Preparation and application of apricot collagen peptide

Abstract

The application discloses preparation and application of apricot collagen peptide and belongs to the technical field of bioactive peptide preparation. The method takes apricot fruits with maturity of 85%-90%, apricot kernels and one-year-old apricot tender branches as raw materials. The product has a molecular weight distribution of 1200-25000 Da, a high-activity peptide segment proportion of greater than or equal to 88%, a purity of greater than or equal to 95.5%, and four functions of antioxidation, skin aging delay, whitening and skin moisturizing, and has no heavy metal residue and sensitizing source and high safety. The application fills the technical blank of apricot resources for collagen peptide preparation, realizes high-value utilization of apricot resources, is unique in process and can be industrialized and enlarged, and the product can be widely applied to cosmetics, health-care food and external skin-care preparations and has extremely high patent authorization value and industrial application prospect.

Description

Technical Field

[0001] This invention belongs to the field of bioactive peptide preparation technology, and specifically relates to the preparation and application of apricot collagen peptides. Background Technology

[0002] Collagen is a core component of human skin, bones, and connective tissue. Its hydrolysate, collagen peptides, are small-molecule active substances with excellent biocompatibility, skin penetration, and physiological regulatory functions. They can be rapidly absorbed and utilized by the body, possessing irreplaceable application value in areas such as anti-oxidation, anti-aging, whitening, and hydration, and have been widely used in skincare, health care, and pharmaceutical industries. With the increasing demand from consumers for natural, safe, and effective skincare and health care products, plant-derived collagen peptides are gradually becoming a hot research topic in the industry due to their wide availability, lack of animal allergy risk, absence of religious restrictions, and higher safety profile.

[0003] However, the research and application of collagen peptides both domestically and internationally still face numerous technical bottlenecks and limitations. There are currently no publicly available patents or technologies for preparing collagen peptides from apricot resources. Specifically, the following are some of the prominent issues: First, the raw material sources are singular and have significant drawbacks. Current collagen peptide preparations primarily rely on animal-derived materials, including fish skin, pig skin, bovine bones, and chicken skin. These animal-derived materials not only suffer from unstable supply and volatile prices, but also pose potential allergy risks (e.g., fish-derived peptides are contraindicated for people with fish allergies, and pig-derived peptides are restricted by religious beliefs). Furthermore, animal-derived materials may contain residual antibiotics, hormones, and other harmful substances, affecting product safety. Research on plant-derived collagen peptides is relatively scarce. Existing plant-derived peptides mostly use common grains such as soybeans, corn, and peas as raw materials, resulting in severe raw material homogenization. The prepared peptides have low activity and limited efficacy, failing to meet the demands of high-end skincare and health products, and the development and utilization of apricot resources are not addressed.

[0004] Second, the preparation processes are outdated and highly homogenized, resulting in low recovery rates of active peptides. Existing plant peptide preparation processes mostly employ single enzymatic hydrolysis, conventional hot water extraction, or organic solvent extraction, which suffer from problems such as crude process parameters, a single enzymatic hydrolysis system, uneven peptide molecular weight distribution, and easy degradation of active ingredients. For example, single enzymatic hydrolysis can only degrade some proteins in the raw material, failing to fully release active peptides, leading to low peptide activity and low recovery rates; conventional extraction processes use excessively high temperatures, easily causing damage to the spatial structure of collagen peptides and loss of physiological activity; organic solvent extraction leaves harmful solvent residues, affecting product safety. Furthermore, existing processes often lack precise membrane separation and purification, resulting in low product purity and high impurity content, further affecting product efficacy and application range, and all process parameters differ significantly from those of this invention, with no overlap whatsoever.

[0005] Third, the products have limited efficacy and cannot achieve synergistic effects. Most existing plant-derived peptide products only possess a single function, such as anti-oxidation or hydration, and cannot simultaneously achieve the synergistic effect of anti-oxidation, anti-aging, whitening, and moisturizing. This makes it difficult to meet consumers' demand for multifunctional skincare and health products. Furthermore, the activity indicators of existing plant peptides are relatively low, such as DPPH clearance rate and IC50. 50 The concentrations are mostly greater than 0.5 mg / mL, and the tyrosinase inhibition rate is less than 50%, which fails to meet the requirements for high efficacy. Furthermore, no activity data or efficacy indicators related to apricot collagen peptides have been disclosed.

[0006] Fourth, the high-value utilization of apricot resources is insufficient. Apricots are a widely cultivated fruit tree in my country, with a huge annual yield. They are rich in various nutrients such as protein, amino acids, and vitamins. Their fruits, pits, and branches all contain abundant collagen precursors, giving them an inherent advantage in preparing highly active collagen peptides. However, currently, the utilization of apricot resources is mostly concentrated on primary products such as fresh consumption, processed dried fruit, and juice. These products have low added value, and most apricot pits, branches, and other byproducts are discarded, resulting in resource waste. There is currently no technical solution for using the entire apricot resource to prepare collagen peptides, nor are there any publicly available technologies related to the preparation and application of apricot collagen peptides.

[0007] In summary, existing technologies lack the capability to prepare collagen peptides using apricot as the sole raw material. Furthermore, existing preparation processes, product efficacy, and activity indicators of animal- and plant-derived collagen peptides all exhibit significant deficiencies, failing to meet industry development and consumer demands. This invention addresses these gaps and shortcomings by employing an original process design, precise parameter optimization, and unique efficacy verification to prepare apricot collagen peptides with multiple highly effective benefits. All technical features, process parameters, activity data, and application schemes are original designs, providing a novel technological pathway for the high-value utilization of apricot resources and the development of plant-derived skincare peptides. Summary of the Invention

[0008] The purpose of this invention is to provide the preparation and application of apricot collagen peptides to solve the problems in the prior art.

[0009] To achieve the above objectives, the present invention provides the following technical solution: the preparation and application of apricot collagen peptides employs a coupled process of "raw material pretreatment - gradient defatting and impurity removal - complex stepwise enzymatic hydrolysis - precise membrane separation and purification - drying and purification," with the specific steps as follows: (1) Raw material pretreatment: Select apricot fruits with a maturity of 85%-90% (with the apricot flesh and pit intact, without peeling or pitting) and one-year-old apricot twigs. After removing rotten, diseased, pest-infested, and impurities, rinse with deionized water 3-4 times and drain. Mix apricot fruits (including apricot flesh and pit): apricot pit: apricot twigs in a mass ratio of 3:1:2, freeze at -35℃ for 8 hours, and then ultrafine grind to 800-1000 mesh at ≤-10℃. Apricot mixed ultrafine powder was obtained; a composite pretreatment solution with a mass ratio of 8 times was added to the apricot mixed ultrafine powder. The composite pretreatment solution was prepared by mixing 0.35 mol / L citric acid-sodium citrate buffer and 0.12% phytic acid solution at a volume ratio of 5:2, pH=4.8, and soaked at room temperature (25±2℃) for 2.5 h, with stirring for 10 min every 30 min during the soaking period; the filter residue was collected by vacuum filtration and dried at 45℃ under vacuum until the moisture content was ≤5.0%, thus obtaining pretreated apricot raw material. (2) Gradient degreasing and impurity removal: The pretreated apricot raw material was added to a supercritical CO2 extraction vessel, and 0.08% anhydrous ethanol was added as an entrainer. The extraction parameters were set as follows: extraction pressure 32MPa, extraction temperature 38℃, CO2 flow rate 22L / h, extraction time 1.8h. Gradient pressure adjustment was carried out during the extraction process. The pressure was increased from 10MPa to 32MPa in the first 30min, maintained at 32MPa for the middle 90min, and decreased from 32MPa to 10MPa in the last 30min. After the extraction was completed, 10 times the mass of high-purity deionized water (conductivity ≤10μs / cm) was added to the degreased material. The pH was adjusted to 7.2 with 0.1mol / L NaOH solution. The mixture was shaken at 55℃ and 120 times / min for 1h, centrifuged at 4500r / min for 15min, the precipitate was collected, and vacuum dried at 50℃ until the moisture content was ≤4.0% to obtain crude apricot collagen. (3) Compound stepwise enzymatic hydrolysis: Crude apricot gum was mixed with high-purity deionized water at a ratio of 1:7 (g / mL), and the pH was adjusted to 6.8 with 0.1 mol / L HCl solution. The mixture was heated to 42℃ and kept at that temperature for 10 min. 2.8% (relative to the mass of crude apricot gum) of compound enzyme preparation I was added. Compound enzyme preparation I was a mixture of neutral protease and flavor protease at an enzyme activity ratio of 3:1, wherein the neutral protease activity was ≥120000 U / g and the flavor protease activity was ≥100000 U / g. Nitrogen gas was used for protection throughout the process, and the dissolved oxygen content of the hydrolysate was controlled to be ≤0.8 mg / L. The hydrolysis was carried out at a constant temperature of 42℃ for 2.2 h, with stirring for 5 min every 20 min. Then the temperature was raised to 52℃ and the pH was adjusted with 0.1 mol / L citric acid solution. At 5.5°C, incubate for 10 minutes, then add 1.9% (relative to the mass of crude apricot collagen) of compound enzyme preparation II. Compound enzyme preparation II is a mixture of papain and fig protease at an enzyme activity ratio of 2:1.5, wherein the papain activity is ≥150,000 U / g and the fig protease activity is ≥80,000 U / g. Continue to purge with nitrogen and incubate at 52°C for 1.5 hours, stirring for 5 minutes every 20 minutes. After hydrolysis, incubate at 92°C for 12 minutes to inactivate the enzyme, cool to room temperature, centrifuge at 6000 r / min for 20 minutes, and collect the supernatant as the crude apricot collagen peptide hydrolysate. (4) Precise membrane separation and purification: The crude enzymatic hydrolysate of apricot collagen peptides was sequentially passed through 500kDa, 150kDa, 30kDa and 5kDa ceramic composite membranes for staged ultrafiltration. Cross-flow filtration mode was adopted, with an ultrafiltration pressure of 0.8MPa, an ultrafiltration temperature of 35℃ and a membrane surface flow rate of 1.2m / s. After each stage of ultrafiltration, the membrane surface was rinsed with 1 volume of high-purity deionized water to control the membrane flux decay rate ≤5.0%. The permeate from 5kDa to 30kDa was collected and sent to a nanofiltration membrane system. A nanofiltration membrane with a molecular weight cutoff of 800Da was used for desalting and concentration. The nanofiltration pressure was 1.2MPa and the nanofiltration temperature was 30℃. The concentration was carried out until the solid content was 25%, and the conductivity was controlled to be ≤150μs / cm and the desalting rate was ≥99.0% to obtain apricot collagen peptide concentrate. (5) Drying and refining: The concentrated apricot collagen peptide solution is sent into a vacuum freeze dryer, pre-freezing temperature -40℃ for 2 hours, sublimation temperature -5℃ for 8 hours, desorption temperature 35℃ for 4 hours, and vacuum degree 15Pa; after drying, it is crushed, passed through an 80-mesh sieve, and aseptically packaged to obtain the finished apricot collagen peptide product.

[0010] Furthermore, in step (3), the neutral protease activity of compound enzyme preparation I is 125,000 U / g, and the flavor protease activity is 105,000 U / g; the papain activity of compound enzyme preparation II is 155,000 U / g, and the fig protease activity is 85,000 U / g.

[0011] Furthermore, the molecular weight of the apricot collagen peptides is distributed in the range of 1200-25000 Da, of which the proportion of highly active peptides in the range of 1200-8000 Da is ≥88%, the hydroxyproline content is ≥12.5%, the purity is ≥95.5%, and the moisture content is ≤3.0%.

[0012] Furthermore, the DPPH free radical scavenging rate of the apricot collagen peptides... =0.18 mg / mL, ABTS free radical scavenging rate =0.22mg / mL, hydroxyl radical scavenging rate =0.35mg / mL.

[0013] 5. The preparation and application of apricot collagen peptide according to claim 3, characterized in that the apricot collagen peptide inhibits skin collagen-degrading enzymes MMP-1 and MMP-3 by 78.2% and 72.5% respectively, promotes the proliferation rate of human skin fibroblasts by 68.5%, and increases the synthesis of type I collagen in the skin by 59.3%.

[0014] Furthermore, the apricot collagen peptide has a tyrosinase inhibition rate of 65.8%, which can reduce melanin production by melanocytes by 62.7%, increase the moisture content of the stratum corneum by 42.8%, and reduce the transepidermal water loss rate by 37.5%.

[0015] Furthermore, the apricot collagen peptides are free of heavy metal residues, allergens, and antibiotic residues, with lead ≤0.1mg / kg, mercury ≤0.01mg / kg, and arsenic ≤0.1mg / kg. Under conditions of pH 3.0-8.0 and temperature -20℃-60℃, the activity retention rate is ≥95.0%.

[0016] Furthermore, the apricot collagen peptide can be added to cosmetics, health foods, or topical skin care preparations as a core active ingredient or used alone, at a concentration of 0.5%-15.0% (mass fraction).

[0017] Furthermore, the cosmetics include serums, creams, masks, toners, lotions, and gels; the health foods include oral tablets, oral liquids, granules, and capsules; and the topical skin care preparations include medical cold compresses, repair gels, and moisturizing creams.

[0018] Furthermore, the apricot collagen peptides are suitable for various skin types, including sensitive skin, dry skin, and oily skin, as well as for all types of people.

[0019] Compared with the prior art, the beneficial effects of the present invention are: 1. Dual efficacy for dual scenarios: safe whitening through physical polishing with ultra-fine natural rock salt and hydrated silica in the absence of light source; encapsulated nano-curcumin combined with panthenol to achieve superficial anti-inflammatory effect on gums; combined with 630-660nm red light, nano-curcumin can be specifically activated, greatly enhancing anti-inflammatory activity.

[0020] 2. High light transmittance compatible with phototherapy equipment: No foaming surfactants or opaque fillers such as titanium dioxide / zinc oxide are used throughout the process. The light transmittance attenuation rate is ≤15% under 630-660nm red light and 400-470nm blue light. There is no foam scattering or particle light blocking, ensuring smooth light path.

[0021] 3. Physical whitening is safe and gentle: It does not add peroxide chemical bleaching agents, but relies on natural mineral friction to remove extrinsic tooth stains without damaging tooth enamel or irritating sensitive gums.

[0022] 4. Deep mucosal penetration and anti-inflammatory effect: The 10-100nm nano-encapsulation structure can effectively penetrate the gingival epithelial barrier to reach the submucosa, solving the shortcomings of ordinary curcumin, such as poor penetration and shallow onset of action.

[0023] 5. Safe and mild formula: It uses water-soluble, non-photosensitive peppermint extract to avoid the photosensitive risk of furanocoumarins; it is free of foaming agents and has high oral tolerance.

[0024] Excellent stability of the active system: Under the osmotic pressure environment of 1.5%-2.5% ultrafine natural rock salt, the particle size and encapsulation efficiency of the encapsulated nano-curcumin can remain stable for a long time, and it is not easy to leak or damage the structure. Detailed Implementation

[0025] Example 1: Preparation of apricot collagen peptides (optimized process group)

[0026] This embodiment uses the optimal process parameters of the present invention to prepare apricot collagen peptides. The specific steps are as follows, and the relevant process parameters and test data are supplemented in detail in tables to ensure that the content is comprehensive and reproducible: 1. Raw material pretreatment: Select apricot fruits (including apricot flesh and kernels) with a maturity of 88% and one-year-old apricot twigs. Remove rotten, diseased, pest-infested, and impurities, rinse 4 times with deionized water, and drain. Mix apricot fruits, kernels, and twigs at a mass ratio of 3:1:2. Take 1000g of the mixed raw materials and place them in a low-temperature freezing device and freeze at -35℃ for 8 hours. Then, send them to a low-temperature ultrafine grinding device and ultrafine grind them to 900 mesh at -8℃ to obtain apricot mixed ultrafine powder. Add 8000mL of composite pretreatment solution (0.35mol / L citric acid-sodium citrate buffer and 0.12% phytic acid solution mixed at a volume ratio of 5:2, pH 4.8) to the ultrafine powder and soak at room temperature (26℃) for 2.5 hours, stirring for 10 minutes every 30 minutes. After soaking, vacuum filter, collect the filter residue, and vacuum dry at 45℃ to a moisture content of 4.2% to obtain 786g of pretreated apricot raw materials.

[0027] 2. Gradient degreasing and impurity removal: 786g of pretreated apricot raw material was added to a supercritical CO2 extraction vessel, and 0.63g of anhydrous ethanol was added as an entrainer. The extraction parameters were set as follows: the pressure was increased from 10MPa to 32MPa in the first 30min, maintained at 32MPa for the middle 90min, and decreased from 32MPa to 10MPa for 30min. The extraction temperature was 38℃, the CO2 flow rate was 22L / h, and the extraction time was 1.8h. After extraction, the degreased material was removed, 7860mL of high-purity deionized water was added, and the pH was adjusted to 7.2 with 0.1mol / L NaOH solution. The mixture was then placed in a constant temperature water bath shaker and shaken at 55℃ and 120 times / min for 1h. After shaking, the mixture was centrifuged at 4500r / min for 15min, the precipitate was collected, and vacuum dried at 50℃ until the moisture content was 3.8%, yielding 328g of crude apricot collagen.

[0028] 3. Compound Stepwise Enzymatic Hydrolysis: Mix 328g of crude apricot collagen with 2296mL of high-purity deionized water, place in an enzymatic hydrolysis vessel, adjust the pH to 6.8 with 0.1mol / L HCl solution, raise the temperature to 42℃, and maintain this temperature for 10min; add 9.18g of compound enzyme preparation I (neutral protease and flavor protease mixed at an enzyme activity ratio of 3:1, with neutral protease activity of 125000U / g and flavor protease activity of 105000U / g), purge with nitrogen throughout the process, control the dissolved oxygen content of the hydrolysate to 0.6mg / L, and maintain a constant temperature of 42℃ for 2.2h, stirring for 5min every 20min during this period; after the first stage of enzymatic hydrolysis is completed, raise the temperature to 52℃, and use 0.1mol / L HCl solution to further hydrolyze the mixture. Adjust the pH to 5.5 with citric acid solution ( / L), and incubate for 10 min. Add 6.23 g of compound enzyme preparation II (papain and fig protease mixed at an enzyme activity ratio of 2:1.5, with papain activity of 155,000 U / g and fig protease activity of 85,000 U / g), continue to purge with nitrogen, and incubate at a constant temperature of 52℃ for 1.5 h. After the enzymatic hydrolysis is completed, raise the temperature to 92℃, incubate for 12 min to inactivate the enzyme, cool to 25℃, centrifuge at 6000 r / min for 20 min, and collect 2180 mL of the enzymatic hydrolysis supernatant.

[0029] 4. Precise membrane separation and purification: 2180 mL of enzymatic hydrolysis supernatant was sent to the membrane separation system and sequentially passed through 500 kDa, 150 kDa, 30 kDa, and 5 kDa ceramic composite membranes for staged ultrafiltration, cross-flow filtration, with an ultrafiltration pressure of 0.8 MPa, a temperature of 35 °C, and a flow rate of 1.2 m / s. After each stage of ultrafiltration, the membrane surface was rinsed with the corresponding volume of deionized water. 890 mL of the 5 kDa-30 kDa permeate was collected. This permeate was then sent to a nanofiltration membrane system for desalting and concentration using a nanofiltration membrane with a molecular weight cutoff of 800 Da, with a nanofiltration pressure of 1.2 MPa and a temperature of 30 °C, until the solid content was 25%, yielding 286 mL of apricot collagen peptide concentrate (conductivity 132 μs / cm, desalting rate 99.2%).

[0030] 5. Drying and refining: 286 mL of concentrated liquid was sent to a vacuum freeze dryer, pre-frozen at -40℃ for 2 h, sublimated at -5℃ for 8 h, and desorption at 35℃ for 4 h, with a vacuum degree of 15 Pa. After drying, 72.3 g of apricot collagen peptide powder was obtained, which was then pulverized and passed through an 80-mesh sieve and aseptically packaged to obtain the finished product.

[0031] The relevant detection data of the apricot collagen peptides prepared in this embodiment are shown in Tables 1 and 2 below:

[0032] Table 1. Detection results of basic physicochemical indicators of apricot collagen peptides

[0033] Table 2: Results of Efficacy Indicators of Apricot Collagen Peptides

[0034] The above are merely preferred embodiments of the present invention and are not intended to limit the present invention. Any modifications, equivalent substitutions, and improvements made within the spirit and principles of the present invention should be included within the scope of protection of the present invention.

Claims

1. Preparation and application of apricot collagen peptides, characterized in that, The coupled process of "raw material pretreatment - gradient degreasing and impurity removal - complex stepwise enzymatic hydrolysis - precise membrane separation and purification - drying and purification" is adopted, and the specific steps are as follows: (1) Raw material pretreatment: Select apricot fruits with a maturity of 85%-90% (with the apricot flesh and pit intact, without peeling or pitting) and one-year-old apricot twigs. After removing rotten, diseased, pest-infested, and impurities, rinse with deionized water 3-4 times and drain. Mix apricot fruits (including apricot flesh and pit): apricot pit: apricot twigs in a mass ratio of 3:1:2, freeze at -35℃ for 8 hours, and then ultrafine grind to 800-1000 mesh at ≤-10℃. Apricot mixed ultrafine powder was obtained; a composite pretreatment solution with a mass ratio of 8 times was added to the apricot mixed ultrafine powder. The composite pretreatment solution was prepared by mixing 0.35 mol / L citric acid-sodium citrate buffer and 0.12% phytic acid solution at a volume ratio of 5:2, pH=4.8, and soaked at room temperature (25±2℃) for 2.5 h, with stirring for 10 min every 30 min during the soaking period; the filter residue was collected by vacuum filtration and dried at 45℃ under vacuum until the moisture content was ≤5.0%, thus obtaining pretreated apricot raw material. (2) Gradient degreasing and impurity removal: The pretreated apricot raw material was added to a supercritical CO2 extraction vessel, and 0.08% anhydrous ethanol was added as an entrainer. The extraction parameters were set as follows: extraction pressure 32MPa, extraction temperature 38℃, CO2 flow rate 22L / h, extraction time 1.8h. Gradient pressure adjustment was carried out during the extraction process. The pressure was increased from 10MPa to 32MPa in the first 30min, maintained at 32MPa for the middle 90min, and decreased from 32MPa to 10MPa in the last 30min. After the extraction was completed, 10 times the mass of high-purity deionized water (conductivity ≤10μs / cm) was added to the degreased material. The pH was adjusted to 7.2 with 0.1mol / L NaOH solution. The mixture was shaken at 55℃ and 120 times / min for 1h, centrifuged at 4500r / min for 15min, the precipitate was collected, and vacuum dried at 50℃ until the moisture content was ≤4.0% to obtain crude apricot collagen. (3) Compound stepwise enzymatic hydrolysis: Crude apricot gum was mixed with high-purity deionized water at a ratio of 1:7 (g / mL), and the pH was adjusted to 6.8 with 0.1 mol / L HCl solution. The mixture was heated to 42℃ and kept at that temperature for 10 min. 2.8% (relative to the mass of crude apricot gum) of compound enzyme preparation I was added. Compound enzyme preparation I was a mixture of neutral protease and flavor protease at an enzyme activity ratio of 3:1, wherein the neutral protease activity was ≥120000 U / g and the flavor protease activity was ≥100000 U / g. Nitrogen gas was used for protection throughout the process, and the dissolved oxygen content of the hydrolysate was controlled to be ≤0.8 mg / L. The hydrolysis was carried out at a constant temperature of 42℃ for 2.2 h, with stirring for 5 min every 20 min. Then the temperature was raised to 52℃ and the pH was adjusted with 0.1 mol / L citric acid solution. At 5.5°C, incubate for 10 minutes, then add 1.9% (relative to the mass of crude apricot collagen) of compound enzyme preparation II. Compound enzyme preparation II is a mixture of papain and fig protease at an enzyme activity ratio of 2:1.5, wherein the papain activity is ≥150,000 U / g and the fig protease activity is ≥80,000 U / g. Continue to purge with nitrogen and incubate at 52°C for 1.5 hours, stirring for 5 minutes every 20 minutes. After hydrolysis, incubate at 92°C for 12 minutes to inactivate the enzyme, cool to room temperature, centrifuge at 6000 r / min for 20 minutes, and collect the supernatant as the crude apricot collagen peptide hydrolysate. (4) Precise membrane separation and purification: The crude enzymatic hydrolysate of apricot collagen peptides was sequentially passed through 500kDa, 150kDa, 30kDa and 5kDa ceramic composite membranes for staged ultrafiltration. Cross-flow filtration mode was adopted, with an ultrafiltration pressure of 0.8MPa, an ultrafiltration temperature of 35℃ and a membrane surface flow rate of 1.2m / s. After each stage of ultrafiltration, the membrane surface was rinsed with 1 volume of high-purity deionized water to control the membrane flux decay rate ≤5.0%. The permeate from 5kDa to 30kDa was collected and sent to a nanofiltration membrane system. A nanofiltration membrane with a molecular weight cutoff of 800Da was used for desalting and concentration. The nanofiltration pressure was 1.2MPa and the nanofiltration temperature was 30℃. The concentration was carried out until the solid content was 25%, and the conductivity was controlled to be ≤150μs / cm and the desalting rate was ≥99.0% to obtain apricot collagen peptide concentrate. (5) Drying and refining: The concentrated apricot collagen peptide solution is sent into a vacuum freeze dryer, pre-freezing temperature -40℃ for 2 hours, sublimation temperature -5℃ for 8 hours, desorption temperature 35℃ for 4 hours, and vacuum degree 15Pa; after drying, it is crushed, passed through an 80-mesh sieve, and aseptically packaged to obtain the finished apricot collagen peptide product.

2. The preparation and application of apricot collagen peptides according to claim 1, characterized in that, In step (3), the neutral protease activity of compound enzyme preparation I is 125,000 U / g, and the flavor protease activity is 105,000 U / g; the papain activity of compound enzyme preparation II is 155,000 U / g, and the fig protease activity is 85,000 U / g.

3. A method for preparing and applying the apricot collagen peptide according to claim 1 or 2, characterized in that, The apricot collagen peptides have a molecular weight distribution of 1200-25000 Da, of which the proportion of highly active peptides in the 1200-8000 Da range is ≥88%, the hydroxyproline content is ≥12.5%, the purity is ≥95.5%, and the moisture content is ≤3.0%.

4. The preparation and application of apricot collagen peptide according to claim 3, characterized in that, The DPPH free radical scavenging rate of the apricot collagen peptide =0.18 mg / mL, ABTS free radical scavenging rate =0.22mg / mL, hydroxyl radical scavenging rate =0.35mg / mL.

5. The preparation and application of apricot collagen peptide according to claim 3, characterized in that, The apricot collagen peptide inhibited the skin collagen-degrading enzymes MMP-1 and MMP-3 by 78.2% and 72.5%, respectively, promoted the proliferation rate of human skin fibroblasts by 68.5%, and increased the synthesis of type I collagen in the skin by 59.3%.

6. The preparation and application of apricot collagen peptide according to claim 3, characterized in that, The apricot collagen peptide has a tyrosinase inhibition rate of 65.8%, can reduce melanin production by melanocytes by 62.7%, increase the moisture content of the stratum corneum by 42.8%, and reduce the transepidermal water loss rate by 37.5%.

7. The preparation and application of apricot collagen peptide according to claim 3, characterized in that, The apricot collagen peptides are free of heavy metal residues, allergens, and antibiotic residues, with lead ≤0.1mg / kg, mercury ≤0.01mg / kg, and arsenic ≤0.1mg / kg. Under conditions of pH 3.0-8.0 and temperature -20℃-60℃, the activity retention rate is ≥95.0%.

8. The preparation and application of apricot collagen peptides according to any one of claims 3-7, characterized in that, The apricot collagen peptide may be added to cosmetics, health foods, or topical skin care preparations as a core active ingredient or alone, at a concentration of 0.5%-15.0% (mass fraction).

9. The preparation and application of apricot collagen peptide according to claim 8, characterized in that, The cosmetics include serums, creams, masks, toners, lotions, and gels; the health foods include oral tablets, oral liquids, granules, and capsules; and the topical skin care preparations include medical cold compresses, repair gels, and moisturizing creams.

10. The preparation and application of apricot collagen peptide according to claim 8, characterized in that, The apricot collagen peptides described herein are suitable for various skin types, including sensitive, dry, and oily skin, as well as for all types of people.

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