CN113925955B

CN113925955B - Antioxidant medicine or antioxidant whitening cosmetic

Info

Publication number: CN113925955B
Application number: CN202111434615.1A
Authority: CN
Inventors: 张冬久; 钟春秀
Original assignee: North American Life Sciences Shanghai Co ltd
Current assignee: North American Life Sciences Shanghai Co ltd
Priority date: 2021-11-29
Filing date: 2021-11-29
Publication date: 2022-10-25
Anticipated expiration: 2041-11-29
Also published as: CN113925955A

Abstract

The invention relates to an antioxidant medicine or an antioxidant whitening cosmetic. According to the invention, the fermentation broth with high oxidation resistance activity is obtained by fermenting the medlar through lactobacillus plantarum and aspergillus niger, three polypeptides with oxidation resistance and melanin synthesis inhibition are separated and identified from the fermentation broth, the polypeptides can enhance the proliferation of skin fibroblasts on one hand and inhibit the synthesis of melanin and improve the oxidation resistance of mice on the other hand, and the polypeptides have good application prospects in the preparation of medicines and whitening cosmetics.

Description

Antioxidant medicine or antioxidant whitening cosmetic

Technical Field

The invention relates to the field of medicines, and particularly relates to an antioxidant medicine or an antioxidant whitening cosmetic.

Background

The aging process of the body results from damage to cells and tissues by free radicals. Free ions are by-products produced by the human body during metabolism. With the age, the body's own redox system is out of balance, and the ability to scavenge free ions in the body is gradually weakened, so that free radicals can invade our body tissues. Antioxidant factors are natural ingredients, and can neutralize oxygen "free radicals" and protect your cells from damage. Poor dietary habits, heavy living pressure, and environmental pollution all consume a large amount of nutrients, and disturb the immune system of a human.

Oxidation is a necessary process for living organisms and can cause damage to biological macromolecules within the organism. Although the body itself has antioxidant defense systems, these systems are not completely effective in defending or repairing damage from oxidation. In this case, some antioxidant is added to help balance oxygen metabolism in vivo. Because of the safety issues associated with many chemically synthesized antioxidants, natural products with antioxidant activity are favored. Lactic acid bacteria (Lactcacid bacteria) are probiotics existing in human body, can tolerate the digestive tract environment, and have the functions of regulating normal flora of gastrointestinal tract, preventing and treating diarrhea, eliminating endotoxin, improving immunity of organism, etc. The research of some scholars at home and abroad shows that part of lactic acid bacteria have antioxidant activity. Animal experiments prove that part of lactobacillus acidophilus (L.acidophilus) has the capabilities of resisting lipid peroxidation and clearing hydroxyl radicals. However, the antioxidant activity and mechanism of these small fractions of lactic acid bacteria have not yet been clarified. It is believed that a small fraction of lactic acid bacteria may have some antioxidant enzyme substances (e.g. superoxide dismutase (SOD), NADH oxidase (NADH oxidase), catalase (CAT), etc.) to make them antioxidant.

In addition, with the progress of society and the improvement of living standard of people, the pursuit of health and happiness becomes a common appeal for people. The oriental people want to get white, ruddy, fine and smooth skin, and the European consumers want to eliminate or reduce chloasma and senile plaque, so the use of antioxidant cosmetics has become a necessity of daily life. However, because the antioxidant cosmetics added with chemical whitening components have cytotoxicity, allergenicity and some potential unsafe factors, the search and development of antioxidant cosmetics which are safe and efficient and have nutrition functions and are added with natural antioxidant components become hot spots of research in the field of cosmetics. China has abundant natural plant resources, extracts antioxidant components in natural products, and further develops medicaments or cosmetics with better antioxidant property, thereby having unique resource advantages.

However, at present, research on antioxidant drugs and corresponding cosmetics developed by fermentation of natural components is few, and the research is not enough.

Disclosure of Invention

The invention adopts specific microorganism to ferment medlar to obtain fermentation liquor, and the fermentation liquor is screened to obtain polypeptide which has the functions of resisting oxidation and inhibiting melanin synthesis.

In one aspect, the invention provides a method for preparing a fermentation broth with high antioxidant activity.

Specifically, the method comprises the steps of pouring dry medlar into a 500mL triangular flask, adding water for soaking until the medlar is full of water, adding water for pulping according to the material-liquid ratio of 1: 6 (m: V), weighing sucrose and yeast extract, adding into the prepared medlar pulp, and adjusting the pH value to 6.0. The bacterial concentration was adjusted to 10% by 2% inoculation ⁷ Mixing cfu/mL Lactobacillus plantarum CGMCC NO.1258 into fructus Lycii pulp, sealing with gauze, and placing into a shaking table (130 r.min.) ^-1 ) Fermenting at 37 deg.C for 48h.

The purchased Aspergillus niger CGMCC 3.3927 is planted on a PDA slant culture medium for activation for 3d, and the activated Aspergillus niger spores are inoculated on the PDA culture medium for constant temperature culture for 5d at 28 ℃. Taking a certain amount of Aspergillus niger spores from PDA culture medium in physiological saline, adjusting thallus concentration to 10 ⁶ cfu/mL. Inoculating and adding the lactobacillus plantarum fermentation liquor which is fermented for 48 hours according to the inoculation amount of 6%, uniformly mixing, fermenting for 80 hours at the temperature of 30 ℃ at the speed of 100r/min, centrifuging at the speed of 4000r/min for 10min after fermentation is finished, and taking supernate, thus obtaining the fermentation liquor.

Furthermore, specific polypeptides with high antioxidant activity for inhibiting melanin synthesis are obtained by screening according to the activity of each component in the fermentation liquor, wherein the specific polypeptides are YX-1 polypeptide, YX-2 polypeptide and YX-3 polypeptide. The three polypeptides have good safety for resisting erythrolysis, and the mouse test in the embodiment also proves that the polypeptides have no animal toxicity and good safety effect.

Furthermore, the invention also provides a pharmaceutical composition with antioxidant activity.

The pharmaceutical composition contains SEQ ID NO:1 and a pharmaceutically acceptable carrier.

Further provided herein is a pharmaceutical composition comprising a therapeutically effective amount of the above-described peptide product or an acceptable salt thereof, and at least one pharmaceutically acceptable carrier or excipient. In some embodiments, the carrier is a water-based carrier. In some embodiments, the carrier is a non-aqueous based carrier. In some embodiments, the non-aqueous based carrier is a hydrofluoroalkane solvent containing submicron anhydrous-lactose or other excipients.

As used herein, "carrier" includes any solvent, dispersion medium, carrier, coating, diluent, isotonic agent, absorption delaying agent, buffer, carrier solution, suspension, colloid, and the like. The use of such media and/or agents for pharmaceutically active substances is well known in the art. Except insofar as any conventional media or agent is incompatible with the active ingredient, its use in the therapeutic compositions is contemplated. Supplementary active ingredients may also be incorporated into the composition. As used herein, "pharmaceutically acceptable" refers to a material that is not biologically or otherwise undesirable, i.e., the material may be administered to an individual along with a polypeptide without causing any undesirable biological effects or interacting in a deleterious manner with any of the other components of the pharmaceutical composition in which it is contained.

The pharmaceutical composition may be formulated in various forms suitable for the preferred route of administration. Thus, the compositions may be administered by known routes, including, for example, orally, parenterally (e.g., intradermally, transdermally, subcutaneously, intramuscularly, intravenously, intraperitoneally, etc.) or topically (e.g., intranasally, intrapulmonary, intramammary, intravaginally, intrauterine, intradermally, transdermally, rectally, etc.). A pharmaceutical composition may be administered to a mucosal surface, for example by administration to, for example, the nasal or respiratory mucosa (e.g. by a spray or aerosol). A composition may also be administered by sustained or delayed release.

In some embodiments, the method may comprise administering to the subject sufficient polypeptide to provide a dose of, for example, about 10ng/kg to about 10mg/kg, although in some embodiments, the method may be performed by administering a dose of the scFv antibody that is outside of this range. Thus, in some embodiments, the method can include administering the polypeptide in an amount effective to provide a minimum dose of at least 100ng/kg, e.g., at least 500ng/kg, at least 5mg/kg, at least 1mg/kg, at least 2mg/kg, at least 5mg/kg, at least 7mg/kg, at least 10mg/kg, at least 250mg/kg, at least 500mg/kg, at least 1mg/kg, at least 5mg/kg, or at least 10mg/kg. In some embodiments, the method can include administering the polypeptide in an amount effective to provide a maximum dose of no more than 10mg/kg, e.g., no more than 10mg/kg, no more than 50g/kg, no more than 2mg/kg, no more than 1mg/kg, no more than 0.1mg/kg. In some embodiments, the method can comprise administering the polypeptide in an amount effective to provide a dose that falls within a range having an endpoint defined by any of the minimum doses listed above and any of the maximum doses listed above that are greater than the minimum dose. In some of these embodiments, the method comprises administering to the subject sufficient polypeptide to provide a dose of about 1mg/kg to about 5 mg/kg.

The pharmaceutical composition of the present invention can be formulated into dosage forms in the form of an external solvent such as an acid agent, granules, a purified capsule, a suspension, a syrup, an aerosol, or a sterile injection solution according to a conventional method, and can be used for the above-mentioned composition. Carrier excipients and diluents which may be included are: lactose, d.k.s.c.hand, kresoxim-methyl, mannitol, xylose, mannitol, starch, locust rubber, phospholipid, calcium, silica gel, cellulose, methyl cellulose, microcrystalline cellulose, polyvinyl pyrrolidone; water; methyl oxybenzone; oxybenzone; magnesium removal; a stearate ester; and mineral oil; when formulated, the composition is formulated with a diluent or excipient such as a filler, an enhancer, a binder, a wetting agent, a disintegrant, or a surfactant. Solid preparations for oral administration include a granular preparation of a refined epoxy resin, a capsule preparation, etc., which contains at least one excipient selected from the above-mentioned compounds, such as calcium carbonate, sucrose or lactose gel. And mixing the components. In addition to the simple excipient, a lubricant such as magnesium foam is used. Liquid phase formulations for hard spheres include: the suspending agent comprises liquid, emulsion, syrup, etc., besides the common simple diluent-water cubic paraffin, it can also comprise various excipients, such as wetting agent, sweetener, aromatic, preservative, etc. The preparation for non-oral administration comprises sterile aqueous solution achiral solvent suspending agent emulsion freeze-drying preparation adjuvant. Achiral solvent suspensions can be used in injectable esters such as propylene glycol (glycol) olive oil. The mechanism of the adjuvant may be gastrin (witepsol), macro Goltwin (tween), 61-Carkol lauryl triglyceride, etc.

The invention further provides an antioxidant whitening cosmetic with antioxidant and melanin synthesis inhibiting functions, which contains the amino acid sequence shown in SEQ ID No: 1.

The cosmetic composition of the present invention contains the effective ingredient, and may contain, in addition to the above-mentioned extract, ingredients generally used in cosmetic compositions, such as stabilizer-dissolving agents, vitamin pigments, perfumes, and other conventional adjuvants, and a carrier.

The cosmetic raw material composition of the present invention can be prepared into any dosage form generally manufactured in the industry, such as emulsion cream, lotion, foundation emulsion, beauty lotion, hair cosmetic, and the like.

Advantageous effects

According to the invention, the fermentation broth with high oxidation resistance activity is obtained by fermenting the medlar through lactobacillus plantarum and aspergillus niger, three polypeptides with oxidation resistance and melanin synthesis inhibition are separated and identified from the fermentation broth, the polypeptides can enhance the proliferation of skin fibroblasts on one hand and inhibit the synthesis of melanin and improve the oxidation resistance of mice on the other hand, and the polypeptides have good application prospects in the preparation of medicines and whitening cosmetics.

Drawings

FIG. 1 is a graph showing the results of the detection of antioxidant activity of the polypeptide

Detailed Description

The following examples and experimental examples are provided to facilitate understanding of the present invention. However, the following examples and experimental examples are provided only to make the present invention more easily understood, and the contents of the present invention are not limited by the following examples and experimental examples.

Example 1 preparation of a fermentation broth of a Lycium barbarum polypeptide

Pouring 20g of dry medlar into a 500mL triangular flask, adding water for soaking until the medlar is full, adding water for pulping according to the material-liquid ratio of 1: 6 (m: V), weighing 1g of sucrose and 0.5g of yeast extract, adding into the prepared medlar pulp, and adjusting the pH value to 6.0. The concentration of the cells was adjusted to 10% by 2% inoculation ⁷ Mixing cfu/mL Lactobacillus plantarum CGMCC NO.1258 into fructus Lycii pulp, sealing with gauze, and placing into a shaking table (130 r.min.) ^－1 ) Fermenting at 37 deg.C for 48h.

The purchased Aspergillus niger CGMCC 3.3927 is planted on a PDA slant culture medium for activation for 3d, and the activated Aspergillus niger spores are inoculated on the PDA culture medium for constant temperature culture for 5d at 28 ℃. Taking a certain amount of Aspergillus niger spores from PDA culture medium, adding into physiological saline, and adjusting thallus concentration to 10 ⁶ cfu/mL. Inoculating according to the inoculation amount of 6 percent, adding the lactobacillus plantarum into lactobacillus plantarum fermentation liquor fermented for 48 hours, uniformly mixing, fermenting for 80 hours at the temperature of 30 ℃ at the speed of 100r/min, centrifuging at the speed of 4000r/min for 10 minutes after fermentation is finished, taking supernate, and storing at the temperature of 4 ℃ for later use.

Example 2 preparation of Lycium barbarum polypeptide fermentation broth comparative example 1

Pouring 20g of dry medlar into a 500mL triangular flask, adding water for soaking until the medlar is full, adding water for pulping according to the material-liquid ratio of 1: 6 (m: V), weighing 1g of sucrose and 0.5g of yeast extract, adding into the prepared medlar pulp, and adjusting the pH value to 6.0. The bacterial concentration was adjusted to 10% by 2% inoculation ⁷ Mixing cfu/mL Lactobacillus plantarum CGMCC NO.1258 into fructus Lycii pulp, sealing with gauze, and placing into a shaking table (130 r.min.) ^－1 ) Fermenting at 37 deg.C for 48h. Centrifuging at 4000r/min for 10min after fermentation, and collecting supernatant, and storing at 4 deg.C for use.

Example 3 preparation of a fermentation broth of Lycium barbarum polypeptide control example 2

The purchased Aspergillus niger CGMCC 3.3927 is planted on a PDA slant culture medium for activation for 3d, and the activated Aspergillus niger spores are inoculated on the PDA culture medium for constant temperature culture for 5d at 28 ℃. Taking a certain amount of Aspergillus niger spores from PDA culture medium, adding into physiological saline, and adjusting thallus concentration to 10 ⁶ cfu/mL. Inoculating the mixture according to 6% inoculum size, and adding into culture medium prepared by adding 20g dryPouring the medlar into a 500mL triangular flask, adding water for soaking until the medlar is full, adding water for pulping according to the material-liquid ratio of 1: 6 (m: V), weighing 1g of sucrose and 0.5g of yeast extract, adding into the prepared medlar pulp, and adjusting the pH value to 6.0. Uniformly mixing, fermenting for 80h at 30 ℃ at 100r/min, centrifuging at 4000r/min for 10min after fermentation, taking supernatant, and storing at 4 ℃ for later use.

Example 4 antioxidant capacity assay of Lycium barbarum polypeptide fermentation broth

Measurement of DPPH scavenging Activity: preparing 0.2mmol/L DPPH by 95% ethanol, mixing 100uL of the fermentation liquid obtained in example 1-3 with 100uL of DPPH solution uniformly in a 96-hole enzyme label plate, reacting 30min at normal temperature in the dark, and measuring the light absorption value A1 at the position of 517nm. 100uL of deionized water was reacted with 100uL of DPPH solution instead of 100uL of 95% ethanol to obtain a blank control group (A0), and 100uL of DPPH solution was reacted with 100uL of deionized water to obtain a negative control group (A2). The DPPH clearance calculation formula is as follows: DPPH clearance (%) = (A2-A1)/(A2-A0) × 100%, and the results are shown in table 1 below.

TABLE 1 DPPH clearance of various groups of fermentation broths

Group of	DPPH clearance (%)
		Example 1 fermentation broth	98.5±6.6
Example 2 fermentation broth	79.3±4.5
		Example 3 fermentation broth	82.5±2.4

From the results in table 1, it can be seen that the fermentation broth obtained by fermenting lycium barbarum with specific lactobacillus plantarum and aspergillus niger has a higher DPPH clearance rate (98.5 ± 6.6)%, which is better than the fermentation effect obtained by fermenting with lactobacillus plantarum or aspergillus niger alone.

EXAMPLE 5 purification and isolation of the antioxidant Polypeptides in fermentation broths

The fermentation liquid of example 1 was centrifuged at 12000r/min for 10min, after ultrafiltration and concentration, DEAE-Sepharose FF anion exchange chromatography was performed, and then linear gradient elution was performed using a buffer solution containing 0 to 1.0mol/L of NaC1 to detect antioxidant activity. Collecting 5 groups of active components with strong antioxidant activity, and respectively ultrafiltering and concentrating. Then loading the SephadexG-15 molecular sieve gel filtration chromatography column, collecting 4 groups of active components, loading the active components on a C18 column balanced by 0.1% TFA double distilled water, performing 0.8mL/min linear gradient elution by using 2% -100% acetonitrile (0.1% TFA), collecting samples by parts, performing ultrafiltration concentration on the active 3 groups of collected peaks again, performing RT-HPLC separation, freeze-drying the samples, hydrolyzing the freeze-dried samples at 110 ℃ by using 6mol/L HC1, then evaporating the hydrolysate to dryness, dissolving the hydrolysate by adding 5mL of 0.02mol/L HCl, and performing amino acid composition analysis on an L-8800 full-automatic amino acid analyzer to obtain 3 polypeptides with better antioxidant activity, which are respectively named as YX-1, YX-2 and YX-3 polypeptides, wherein the YX-2 sequence is shown as SEQ ID NO:1 is shown. And (3) preparing the polypeptide for later use after the polypeptide is consigned to Shanghai for synthesis.

Example 6 determination of antioxidant Activity of YX-2 Polypeptides

The hydroxyl radical (OH) scavenging capacity is measured by adopting an o-diazaphenanthrene-Fe 2+ oxidation method, taking 1mL of 0.75mmol/L o-diazaphenanthrene solution in a test tube, sequentially adding 2mL of phosphate buffer solution (0.2 mol/L, pH7.4) and 1mL of distilled water and 1mL of 0.75mmol/L ferrous sulfate solution, fully and uniformly mixing, adding 0.01% H by volume fraction ₂ O ₂ 1mL, reacting at 37 ℃ for 60min, and measuring the absorbance at 536nm to obtain Ap. The formula for the hydroxyl radical scavenging ability is as follows: clearance (%) = As-Ap/Ao-Ap × 100 formula: replacement of H with 1mL polypeptide solution ₂ O ₂ The absorbance measured was taken As; 1mL of distilled water was used in place of H ₂ O ₂ The absorbance measured was designated as Ao. Taking VC asAnd (4) positive control. The results are shown in FIG. 1.

As can be seen from FIG. 1, the clearance of the polypeptide to the hydroxyl free radical also rapidly increases with the increase of the concentration of the YX-2 polypeptide and the VC, and when the concentration is 250 mug/mL, the clearance of the polypeptide reaches about 82 percent, is basically similar to the clearance of the Vc, and has better effect.

Example 7 Activity assay of YX-2 Polypeptides on fibroblasts

Fibroblast proliferation assay: selecting fibroblasts with good logarithmic growth phase state, digesting with 0.25% trypsin, centrifuging, suspending in DMEM medium containing 10% fetal calf serum, and counting; fibroblasts were seeded in 96-well culture plates at about 5X 10 cells per well ³ And a blank control without added cells, the marginal wells filled with sterile Phosphate Buffered Saline (PBS), at 37 ℃ C. And 5% CO ₂ Culturing overnight in the environment; adding the polypeptide solution to be tested according to the respective final volume fraction, using the untreated group as a cell control group, each group having 3 replicate wells, at 37 deg.C, 5% CO ₂ Culturing in the environment for 48h. Adding 5g/L MTT solution 4h before the culture is finished, and terminating the culture after continuing the culture for 4 h; the liquid in the hole is sucked and removed, washed by PBS for 1 time, and added with DMSO to dissolve the crystal; the absorbance of each well was measured at a wavelength of 570nm using an M3 plate reader. Cell viability = (assay well absorbance value-blank control group absorbance value)/(cell control group absorbance value-blank control group absorbance value) X100%. The results are shown in Table 2.

TABLE 2 cell viability after treatment with different concentrations of polypeptide

Concentration group	Cell survival rate (%)
		0	100±2.8
10μg/mL	122.6±3.5
		100μg/mL	139.1±5.1
200μg/mL	165.2±7.5
		1mg/mL	171.4±8.1

Fibroblasts have an important role in maintaining the elastic and elastic properties of the skin and aging. As can be seen from Table 2, the polypeptide has a certain promotion effect on the proliferation of fibroblasts, and the highest promotion effect of 171.4 +/-8.1 percent can be achieved at the concentration of 1 mg/mL.

EXAMPLE 8 YX-2 whitening Capacity test

Intracellular tyrosinase activity inhibition assay: b16 cells in the logarithmic growth phase were seeded on 6-well cell culture plates and cultured overnight. The polypeptide with a final volume fraction of 200. Mu.g/mL was added separately, and the untreated group was used as a cell control group, with 2 duplicate wells per group. After 48h of culture, the cells were washed 1 time with PBS, 100. Mu.L of lysate was added to each well, the cells were scraped off and collected, and the supernatant was centrifuged. The 5OL cell supernatant was transferred to a 96-well plate, followed by addition of 50. Mu.L of 1% L-dopa solution and incubation at 37 ℃ for 1 hour. The M3 plate reader reads the absorbance at 475 nm. Relative tyrosinase activity = (assay well absorbance value — blank control absorbance value)/(cell control absorbance value — blank control absorbance value) x100%. The result shows that the relative tyrosinase activity in the cell is only (40.1 +/-4.1)%, which indicates that the relative tyrosinase activity of B16 is obviously reduced under the action of the YX-2 polypeptide, and the polypeptide has an inhibition effect on the tyrosinase activity.

Example 9 antioxidant assay of YX-2 Polypeptides in mice

40 male Kunming mice with the weight of 20-25 g are randomly divided into four groups, namely a normal control group, a D-galactose oxidative damage model group, a polypeptide treatment group and a Vc positive control group. Except for the normal control group, the mice of other groups are injected with D-galactose 400mg/kg bw subcutaneously every day for 32 days, the mice of the control group are injected with physiological saline with the same amount every day subcutaneously, the polypeptide group and the Vc group are respectively irrigated with stomach at the dosage of 1mg/kg bw every day, the normal control group and the model group are irrigated with distilled water with the same amount, and the mice are weighed for 1 time every 3 days. After injecting D-galactose and gavage polypeptide for 2h at 32D, dissecting the mouse, taking 0.2g of liver tissue, cutting into pieces, placing in a glass homogenizer, adding 9 times of cold normal saline to prepare 10% (W/V) liver tissue homogenate, centrifuging at 3000r/min for 10min, and taking the supernatant to measure the activity of the liver cell SOD and GSH-Px and the content of MDA. Determining the MDA content of the liver by adopting a thiobarbituric acid (TBA) colorimetric method; SOD is measured by xanthine oxidase; GSH-Px activity was determined by the DTNB method. The results are shown in Table 3.

TABLE 3 polypeptide vs mouse liver MDA and Effect of SOD and GSH-Px Activity

Group of	MDA(μmol/g)	SOD(U/mg)	GSH-Px(U/mg)
				Control group	14.5±1.2	517±21	616±30
Model set	23.1±1.1	454±12	424±31
				Polypeptide group	18.0±1.2	533±24	592±23
Vc control group	19.5±1.1	490±24	573±33

As can be seen from Table 3, compared with the control group, the MDA content in the liver of the mice in the oxidation model group is remarkably increased, and the SOD activity and the GSH-Px activity are remarkably reduced. Compared with the model group, the MDA content of the mouse livers of the polypeptide group and the positive control Vc group is obviously reduced, and the GSH-Px activity and the SOD activity are both obviously improved. Particularly, MDA of the polypeptide group reaches 18.0 +/-1.2 mu mol/g, SOD reaches 533 +/-24U/mg, GSH-Px reaches 592 +/-23U/mg, and the result has statistical significance compared with the P <0.05 of a control group.

The foregoing description of the present invention is intended to be exemplary, and a person having ordinary skill in the art to which the present invention pertains can easily transform the present invention into other specific forms without changing the technical idea or essential features of the present invention. As can be understood in the affirmative. Therefore, the above-described examples and experimental examples should be construed as being indicative, but not limiting, of all aspects.

Sequence listing

<110> Beijing Yunshenda Biotechnology development Co., ltd

<120> an antioxidant drug or an antioxidant whitening cosmetic

<160> 1

<170> SIPOSequenceListing 1.0

<210> 1

<211> 16

<212> PRT

<213> Artificial Sequence (Artificial Sequence)

<400> 1

Arg Ile Trp Glu Ser Ala Phe Ile Ser Tyr Val Ile Cys Asn Tyr Lys

1 5 10 15

Claims

1.SEQ ID NO:1 in the preparation of a medicament for enhancing the oxidation resistance and inhibiting the synthesis of melanin.

2. The use according to claim 1, wherein the medicament further comprises a pharmaceutically acceptable carrier.

3, SEQ ID NO:1 in the preparation of antioxidant whitening cosmetics.

4. An antioxidant whitening cosmetic with antioxidant and melanin synthesis inhibiting functions contains an amino acid sequence shown in SEQ ID No:1, or a polypeptide YX-2.

5. Use according to claim 3, characterized in that the cosmetic comprises stabilizers and solubilizers.

6. A cosmetic product according to claim 4, wherein the cosmetic product comprises a stabilizing agent and a solubilizing agent.

7. Use according to claim 3, wherein the cosmetic formulation is an emulsion.

8. The cosmetic of claim 4, wherein the cosmetic is in the form of an emulsion.