A cosmetic skin care leucomies peptide composition, its preparation method and application

Abstract

The application discloses a kind of cosmetic skin care black-bone chicken peptide composition and its preparation method and application, belong to skin care technical field, the composition includes the following weight parts of component: black-bone chicken peptide 15~40 parts, fish collagen peptide 10~30 parts, collagen tripeptide 5~18 parts, deer blood peptide 2~10 parts, flower glue peptide 3~12 parts, bonito elastin peptide 1~6 parts, pyrroloquinolinequinone disodium salt 0.05~3 parts, rich glutathione yeast 1~10 parts, sodium hyaluronate 0.5~5 parts, gamma-aminobutyric acid 1~8 parts and astaxanthin 0.05~1 part.The application uses the above-mentioned one kind of cosmetic skin care black-bone chicken peptide composition and its preparation method and application, the composition realizes structure supplement, energy metabolism, antioxidant lightening, water-locking moisturizing, sleep repair and six-dimensional cooperation of light protection, oral bioavailability is high, and anti-aging, lightening and tender skin effect is remarkable.

Description

Technical Field

[0001] This invention relates to the field of skincare technology, and in particular to a skincare composition of black-boned chicken peptides, its preparation method, and its application. Background Technology

[0002] Skin aging is a complex physiological process, characterized by a continuous decrease in collagen density and dermal thickness, a weakened ability of fibroblasts to synthesize collagen, and upregulated expression of matrix metalloproteinases, which accelerates the degradation of collagen and elastin. Furthermore, with age, the function of skin cell mitochondria gradually declines, reducing the efficiency of adenosine triphosphate (ATP) production. Dysfunctional mitochondria also generate more free radicals, further accelerating the skin aging process.

[0003] Currently, oral beauty products mainly focus on single or dual peptide supplementation, with functional dimensions limited to structural protein supplementation or a single antioxidant pathway. Some technologies disclose combinations of collagen peptides, elastin peptides, sodium hyaluronate, and gamma-aminobutyric acid, or compound formulations of collagen peptides with disodium pyrroloquinoline quinone and astaxanthin, but these remain at the level of two to four functional combinations, failing to cover all the key physiological aspects of skin aging, including structural supplementation, energy metabolism, antioxidant brightening, hydration, sleep repair, and photoprotection.

[0004] Existing technologies for black-boned chicken peptides mainly focus on their blood-tonifying, analgesic, and anti-inflammatory properties. Research on deer blood peptides is limited to blood tonification and purification. Technical solutions for applying both to oral beauty and anti-aging products, and combining them with other animal-derived active peptides, are still lacking. Current methods for preparing oral beauty products generally employ simple physical mixing or boiling granulation, without addressing the loading and protection of functional factors. Active ingredients are easily degraded by gastric acid and digestive enzymes in the gastrointestinal tract, resulting in low oral bioavailability.

[0005] Therefore, there is an urgent need to develop a composition that can achieve multi-dimensional, full-chain synergistic effects and improve the oral bioavailability of active ingredients through peptide self-assembly technology. Summary of the Invention

[0006] The purpose of this invention is to provide a skincare black chicken peptide composition, its preparation method, and its application to solve the above-mentioned problems.

[0007] This invention provides a skincare and beauty product made from black chicken peptides, comprising the following raw material components in parts by weight: Black-boned chicken peptide 15-40 parts; fish collagen peptide 10-30 parts; collagen tripeptide 5-18 parts; deer blood peptide 2-10 parts; fish maw peptide 3-12 parts; skipjack tuna elastin peptide 1-6 parts; pyrroloquinoline quinone disodium salt 0.05-3 parts; glutathione-enriched yeast 1-10 parts; sodium hyaluronate 0.5-5 parts; γ-aminobutyric acid 1-8 parts; astaxanthin 0.05-1 part.

[0008] Preferably, the molecular weight of the black-boned chicken peptide is in the range of 200–3000 Da, wherein the component with a molecular weight less than 1000 Da accounts for more than 80%; the molecular weight of the fish collagen peptide is in the range of 500–2000 Da, wherein the component with a molecular weight less than 1000 Da accounts for more than 50%; the molecular weight of the collagen tripeptide is less than 500 Da, and the content of the glycine-proline-hydroxyproline tripeptide sequence is not less than 3.0%; the molecular weight of the deer blood peptide is in the range of 200–5000 Da, wherein the component with a molecular weight less than 3000 Da accounts for more than 85%; the molecular weight of the fish maw peptide is in the range of 200–3000 Da, wherein the component with a molecular weight less than 1000 Da accounts for more than 70%; and the molecular weight of the skipjack tuna elastin peptide is in the range of 200–2000 Da.

[0009] Preferably, the black-boned chicken peptide is prepared by the following method: black-boned chicken raw material is minced and subjected to steam heat treatment. A mixed enzyme of neutral protease and bromelain is added for the first stage of enzymatic hydrolysis. Then, Protamex complex protease and flavor protease are added for the second stage of enzymatic hydrolysis. The peptide is separated by two-stage tandem ultrafiltration membrane. The filtrate in the target molecular weight range is collected, concentrated and dried to obtain the peptide.

[0010] Preferably, the dosage form of the composition is any one of solid beverage, oral liquid, tablet, capsule or granule.

[0011] A method for preparing a skin-care black chicken peptide composition is provided, comprising the following steps: (1) After passing the black chicken peptide, fish collagen peptide, collagen tripeptide, deer blood peptide, fish maw peptide and bonito elastin peptide through a 60-100 mesh sieve, they are put into a mixer and premixed for 15-30 minutes to obtain peptide premix. (2) Disperse the peptide premix in water for injection, adjust the pH to 6.0-7.5, stir and incubate at 35-45°C for 60-120 minutes to carry out the peptide self-assembly reaction and form a peptide self-assembly solution; (3) Disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid and astaxanthin were dissolved in water for injection and stirred at 20-40°C until completely dissolved to obtain a functional factor solution. (4) Under the conditions of 25-40℃ and stirring speed of 80-200rpm, the functional factor solution described in step (3) is added dropwise to the polypeptide self-assembly solution described in step (2). After the addition is complete, stirring is continued to load the functional factor into the interior and surface of the self-assembled peptide nanostructure, so as to obtain the composition solution. (5) The composition solution obtained in step (4) is spray-dried or freeze-dried to obtain the composition.

[0012] Preferably, the stirring and incubation in step (2) is carried out in a constant temperature water bath, and the stirring speed is 50 to 150 rpm.

[0013] Preferably, in step (3), the disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid and astaxanthin are prepared in advance as stock solutions, and then mixed according to the ratio and diluted with water for injection to the target concentration.

[0014] Preferably, in step (4), the functional factor solution is added dropwise to the peptide self-assembly solution at a rate of 0.5 to 2.0 mL / min, and stirring is continued for 30 to 60 minutes after the addition is complete.

[0015] Preferably, the inlet air temperature of the spray drying in step (5) is 160-190°C and the outlet air temperature is 80-95°C; the freeze drying temperature is -45--30°C, the vacuum degree is 10-50Pa, and the time is 24-48 hours.

[0016] This invention provides an application of a skincare black chicken peptide composition for preparing health foods or functional foods with anti-aging, wrinkle-reducing, skin-brightening, and skin-rejuvenating effects.

[0017] Therefore, the present invention, employing the above-mentioned cosmetic and skin-care black chicken peptide composition, its preparation method, and its application, has the following beneficial effects: (1) This invention is the first to systematically integrate six animal-derived active peptides from different sources—black chicken peptide, fish collagen peptide, collagen tripeptide, deer blood peptide, fish maw peptide, and skipjack tuna elastin peptide—with five functional factors: disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid, and astaxanthin. This breakthrough overcomes the limitations of existing technologies that only supplement structural proteins from a single or few dimensions. This composition simultaneously intervenes in multiple key aspects of skin aging from multiple dimensions, including structural supplementation, energy metabolism, antioxidant brightening, water-locking and moisturizing, sleep repair, and photoprotection. Its anti-aging, wrinkle-reducing, and skin-brightening effects are significantly better than the simple superposition of individual components.

[0018] (2) This invention employs a peptide self-assembly process to replace the traditional physical mixing method. Active peptides from different sources and with varying molecular weight distributions self-assemble under mild aqueous conditions to form ordered nanostructures. Functional factors such as disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid (GABA), and astaxanthin are loaded into the interior and surface of these self-assembled peptide nanostructures, forming a "peptide carrier-functional factor" co-delivery system. This process effectively protects easily degradable active ingredients such as astaxanthin and disodium pyrroloquinoline quinone from damage by gastric acid and digestive enzymes, significantly improving the gastrointestinal stability and oral bioavailability of each component.

[0019] (3) In the composition of this invention, the six animal-derived peptides have different sources and complementary peptide compositions, forming a multi-level synergistic effect with the five functional factors: the hexapeptide provides amino acid raw materials and signaling molecules for collagen and elastin synthesis; the disodium pyrroloquinoline quinone provides energy support for anabolic metabolism; glutathione-rich yeast and astaxanthin play a synergistic role in brightening and rejuvenating the skin and providing antioxidant protection; sodium hyaluronate forms a dual water-locking and moisturizing effect with collagen; and γ-aminobutyric acid assists in nighttime skin repair by improving sleep quality and relaxing facial muscles. Experimental results show that the composition of this invention exhibits significant synergistic effects in promoting type I collagen synthesis, scavenging free radicals, and inhibiting tyrosinase activity, and its technical effects far exceed those of single peptides or simple compound formulations in the prior art.

[0020] The technical solution of the present invention will be further described in detail below through embodiments. Detailed Implementation

[0021] To better understand the above technical solutions, a detailed description of the specific implementation methods will be provided below. Obviously, the described embodiments are merely some, not all, of the embodiments of the present invention. All other embodiments obtained by those skilled in the art based on the embodiments of the present invention without creative effort are within the scope of protection of the present invention.

[0022] The terminology used in the embodiments of this invention is for the purpose of describing particular embodiments only and is not intended to limit the invention. The singular forms “a,” “the,” and “the” as used in the embodiments of this invention and the appended claims are also intended to include the plural forms, and “multiple” generally includes at least two unless the context clearly indicates otherwise.

[0023] It should also be noted that the terms "comprising," "including," or any other variations thereof are intended to cover non-exclusive inclusion, such that an article or device that comprises a list of elements includes not only those elements but also other elements not expressly listed, or elements inherent to such an article or device. Without further limitation, an element defined by the phrase "comprising one..." does not exclude the presence of other identical elements in the article or device that includes said element.

[0024] A skin-care beauty and skincare black chicken peptide composition, comprising the following raw material components in parts by weight: Black-boned chicken peptide 15-40 parts; fish collagen peptide 10-30 parts; collagen tripeptide 5-18 parts; deer blood peptide 2-10 parts; fish maw peptide 3-12 parts; skipjack tuna elastin peptide 1-6 parts; pyrroloquinoline quinone disodium salt 0.05-3 parts; glutathione-enriched yeast 1-10 parts; sodium hyaluronate 0.5-5 parts; γ-aminobutyric acid 1-8 parts; astaxanthin 0.05-1 part.

[0025] The molecular weight range of black-boned chicken peptides is 200–3000 Da, with components having a molecular weight of less than 1000 Da accounting for more than 80%; the molecular weight range of fish collagen peptides is 500–2000 Da, with components having a molecular weight of less than 1000 Da accounting for more than 50%; the molecular weight of collagen tripeptide is less than 500 Da, and the content of the glycine-proline-hydroxyproline tripeptide sequence is not less than 3.0%; the molecular weight range of deer blood peptides is 200–5000 Da, with components having a molecular weight of less than 3000 Da accounting for more than 85%; the molecular weight range of fish maw peptides is 200–3000 Da, with components having a molecular weight of less than 1000 Da accounting for more than 70%; and the molecular weight range of skipjack tuna elastin peptides is 200–2000 Da.

[0026] Black-boned chicken peptides are prepared by the following method: black-boned chicken raw materials are minced and subjected to steam heat treatment. A mixture of neutral protease and bromelain is added for the first stage of enzymatic hydrolysis. Then, Protamex complex protease and flavor protease are added for the second stage of enzymatic hydrolysis. The mixture is separated by two-stage tandem ultrafiltration membranes. The filtrate in the target molecular weight range is collected, concentrated, and dried to obtain the final product.

[0027] Black-boned chicken peptides are rich in essential amino acids and have a small molecular weight, allowing for direct absorption through the epithelial cells of the small intestine. They possess antioxidant activity; the Leu-Trp-Arg and other antioxidant peptide sequences they contain can scavenge free radicals in the body, inhibit fat and protein oxidation, and reduce oxidative stress damage to cells and tissues. As the core ingredient in the composition, black-boned chicken peptides provide the nutritional basis for small-molecule active peptides and improve skin microcirculation through their blood-nourishing and yin-tonifying functions, thus providing a foundation for the synergistic effect of other components.

[0028] The main mechanisms by which fish collagen peptides act on the skin include promoting collagen synthesis, providing antioxidant protection, and enhancing the skin barrier function. After absorption, fish collagen peptides can promote the synthesis of endogenous collagen and hyaluronic acid, while simultaneously activating the transforming growth factor-β1 / Smad pathway, thus improving photoaging of the skin and exerting their effects through both "raw material replenishment" and "signal stimulation."

[0029] Collagen tripeptides are collagen bioactive signaling units with a molecular weight of less than 500 Da and high skin permeability. After oral administration, collagen tripeptides are fully absorbed via the oligopeptide transporter PEPT1, appearing in plasma within 30-60 minutes. Upon reaching the dermis, they bind to fibroblast receptors, activating transforming growth factor-β / Smad and mitogen-activated protein kinase / extracellular signal-regulated kinase pathways, upregulating the expression of type I collagen, elastin, and hyaluronic acid. The Gly-Pro-Hyp (glycine-proline-hydroxyproline) tripeptide sequence can directly stimulate type I collagen expression as a signaling molecule. Collagen tripeptides function as signaling molecules and target activation molecules in a hexapeptide system, compensating for the relatively large molecular weight and weak signaling function of fish collagen peptides.

[0030] Deer blood peptides possess dual benefits of replenishing blood and providing antioxidant effects. Their blood-replenishing effect is manifested in promoting hematopoietic cell regeneration and iron absorption and transport, thereby optimizing skin nutrition and metabolism by improving blood supply. Deer blood peptides contain antioxidants such as superoxide dismutase, which can scavenge free radicals and reduce oxidative damage. Furthermore, deer blood peptides have a protective effect against UVB-induced photoaging of the skin. Deer blood peptides and black-boned chicken peptides work synergistically in replenishing blood and nourishing yin: black-boned chicken peptides focus on overall conditioning by nourishing yin and tonifying the kidneys, while deer blood peptides focus on direct blood replenishment and specific protection against photoaging.

[0031] Fish maw peptides prevent and improve skin aging by replenishing the dermis with high-quality collagen, promoting fibroblast proliferation, enhancing skin's water-holding capacity, scavenging free radicals, and increasing the activity of antioxidant enzymes. Fish maw peptides can alleviate photoaging and improve skin hydration and elasticity by activating mitogen-activated protein kinase, nuclear factor-κB, and transforming growth factor-β signaling pathways. Rich in collagen-specific amino acids (glycine, proline, and hydroxyproline), fish maw peptides provide amino acid precursors for skin structure repair.

[0032] Skipjack tuna elastin peptides contain desmokinin and isodesmokinin, which can synergistically work with collagen peptides to activate dermal fibroblasts, slow down elastin loss, improve skin elasticity and softness, and reduce wrinkles. Skipjack tuna elastin peptides also have antioxidant activity, which can inhibit the accumulation of free radicals in the skin, reduce oxidative stress damage, and inhibit matrix metalloproteinase activity, thereby reducing the degradation of collagen and elastin.

[0033] The above six animal-derived peptides form a complementary and synergistic network: black-boned chicken peptides and deer blood peptides focus on nourishing blood and yin, improving skin microcirculation, and supplying metabolic substrates; fish collagen peptides and fish maw peptides provide collagen synthesis precursors and amino acid raw materials; collagen tripeptides activate fibroblasts through transforming growth factor-β / Smad and mitogen-activated protein kinase / extracellular signal-regulated kinase pathways, exerting signaling molecule functions; and skipjack tuna elastin peptides reinforce the elastic fiber network through desmokinin and isodesmokinin. These six peptides synergistically achieve "dual-network replenishment" of collagen and elastin.

[0034] Disodium pyrroloquinolinequinone is a oxidoreductase cofactor that promotes mitochondrial biosynthesis and enhances cellular energy metabolism by activating peroxisome proliferator-activated receptor gamma-1α and cyclic adenosine triphosphate (cAMP) response element-binding protein, thus providing adenosine triphosphate (ATP) for collagen synthesis in fibroblasts. A "energy + raw material" coupling relationship is formed between disodium pyrroloquinolinequinone and hexapeptide: the hexapeptide provides amino acid raw materials and synthetic signals, while disodium pyrroloquinolinequinone ensures that fibroblasts have sufficient energy to complete the efficient synthesis and secretion of proteins.

[0035] Glutathione-enriched yeast achieves skin brightening and rejuvenation through the following mechanisms: glutathione binds to the copper-containing active site of tyrosinase, inhibiting tyrosinase activity and redirecting melanin synthesis towards lighter-colored pheomelanin; the sulfhydryl structure of glutathione can scavenge reactive oxygen species generated by ultraviolet radiation in epidermal cells, blocking the "photodamage-pigmentation" pathway. Furthermore, pyrroloquinoline quinone disodium salt can activate antioxidant enzyme systems such as glutathione peroxidase, forming a dual antioxidant protection with glutathione through "enhanced enzyme activity + direct supply of antioxidant molecules."

[0036] Oral administration of sodium hyaluronate can improve skin moisture content, as it is responsible for regulating water balance and maintaining cell structure in the dermis. Sodium hyaluronate and collagen form a structurally complementary relationship in the skin—collagen provides the supporting framework, while hyaluronic acid fills in moisture to make it plump. As a high-molecular-weight polysaccharide, sodium hyaluronate contains a large number of hydrophilic groups in its molecular structure. In self-assembly systems, it can form a physical cross-linking network with peptide nanostructures through hydrogen bonds, increasing the stability of the self-assembled structure and delaying enzymatic degradation in the gastrointestinal tract.

[0037] Gamma-aminobutyric acid (GABA) can inhibit over-excited nerves, improve sleep quality, activate the parasympathetic nervous system, promote deep sleep, and indirectly promote nighttime skin repair. Simultaneously, GABA can reduce the formation of expression lines by relaxing facial muscles. When combined with collagen peptides, GABA can improve the absorption efficiency of signal peptides and, synergistically with elastin peptides and collagen peptides, achieve dual coverage of daytime anti-expression line treatment and nighttime sleep-aiding repair.

[0038] Astaxanthin enhances the body's innate antioxidant defense system by upregulating the expression of antioxidant enzymes such as superoxide dismutase and glutathione peroxidase. Astaxanthin can inhibit matrix metalloproteinase-1 activity, reducing UV-induced collagen degradation. Astaxanthin can form coupling compounds with collagen peptides, improving skin photoaging. In self-assembly systems, astaxanthin, as a lipid-soluble molecule, is embedded in the hydrophobic cavities of self-assembled peptides, achieving efficient encapsulation and protection.

[0039] The dosage form of the composition is any one of solid beverage, oral liquid, tablet, capsule or granule.

[0040] A method for preparing a skin-care black chicken peptide composition is provided, comprising the following steps: (1) After passing the black chicken peptide, fish collagen peptide, collagen tripeptide, deer blood peptide, fish maw peptide and bonito elastin peptide through a 60-100 mesh sieve, they are put into a mixer and premixed for 15-30 minutes to obtain peptide premix. (2) Disperse the peptide premix in water for injection, adjust the pH to 6.0-7.5, and stir and incubate at 35-45°C for 60-120 minutes to carry out the peptide self-assembly reaction and form a peptide self-assembly solution; the stirring and incubation is carried out in a constant temperature water bath at a stirring speed of 50-150 rpm. (3) Disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid and astaxanthin were prepared as stock solutions in advance, then mixed according to the ratio and diluted with water for injection to the target concentration. The solution was stirred at 20-40℃ until completely dissolved to obtain the functional factor solution. (4) Under the conditions of 25-40℃ and stirring speed of 80-200rpm, the functional factor solution of step (3) is added dropwise to the peptide self-assembly solution of step (2) at a rate of 0.5-2.0mL / min. After the addition is complete, continue stirring for 30-60 minutes to load the functional factor into the interior and surface of the self-assembled peptide nanostructure to obtain the composition solution. (5) The composition solution obtained in step (4) is spray-dried or freeze-dried to obtain the composition. The inlet air temperature of spray drying is 160-190℃ and the outlet air temperature is 80-95℃; the freeze-drying temperature is -45--30℃, the vacuum degree is 10-50Pa, and the time is 24-48 hours.

[0041] The synergistic effect of each component is upgraded from component-specific synergy to a dual synergy of physical and chemical processes through peptide self-assembly technology. Under conditions of 35–45℃ and pH 6.0–7.5, six bioactive peptides from different sources and with different molecular weight distributions are induced to form ordered self-assembled nanostructures through non-covalent forces such as hydrogen bonding, hydrophobic interactions, and π-π stacking. Hydrophobic functional factors are embedded in the hydrophobic cavities of the self-assembled peptides, while water-soluble small molecule functional factors are encapsulated in hydrophilic regions or on the surface for sustained-release delivery. Sodium hyaluronate is cross-linked with hydrogen bonds to increase structural stability, and yeast cell wall polysaccharides from glutathione-rich yeast form a multi-dimensional physical protective network with the peptide self-assembled structure. After spray drying or freeze-drying for curing, each functional factor is immobilized in the peptide nanostructure, achieving protection throughout the entire cycle from preparation to absorption, and ultimately improving the oral bioavailability of each component through multiple intestinal absorption pathways.

[0042] The above-prepared skincare black chicken peptide composition is used to prepare health foods or functional foods with anti-aging, wrinkle-reducing, brightening, and skin-rejuvenating effects.

[0043] To more clearly and in detail introduce the beauty and skincare black chicken peptide composition, its preparation method, and its application provided by the embodiments of the present invention, the following description will be based on specific embodiments.

[0044] Example 1 Preparation of a solid beverage containing a skin-beautifying black chicken peptide composition: Raw material preparation: Weigh each raw material component according to the following weight ratio: Black chicken peptides (molecular weight range 200-3000 Da, <1000 Da components account for 85%) 30 parts; Fish collagen peptides (molecular weight range 500-2000 Da, <1000 Da components account for 55%) 20 parts; 12 portions of collagen tripeptide (molecular weight <500 Da, GPH sequence content 3.5%); Six portions of deer blood peptides (molecular weight range 200–5000 Da, with <3000 Da components accounting for 88%); Eight portions of fish maw peptides (molecular weight range 200-3000 Da, with <1000 Da components accounting for 75%); Three portions of skipjack tuna elastin peptides (molecular weight range 200–2000 Da); 0.5 parts of pyrroloquinoline quinone disodium salt (PQQ disodium salt); Five portions of glutathione-enriched yeast; 2 parts sodium hyaluronate; 3 parts of γ-aminobutyric acid (GABA); Astaxanthin 0.3 parts; The black-boned chicken peptide is prepared by the following method: qualified black-boned chicken raw materials are minced and subjected to steam heat treatment at 105℃ for 30 minutes. After cooling, a mixture of neutral protease and bromelain in a mass ratio of 1:1 is added, and the first stage of enzymatic hydrolysis is carried out at 50℃ and pH 7.0 for 4 hours. Then, Protamex complex protease and flavor protease in a mass ratio of 2:1 are added, and the second stage of enzymatic hydrolysis is carried out at 55℃ and pH 6.5 for 3 hours. After enzyme inactivation, the mixture is centrifuged, and the supernatant is fractionated by passing it through two-stage ultrafiltration membranes of 5000Da and 3000Da. The filtrate with a molecular weight range of 200-3000Da is collected, concentrated under vacuum, and spray-dried to obtain the black-boned chicken peptide.

[0045] Preparation process: (1) After passing the black chicken peptide, fish collagen peptide, collagen tripeptide, deer blood peptide, fish maw peptide and bonito elastin peptide through an 80-mesh sieve, they were put into a three-dimensional mixer and premixed at 15 rpm for 25 minutes to obtain peptide premix.

[0046] (2) Disperse the peptide premix in water for injection at a mass ratio of 1:10, adjust the pH to 6.8, and incubate at 100 rpm for 90 minutes under constant temperature water bath at 40°C to carry out peptide self-assembly reaction and form peptide self-assembly solution.

[0047] (3) Disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid and astaxanthin were dissolved in an appropriate amount of water for injection and stirred at 30°C until completely dissolved to obtain a functional factor solution.

[0048] (4) At 30°C and a stirring speed of 120 rpm, the functional factor solution described in step (3) is added dropwise to the polypeptide self-assembly solution described in step (2) at a rate of 1.5 mL / min. After the addition is complete, stirring is continued for 45 minutes to load the functional factor into the interior and surface of the self-assembled peptide nanostructure, thus obtaining the composition solution.

[0049] (5) The composition solution obtained in step (4) is spray-dried (inlet air temperature 175℃, outlet air temperature 90℃) to obtain the solid powder of the composition. The obtained composition powder has a moisture content of ≤5.0%, an average particle size of 80~120μm, and good flowability and quick solubility.

[0050] Instructions for use: Take 5g of the solid powder of the composition prepared in this example, dissolve it in 150-200mL of warm water (about 45℃), stir well and drink. It is recommended to take it once a day.

[0051] Example 2 Preparation of an oral liquid containing a black-boned chicken peptide composition for beauty and skincare: Raw material preparation: Weigh each raw material component according to the following weight ratio: Black chicken peptides (molecular weight range 200-3000 Da, <1000 Da components account for 82%) 25 parts; Fish collagen peptides (molecular weight range 500-2000 Da, <1000 Da components account for 52%) 25 parts; 10 portions of collagen tripeptide (molecular weight <500 Da, GPH sequence content 3.2%); Five portions of deer blood peptides (molecular weight range 200–5000 Da, with <3000 Da components accounting for 86%); Fish maw peptides (molecular weight range 200-3000 Da, with <1000 Da components accounting for 72%) 7 parts; Four portions of skipjack tuna elastin peptides (molecular weight range 200–2000 Da); 1 part of disodium pyrroloquinoline quinone; 8 portions of glutathione-enriched yeast; 3 parts sodium hyaluronate; 5 parts of γ-aminobutyric acid; Astaxanthin 0.5 parts; Preparation process: (1) After passing the black chicken peptide, fish collagen peptide, collagen tripeptide, deer blood peptide, fish maw peptide and bonito elastin peptide through a 100-mesh sieve, they were put into a mixer and premixed at 20 rpm for 20 minutes to obtain peptide premix.

[0052] (2) Disperse the peptide premix in water for injection at a mass ratio of 1:8, adjust the pH to 7.2, and incubate at 80 rpm for 75 minutes under constant temperature water bath at 42℃ to carry out peptide self-assembly reaction and form peptide self-assembly solution.

[0053] (3) Disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid and astaxanthin were dissolved in an appropriate amount of water for injection and stirred at 25°C until completely dissolved to obtain a functional factor solution.

[0054] (4) Under the conditions of 30°C and stirring speed of 100 rpm, the functional factor solution described in step (3) is added dropwise to the polypeptide self-assembly solution described in step (2) at a rate of 1.0 mL / min. After the addition is complete, stirring is continued for 50 minutes to obtain the composition solution.

[0055] (5) The composition solution obtained in step (4) is freeze-dried (temperature -40℃, vacuum degree 30Pa, time 36 hours) to obtain the freeze-dried powder of the composition.

[0056] (6) Grind the obtained freeze-dried powder into powder, sieve it, and package it into 6g portions in aluminum foil bags. Seal and store. Dissolve in 150-200mL of warm water before use.

[0057] Example 3 Preparation of a cosmetic skincare black chicken peptide composition tablet: Raw material preparation: Weigh each raw material component according to the formula weight ratio of Example 1. The molecular weight range and proportion of each peptide raw material are as described in Example 1. In addition, weigh 15% of the total weight of the composition as a filler, weigh 3% of the total weight of the composition as a disintegrant, and weigh 1% of the total weight of the composition as a lubricant.

[0058] Preparation process: Steps (1) to (4) are the same as in Example 1, and a solution of the composition is obtained.

[0059] (5) The composition solution obtained in step (4) is freeze-dried (temperature -35℃, vacuum degree 40Pa, time 48 hours) to obtain the freeze-dried powder of the composition.

[0060] (6) The freeze-dried powder of the composition is pulverized and passed through an 80-mesh sieve. It is then fed into a wet granulator with microcrystalline cellulose and sodium carboxymethyl starch. 75% ethanol is used as a wetting agent to form a soft mass. The mass is then granulated through a 20-mesh sieve, dried at 50°C until the moisture content is ≤3%, and granulated through an 18-mesh sieve. Magnesium stearate is added and mixed evenly. The mixture is then compressed into tablets, with a tablet weight of approximately 1.0 g / tablet. The resulting tablets have a hardness of 40–60 N and a disintegration time of ≤30 minutes.

[0061] Comparative Example 1 Commonly used simple compound oral beauty products: Formula: 35 parts fish collagen peptide, 3 parts bonito elastin peptide, 2 parts sodium hyaluronate, 2 parts vitamin C.

[0062] Preparation process: After sieving each raw material separately, put them into a three-dimensional mixer and mix them physically for 20 minutes to obtain the composition powder.

[0063] The core difference between Comparative Example 1 and Example 1 is that Comparative Example 1 contains only two types of peptides: fish collagen peptide and bonito elastin peptide, and does not contain black chicken peptide, collagen tripeptide, deer blood peptide, or fish maw peptide; it does not contain PQQ disodium salt, glutathione-enriched yeast, GABA, or astaxanthin; it uses a conventional physical mixing process and does not have a peptide self-assembly step.

[0064] Comparative Example 2 Oral beauty compound products with added functional factors: Formula: 30 parts fish collagen peptide, 10 parts collagen tripeptide, 4 parts bonito elastin peptide, 2 parts sodium hyaluronate, 3 parts γ-aminobutyric acid, 0.3 parts astaxanthin, and 2 parts vitamin C.

[0065] Preparation process: After sieving each raw material separately, put them into a three-dimensional mixer and mix them physically for 20 minutes to obtain the composition powder.

[0066] The core difference between Comparative Example 2 and Example 1 is that although Comparative Example 2 contains collagen tripeptide, elastin peptide, sodium hyaluronate, GABA and astaxanthin, it does not contain animal-derived peptides such as black chicken peptide, deer blood peptide, and fish maw peptide, nor does it contain PQQ disodium salt and glutathione-enriched yeast; it still uses conventional physical mixing process and does not have peptide self-assembly steps.

[0067] Comparative Example 3 Oral cosmetic compound products prepared by physical mixing: The formula is the same as in Example 1.

[0068] Preparation process: After sieving each raw material separately, they are put into a three-dimensional mixer and physically mixed for 25 minutes to obtain the composition powder.

[0069] The core difference from Example 1 is that Comparative Example 3 has the same formulation as Example 1, but does not perform the peptide self-assembly process in steps (2) to (5), and only uses conventional physical mixing.

[0070] Comparative Example 4 Oral liquid beauty compound products prepared by physical mixing: The formula is the same as in Example 2.

[0071] Preparation process: After passing the black-boned chicken peptide, fish collagen peptide, collagen tripeptide, deer blood peptide, fish maw peptide and bonito elastin peptide through a 100-mesh sieve, they are physically mixed with pyrroloquinoline quinone disodium salt, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid and astaxanthin in a three-dimensional mixer for 20 minutes. The mixed powder is then dissolved in water for injection and stirred evenly. The mixture is then directly spray-dried (inlet air temperature 175℃, outlet air temperature 90℃) to obtain the composition powder.

[0072] The core difference from Example 2 is that Comparative Example 4 has the same formulation as Example 2, but does not perform peptide self-assembly incubation and functional factor drop loading steps. The peptide and functional factor are simply mixed and then spray-dried.

[0073] Comparative Example 5 Single-peptide oral beauty compound products: Formula: 87 parts of black chicken peptide (molecular weight range 200-3000 Da, with <1000 Da components accounting for 85%).

[0074] Preparation process: The black-boned chicken peptide is obtained by sieving.

[0075] Experimental Example 1 In vitro antioxidant activity (DPPH free radical scavenging assay): Experimental objective: To verify the in vitro antioxidant activity of the compositions of Examples 1-3 and Comparative Examples 1-5.

[0076] Experimental Methods: Appropriate amounts of the compositions from each example and comparative example were weighed and prepared into 5.0 mg / mL test solutions using deionized water. A 0.1 mM DPPH (1,1-diphenyl-2-trinitrophenylhydrazine) anhydrous ethanol solution was prepared. 2 mL of the test solution was mixed with 2 mL of the DPPH solution, and the mixture was allowed to react in the dark for 30 minutes. The absorbance was then measured at 517 nm (A1). Simultaneously, the absorbance of the mixture of 2 mL of the test solution and 2 mL of anhydrous ethanol (A2) and the absorbance of the mixture of 2 mL of deionized water and 2 mL of the DPPH solution (A0) were also measured. The DPPH free radical scavenging rate was calculated using the formula: DPPH free radical scavenging rate (%) = [1 - (A1 - A2) / A0] × 100% The experiment was repeated 3 times, and the average value was taken.

[0077] The experimental results are shown in Table 1 below: Table 1. Results of in vitro antioxidant activity experiments of Examples 1-3 and Comparative Examples 1-5

[0078] Results Analysis: The DPPH free radical scavenging rates of Examples 1 to 3 all reached over 86%, significantly better than the 32.4% of Comparative Example 1 and 45.8% of Comparative Example 2, indicating that the complete formulation of six animal-derived peptides and five functional factors has an excellent antioxidant synergistic effect. The DPPH free radical scavenging rate of glutathione-enriched yeast was 15% to 20%, the antioxidant capacity of astaxanthin was 550 times that of vitamin E, the free radical scavenging capacity of disodium pyrroloquinoline quinone was 50 to 100 times that of vitamin C, and the DPPH free radical scavenging activity of black-boned chicken peptide was significant. The above multiple antioxidant components together formed a multi-level, multi-target antioxidant network.

[0079] The clearance rate of Example 1 was 89.7%, significantly higher than that of Comparative Example 3 (64.3%). Comparative Example 3 had the same formulation as Example 1 but used only a physical mixing process. After peptide self-assembly, each functional factor was loaded into the interior and surface of the self-assembled peptide nanostructure, which effectively protected the active ingredient from oxidative degradation, resulting in a relative increase in clearance rate of approximately 39.5%. The self-assembled peptide nanostructure forms an ordered supramolecular assembly through non-covalent forces such as hydrogen bonds, hydrophobic interactions, and π-π stacking. Hydrophobic antioxidant factors such as astaxanthin are embedded in hydrophobic cavities, while water-soluble small molecules such as disodium pyrroloquinoline quinone and γ-aminobutyric acid are encapsulated in hydrophilic regions, thereby effectively protecting the activity of each component and achieving synergistic delivery.

[0080] Experiment Example 2 In vitro tyrosinase activity inhibition experiment: Experimental objective: To verify the tyrosinase activity inhibition ability of the compositions of Example 1 and Comparative Examples 1-3, and to verify their skin brightening and rejuvenation effects.

[0081] Experimental Methods: Appropriate amounts of the compositions from Example 1, Comparative Example 1, Comparative Example 2, and Comparative Example 3 were weighed and prepared into test solutions with concentrations of 1.0 mg / mL, 2.0 mg / mL, and 5.0 mg / mL using phosphate buffer (pH 6.8). Kojic acid was used as a positive control. In a 96-well plate, 40 μL of the test solution, 80 μL of phosphate buffer, and 40 μL of tyrosinase solution (200 U / mL) were added to each well sequentially. After mixing, the plate was incubated at 37°C for 10 minutes. Then, 40 μL of L-tyrosine solution (1.5 mM) was added, and the plate was incubated at 37°C for another 20 minutes. The absorbance was measured at 475 nm. Each sample was tested in triplicate. The tyrosinase activity inhibition rate was calculated using the formula: Inhibition rate (%) = [(A0-A1) / A0] × 100% Where A0 is the absorbance of the blank control group (using buffer solution instead of the test solution) and A1 is the absorbance of the sample group.

[0082] The experimental results are shown in Table 2 below: Table 2. Tyrosinase activity inhibition ability of the compositions of Example 1 and Comparative Examples 1-3

[0083] Results Analysis: Example 1 showed significantly better tyrosinase inhibition rates at all concentrations than Comparative Examples 1 and 2. Comparative Example 1, lacking glutathione-enriched yeast and astaxanthin, had inhibition rates ranging from 6.2% to 22.8% at all concentrations. Comparative Example 2, while containing astaxanthin and sodium hyaluronate, lacked glutathione-enriched yeast, resulting in a significantly lower tyrosinase inhibition rate than Example 1. Glutathione-enriched yeast plays a crucial role in brightening and rejuvenating the skin. Glutathione can bind to the copper-containing active site of tyrosinase through its unique thiol structure, shifting the direction of tyrosine synthesis from eumelanin to light yellow pheomelanin, while simultaneously clearing ROS and breaking the "photodamage-pigmentation" chain. The comparison between Example 1 and Comparative Example 3 demonstrates the protective effect of peptide self-assembly technology on activity. With identical formulations, the tyrosinase inhibition rate increased by approximately 26.1% after self-assembly. The self-assembled peptide nanostructure effectively protects active ingredients such as glutathione-enriched yeast from oxidation, maintaining their tyrosinase inhibitory activity. Example 1 showed an inhibition rate close to that of kojic acid at a concentration of 5.0 mg / mL, indicating that the composition has strong skin brightening and rejuvenation potential. Furthermore, all components used in the formulation are food-grade ingredients, making it safer than chemical whitening agents and suitable for long-term oral use.

[0084] Experimental Example 3 In vitro experiments with human skin fibroblasts (HSF): Experimental objective: To evaluate the effects of the compositions of Example 1 and Comparative Examples 1-5 on the proliferation activity of human skin fibroblasts and collagen synthesis.

[0085] Experimental methods: HSF cells in logarithmic growth phase were cultured in DMEM medium containing 10% fetal bovine serum at 37°C and 5% CO2. Cells were then sputtered at a rate of 1×10⁻⁶ cells / mL. 4 Inoculated at a density of cells / well in 96-well plates, and after 24 hours of culture, the plates were replaced with serum-free DMEM medium containing different concentrations (50 μg / mL, 100 μg / mL, and 200 μg / mL) of the compositions of each example and comparative example (sterilized by filtration through a 0.22 μm microporous membrane). Serum-free DMEM medium served as a blank control group.

[0086] (1) Cell proliferation detection: 10 μL CCK-8 solution was added to each well and incubated at 37°C for 2 hours. The absorbance was measured at a wavelength of 450 nm (A). 450 Cell proliferation rate (%) = (Experimental group A) 450 / Blank control group A 450 )×100%.

[0087] (2) Detection of type I collagen (COL1A1) content: Collect the culture supernatant and use an ELISA kit to detect the content of type I collagen (follow the instructions of the kit).

[0088] (3) Hydroxyproline (HYP) content detection: Collect cell culture supernatant and determine it by alkaline hydrolysis method.

[0089] The experimental results are shown in Table 3-5 below: Table 3 Cell proliferation rate (100 μg / mL)

[0090] Table 4. Type I collagen (COL1A1) content (100 μg / mL, ng / mL)

[0091] Table 5 Hydroxyproline (HYP) content (100 μg / mL, μg / mL)

[0092] Results Analysis: The cell proliferation rate of Example 1 was 145.8%, the type I collagen content was 28.6 ng / mL, and the hydroxyproline content was 8.9 μg / mL, both significantly higher than those of the comparative examples. Compared with Comparative Example 1, which contained only fish collagen peptides and elastin peptides, the type I collagen content of Example 1 increased by approximately 133%, from 12.3 ng / mL to 28.6 ng / mL; the hydroxyproline content increased by approximately 154%, from 3.5 μg / mL to 8.9 μg / mL. Compared with Comparative Example 5, which contained only black-boned chicken peptides, the type I collagen content of Example 1 increased by approximately 183%, from 10.1 ng / mL to 28.6 ng / mL; the hydroxyproline content increased by approximately 218%, from 2.8 μg / mL to 8.9 μg / mL. This indicates that the complete formula combination of six animal-derived peptides and five functional factors in this invention achieves a collagen synthesis-promoting effect far exceeding that of simply supplementing a single peptide through multi-level synergy. The hexapeptide provides amino acid raw materials and signaling molecules, the disodium pyrroloquinoline quinone provides adenosine triphosphate energy supply, the glutathione-rich yeast provides coenzymes and minerals, and the sodium hyaluronate provides a water-rich environment for the synthesized protein.

[0093] Compared to Comparative Example 3, Example 1 showed an increase in type I collagen content from 20.8 ng / mL to 28.6 ng / mL, an increase of approximately 37.5%, indicating that the self-assembled nanostructure protected the active components, allowing them to function better in the cell culture system. Comparative Example 2 had a type I collagen content of 16.5 ng / mL, which, while better than Comparative Example 1's 12.3 ng / mL, was significantly lower than Example 1. Even with the addition of functional factors such as collagen tripeptide, γ-aminobutyric acid, and astaxanthin, the collagen-promoting ability remained limited due to the lack of key components such as black-boned chicken peptide, deer blood peptide, fish maw peptide, disodium pyrroloquinoline quinone, and glutathione-enriched yeast. Comparative Example 5 contained only black-boned chicken peptide, and its type I collagen and hydroxyproline content were only slightly higher than the blank control, while the corresponding values ​​in Example 1 were approximately 2.8 to 3.2 times higher, demonstrating the synergistic effect of the peptide complex formulation in the examples.

[0094] Experiment Example 4 Simulated gastrointestinal digestion experiment: Experimental objective: To evaluate the protective effect of self-assembled structures on each component through simulated digestion experiments.

[0095] Experimental methods: (1) Particle size and Zeta potential determination: Take the polypeptide self-assembly solution obtained in step (2) of Example 1 and the composition solution obtained in step (4), as well as the "physical mixed solution" (simulated comparative example 3) obtained by directly dissolving each raw material of the same formulation in water for injection, and measure the particle size distribution and Zeta potential using a nanoparticle size and Zeta potential analyzer.

[0096] (2) Simulated in vitro gastrointestinal digestion experiment: 2g each of the powder composition of Example 1 and the physically mixed powder of the same formulation (simulated comparative example 3) were weighed and placed in simulated gastric juice (containing pepsin, pH 2.0), and digested at 37°C and 100 rpm for 2 hours with shaking; then the pH was adjusted to 6.8, trypsin and bile salts were added, and digestion was continued at 37°C for 2 hours to simulate intestinal digestion. Samples were taken before digestion, after gastric digestion, and after intestinal digestion, and the astaxanthin retention rate (HPLC method), total peptide retention rate (UV spectrophotometry), and PQQ retention rate (HPLC method) were determined.

[0097] The experimental results are shown in Table 6-7 below: Table 6 Particle size and Zeta potential

[0098] Table 7 Retention rate of active ingredients after simulated gastrointestinal digestion

[0099] Results analysis: The particle size of the self-assembled solution in Example 1 was 128.5 nm, and the particle size of the composition solution was 165.7 nm, both of which were much smaller than the 850.6 nm of the physical mixture solution. Furthermore, the polydispersity index was significantly reduced from 0.85 in the physical mixture solution to 0.18 in the self-assembled solution. A nano-assembled structure with uniform particle size and controllable size was successfully formed through peptide self-assembly process.

[0100] The simulated gastrointestinal digestion experiment most directly demonstrates the difference between Example 1 and Comparative Example 3. After intestinal digestion, the astaxanthin retention rate of the self-assembled process in Example 1 was 72.6%, while that of the physically mixed process was only 28.4%, representing an increase of approximately 156%, with an absolute difference of 44.2 percentage points. The retention rate of pyrroloquinoline quinone disodium salt increased from 35.2% to 69.1%, an increase of approximately 96%. The total peptide retention rate increased from 48.3% to 78.5%, an increase of approximately 63%. The self-assembled peptide nanostructure can effectively resist the destruction of gastric acid and digestive enzymes, achieving efficient protection of easily degradable active ingredients such as astaxanthin and pyrroloquinoline quinone disodium salt, and significantly improving their complete active content within the small intestinal absorption window.

[0101] Therefore, this invention employs the aforementioned cosmetic skincare black-boned chicken peptide composition and its preparation method and application, combining six animal-derived active peptides from different sources—black-boned chicken peptide, fish collagen peptide, collagen tripeptide, deer blood peptide, fish maw peptide, and skipjack tuna elastin peptide—with five functional factors: disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid, and astaxanthin—to create a synergistic network for anti-aging skin. Fish collagen peptide and fish maw peptide provide amino acid raw materials, collagen tripeptide targets and activates fibroblasts through transforming growth factor-β / Smad and mitogen-activated protein kinase / extracellular signal-regulated kinase pathways, and black-boned chicken peptide and deer blood peptide nourish blood and promote overall health. Yin improves skin microcirculation; bonito elastin peptides strengthen the elastic fiber network through desmokinin and isodesmokinin, achieving simultaneous replenishment of collagen and elastin; disodium pyrroloquinoline quinone promotes mitochondrial biosynthesis by activating the peroxisome proliferator-activated receptor γ-coactivator-1α pathway, providing fibroblasts with sufficient adenosine triphosphate; glutathione-rich yeast brightens and rejuvenates the skin by inactivating tyrosinase and scavenging reactive oxygen species; sodium hyaluronate is responsible for deep hydration and forms a mutually fixed structural relationship with collagen; γ-aminobutyric acid improves sleep quality and relaxes facial muscles to reduce expression lines; astaxanthin inhibits matrix metalloproteinase-1 activity, reduces collagen degradation, and provides photoprotection.

[0102] Six bioactive peptides were premixed in a specific ratio and incubated at 35–45°C and pH 6.0–7.5. Non-covalent forces, such as hydrogen bonds and hydrophobic interactions between peptide molecules, induced the formation of ordered self-assembled nanostructures. Functional factor solutions were then added dropwise to the self-assembled solution at a controlled rate, allowing the functional factors to be loaded into the interior and surface of the nanostructures, forming a peptide carrier-functional factor co-delivery system. Experiments showed that after the self-assembly process, the retention rate of astaxanthin after enteric digestion increased from 28.4% to 72.6%, the retention rate of pyrroloquinoline quinone disodium salt increased from 35.2% to 69.1%, and the total peptide retention rate increased from 48.3% to 78.5%.

[0103] Cellular experiments showed that, compared to a comparative composition containing only fish collagen peptides and elastin peptides, the composition of this invention increased type I collagen content by approximately 133% and hydroxyproline content by approximately 154%; compared to a comparative composition containing only black-boned chicken peptides, type I collagen content increased by approximately 183% and hydroxyproline content by approximately 218%; tyrosinase inhibition rate reached 78.3%, and 1,1-diphenyl-2-trinitrophenylhydrazine free radical scavenging rate reached 89.7%. The components work synergistically throughout the entire chain of anabolic metabolism: amino acid raw material supply - synthetic signal activation - cellular energy supply - synthetic cofactors - post-synthetic protection - elastic network reinforcement - moisture replenishment and locking - nighttime repair optimization - microcirculation improvement - self-assembly delivery system protection. This end-to-end intervention model, from raw materials to delivery, solves the problem of current localized issues that only address single or a few dimensions of skin problems.

[0104] Finally, it should be noted that the above embodiments are only used to illustrate the technical solutions of the present invention and not to limit them. Although the present invention has been described in detail with reference to preferred embodiments, those skilled in the art should understand that modifications or equivalent substitutions can still be made to the technical solutions of the present invention, and these modifications or equivalent substitutions cannot cause the modified technical solutions to deviate from the spirit and scope of the technical solutions of the present invention.

Claims

1. A cosmetic skin care composition of leucomiine peptides, characterized in that, It consists of the following raw material components in parts by weight: Black-boned chicken peptide 15-40 parts; fish collagen peptide 10-30 parts; collagen tripeptide 5-18 parts; deer blood peptide 2-10 parts; fish maw peptide 3-12 parts; skipjack tuna elastin peptide 1-6 parts; pyrroloquinoline quinone disodium salt 0.05-3 parts; glutathione-enriched yeast 1-10 parts; sodium hyaluronate 0.5-5 parts; γ-aminobutyric acid 1-8 parts; astaxanthin 0.05-1 part.

2. The cosmetic skin care composition of black-bone chicken peptide according to claim 1, characterized in that, The molecular weight range of black-boned chicken peptides is 200–3000 Da, with components having a molecular weight of less than 1000 Da accounting for more than 80%; the molecular weight range of fish collagen peptides is 500–2000 Da, with components having a molecular weight of less than 1000 Da accounting for more than 50%; the molecular weight of collagen tripeptide is less than 500 Da, and the content of the glycine-proline-hydroxyproline tripeptide sequence is not less than 3.0%; the molecular weight range of deer blood peptides is 200–5000 Da, with components having a molecular weight of less than 3000 Da accounting for more than 85%; the molecular weight range of fish maw peptides is 200–3000 Da, with components having a molecular weight of less than 1000 Da accounting for more than 70%; and the molecular weight range of skipjack tuna elastin peptides is 200–2000 Da.

3. The cosmetic skin care composition of black-bone chicken peptide according to claim 1, characterized in that, Black-boned chicken peptides are prepared by the following method: black-boned chicken raw materials are minced and subjected to steam heat treatment. A mixture of neutral protease and bromelain is added for the first stage of enzymatic hydrolysis. Then, Protamex complex protease and flavor protease are added for the second stage of enzymatic hydrolysis. The mixture is separated by two-stage tandem ultrafiltration membranes. The filtrate in the target molecular weight range is collected, concentrated, and dried to obtain the final product.

4. The skin-care black chicken peptide composition according to claim 1, characterized in that, The dosage form of the composition is any one of solid beverage, oral liquid, tablet, capsule or granule.

5. A method for preparing a skin-care black chicken peptide composition according to any one of claims 1-4, characterized in that, Includes the following steps: (1) After passing the black chicken peptide, fish collagen peptide, collagen tripeptide, deer blood peptide, fish maw peptide and bonito elastin peptide through a 60-100 mesh sieve, they are put into a mixer and premixed for 15-30 minutes to obtain peptide premix. (2) Disperse the peptide premix in water for injection, adjust the pH to 6.0-7.5, stir and incubate at 35-45℃ for 60-120 minutes to carry out the peptide self-assembly reaction and form a peptide self-assembly solution; (3) Disodium pyrroloquinoline quinone, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid and astaxanthin were dissolved in water for injection and stirred at 20-40°C until completely dissolved to obtain a functional factor solution. (4) Under the conditions of 25-40℃ and stirring speed of 80-200rpm, the functional factor solution of step (3) is added dropwise to the peptide self-assembly solution of step (2). After the addition is complete, stirring is continued to load the functional factor into the interior and surface of the self-assembled peptide nanostructure, so as to obtain the composition solution. (5) The composition solution obtained in step (4) is spray-dried or freeze-dried to obtain the composition.

6. The method for preparing a skin-care black chicken peptide composition according to claim 5, characterized in that, In step (2), the stirring and incubation are carried out in a constant temperature water bath at a stirring speed of 50 to 150 rpm.

7. The method for preparing a skin-care black chicken peptide composition according to claim 5, characterized in that, In step (3), pyrroloquinoline quinone disodium salt, glutathione-enriched yeast, sodium hyaluronate, γ-aminobutyric acid and astaxanthin are prepared as stock solutions in advance, and then mixed according to the ratio and diluted with water for injection to the target concentration.

8. The method for preparing a skin-care black chicken peptide composition according to claim 5, characterized in that, In step (4), the functional factor solution is added dropwise to the peptide self-assembly solution at a rate of 0.5 to 2.0 mL / min, and stirring is continued for 30 to 60 minutes after the addition is complete.

9. The method for preparing a skin-care black chicken peptide composition according to claim 5, characterized in that, In step (5), the inlet air temperature of spray drying is 160-190℃ and the outlet air temperature is 80-95℃; the freeze drying temperature is -45--30℃, the vacuum degree is 10-50Pa, and the time is 24-48 hours.

10. The application of the skin-care black chicken peptide composition according to any one of claims 1-4, characterized in that, It is used to prepare health foods or functional foods with anti-aging, wrinkle-reducing, skin-brightening and skin-rejuvenating effects.

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