A collagen peptide capable of effectively delaying skin aging and its preparation method

Abstract

The present invention relates to the technical field of collagen peptides, and specifically relates to a collagen peptide capable of effectively delaying skin aging and a preparation method thereof. After washing and drying animal bones, they are crushed to obtain bone particles. After degreasing and decalcifying the bone particles, organic acids and protease are added for enzymatic hydrolysis. After the enzymatic hydrolysis is completed, the enzyme is inactivated and the supernatant is collected and filtered through a 3 kDa ultrafiltration membrane. The filtrate is collected and freeze-dried to obtain a crude collagen peptide. The crude collagen peptide is added to an ethanol aqueous solution to obtain a mixed solution. The mixed solution is transported to a reactor filled with ionic liquid by a high-pressure constant flow pump for deodorization. The deodorized reaction solution is collected and filtered again through a 3 kDa ultrafiltration membrane and then spray-dried. The finished collagen peptide prepared by the method of the present invention can be completely odorless. Moreover, through mouse experiments, it can be seen that the collagen peptide of the present invention can delay skin aging by increasing the activity of antioxidant enzymes and reducing the generation of free radicals.

Description

Technical Field

[0001] The present invention relates to the technical field of collagen peptides, in particular to a collagen peptide capable of effectively delaying skin aging and a preparation method thereof. Background Art

[0002] Collagen peptides are the hydrolysis products of collagen. Compared with collagen, the bioactive amino acids in the peptide molecules have obvious antioxidant effects, and have the effects of delaying skin aging, preventing atherosclerosis, and promoting bone cell growth.

[0003] Animal bones are rich in nutrients such as protein, minerals, and fat, among which collagen is the main component of bone-derived protein. Therefore, extracting collagen from animal bones and further preparing it into collagen peptides is a promising way to transform scientific and technological achievements. The comprehensive utilization of bone by-products can not only reduce environmental pollution, but also have high economic and social benefits. However, bone-derived collagen peptides will produce some unpleasant odors during the preparation and processing process, which seriously restricts their application and market promotion prospects. Summary of the Invention

[0004] In response to the above technical problems, the present invention proposes a collagen peptide that can effectively delay skin aging and a preparation method thereof.

[0005] The technical solutions adopted are as follows:

[0006] A method for preparing collagen peptide that can effectively delay skin aging is as follows:

[0007] The animal bones are washed, dried, and crushed to obtain bone particles. The bone particles are defatted and decalcified, and then organic acid and protease are added for enzymatic hydrolysis. After the enzymatic hydrolysis, the enzyme is inactivated, the clear liquid is collected, and filtered with a 3kDa ultrafiltration membrane. The filtrate is collected and freeze-dried to obtain a crude collagen peptide. The crude collagen peptide is added to an ethanol aqueous solution to obtain a mixed solution. The mixed solution is transported to a reactor filled with an ionic liquid by a high-pressure constant flow pump for deodorization. The deodorized reaction liquid is collected, filtered again with a 3kDa ultrafiltration membrane, and spray-dried.

[0008] Furthermore, the degreasing method is as follows:

[0009] Add the bone particles into a Soxhlet extractor, use petroleum ether as the extraction solvent, and reflux extraction for 1-5 hours.

[0010] Furthermore, the decalcification method is as follows:

[0011] Add the defatted bone particles into the EDTA solution and continue to stir and decalcify for 16-40 hours. During this period, replace the fresh EDTA solution every 4-8 hours. After decalcification, collect the precipitate, wash it, and dry it.

[0012] Further, the organic acid is a composition of lauric acid, citric acid and glacial acetic acid;

[0013] The mass ratio of lauric acid, citric acid and glacial acetic acid is 1-10:1-10:1-10.

[0014] Further, the protease is any one or a combination of two or more of pepsin, alkaline protease, neutral protease, papain and trypsin.

[0015] Further, the ionic liquid is loaded on a molecular sieve.

[0016] Further, the molecular sieve is SBA-15 molecular sieve.

[0017] Further, the ionic liquid has a dual acidic group.

[0018] Further, the ionic liquid is 1-sulfobutyl-3-methylimidazolium hydrogen sulfate.

[0019] The present invention also provides a collagen peptide capable of effectively delaying skin aging, which is prepared by the above preparation method.

[0020] Advantages of the present invention:

[0021] The present invention provides a collagen peptide capable of effectively delaying skin aging and a preparation method thereof. Aiming at the problem that the off-odor of bone-derived collagen peptide affects the product quality in the prior art, an ionic liquid with a dual acidic group is used as a highly active catalyst to catalyze the reaction of impurities such as isobutyric acid, hexanoic acid, butyric acid and other fatty acids that produce odor in the crude collagen peptide with ethanol to form low-boiling esters, and then spray drying is used to remove them, realizing the improvement of the quality of collagen peptide. SBA-15 molecular sieve can not only form a covalent bond with the ionic liquid as a carrier to firmly fix it, improve the stability and make it not easy to lose, but also make the ionic liquid have a high degree of dispersion, increase the contact area between the reactants and the ionic liquid, and improve the reaction rate. In addition, SBA-15 molecular sieve also has certain catalytic activity for the esterification reaction and can cooperate with the ionic liquid to improve the reaction rate. Compared with activated carbon deodorization, the finished collagen peptide prepared by the method of the present invention can be completely odorless. Moreover, through mouse experiments, it can be seen that the collagen peptide of the present invention can delay skin aging by increasing the activity of antioxidant enzymes and reducing the generation of free radicals. Specific embodiments

[0022] For those without specific conditions indicated in the examples, they are carried out according to conventional conditions or the conditions recommended by the manufacturer. For reagents or instruments without the manufacturer indicated, they are all conventional products that can be obtained through commercial purchase. Technologies not mentioned in the present invention refer to the prior art. Unless otherwise specified, the following examples and comparative examples are parallel tests and adopt the same treatment steps and parameters.

[0023] Example 1:

[0024] This example provides a preparation method of collagen peptide that can effectively delay skin aging:

[0025] After thoroughly washing fresh horse tibia with deionized water, it is dried, pulverized, and passed through a 20-mesh sieve to obtain bone particles. The bone particles are added to a Soxhlet extractor, and petroleum ether is used as the extraction solvent. After reflux extraction for 1 - 5 h, degreased bone particles are obtained. The degreased bone particles are added to a 5% (mass concentration) EDTA solution, and the mass ratio of solid to liquid is 1:10. Stir continuously for 36 h for decalcification, and fresh EDTA solution is replaced every 6 h during this period. After decalcification, the precipitate is collected, washed thoroughly with deionized water, and dried to obtain degreased and decalcified bone particles. According to the mass ratio of 1:10, the degreased and decalcified bone particles are added to deionized water, and an organic acid and pepsin accounting for 5% and 1% of the mass of the degreased and decalcified bone particles are added respectively. The organic acid is composed of lauric acid, citric acid, and glacial acetic acid with a mass ratio of 1:4:10. Stir continuously at 4 °C for 24 h for enzymatic hydrolysis, then inactivate the enzyme and centrifuge. The supernatant is collected and filtered through a 3 kDa ultrafiltration membrane, and the filtrate is collected and freeze-dried to obtain the crude collagen peptide. The crude collagen peptide is added to an ethanol aqueous solution with a mass concentration of 10% to obtain a mixed solution with a concentration of 0.05 g / ml. The mixed solution is pumped into a fixed-bed reactor through a high-pressure constant-flow pump at a flow rate of 0.5 ml / min for deodorization. The fixed-bed reactor is filled with 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve, the bed height is 5 cm, and the deodorization temperature is 70 °C. The deodorized reaction solution is collected, filtered again through a 3 kDa ultrafiltration membrane, and spray-dried at 140 °C to obtain the finished collagen peptide. The short peptide yield measured by the trichloroacetic acid-soluble polypeptide method is 58.3%.

[0026] Among them, the preparation method of 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve is as follows:

[0027] The SBA-15 molecular sieve is added to an ethanol aqueous solution with a mass concentration of 10% according to the mass ratio of solid to liquid of 1:10 and mixed evenly. Then, 1-sulfobutyl-3-methylimidazolium hydrogen sulfate accounting for 5% of the mass of the SBA-15 molecular sieve is added, and after rapid stirring for 30 min, the water is evaporated by heating.

[0028] Example 2:

[0029] This embodiment provides a preparation method of collagen peptides that can effectively delay skin aging:

[0030] The fresh horse tibia is thoroughly washed with deionized water, dried, pulverized, and passed through a 20-mesh sieve to obtain bone particles. The bone particles are added to a Soxhlet extractor, and petroleum ether is used as the extraction solvent. After reflux extraction for 1 - 5 h, defatted bone particles are obtained. The defatted bone particles are added to an EDTA solution with a mass concentration of 5%, and the mass ratio of the material to the liquid is 1:10. Decalcification is carried out with continuous stirring for 36 h, and the fresh EDTA solution is replaced every 6 h. After decalcification, the precipitate is collected, thoroughly washed with deionized water, and dried to obtain defatted and decalcified bone particles. The defatted and decalcified bone particles are added to deionized water according to a mass ratio of 1:10, and an organic acid and pepsin accounting for 5% and 1% of the mass of the defatted and decalcified bone particles are added respectively. The organic acid is composed of lauric acid, citric acid, and glacial acetic acid with a mass ratio of 1:4:10. Enzymolysis is carried out with continuous stirring at 4°C for 24 h, then the enzyme is inactivated and centrifuged. The supernatant is collected and filtered through a 3 kDa ultrafiltration membrane, and the filtrate is collected and freeze-dried to obtain the crude collagen peptides. The crude collagen peptides are added to an ethanol aqueous solution with a mass concentration of 10% to obtain a mixed solution with a concentration of 0.05 g / ml. The mixed solution is delivered to a fixed-bed reactor through a high-pressure constant-flow pump at a flow rate of 0.5 ml / min for deodorization. The fixed-bed reactor is filled with 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve, the bed height is 5 cm, and the deodorization temperature is 40°C. The reaction solution after deodorization is collected, filtered again through a 3 kDa ultrafiltration membrane, and spray-dried at 140°C to obtain the finished collagen peptides. The short peptide yield measured by the trichloroacetic acid-soluble polypeptide method is 50.2%.

[0031] Among them, the preparation method of 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve is the same as that in Example 1.

[0032] Example 3:

[0033] This embodiment provides a preparation method of collagen peptides that can effectively delay skin aging:

[0034] The fresh horse tibia was thoroughly washed with deionized water and then dried. After being crushed, it was passed through a 20-mesh sieve to obtain bone particles. The bone particles were added to a Soxhlet extractor, and petroleum ether was used as the extraction solvent. After reflux extraction for 1 - 5 h, defatted bone particles were obtained. The defatted bone particles were added to an EDTA solution with a mass concentration of 5%, and the mass ratio of the material to the liquid was 1:10. It was continuously stirred for 36 h for decalcification, and the fresh EDTA solution was replaced every 6 h during this period. After decalcification, the precipitate was collected, thoroughly washed with deionized water and dried to obtain defatted and decalcified bone particles. According to the mass ratio of 1:10, the defatted and decalcified bone particles were added to deionized water, and an organic acid and pepsin accounting for 5% and 1% of the mass of the defatted and decalcified bone particles were added respectively. The organic acid was composed of lauric acid, citric acid and glacial acetic acid with a mass ratio of 1:4:10. It was continuously stirred and enzymolyzed at 4°C for 24 h, then inactivated and centrifuged. The supernatant was collected and filtered through a 3 kDa ultrafiltration membrane, and the filtrate was collected and freeze-dried to obtain a crude collagen peptide product. The crude collagen peptide product was added to an ethanol aqueous solution with a mass concentration of 10% to obtain a mixed solution with a concentration of 0.05 g / ml. The mixed solution was delivered to a fixed-bed reactor through a high-pressure constant-flow pump at a flow rate of 0.5 ml / min for deodorization. The fixed-bed reactor was filled with 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve, the bed height was 5 cm, and the deodorization temperature was 50°C. The reaction solution after deodorization was collected, filtered again through a 3 kDa ultrafiltration membrane and spray-dried at 140°C to obtain the finished collagen peptide product. The short peptide yield was measured to be 53.5% by the trichloroacetic acid-soluble polypeptide method.

[0035] Among them, the preparation method of 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve was the same as that in Example 1.

[0036] Example 4:

[0037] This example provides a preparation method of collagen peptide that can effectively delay skin aging:

[0038] After thoroughly washing fresh horse tibia with deionized water, it was dried, crushed, and passed through a 20-mesh sieve to obtain bone particles. The bone particles were added to a Soxhlet extractor, and petroleum ether was used as the extraction solvent. After reflux extraction for 1 - 5 h, defatted bone particles were obtained. The defatted bone particles were added to an EDTA solution with a mass concentration of 5%, and the mass ratio of solid to liquid was 1:10. Decalcification was carried out with continuous stirring for 36 h, and fresh EDTA solution was replaced every 6 h. After decalcification, the precipitate was collected, thoroughly washed with deionized water, and dried to obtain defatted and decalcified bone particles. According to a mass ratio of 1:10, the defatted and decalcified bone particles were added to deionized water, and an organic acid and pepsin accounting for 5% and 1% of the mass of the defatted and decalcified bone particles were added respectively. The organic acid was composed of lauric acid, citric acid, and glacial acetic acid with a mass ratio of 1:4:10. Enzymatic hydrolysis was carried out with continuous stirring at 4°C for 24 h, then the enzyme was inactivated and centrifuged. The supernatant was collected and filtered through a 3 kDa ultrafiltration membrane. The filtrate was collected and freeze-dried to obtain a crude collagen peptide product. The crude collagen peptide product was added to an ethanol aqueous solution with a mass concentration of 10% to obtain a mixed solution with a concentration of 0.05 g / ml. The mixed solution was pumped into a fixed-bed reactor through a high-pressure constant-flow pump at a flow rate of 0.5 ml / min for deodorization. The fixed-bed reactor was filled with 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve, the bed height was 5 cm, and the deodorization temperature was 60°C. The reaction solution after deodorization was collected, filtered again through a 3 kDa ultrafiltration membrane, and spray-dried at 140°C to obtain the finished collagen peptide product. The short peptide yield was measured to be 55.4% by the trichloroacetic acid-soluble polypeptide method.

[0039] Among them, the preparation method of 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve was the same as that in Example 1.

[0040] Example 5:

[0041] This example provides a preparation method of collagen peptide that can effectively delay skin aging:

[0042] The fresh horse tibia was thoroughly washed with deionized water and then dried. After being crushed, it was passed through a 20-mesh sieve to obtain bone particles. The bone particles were added to a Soxhlet extractor, and petroleum ether was used as the extraction solvent. After reflux extraction for 1 - 5 h, defatted bone particles were obtained. The defatted bone particles were added to a 5% (mass concentration) EDTA solution, and the mass ratio of the solid to the liquid was 1:10. Decalcification was carried out with continuous stirring for 36 h, and the fresh EDTA solution was replaced every 6 h. After decalcification, the precipitate was collected, thoroughly washed with deionized water and dried to obtain defatted and decalcified bone particles. The defatted and decalcified bone particles were added to deionized water according to a mass ratio of 1:10, and an organic acid and pepsin, which were 5% and 1% of the mass of the defatted and decalcified bone particles respectively, were added. The organic acid was composed of lauric acid, citric acid and glacial acetic acid with a mass ratio of 1:4:10. Enzymatic hydrolysis was carried out with continuous stirring at 4°C for 24 h, then the enzyme was inactivated and centrifuged. The supernatant was collected and filtered through a 3 kDa ultrafiltration membrane. The filtrate was collected and freeze-dried to obtain a crude collagen peptide product. The crude collagen peptide product was added to an ethanol aqueous solution with a mass concentration of 10% to obtain a mixed solution with a concentration of 0.05 g / ml. The mixed solution was pumped into a fixed-bed reactor through a high-pressure constant-flow pump at a flow rate of 0.5 ml / min for deodorization. The fixed-bed reactor was filled with 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve, the bed height was 5 cm, and the deodorization temperature was 80°C. The deodorized reaction solution was collected, filtered again through a 3 kDa ultrafiltration membrane and spray-dried at 140°C to obtain the finished collagen peptide product. The short peptide yield was measured to be 56.9% by the trichloroacetic acid-soluble polypeptide method.

[0043] Among them, the preparation method of 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve was the same as that in Example 1.

[0044] Comparative Example 1:

[0045] It was basically the same as Example 1, except that lauric acid was not included in the organic acid. [[ID=ll]]

[0046] This comparative example provides a preparation method of a collagen peptide that can effectively delay skin aging:

[0047] The fresh horse tibia was thoroughly washed with deionized water and then dried. After being crushed, it was passed through a 20-mesh sieve to obtain bone particles. The bone particles were added to a Soxhlet extractor, and petroleum ether was used as the extraction solvent. After reflux extraction for 1 - 5 h, defatted bone particles were obtained. The defatted bone particles were added to a 5% (mass concentration) EDTA solution, and the mass ratio of the material to the liquid was 1:10. Stirring was carried out continuously for 36 h for decalcification, and fresh EDTA solution was replaced every 6 h during this period. After decalcification, the precipitate was collected, washed thoroughly with deionized water, and dried to obtain defatted and decalcified bone particles. According to a mass ratio of 1:10, the defatted and decalcified bone particles were added to deionized water, and an organic acid and pepsin accounting for 5% and 1% of the mass of the defatted and decalcified bone particles were added respectively. The organic acid was composed of citric acid and glacial acetic acid with a mass ratio of 4:10. Stirring was carried out continuously at 4 °C for enzymatic hydrolysis for 24 h, then the enzyme was inactivated and centrifuged. The supernatant was collected and filtered through a 3 kDa ultrafiltration membrane, and the filtrate was collected and freeze-dried to obtain the crude collagen peptide. The crude collagen peptide was added to an ethanol aqueous solution with a mass concentration of 10% to obtain a mixed solution with a concentration of 0.05 g / ml. The mixed solution was pumped into a fixed-bed reactor through a high-pressure constant-flow pump at a flow rate of 0.5 ml / min for deodorization. The fixed-bed reactor was filled with 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve, the bed height was 5 cm, and the deodorization temperature was 70 °C. The reaction solution after deodorization was collected, filtered again through a 3 kDa ultrafiltration membrane, and spray-dried at 140 °C to obtain the finished collagen peptide. The short peptide yield measured by the trichloroacetic acid-soluble polypeptide method was 51.3%. The hydrolysis of collagen is the breaking of peptide bonds in the molecule. Acid can attack peptide bonds and cause them to break. Lauric acid contains an alkyl long chain, and its addition may cause changes in the spatial structure during the hydrolysis of collagen, improve the efficiency of the action of acid, and increase the target sites of the enzyme, thereby enhancing the enzymatic hydrolysis efficiency and increasing the yield.

[0048] Among them, the preparation method of 1-sulfobutyl-3-methylimidazolium hydrogen sulfate / SBA-15 molecular sieve is the same as that in Example 1.

[0049] Comparative Example 2:

[0050] It is basically the same as Example 1, except that the crude collagen peptide was deodorized with activated carbon. The specific method is as follows:

[0051] The crude collagen peptide was added to deionized water to obtain a solution with a concentration of 0.05 g / ml, and 1% (by mass of the crude collagen peptide) powdered activated carbon was added. It was heated to 70 °C in an ultrasonic water bath and stirred for 1 h, then filtered. The obtained filtrate was filtered again through a 3 kDa ultrafiltration membrane and spray-dried at 140 °C to obtain the finished collagen peptide. The short peptide yield measured by the trichloroacetic acid-soluble polypeptide method was 34.6%.

[0052] Comparative Example 3:

[0053] Basically the same as Example 1, except that only 1-sulfobutyl-3-methylimidazolium hydrogensulfate is filled in the fixed-bed reactor, that is, SBA-15 molecular sieve is not used as a carrier.

[0054] This comparative example provides a method for preparing collagen peptides that can effectively delay skin aging:

[0055] The fresh horse tibia is thoroughly washed with deionized water and then dried, crushed and sieved through a 20-mesh sieve to obtain bone particles. The bone particles are added to a Soxhlet extractor, and petroleum ether is used as the extraction solvent. After reflux extraction for 1-5 h, defatted bone particles are obtained. The defatted bone particles are added to a 5% (mass concentration) EDTA solution, and the mass ratio of the material to the liquid is 1:10. Stir continuously for 36 h to remove calcium, and replace the fresh EDTA solution every 6 h during this period. After the calcium removal is completed, collect the precipitate, wash it thoroughly with deionized water and dry it to obtain defatted and decalcified bone particles. Add the defatted and decalcified bone particles to deionized water according to a mass ratio of 1:10, and add an organic acid and pepsin accounting for 5% and 1% of the mass of the defatted and decalcified bone particles respectively. The organic acid is composed of lauric acid, citric acid and glacial acetic acid with a mass ratio of 1:4:10. Stir and enzymatically hydrolyze at 4 °C for 24 h, then inactivate the enzyme and centrifuge. Collect the supernatant, filter it through a 3 kDa ultrafiltration membrane, and freeze-dry the filtrate to obtain a crude collagen peptide product. Add the crude collagen peptide product to an ethanol aqueous solution with a mass concentration of 10% to obtain a mixed solution with a concentration of 0.05 g / ml. The mixed solution is pumped into a fixed-bed reactor through a high-pressure constant flow pump at a flow rate of 0.5 ml / min for deodorization. The fixed-bed reactor is filled with 1-sulfobutyl-3-methylimidazolium hydrogensulfate, the bed height is 5 cm, and the deodorization temperature is 70 °C. Collect the deodorized reaction solution, filter it again through a 3 kDa ultrafiltration membrane and spray-dry it at 140 °C to obtain the finished collagen peptide product. The short peptide yield measured by the trichloroacetic acid soluble polypeptide method is 57.7%.

[0056] Performance testing:

[0057] ① The crude collagen peptide products and finished collagen peptide products prepared in Examples 1-5 and Comparative Examples 1-3 of the present invention are subjected to olfactory perception judgment, and the olfactory perception judgment criteria are shown in Table 1 below:

[0058] Table 1:

[0059]

[0060] The test results are shown in Table 2 below:

[0061] Table 2:

[0062]

[0063] It can be seen from Table 2 that compared with activated carbon deodorization, the finished collagen peptide product prepared by the method of the present invention can achieve complete odorlessness.

[0064] ② Take 110 clean-grade 3-month-old female ICR mice, allow them to freely eat and drink, and maintain natural light. Randomly divide the mice into 11 groups (10 mice in each group), denoted as the normal group, the model group, and experimental groups 1-9. The normal group is subcutaneously injected with normal saline on the neck and back daily as a control, and the other groups are injected with D-galactose (1200 mg / kg bw) to establish a subacute aging model. The normal group and the model group are intragastrically administered normal saline daily, and experimental groups 1-9 are intragastrically administered the collagen peptide products prepared in Examples 1-5 and Comparative Examples 1-3 and commercially available collagen (Xi'an Ruierli Biology) (500 mg / kg bw) for 8 consecutive weeks. After the last intragastric administration of the mice, fast them for 12 h, draw blood by eye enucleation and sacrifice them, and test the SOD, GSH-P x activity and MDA content according to the kit instructions.

[0065] The above test results are shown in Table 3 below:

[0066] Table 3:

[0067]

[0068] The free radical theory is one of the internationally recognized aging theories. Reducing free radical production and increasing the activity of antioxidant enzymes have become effective methods for delaying skin aging at present. SOD and GSH-P x As the main enzymes for scavenging free radicals in the body, they are used as important reference indicators in the study of delaying aging. It can be seen from Table 3 above that the activities of SOD and GSH-P in the skin of the mice in the model group x significantly decreased, and the MDA content significantly increased, indicating that the antioxidant ability of the skin of the mice in the model group decreased, the free radical generation increased, and the intermolecular crosslinking intensified. The activities of SOD and GSH-P in the skin of the mice in experimental groups 1-9 x were significantly higher than those in the model group, and at the same time, the MDA content was significantly lower than that in the model group. This shows that the collagen peptide can delay skin aging by increasing the activity of antioxidant enzymes, and by comparison, it can be known that the anti-aging activity of the collagen peptide prepared by the present invention is superior to that of the commercially available collagen peptide.

[0069] The above embodiments are only used to illustrate the technical solutions of the present invention, rather than to limit it; although the present invention has been described in detail with reference to the foregoing embodiments, those of ordinary skill in the art should understand that they can still modify the technical solutions recorded in the foregoing embodiments, or perform equivalent replacements on some of the technical features; and these modifications or replacements do not make the essence of the corresponding technical solutions deviate from the spirit and scope of the technical solutions of the embodiments of the present invention.

Claims

1. A preparation method of collagen peptide capable of effectively delaying skin aging, characterized in that, The details are as follows: Wash the animal bones, dry them, and crush them to obtain bone particles. After degreasing and decalcifying the bone particles, add organic acids and protease for enzymatic hydrolysis. After the enzymatic hydrolysis is completed, inactivate the enzyme, collect the clear liquid, filter it with a 3 kDa ultrafiltration membrane, collect the filtrate, and freeze-dry it to obtain a crude collagen peptide. Add the crude collagen peptide to an ethanol aqueous solution to obtain a mixed solution. Transport the mixed solution to a reactor filled with ionic liquid through a high-pressure constant-flow pump for deodorization. Collect the deodorized reaction solution, filter it again with a 3 kDa ultrafiltration membrane, and spray-dry it. The ionic liquid is loaded on SBA-15 molecular sieve. The ionic liquid is 1-sulfobutyl-3-methylimidazolium hydrogen sulfate.

2. The preparation method of the collagen peptide capable of effectively delaying skin aging according to claim 1, characterized in that, The method for degreasing is as follows: Add the bone particles to a Soxhlet extractor, use petroleum ether as the extraction solvent, and reflux for 1 - 5 h.

3. The preparation method of the collagen peptide capable of effectively delaying skin aging as described in claim 1, characterized in that, The method for decalcifying is as follows: Add the degreased bone particles to an EDTA solution, continuously stir for decalcification for 16 - 40 h, and replace the fresh EDTA solution every 4 - 8 h during this period. After the decalcification is completed, collect the precipitate, wash it, and dry it.

4. The preparation method of the collagen peptide capable of effectively delaying skin aging according to claim 1, characterized in that, The organic acid is a composition of lauric acid, citric acid, and glacial acetic acid. The mass ratio of lauric acid, citric acid, and glacial acetic acid is 1 - 10:1 - 10:1 - 10.

5. The preparation method of the collagen peptide capable of effectively delaying skin aging as described in claim 1, characterized in that, The protease is any one or a combination of two or more of pepsin, alkaline protease, neutral protease, papain, and trypsin.

6. A collagen peptide that can effectively delay skin aging, characterized in that, Prepared by the preparation method described in any one of claims 1 - 5.

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