ml chloroform) (1.0 ml) were placed in a 200 ml Erlenmeyer flask, and after removing chloroform completely with nitrogen gas, 100 ml of distilled water was added to dissolve. Further, 8.9 ml of 0.2 M phosphate buffer (pH 7.0) was added to prepare a linoleic acid / β-carotene solution. Next, 4.9 ml of the above linoleic acid / β-carotene solution was added to a spectrophotometer test tube cell into which 0.1 ml of the water-soluble peptide fraction had been dispensed in advance, and the absorbance (S ₀ ) at 470 nm was measured immediately after stirring. did. In the preparation of the linoleic acid / β-carotene solution, the amount of β-carotene solution added was appropriately increased or decreased so that S ₀ was about 1.2 (1.1 to 1.3). After S ₀ measured immediately placed tube cells in a thermostat at 50 ° C., and incubated for 30 min. After incubation,
Immediately absorbance (S3 ₀₎ was measured, the amount of decrease 470nm of absorbance at 30 minutes, was calculated ΔS = S ₀ -S3 _0. The blank was subjected to the same operation using 70% ethanol instead of the sample. That is, the absorbance immediately after the addition of the linoleic acid / β-carotene solution (B ₀ ) and the absorbance after holding at 50 ° C. for 30 minutes (B 3 ₀ ) were measured, and the decrease in absorbance at 470 nm in 30 minutes, ΔB = B ₀
-B3 ₀ were determined. Antioxidant activity was substituted into the following formula and expressed as an antioxidant rate (%).

[Equation 1]
Antioxidation rate (%) = [(ΔB−ΔS) / (ΔB)] × 100

As a positive control, a synthetic antioxidant BHT (butylhydroxyl toluene) prepared at 20 μM, 50 μM, 100 μM, and 200 μM was used. As a control, casein was treated in the same manner and evaluated for antioxidant activity. As a result, a strong antioxidant activity was confirmed in the fraction at the arrow position in FIG. Further, strong antioxidant activity was confirmed in the fractions 5, 6, 8, 9, and 10 in FIG.

(Peptide synthesis)
Seven types of peptides having the amino acid sequences represented by the above formulas (1) to (7) were synthesized with a peptide synthesizer. By using peptide synthesizer 431A (Applied Biosystems), parahydroxymethylphenoxymethyl polystyrene (
HMP) resin was used, and a 9-fluorenylmethyloxycarbonyl (Fmoc) group was used as the amino-terminal protecting group to sequentially extend the peptide chain from the C-terminal side to synthesize a linear protected peptide on a 0.25 mmol scale. In the presence of phenol, 1,2-ethanedithiol and thioanisole, the obtained HMP resin-bound protected peptide was simultaneously cleaved from the HMP resin and removed the protecting group with trifluoroacetic acid (TFA). After removing TFA by concentration under reduced pressure, the crude peptide was crystallized with ethyl ether, dissolved in 5% acetic acid, and lyophilized. The obtained linear crude peptide was subjected to HPLC [column: octadecyl 4P.
W (21.5 × 150 mm, Tosoh Corporation), elution: water-acetonitrile containing 0.1% TFA, gradient elution) to obtain a linear purified peptide (Phe-Gln-Ser-Glu-Glu-Gln).
The purity of the obtained purified peptide was 98% as a result of analysis by HPLC.
The other six types of peptides were synthesized in the same manner. All the purity was 98%. When the antioxidant activity of the peptides thus obtained was measured by the method of Test Example 2 shown below, strong antioxidant activity was confirmed for all peptides.
The peptide having the antioxidant action thus obtained can be used as an antioxidant as it is.

Test example 2

(Antioxidant activity of peptides)
Antioxidant activity of various peptides obtained in Example 3 was measured by the method of Osawa et al. (J. Agric. Food Chem.
, Vol.35, No.5, p.809-812, 1987). That is, rabbit stored blood and isotonic solution (10 mM phosphate buffer / 152 mM NaCl, pH 7.4) are mixed in equal amounts and mixed at 4 ° C. and 1,500 × g (3,500 rpm).
Then, it was washed by performing centrifugation for 20 minutes three times. A hypotonic solution (10 mM phosphate buffer, pH 7.4) was thoroughly mixed with the washed blood cells, and centrifugation was performed 4 times at 4 ° C., 20,000 × g (11,000 rpm) for 40 minutes. Antioxidant activity of the peptide was examined using the obtained loose precipitate (ghost). Each peptide obtained in Example 3 was prepared to have initial concentrations of 0, 0.01, 0.1, 1, and 10 mM, mixed with the erythrocyte membrane ghost, and an oxidizing agent was added to carry out an oxidation reaction. As a control, the same treatment was performed using vitamin E, which is a known antioxidant. Then perform TBA reaction, 532nm
The oxidation product was quantified by measuring the absorbance at. Antioxidant activity was evaluated by calculating the ghost oxidation rate defined by the following equation from the absorbance when each sample was added, with the absorbance when no sample was added as 100%. Note that the lower the ghost oxidation rate, the more ghost oxidation is suppressed, indicating that the antioxidant activity is high. In measuring the absorbance, the absorbance obtained by carrying out the TBA reaction without adding ghost as a control was subtracted from the absorbance as a blank value. The results are shown in Table 1.

[Equation 2]
Ghost oxidation rate (%) = (absorbance / absorbance without addition of sample) x 100

As can be seen in Table 1, when each peptide was added, it showed a concentration-dependent antioxidant activity.
From the results of this test example, Phe-Gln-Ser-Glu-Glu-Gln (however, serine (Ser) may be phosphorylated), Phe-Gln-Ser-Glu-Glu (however, Serine (Ser) may be phosphorylated.), Tyr-Leu-Lys-Thr-Val-Tyr-Gln-His-Gln, Met-His
Antioxidant activity (radical scavenger activity) for peptides consisting of amino acid sequences represented by -Gln-Pro-His-Gln, Asp-Lys-Ile-His-Pro, Asp-Lys-His-Tyr, or Ile-His This was found to be useful for the prevention and improvement of oxidative cell damage caused by active oxygen and lipid peroxide.

[Table 1]
Ghost oxidation rate (%)
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Sample concentration (mM) 0 0.01 0.1 1 10
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Vitamin E 100 93 88 74 59
Phe-Gln-Ser-Glu-Glu-Gln 100 82 67 32 15
Phe-Gln-Ser-Glu-Glu 100 80 68 40 20
Tyr-Leu-Lys-Thr-Val-Tyr-Gln-His-Gln 100 90 81 43 18
Met-His-Gln-Pro-His-Gln 100 89 77 61 15
Asp-Lys-Ile-His-Pro 100 82 57 42 25
Asp-Lys-His-Tyr 100 80 62 40 14
Ile-His 100 80 71 43 12
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Each component was mixed with the composition shown in Table 2, filled in a container, and then heat sterilized to produce an antioxidant beverage blended with the antioxidant peptide of the present invention.

[Table 2]
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Mixed isomerized sugar 15.4 (wt%)
Fruit juice 10.0
Citric acid 0.5
Phe-Gln-Ser-Glu-Glu (Example 1) 0.1
Fragrance 0.2
Water 73.8
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A dough having the composition shown in Table 3 was prepared, molded, and then baked to produce an antioxidant biscuit containing the antioxidant peptide of the present invention.

[Table 3]
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Flour 51.0 (wt%)
Sugar 20.0
Salt 0.5
Margarine 12.5
Egg 12.5
Water 2.5
Mineral mixture 0.8
Phe-Gln-Ser-Glu-Glu-Gln (Example 1) 0.2
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Each component was mixed by the composition shown in Table 4, and the feed for dog breeding which mix | blended the antioxidant peptide of this invention was manufactured.

[Table 4]
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Soybean cake 12.0 (wt%)
Nonfat dry milk 14.9
Soybean oil 4.0
Corn oil 2.0
Palm oil 28.0
Corn starch 15.0
Flour 8.0
Bran 2.0
Vitamin mixture 9.0
Mineral mixture 2.0
Cellulose 3.0
Met-His-Gln-Pro-His-Gln (Example 1) 0.1
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Claims (4)

A peptide having an antioxidative action consisting of an amino acid sequence represented by the following formula (4).
Met-His-Gln-Pro-His-Gln Formula (4) A peptide having an antioxidative action consisting of an amino acid sequence represented by the following formula (6).
Asp-Lys-His-Tyr formula (6)   A peptide having an antioxidative action, comprising an amino acid sequence according to claim 1 or 2 derived from milk protein. The antioxidant which uses any peptide represented by following formula (4) and (6) as an active ingredient.
Met-His-Gln-Pro-His-Gln Formula (4)
Asp-Lys-His-Tyr formula (6)

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