A polypeptide and its use in the preparation of a whitening product
By providing a peptide with the amino acid sequence IVHRKCF, the problem of peptide resource scarcity in whitening products is solved, achieving effective tyrosinase inhibition, melanin inhibition, and antioxidant effects, making it suitable for the preparation of whitening products.
Patent Information
- Application Number
- CN202510263330.8
- Authority / Receiving Office
- CN · China
- Patent Type
- Patents(China)
- Current Assignee / Owner
- Filing Date
- 2025-03-06
- Publication Date
- 2025-11-18
- Estimated Expiration
- 2045-03-06
AI Technical Summary
Existing skin whitening products lack peptide resources, chemical and physical whitening methods are irritating, and natural whitening methods have weak effects and slow onset of action.
A polypeptide with the amino acid sequence IVHRKCF is provided for the preparation of tyrosinase inhibitors, melanin inhibitors, and antioxidant products, which achieve whitening effects by inhibiting tyrosinase activity, inhibiting melanin production, and having antioxidant effects.
Peptides can effectively inhibit tyrosinase activity, significantly suppress melanin production, and have excellent antioxidant activity, making them suitable for preparing skin whitening products.
Smart Images
Figure CN120098074B_ABST
Abstract
Description
TECHNICAL FIELD
[0001] The present application belongs to the technical field of polypeptides. More particularly, it relates to a polypeptide and its application in preparing whitening products. BACKGROUND
[0002] With the enhancement of ultraviolet radiation and the increase of work pressure, people are more likely to have problems such as dull skin and increased color spots. In order to improve skin color, the commonly used methods at present are chemical whitening, physical whitening, natural whitening and the like. Chemical whitening is to use cosmetics containing chemical whitening ingredients such as arbutin to inhibit the generation of melanin, and physical whitening is to use means such as photorejuvenation and laser whitening to remove melanin on the surface of the skin, but both of these two methods have certain irritation and are not suitable for long-term use. Natural whitening is to use cosmetics containing natural whitening ingredients such as pearl powder, but the whitening effect of natural whitening ingredients is relatively weak and slow.
[0003] Polypeptides are highly valued in the development of whitening products due to their high safety, fast effect and the like, but the existing polypeptide resources available for whitening are still relatively scarce. SUMMARY
[0004] The present application aims at the deficiencies of the prior art, and provides a polypeptide with an amino acid sequence as shown in SEQ ID NO: 1, enriches the polypeptide resource library with whitening effect, and provides more raw material options for whitening products.
[0005] The first object of the present application is to provide a polypeptide.
[0006] The second object of the present application is to provide the application of the above-mentioned polypeptide in preparing whitening products.
[0007] The third object of the present application is to provide the application of the above-mentioned polypeptide in preparing tyrosinase inhibitors.
[0008] The fourth object of the present application is to provide the application of the above-mentioned polypeptide in preparing melanin inhibitors.
[0009] The fifth object of the present application is to provide the application of the above-mentioned polypeptide in preparing antioxidant products.
[0010] The sixth object of the present application is to provide related biological materials of polypeptides.
[0011] The seventh object of the present application is to provide the application of the above-mentioned related biological materials in preparing whitening products.
[0012] The eighth object of the present application is to provide the application of the above-mentioned related biological materials in preparing tyrosinase inhibitors.
[0013] The ninth object of the present application is to provide the application of the above-mentioned related biological materials in preparing melanin inhibitors.
[0014] The tenth objective of this invention is to provide the application of the aforementioned biomaterials in the preparation of antioxidant products.
[0015] The above-mentioned objective of this invention is achieved through the following technical solution:
[0016] This invention provides a polypeptide whose amino acid sequence is shown in SEQ ID NO:1. SEQ ID NO:1: IVHRKCF.
[0017] The effects of the above-mentioned polypeptides are: (1) they can effectively inhibit the activity of tyrosinase and are suitable for the preparation of tyrosinase inhibitors; (2) they can significantly inhibit the production of melanin and are suitable for the preparation of melanin inhibitors; (3) they have excellent antioxidant activity and are suitable for the preparation of antioxidant products.
[0018] In summary, the above-mentioned polypeptides are also suitable for preparing skin whitening products. Therefore, the application of the above-mentioned polypeptides in the preparation of skin whitening products, tyrosinase inhibitors, melanin inhibitors, and antioxidant products should all be within the scope of protection of this invention.
[0019] Based on this, the present invention also provides related biomaterials of the above-mentioned polypeptides and their applications in the preparation of whitening products, tyrosinase inhibitors, melanin inhibitors, and antioxidant products. The related biomaterials are nucleic acid molecules that can express the polypeptides, or recombinant DNA, expression cassettes, transposons, vectors, or host cells containing the nucleic acid molecules.
[0020] In addition, the present invention also provides a product comprising the above-mentioned polypeptide and / or its related biomaterials.
[0021] Preferably, the relevant biological material is a nucleic acid molecule capable of expressing the polypeptide, or recombinant DNA, expression cassette, transposon, vector, or host cell containing the nucleic acid molecule.
[0022] Preferably, the product is a cosmetic or a pharmaceutical.
[0023] More preferably, it also contains excipients acceptable for use in cosmetics or pharmaceuticals.
[0024] The present invention has the following beneficial effects:
[0025] The polypeptides of this invention not only effectively inhibit tyrosinase activity, making them suitable for preparing tyrosinase inhibitors; they also significantly inhibit melanin production, making them suitable for preparing melanin inhibitors; and they possess excellent antioxidant activity, making them suitable for preparing antioxidant products. Therefore, the polypeptides of this invention are highly suitable for preparing skin-whitening products. Attached Figure Description
[0026] Figure 1 This is the result of purity identification of the polypeptide.
[0027] Figure 2 This is the mass spectrometry identification result of the polypeptide.
[0028] Figure 3 These are the results of the peptide toxicity test.
[0029] Figure 4 The image is a Lineweaver-Burk diagram.
[0030] Figure 5 This is a graph showing the relationship between the slope of the straight line and the peptide concentration.
[0031] Figure 6 The graph shows the results of tyrosinase activity assay after peptide treatment.
[0032] Figure 7 The graph shows the results of melanin content determination after peptide treatment.
[0033] Figure 8 This is a graph showing the results of SOD activity determination after peptide treatment.
[0034] Figure 9 The image shows the results of GSH-PX activity determination after peptide treatment.
[0035] Figure 10 The graph shows the results of the determination of the relative ROS activity after peptide treatment. Detailed Implementation
[0036] The present invention will be further described below with reference to the accompanying drawings and specific embodiments, but the embodiments do not limit the present invention in any way. Unless otherwise specified, the reagents, methods and equipment used in the present invention are conventional reagents, methods and equipment in this technical field.
[0037] Unless otherwise specified, all reagents and materials used in the following examples are commercially available.
[0038] All experiments in this embodiment of the invention consisted of three parallel groups, and the final data were expressed as mean ± standard deviation. Statistical graphs were generated using Origin 2019 software, and the experimental results were analyzed using IBM SPSS Statistics 26 software with one-way ANOVA of the group means. P < 0.05 indicated that the difference was statistically significant.
[0039] Example 1: Synthesis and Identification of Polypeptides
[0040] The peptide (amino acid sequence shown in SEQ ID NO:1: IVHRKCF) was synthesized with the assistance of Shanghai Aminolink Biotechnology Co., Ltd., and the purity of the peptide was identified by mass spectrometry.
[0041] I. Purity Identification
[0042] The purity of peptides was determined using high performance liquid chromatography (HPLC).
[0043] The identification conditions for high-performance liquid chromatography (HPLC) are as follows:
[0044] Column: Inertsil ODS-SP (4.6×250mm);
[0045] Mobile phase A: Water (containing 0.1% (v / v) trifluoroacetic acid);
[0046] Mobile phase B: Acetonitrile (containing 0.1% (v / v) trifluoroacetic acid);
[0047] Elution gradient: 0→25 min, 99% (v / v)→50% (v / v) A;
[0048] Flow rate: 1 mL / min;
[0049] Detection wavelength: 220nm;
[0050] Sample loading volume: 30 μL.
[0051] The results of purity testing are as follows Figure 1 As shown, the main peak in the polypeptide of this embodiment accounts for the majority, with only a few impurity peaks appearing, and the purity is as high as 96.86%.
[0052] II. Mass Spectrometry Identification
[0053] The molecular weight of the peptides was identified using ESI-MS mass spectrometry.
[0054] The identification conditions for ESI-MS mass spectrometry are as follows:
[0055] Mobile phase A: Water (containing 0.1% (v / v) trifluoroacetic acid);
[0056] Mobile phase B: Acetonitrile (containing 0.1% (v / v) trifluoroacetic acid);
[0057] Flow rate: 2 mL / min;
[0058] Running time: 4 minutes;
[0059] Operating mode: Positive ion mode;
[0060] Scan range: 0–2000 Da.
[0061] The results of mass spectrometry identification are as follows Figure 2 As shown, the molecular ion peak m / z of the polypeptide in this embodiment is 903.26, carrying one charge, which is consistent with its theoretical molecular weight value, indicating that the polypeptide synthesized in this embodiment is the polypeptide with the amino acid sequence shown in SEQ ID NO:1.
[0062] Example 2: The polypeptide is non-toxic to cells.
[0063] I. Solution Preparation
[0064] Sample solution: In a clean bench, the polypeptide obtained in Example 1 was dissolved in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics to make the final concentrations 100, 200 and 400 μM respectively, and then sterilized with a 0.22 μm needle filter.
[0065] Kojic acid solution: In a clean bench, dissolve kojic acid in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics to a final concentration of 300 μM, and then sterilize with a 0.22 μm syringe filter.
[0066] II. Experimental Grouping and Processing
[0067] Dosing sample well (A) 样 Logarithmic growth phase melanoma cells (B16F10) were seeded at a density of 3000 cells / well in 96-well plates and cultured at 37°C for 24 h. After acclimatization, the supernatant was discarded, and 100 μL of sample solution / kojic acid solution was added to each well. After culturing at 37°C for 24 h, the supernatant was discarded, and 110 μL of 10% (v / v) CCK-8 solution was added under light-protected conditions. After incubation at 37°C for 30 min, the absorbance of each well was measured at 450 nm.
[0068] Blank hole (A) 空 Add 100 μL of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin antibiotics to a 96-well plate. After acclimatization culture at 37°C for 24 h, discard the supernatant. Add 100 μL of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin antibiotics to the plate. After culturing at 37°C for 24 h, discard the supernatant. Add 110 μL of 10% (v / v) CCK-8 solution under dark conditions. Incubate at 37°C for 30 min. Measure the absorbance of each well at 450 nm.
[0069] Control well (A0): Logarithmic growth phase melanoma cells (B16F10) were seeded at a density of 3000 cells / well in 96-well plates and cultured at 37°C for 24 h. After acclimatization, the supernatant was discarded, and 100 μL of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin-streptomycin antibiotics was added. After culturing at 37°C for 24 h, the supernatant was discarded, and 110 μL of 10% (v / v) CCK-8 solution was added under light-protected conditions. After incubation at 37°C for 30 min, the absorbance of each well was measured at 450 nm.
[0070] According to the formula "Cell viability (%) = [(A)", 样 -A 空 ) / (A0-A 空 The cell viability after treatment with the sample solution / kojic acid solution was calculated using the formula 100% × 100% to evaluate the toxicity of the peptide.
[0071] III. Experimental Results
[0072] The results are as follows Figure 3 As shown, compared with the blank wells, there was no significant difference in the activity of B16F10 cells after treatment with the 100–400 μM peptide. This indicates that the peptide of the present invention is non-toxic to cells and has high safety.
[0073] Example 3: The peptide can inhibit tyrosinase activity in vitro.
[0074] I. Solution Preparation
[0075] Sample solutions: The polypeptide obtained in Example 1 was dissolved in phosphate buffer at pH 6.8 to achieve final concentrations of 0.2, 0.4, 0.6, 0.8, and 1.0 mg / mL.
[0076] L-Tyrosine Solution: Dissolve L-tyrosine in phosphate buffer solution at pH 6.8 to achieve a final concentration of 0.5 mg / mL.
[0077] Tyrosinase solution: Dissolve tyrosinase in phosphate buffer at pH 6.8 to achieve a final concentration of 500 U / mL.
[0078] II. Experimental Grouping and Processing
[0079] Solvent blank well (A1): Add 40 μL of PBS solvent to the 96-well plate.
[0080] Solvent background well (A2): Add 40 μL of L-tyrosine solution to the 96-well plate.
[0081] Sample background well (A3): Add 40 μL of sample solution to the 96-well plate.
[0082] Sample reaction well (A4): Add 40 μL of L-tyrosine solution and 40 μL of sample solution to the 96-well plate.
[0083] The total solution volume was 110 μL (made up with PBS). After incubation at 37 °C for 15 min, 20 μL of tyrosinase solution was added to each well, and the mixture was incubated at 37 °C for another 10 min. The absorbance was measured at 475 nm, and the tyrosinase inhibition rate was calculated using the formula "tyrosinase inhibition rate (%) = [1 - (A4 - A3) / (A2 - A1)] × 100%".
[0084] III. Experimental Results
[0085] The results showed that the IC50 of the peptide was... 50 The value was 0.80±0.03mM, indicating that the polypeptide of the present invention can significantly inhibit the activity of tyrosinase and is suitable for the preparation of whitening products.
[0086] Example 4: The peptide inhibits tyrosinase in a mixed manner.
[0087] I. Solution Preparation
[0088] Sample solutions: The polypeptide obtained in Example 1 was dissolved in phosphate buffer at pH 6.8 to achieve final concentrations of 0, 0.10, 0.15, and 0.20 mM.
[0089] L-Tyrosine Solution: L-tyrosine was dissolved in phosphate buffer solution at pH 6.8 to achieve final concentrations of 0.75, 1.00, 1.25, 2.00, and 3.00 mM.
[0090] Tyrosinase solution: Dissolve tyrosinase in phosphate buffer at pH 6.8 to achieve a final concentration of 500 U / mL.
[0091] II. Experimental Grouping and Processing
[0092] In a 96-well plate, add 40 μL of L-tyrosine solution, 40 μL of sample solution, and 30 μL of phosphate buffer (pH = 6.8). Incubate at 37°C for 10 min, then add 20 μL of tyrosinase solution, and incubate again at 37°C for 10 min. Measure the absorbance at 475 nm at 0 and 10 min of incubation. Calculate the absorbance using the formula: "Reaction rate (%) = (A... 10 -A0) / 10]×100%""A 10 The absorbance at time A1 is the value at time 10 min, and A0 is the absorbance at time 0 min. The reaction rate of the peptide with tyrosinase was calculated, and a Lineweaver-Burk plot was plotted based on the calculation results. The results are shown below. Figure 4 As shown, and according toFigure 4 The relationship between the slope of each straight line and the peptide concentration is plotted. Figure 5 .
[0093] III. Experimental Results
[0094] Depend on Figure 4 As can be seen, the maximum reaction rate (Vmax, the reciprocal of the y-intercept) and the Michaelis constant (Km, the reciprocal of the x-intercept) in the coordinate graph both change with the peptide concentration, and all four straight lines intersect in the second quadrant of the coordinate axis, indicating that the inhibition of tyrosinase by the peptide is a mixed result of competitive and non-competitive reactions, that is: the type of inhibition of tyrosinase by the peptide of the present invention is a mixed inhibition.
[0095] Depend on Figure 5 As can be seen, the slope of each straight line in the Lineweaver-Burk plot is linearly related to the peptide concentration, indicating that the peptide of the present invention can bind to a single site on tyrosinase.
[0096] Example 5: The peptide can inhibit tyrosinase activity at the cellular level.
[0097] I. Solution Preparation
[0098] Sample solution: The polypeptide obtained in Example 1 was dissolved in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics, so that the final concentrations were 100 and 200 μM, respectively.
[0099] Kojic acid solution: Dissolve kojic acid in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics to achieve a final concentration of 300 μM.
[0100] II. Experimental Grouping and Processing
[0101] Sample measurement well (A) 测 ): Melanoma cells (B16F10) in logarithmic growth phase were harvested at a concentration of 5 × 10⁻⁶. 5 Cells were seeded at a density of 100 cells / well in 6-well plates and cultured at 37°C for 24 h. After acclimatization, the supernatant was discarded and the cells were washed twice with PBS solution (pH=7.4). 2 mL of sample solution / kojic acid solution was added to each well, and the cells were cultured at 37°C for 24 h. After discarding the supernatant, the cells were washed twice with PBS solution (pH=7.4) to remove non-adherent cells. 400 μL of lysis buffer (PMSF:RIPA volume ratio of 1:100) was added to each well, and the cells were lysed at 4°C for 30 min. The supernatant was collected by centrifugation.
[0102] Blank hole (A) 空): The same sample assay well, except that 2 mL of sample solution is replaced with an equal volume of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics.
[0103] After determining the protein concentration of the supernatant using a BCA kit and normalizing it, 50 μL of the protein solution was mixed with 50 μL of PBS and 50 μL of L-DOPA (10 mM). The mixture was incubated at 37°C for 30 min, and the absorbance was measured at 475 nm. The absorbance was then calculated using the formula: "Tyrosinase activity (%) = A..." 测 / A 空 The tyrosinase activity after the sample solution / kojic acid solution was reacted was calculated using the formula "×100%".
[0104] III. Experimental Results
[0105] The results are as follows Figure 6 As shown, compared with the blank well, the tyrosinase activity of B16F10 cells was significantly reduced after treatment with 100-200 μM peptide, even lower than the tyrosinase activity after treatment with kojic acid. This indicates that the peptide of the present invention can significantly inhibit the activity of tyrosinase and is suitable for the preparation of skin whitening products.
[0106] Example 6: The peptide can inhibit melanin production.
[0107] I. Solution Preparation
[0108] Sample solution: In a clean bench, the polypeptide obtained in Example 1 was dissolved in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics to make the final concentrations 100 and 200 μM respectively, and then sterilized with a 0.22 μm needle filter.
[0109] Kojic acid solution: In a clean bench, dissolve kojic acid in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics to a final concentration of 300 μM, and then sterilize with a 0.22 μm syringe filter.
[0110] II. Experimental Grouping and Processing
[0111] Sample measurement well (A) 测 ): Melanoma cells (B16F10) in logarithmic growth phase were harvested at a concentration of 5 × 10⁻⁶. 5Cells were seeded at a density of 100 cells / well in 6-well plates and cultured at 37°C for 24 h. After acclimatization, the supernatant was discarded and the cells were washed twice with PBS solution (pH=7.4). 2 mL of sample solution / kojic acid solution was added to each well, and the cells were cultured at 37°C for 24 h. After discarding the supernatant, the cells were washed twice with PBS solution (pH=7.4) to remove non-adherent cells. The cells were then digested with trypsin, and the digestion products were collected and centrifuged at 1500 r / min for 10 min. 1 mL of NaOH solution (1 mol / L) containing 10% (v / v) DMSO was added to the precipitate, and the cells were extracted in a water bath at 80°C for 1 h. The absorbance of each well was then measured at 450 nm.
[0112] Blank hole (A) 空 ): The same sample assay well, except that 2 mL of sample solution is replaced with an equal volume of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics.
[0113] According to the formula "Melanin content (%) = A 测 / A 空 The melanin content after the sample solution / kojic acid solution was treated was calculated using the formula "×100%".
[0114] III. Experimental Results
[0115] The results are as follows Figure 7 As shown, compared with the blank well, the melanin content of B16F10 cells was significantly reduced after treatment with 100-200 μM peptide, even lower than the melanin content after treatment with kojic acid. This indicates that the peptide of the present invention can significantly inhibit the production of melanin and is suitable for the preparation of whitening products.
[0116] Furthermore, after treatment with 100 and 200 μM peptides, the melanin content of B16F10 cells was 75.34% and 61.87%, respectively, with the latter being significantly lower than the former, indicating that the inhibitory effect of the peptides of this invention on melanin content is dose-dependent; and according to Figure 6 It is evident that the inhibitory effect of the polypeptide of this invention on tyrosinase activity is not dose-dependent. (Comprehensive analysis) Figure 6 and Figure 7 It is understood that the inhibitory effect of the polypeptide of the present invention on melanin content does not solely depend on the inhibition of tyrosinase activity.
[0117] Example 7: The peptide can effectively exert antioxidant activity.
[0118] I. Solution Preparation
[0119] Sample solution: In a clean bench, the polypeptide obtained in Example 1 was dissolved in DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics to make the final concentrations 0, 100 and 200 μM respectively, and then sterilized with a 0.22 μm needle filter.
[0120] II. Experimental Grouping and Processing
[0121] (1) Assay of SOD and GSH-PX activity
[0122] Melanoma cells (B16F10) in logarithmic growth phase were harvested at a concentration of 5 × 10⁻⁶. 5 Cells were seeded at a density of 100 cells / well in 6-well plates and cultured at 37°C for 24 h. The supernatant was discarded, and the cells were washed twice with PBS (pH 7.4). 2 mL of sample solution was added, and the cells were cultured at 37°C for another 24 h. The supernatant was discarded, and the cells were washed twice with PBS (pH 7.4) to remove non-adherent cells. 400 μL of lysis buffer (PMSF:RIPA ratio 1:100) was added to each well, and the cells were lysed at 4°C for 30 min. The supernatant was collected by centrifugation. The activities of SOD and GSH-PX in the supernatant were determined according to the instructions of the SOD and GSH-PX kits from Nanjing Jiancheng Biotechnology Institute.
[0123] (2) ROS activity assay
[0124] Sample measurement well (A) 测 Log-phase melanoma cells (B16F10) were seeded at a density of 3000 cells / well in 96-well plates and cultured at 37°C for 24 h. After acclimatization, the supernatant was discarded and the cells were washed twice with PBS solution (pH=7.4). 100 μL of sample solution was added and the cells were incubated at 37°C and 5% CO2 for 24 h. After discarding the culture medium, 100 μL of DCFH-DA diluted to 10 μM with DMEM medium was added and incubated at 37°C for 30 min. After discarding the supernatant, the cells were washed with PBS solution (pH=7.4) and the absorbance was measured using a microplate reader (excitation wavelength set to 488 nm, emission wavelength set to 525 nm).
[0125] Blank hole (A) 空 ): The same sample assay wells, except that 100 μL of sample solution is replaced with an equal volume of DMEM medium containing 10% (v / v) fetal bovine serum + 1% (v / v) penicillin and streptomycin antibiotics.
[0126] According to "ROS relative activity (%) = A 测 / A 空 The relative activity of ROS was calculated by multiplying the value by 100%.
[0127] III. Experimental Results
[0128] SOD activity results are as follows Figure 8 As shown, the GSH-PX activity results are as follows: Figure 9 As shown, the relative activity results of ROS are as follows: Figure 10 As shown, compared with the blank group, the SOD and GSH-PX activities of B16F10 cells were significantly increased and the relative ROS activity was significantly decreased after treatment with 100-200 μM peptides, indicating that the peptides of the present invention have excellent antioxidant activity and are suitable for the preparation of skin whitening products.
[0129] The above embodiments are preferred embodiments of the present invention, but the embodiments of the present invention are not limited to the above embodiments. Any changes, modifications, substitutions, combinations, or simplifications made without departing from the spirit and principle of the present invention shall be considered equivalent substitutions and shall be included within the protection scope of the present invention.
Claims
1. A polypeptide, characterized in that, The amino acid sequence is shown in SEQ ID NO:
1.
2. The application of the polypeptide according to claim 1 in the preparation of skin whitening products, characterized in that, The product in question is either a cosmetic or a pharmaceutical.
3. The use of the polypeptide of claim 1 in the preparation of melanin inhibitors.
4. The application of the polypeptide according to claim 1 in the preparation of antioxidant products, characterized in that, The product in question is either a cosmetic or a pharmaceutical.
5. The biomaterials related to the polypeptide of claim 1, characterized in that, The relevant biological material is a nucleic acid molecule encoding the polypeptide, or a recombinant DNA, expression cassette, vector, or host cell containing the nucleic acid molecule.
6. The application of the related biomaterials of claim 5 in the preparation of skin whitening products, characterized in that, The product in question is either a cosmetic or a pharmaceutical.
7. The use of the biomaterial described in claim 5 in the preparation of melanin inhibitors.
8. The application of the related biomaterials of claim 5 in the preparation of antioxidant products, characterized in that, The product in question is either a cosmetic or a pharmaceutical.