Composition containing elastin peptide as well as preparation method and application thereof

Abstract

The invention provides an elastin peptide-containing composition as well as a preparation method and application thereof. The elastin peptide-containing composition comprises elastin peptide, camel milk active small molecule peptide and water lily oligopeptide in a mass ratio of 1: (1-3): (1.8-2.5). The elastin peptide, the camel milk active small molecule peptide and the water lily oligopeptide which are obtained through a specific treatment mode are compounded according to a specific proportion, synthesis of aquaporin AQP3 can be promoted, the content of sodium hyaluronate is increased, and the free radical scavenging activity is improved. The composition containing the elastin peptide can quickly and efficiently improve the skin state, repair the skin, delay the skin aging, enhance the skin function and recover the elasticity. The composition containing elastin peptide can promote the proliferation and growth of fibroblasts, improve the cell viability and promote the healing of skin wounds, and is non-toxic to cells.

Description

Technical Field

[0001] The present invention relates to the technical field of skin care, and particularly relates to a composition containing elastin peptides, a preparation method thereof, and an application thereof. Background Art

[0002] The main body of the skin is the dermis layer, which is mainly composed of fibroblasts and matrix components. Fibroblasts produce glycosaminoglycans such as collagen and hyaluronic acid to form connective tissue, which plays an important role in the skin. The reduction of fibroblast function due to aging or other influences such as ultraviolet rays may lead to the reduction and denaturation of matrix components such as collagen and hyaluronic acid. Oxidative stress such as ultraviolet rays causes skin damage, making it rough and causing other adverse reactions. Due to the reduction of matrix components and oxidative stress, the skin ages rapidly, resulting in signs of aging such as wrinkles, spots, dull appearance, loss of smooth texture, and reduced elasticity. With the rapid development of the economy and the progress of science, people are increasingly concerned about how to scientifically and correctly maintain the skin to make it smooth and elastic again.

[0003] In addition, fibroblasts, as the main cell components of loose connective tissue, are the most important functional cells in the process of wound repair. Under the regulation of factors such as cytokines, fibroblasts proliferate, migrate, and synthesize and secrete collagen, extracellular matrix components, and collagenase, etc., participating in the processes of granulation tissue formation, wound contraction, scar formation, and tissue reconstruction. Protecting and promoting the growth of fibroblasts is the basis and key to accelerating wound healing. At the same time, the increase in the number of fibroblasts helps the formation of hair follicles during the wound healing process, thereby reducing the probability of scars left after skin healing. Summary of the Invention

[0004] In view of this, the present invention provides a composition containing elastin peptides, a preparation method thereof, and an application thereof.

[0005] The technical solution of the present invention is realized as follows:

[0006] A composition containing elastin peptides, comprising elastin peptides, camel milk active small molecule peptides, and water lily oligopeptides in a mass ratio of 1:1 - 3:1.8 - 2.5.

[0007] Further, the preparation method of the elastin peptides includes:

[0008] (1) After pretreating bovine cardiopulmonary artery tubes, making them into pulp, adding the pulp into a eutectic solvent, and performing ultrasonic extraction, then collecting the extract;

[0009] (2) Adding a composite enzyme to the extract for enzymatic hydrolysis, and then separating and purifying to obtain elastin peptides.

[0010] Further, in step (1), the material ratio of the bovine cardiopulmonary artery tube to the deep eutectic solvent is 1:8 - 12 g / mL; in the deep eutectic solvent, the hydrogen bond acceptor is betaine, the hydrogen bond donor is lactic acid, and the molar ratio of betaine to lactic acid is 1:1 - 2; the ultrasonic extraction is carried out at 50 - 60 °C and 100 - 200 rpm for 5 - 7 h;

[0011] In step (2), the composite enzyme is pepsin, lipase and alkaline protease with a mass ratio of 1:3 - 5:1 - 4, and the enzyme activity is 10000 - 12000 U / g; the addition amount of the composite enzyme is 1% - 3% of the mass of the bovine cardiopulmonary artery tube; the temperature of the enzymatic hydrolysis is 40 - 50 °C, the pH is 6.5 - 6.8, and the time is 6 - 8 h.

[0012] Further, the preparation method of the camel milk active small molecule peptide includes:

[0013] (1) Centrifuge fresh camel milk to separate camel milk protein;

[0014] (2) Add the composite enzyme to the camel milk protein, carry out microwave enzymatic hydrolysis, inactivate the enzyme, ultrafilter, and freeze-dry to obtain the camel milk active small molecule peptide.

[0015] Further, in step (1), the centrifugation is carried out at 8 - 15 °C and 8000 - 10000 rpm for 20 - 30 min;

[0016] In step (2), the composite enzyme is lactase, pepsin, lipase and papain with a mass ratio of (3.5 - 4.8):(2.3 - 3.6):(2.5 - 4.5):1, and the enzyme activity is 8000 - 9000 U / g; the addition amount of the composite enzyme is 4% - 7% of the mass of the camel milk protein; the microwave enzymatic hydrolysis is carried out at 400 - 500 W and 50 - 60 °C for 2 - 4 h; the molecular weight of the camel milk active small molecule peptide is 1 - 3 kDa.

[0017] Further, the preparation method of the water lily oligopeptide includes:

[0018] (1) Carry out low-temperature freeze-thawing, freeze-drying and pulverizing of fresh water lilies to obtain water lily powder;

[0019] (2) Add the water lily powder to water for soaking, add the composite enzyme, carry out enzymatic hydrolysis, inactivate the enzyme, filter, concentrate the hydrolysate, and dry to obtain the water lily oligopeptide.

[0020] Further, in step (2), the material-liquid ratio of the water lily powder to water is 1:10-15 g / mL; the composite enzyme is neutral protease, alkaline protease and trypsin with a mass ratio of 1:0.8-1.6:2.2-4.4, and the enzyme activity is 10,000-12,000 U / g; the addition amount of the composite enzyme is 3%-5% of the mass of the water lily powder; the temperature of the enzymatic hydrolysis is 30-40 °C, and the enzymatic hydrolysis is carried out at a pH of 6.5-7.5 for 1-3 h.

[0021] A preparation method of an elastin peptide-containing composition, the specific steps are: mixing elastin peptide, camel milk active small molecule peptide and water lily oligopeptide evenly.

[0022] Application of an elastin peptide-containing composition in the preparation of products for repair and anti-aging.

[0023] Application of an elastin peptide-containing composition in any one of (1)-(4):

[0024] (1) Promote the synthesis of aquaporin AQP3;

[0025] (2) Promote the growth of fibroblasts;

[0026] (3) Increase the content of sodium hyaluronate;

[0027] (4) Increase the production amount of collagen (hydroxyproline).

[0028] Compared with the prior art, the beneficial effects of the present invention are:

[0029] 1. The elastin peptide, camel milk active small molecule peptide and water lily oligopeptide obtained by the specific treatment method of the present invention are compounded in a specific ratio, which can promote the synthesis of aquaporin AQP3, increase the content of sodium hyaluronate and improve the free radical scavenging activity. The elastin peptide-containing composition of the present invention can quickly and efficiently improve the skin state, repair the skin, delay skin aging, enhance skin function and restore elasticity.

[0030] 2. The elastin peptide-containing composition of the present invention promotes the proliferation and growth of fibroblasts, improves cell viability, promotes skin wound healing, and has almost no toxicity to cells. Detailed implementation manners

[0031] In order to better understand the technical content of the present invention, specific examples are provided below to further illustrate the present invention.

[0032] The experimental methods used in the embodiments of the present invention are all conventional methods unless otherwise specified.

[0033] The materials, reagents, etc. used in the embodiments of the present invention can be obtained from commercial channels unless otherwise specified.

[0034] Example 1

[0035] The preparation method of elastin peptide includes:

[0036] (1) According to the material-liquid ratio of 1:10 g / mL, after removing impurities and pre-treating bovine cardiopulmonary artery tubes, they are pulped and then added into a betaine-lactic acid eutectic solvent (the molar ratio of betaine to lactic acid is 1:1.5), and ultrasonic extraction is carried out at 55 °C and 150 rpm for 6 h, and the extract is collected;

[0037] (2) Add a complex enzyme composed of pepsin, lipase and alkaline protease with a mass ratio of 1:4:2, and the enzyme activity of each is 11000 U / g. The addition amount of the complex enzyme is 2% of the mass of bovine cardiopulmonary artery tubes, and enzymatic hydrolysis is carried out at 45 °C and pH = 6.6 ± 0.1 for 7 h, and then separation and purification are carried out to obtain elastin peptide.

[0038] The preparation method of active small molecule peptides from camel milk includes:

[0039] (1) Centrifuge fresh camel milk at 10 °C and 90000 rpm for 25 min to separate camel milk protein;

[0040] (2) Add a complex enzyme composed of lactase, pepsin, lipase and papain with a mass ratio of 4:3:3.5:1, and the enzyme activity of each is 8000 U / g. The addition amount of the complex enzyme is 5% of the mass of camel milk protein, and enzymatic hydrolysis is carried out at 450 W, 55 °C and pH = 7.0 ± 0.1 for 3 h, then inactivate the enzyme, ultrafiltrate, and freeze-dry to obtain active small molecule peptides from camel milk with a molecular weight of 2 kDa.

[0041] The preparation method of water lily oligopeptides includes:

[0042] (1) Freeze-thaw fresh water lilies at low temperature, freeze-dry and pulverize them to obtain water lily powder;

[0043] (2) According to the material-liquid ratio of 1:13 g / mL, add the water lily powder into water and soak for 2 h, then add a complex enzyme composed of neutral protease, alkaline protease and trypsin with a mass ratio of 1:1.2:3, and the enzyme activity of each is 11000 U / g. The addition amount of the complex enzyme is 4% of the mass of water lily powder, and enzymatic hydrolysis is carried out at 35 °C and pH = 7.0 ± 0.1 for 2 h, then inactivate the enzyme, filter, concentrate the hydrolysate, and dry to obtain water lily oligopeptides.

[0044] A preparation method of a composition containing elastin peptide, specifically the steps are: mixing elastin peptide, active small molecule peptides from camel milk and water lily oligopeptides with a mass ratio of 1:2:2.2 evenly.

[0045] Example 2

[0046] The preparation method of elastin peptide includes:

[0047] (1) Pretreat the bovine cardiopulmonary artery tube to remove impurities according to a material-liquid ratio of 1:8 g / mL. After pulping, add it to a betaine-lactic acid eutectic solvent (molar ratio of betaine to lactic acid is 1:1), and perform ultrasonic extraction at 50 °C and 100 rpm for 5 h. Collect the extract.

[0048] (2) Add a complex enzyme composed of pepsin, lipase and alkaline protease with a mass ratio of 1:3:1 to the extract. The enzyme activities are all 10,000 U / g, and the addition amount of the complex enzyme is 1% of the mass of the bovine cardiopulmonary artery tube. Perform enzymatic hydrolysis at 40 °C and pH = 6.6 ± 0.1 for 6 h, then separate and purify to obtain elastin peptides.

[0049] The preparation method of camel milk active small molecule peptides includes:

[0050] (1) Centrifuge fresh camel milk at 8 °C and 8000 rpm for 20 min to separate camel milk protein.

[0051] (2) Add a complex enzyme composed of lactase, pepsin, lipase and papain with a mass ratio of 3.5:2.3:2.5:1 to the camel milk protein. The enzyme activities are all 8000 U / g, and the addition amount of the complex enzyme is 4% of the mass of the camel milk protein. Perform enzymatic hydrolysis at 400 W, 50 °C and pH = 6.6 ± 0.1 for 2 h, inactivate the enzyme, ultrafilter, and freeze-dry to obtain camel milk active small molecule peptides with a molecular weight of 1 kDa.

[0052] The preparation method of water lily oligopeptides includes:

[0053] (1) Freeze-thaw fresh water lilies at low temperature, freeze-dry and crush to obtain water lily powder.

[0054] (2) According to a material-liquid ratio of 1:10 g / mL, add the water lily powder to water and soak for 2 h. Add a complex enzyme composed of neutral protease, alkaline protease and trypsin with a mass ratio of 1:0.8 - 1.6:2.2 - 4.4. The enzyme activities are all 10,000 U / g, and the addition amount of the complex enzyme is 3% of the mass of the water lily powder. Perform enzymatic hydrolysis at 30 °C and pH = 6.6 ± 0.1 for 1 h, inactivate the enzyme, filter, concentrate the hydrolysate, and dry to obtain water lily oligopeptides.

[0055] A preparation method of a composition containing elastin peptides is as follows: Mix elastin peptides, camel milk active small molecule peptides and water lily oligopeptides with a mass ratio of 1:1:1.8 evenly.

[0056] Example 3

[0057] The preparation method of elastin peptides includes:

[0058] (1) After removing impurities and pre-treating bovine cardiopulmonary artery tubes according to a material-liquid ratio of 1:12 g / mL, they were pulped and then added to a betaine-lactic acid eutectic solvent (molar ratio of betaine to lactic acid 1:2). Ultrasonic extraction was carried out at 60 °C and 200 rpm for 7 h, and the extract was collected;

[0059] (2) The extract was added with a composite enzyme composed of pepsin, lipase and alkaline protease with a mass ratio of 1:5:4, and the enzyme activities were all 12,000 U / g. The addition amount of the composite enzyme was 3% of the mass of the bovine cardiopulmonary artery tube. Enzymolysis was carried out at 50 °C and pH = 6.6 ± 0.1 for 8 h, followed by separation and purification to obtain elastin peptides.

[0060] The preparation method of camel milk active small molecule peptides includes:

[0061] (1) Fresh camel milk was centrifuged at 15 °C and 10,000 rpm for 30 min to separate camel milk protein;

[0062] (2) A composite enzyme of lactase, pepsin, lipase and papain with a mass ratio of 4.8:3.6:4.5:1 was added to the camel milk protein, and the enzyme activities were all 9,000 U / g. The addition amount of the composite enzyme was 7% of the mass of the camel milk protein. Enzymolysis was carried out at 500 W, 60 °C and pH = 7.4 ± 0.1 for 4 h, then the enzyme was inactivated, ultrafiltered and freeze-dried to obtain camel milk active small molecule peptides with a molecular weight of 3 kDa.

[0063] The preparation method of water lily oligopeptides includes:

[0064] (1) Fresh water lilies were frozen and thawed at low temperature, freeze-dried and pulverized to obtain water lily powder;

[0065] (2) According to a material-liquid ratio of 1:15 g / mL, the water lily powder was added to water and soaked for 2 h. A composite enzyme composed of neutral protease, alkaline protease and trypsin with a mass ratio of 1:1.6:4.4 was added, and the enzyme activities were all 12,000 U / g. The addition amount of the composite enzyme was 5% of the mass of the water lily powder. Enzymolysis was carried out at 40 °C and pH = 7.4 ± 0.1 for 3 h, then the enzyme was inactivated, filtered, the hydrolysate was concentrated and dried to obtain water lily oligopeptides.

[0066] A preparation method of a composition containing elastin peptides is as follows: Mix elastin peptides, camel milk active small molecule peptides and water lily oligopeptides with a mass ratio of 1:3:2.5 evenly.

[0067] Comparative Example 1

[0068] The difference from Example 1 is that camel milk active small molecule peptides are missing, and the others are the same as Example 1.

[0069] Comparative Example 2

[0070] The difference from Example 1 is that it lacks water lily oligopeptide, and the rest is the same as Example 1.

[0071] Comparative Example 3

[0072] The difference from Example 1 is that in the preparation method of elastin peptide, the betaine-lactic acid eutectic solvent is replaced by deionized water, and the rest is the same as Example 1.

[0073] Test Example 1 - Anti-aging test

[0074] Experimental method: Prepare complete medium (DMEM + 15% FBS + 1% P / S, take 42 mL of DMEM medium, add 7.5 mL of serum, and 0.5 mL of double antibody to prepare it). Observe the cell growth under the microscope until it reaches 80 - 90%, then perform cell passage. Discard the old medium, wash it 1 - 2 times with PBS, add 1 mL of trypsin, place it in a 37°C incubator for digestion. Take it out every 1 minute and observe the cell digestion degree under the microscope. Stop digestion when the cells become round. Terminate digestion with 2 mL of complete medium, collect the cells, centrifuge at 1000 rpm for 5 minutes, discard the supernatant, and resuspend the cells with the medium. Transfer the cells to a six-well plate at a density of 1×10 5 cells / well, place it in a 5% CO2, 37°C incubator for 24 h. Randomly divide the cells into a control group, a model group, and experimental groups (Examples 1 - 3 and Comparative Examples 1 - 3), a total of 8 groups, with 6 replicates in each group. Add 100 μL / well of DMEM complete culture medium to the control group. Treat the model group and experimental groups with 100 μL of DMEM complete culture medium containing 0.8 mmol / L of H2O2 for oxidative damage treatment. Remove the liquid, then wash it 3 times with sterile PBS, and continue to culture it in a CO2 incubator for 24 h.

[0075] Determine the production amount of hydroxyproline: Cell plating: Transfer cells to a 6-well plate at a density of 2×10 5 cells / mL and culture for 24 h. Add the test sample to the oxidative damage model at an addition amount of 200 μg / mL for the experimental groups, and treat the cells with the test sample for 24 h. After incubation for 24 h, take out the supernatant from all cell plates and collect it in pre-labeled centrifuge tubes for estimating the hydroxyproline level, and detect the hydroxyproline content in the cells according to the kit.

[0076] Collagen can be evaluated by the content of hydroxyproline in cells.

[0077] Collagen promotion rate = (Collagen production amount in the experimental group - Collagen production amount in the model group) / Collagen production amount in the model group × 100%

[0078] The results are shown in Table 1.

[0079] Table 1

[0080] Sample Collagen production (hydroxyproline) (μg / mL) Collagen promotion rate / % Control group 10.47 - Model group 4.24 - Example 1 7.21 70.05 Example 2 7.03 65.80 Example 3 7.14 68.40 Comparative example 1 5.70 34.43 Comparative example 2 5.98 41.04 Comparative example 3 6.32 49.06

[0081] As can be seen from Table 1, compared with the model group, the collagen production of the elastin peptide-containing compositions in Examples 1-3 of the present invention increased, and the collagen production of Comparative Examples 1-3 was lower than that of Examples 1-3, indicating that the rational compounding of elastin peptides, active small molecule peptides from camel milk, and lotus seed oligopeptides had a synergistic effect. The collagen promotion rates in Examples 1-3 were 65.80%-70.05%, indicating that it could promote collagen production, improve skin condition, delay skin aging, and restore elasticity.

[0082] Test Example 2 - Moisture Retention Test

[0083] Experimental method: Human immortalized keratinocytes HaCaT were selected. When HaCaT reached 70% confluence in a 12-well plate, the cells were randomly divided into a control group, a model group, and experimental groups (Examples 1-3 and Comparative Examples 1-3), a total of 8 groups. The cells in the control group were not dried, and the model group and experimental groups were placed in a laminar flow hood and exposed for 20 min under the control conditions of no wind and a temperature of 25°C. When the cell viability decreased to 45%-70%, dry damage treatment was carried out.

[0084] ELISA detection of the content of sodium hyaluronate in cell supernatant: The test samples were added to the dry damage model at an addition amount of 200 μg / mL, and the cells were treated with the test samples for 24 h. The cell supernatant was aspirated, centrifuged at 3000 rpm for 20 min to remove cell debris, etc. Since the content of sodium hyaluronate in the cell supernatant was relatively high, it needed to be diluted 10 times and reserved. According to the operation instructions of the ELISA kit, a standard curve was drawn, and the corresponding content of sodium hyaluronate was calculated based on the OD value. The results are shown in Table 2.

[0085] Promotion rate of sodium hyaluronate production = (amount of sodium hyaluronate produced in the experimental group - amount of sodium hyaluronate produced in the model group) / amount of sodium hyaluronate produced in the model group × 100%

[0086] Determination of the expression level of AQP3: The test samples were added to the dry damage model at an addition amount of 200 μg / mL, and the cells were treated with the test samples for 24 h. The cells were digested with pre-warmed trypsin and stopped with medium, and then counted. Each tube contained about 100,000 cells, which were fixed with 4% paraformaldehyde for 10 min, washed once with ice-cold PBS, permeabilized with 0.5% Triton-100 at room temperature for 5 min, washed once with PBS, blocked with 1% BSA at room temperature for 60 min, centrifuged to remove the blocking solution, 1 μL of AQP3 primary antibody was added, and incubated at room temperature for 30 min. After washing once with PBS, 0.5 μL of AQP3 secondary antibody was added, and incubated at room temperature for 30 min. After washing once with PBS, 200 μL of Buffer was added, and the cells were detected by flow cytometry. The results are shown in Table 3.

[0087] AQP3 promotion rate = (Expression level of AQP3 in the experimental group - Expression level of AQP3 in the model group) / Expression level of AQP3 in the model group × 100%

[0088] Table 2

[0089] Sample Hyaluronic acid sodium production (ng / mL) Hyaluronic acid sodium promotion rate / % Control group 23.04 - Model group 19.06 - Example 1 38.14 100.10 Example 2 37.99 99.32 Example 3 38.18 100.31 Comparative example 1 31.10 63.17 Comparative example 2 31.64 66.00 Comparative example 3 33.69 76.76

[0090] As can be seen from Table 2, compared with the model group, the hyaluronic acid sodium production of the elastin peptide-containing compositions in Examples 1-3 of the present invention increased, and the hyaluronic acid sodium production of Comparative Examples 1-3 was lower than that of Examples 1-3, indicating that the reasonable compounding of elastin peptide, camel milk active small molecule peptide and water lily oligopeptide had synergistic effects. The promotion rates of hyaluronic acid sodium production in Examples 1-3 were 99.32% - 100.31%, indicating that it could improve the skin condition, moisturize and restore elasticity.

[0091] Table 3

[0092] Sample Expression level of AQP3 (fluorescence intensity value mean) AQP3 promotion rate / % Control group 68415 - Model group 47256 - Example 1 98724 108.91 Example 2 95684 102.48 Example 3 96148 103.46 Comparative example 1 81547 72.56 Comparative example 2 80924 71.25 Comparative example 3 91204 93.00

[0093] As can be seen from Table 3, compared with the model group, the expression level of aquaporin AQP3 in the elastin peptide-containing compositions in Examples 1-3 of the present invention increased, and the expression level of aquaporin AQP3 in Comparative Examples 1-3 was lower than that of Examples 1-3, indicating that the reasonable compounding of elastin peptide, camel milk active small molecule peptide and water lily oligopeptide had synergistic effects. The promotion rates of the expression level of aquaporin AQP3 in Examples 1-3 were 102.48% - 108.91%, indicating that it could improve the skin condition, moisturize and restore elasticity.

[0094] Test Example 3 - Fibroblast Proliferation Experiment

[0095] Experimental method: Take NIH-3T3 cells in good growth state and in logarithmic phase, inoculate them at 1.0×10 4 cells / well in a 96-well culture plate, incubate at 37°C and 5% CO2 for 24 h, then randomly divide them into a control group and an experimental group (Examples 1-3 and Comparative Examples 1-3), with 6 replicate wells in each group. Discard the supernatant. The control group is added with DMEM complete culture medium (purchased from Shanghai Yiji Industrial Co., Ltd.). The experimental group (Examples 1-3 and Comparative Examples 1-3) sets 3 parallel experiments. The experimental group adds the sample to be tested at an addition amount of 200 μg / mL, 100 μL per well. After continuing to culture for 24 h, add 20 μL of MTT (5 mg / ml) to each well, incubate for 4 h, discard the supernatant, add 150 μL of DMSO complete culture medium to completely dissolve it, place it on an enzyme-linked immunosorbent assay (ELISA) reader, and measure the absorbance of each group at 490 nm. The cell viability is measured by the MTT method, and the effects of Examples 1-3 and Comparative Examples 1-3 on the proliferation ability of fibroblasts are compared. Each experiment is repeated 3 times, and the experimental results are shown in Table 4.

[0096] Table 4

[0097] Sample Cell viability / % Control group 100 Example 1 151.5 Example 2 148.9 Example 3 149.4 Comparative example 1 121.5 Comparative example 2 119.7 Comparative example 3 135.4

[0098] As can be seen from Table 4, the elastin peptide-containing compositions of Examples 1-3 of the present invention can effectively promote the proliferation of fibroblasts, with a 48.9%-51.5% increase compared to the control group. This indicates that the elastin peptide-containing composition of the present invention promotes the proliferation and growth of fibroblasts, improves cell viability, and promotes the healing of skin wounds.

[0099] The above are only the preferred embodiments of the present invention and are not intended to limit the present invention. Any modifications, equivalent substitutions, improvements, etc. made within the spirit and principles of the present invention shall be included within the protection scope of the present invention.

Claims

1. An elastin peptide-containing composition, characterized in that, It includes elastin peptide, camel milk active small molecule peptide and water lily oligopeptide with a mass ratio of 1:1 - 3:1.8 - 2.

5.

2. The elastin peptide-containing composition according to claim 1, characterized in that, The preparation method of the elastin peptide includes: (1) After pretreating bovine cardiopulmonary artery tubes, making them into slurry, adding the slurry into a eutectic solvent, and performing ultrasonic extraction, then collecting the extract; (2) Adding a composite enzyme to the extract for enzymatic hydrolysis, separating and purifying to obtain elastin peptide.

3. The elastin peptide-containing composition according to claim 2, wherein In step (1), the material - liquid ratio of the bovine cardiopulmonary artery tubes to the eutectic solvent is 1:8 - 12 g / mL; in the eutectic solvent, the hydrogen - bond acceptor is betaine, the hydrogen - bond donor is lactic acid, and the molar ratio of betaine to lactic acid is 1:1 - 2; the ultrasonic extraction is carried out at 50 - 60 °C and 100 - 200 rpm for 5 - 7 h; In step (2), the composite enzyme is a composite of pepsin, lipase and alkaline protease with a mass ratio of 1:3 - 5:1 - 4, and the enzyme activity of each is 10000 - 12000 U / g; the addition amount of the composite enzyme is 1% - 3% of the mass of the bovine cardiopulmonary artery tubes; the temperature of the enzymatic hydrolysis is 40 - 50 °C, the pH is 6.5 - 6.8, and the time is 6 - 8 h.

4. The elastin peptide-containing composition according to claim 1, wherein, The preparation method of the camel milk active small molecule peptide includes: (1) Centrifuging fresh camel milk to separate camel milk protein; (2) Adding a composite enzyme to the camel milk protein, performing microwave enzymatic hydrolysis, inactivating the enzyme, ultrafiltrating, and freeze - drying to obtain camel milk active small molecule peptide.

5. The elastin peptide-containing composition according to claim 4, characterized in that In step (1), the centrifugation is carried out at 8 - 15 °C and 8000 - 10000 rpm for 20 - 30 min; In step (2), the composite enzyme is a composite of lactase, pepsin, lipase and papain with a mass ratio of (3.5 - 4.8):(2.3 - 3.6):(2.5 - 4.5):1, and the enzyme activity of each is 8000 - 9000 U / g; the addition amount of the composite enzyme is 4% - 7% of the mass of the camel milk protein; the microwave enzymatic hydrolysis is carried out at 400 - 500 W and 50 - 60 °C for 2 - 4 h; the molecular weight of the camel milk active small molecule peptide is 1 - 3 kDa.

6. The elastin peptide-containing composition according to claim 1, wherein The preparation method of the water lily oligopeptide includes: (1) Freezing and thawing fresh water lilies at low temperature, freeze - drying, and pulverizing to obtain water lily powder; (2) Adding the water lily powder to water for soaking, adding a composite enzyme, performing enzymatic hydrolysis, inactivating the enzyme, filtering, concentrating the hydrolysis solution, and drying to obtain water lily oligopeptide.

7. The elastin peptide-containing composition according to claim 6, wherein In step (2), the material - liquid ratio of the water lily powder to water is 1:10 - 15 g / mL; the composite enzyme is a composite of neutral protease, alkaline protease and trypsin with a mass ratio of 1:0.8 - 1.6:2.2 - 4.4, and the enzyme activity of each is 10000 - 12000 U / g; the addition amount of the composite enzyme is 3% - 5% of the mass of the water lily powder; the enzymatic hydrolysis is carried out at 30 - 40 °C and pH 6.5 - 7.5 for 1 - 3 h.

8. The preparation method of an elastin peptide composition according to claim 1, characterized in that, The specific step is: mixing the elastin peptide, camel milk active small molecule peptide and water lily oligopeptide evenly.

9. Application of a composition containing elastin peptide according to claim 1 in the preparation of products for repair and anti - aging.

10. Application of a composition containing elastin peptide according to claim 1 in any one of (1)-(4): (1) Promote the synthesis of aquaporin AQP3; (2) Promote the growth of fibroblasts; (3) Increase the content of sodium hyaluronate; (4) Increase the production of collagen (hydroxyproline).