CN110713534A - Collagen peptide with photoaging improvement effect and preparation method thereof - Google Patents
Collagen peptide with photoaging improvement effect and preparation method thereof Download PDFInfo
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- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/78—Connective tissue peptides, e.g. collagen, elastin, laminin, fibronectin, vitronectin or cold insoluble globulin [CIG]
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- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/06—Preparation of peptides or proteins produced by the hydrolysis of a peptide bond, e.g. hydrolysate products
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Abstract
The invention discloses a collagen peptide with photoaging improvement effect and a preparation method thereof. The method comprises the steps of chopping and cleaning eel skin, soaking the eel skin in NaOH solution and butanol solution in sequence to remove non-collagen and fat, extracting the soaked eel skin by adopting an acid method and an enzyme method to obtain collagen, and finally performing in-vitro simulated digestion on the collagen to obtain collagen peptide powder. The invention adopts the acid method and the enzyme method to extract the collagen in the fish skin, the extraction rate is more than 80 percent, the purity is more than 85 percent, the finally hydrolyzed collagen peptide can improve the symptoms of skin collagen loss and the like caused by photoaging, and has good effects of beautifying and protecting the skin and delaying senility.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to fish skin collagen peptide with a photoaging improvement effect and a preparation method thereof.
Background
Photo-aging is a series of functional degradation changes caused by repeated irradiation of ultraviolet rays. The effects of photoaging on the skin are mainly manifested by skin laxity, dark yellow, wrinkles, pigmentation, etc., and severe cases may even cause malignant tumors of the skin. There are many bioactive substances in nature that can protect against uv damage, such as vitamins and their derivatives, antioxidant enzymes, plant extracts such as aloe, oat and grape seed extracts, etc., which block or slow tissue damage, primarily by scavenging or reducing free radicals and their intermediates. Therefore, the intake of bioactive substances can physiologically prevent skin aging without causing damage to the body.
Collagen, as a bioactive substance, has received a great deal of attention from the biomedical field due to its properties such as low antigenicity, high biocompatibility, and high nutritional value. However, collagen, as a macromolecular protein, is not easily absorbed directly by the human body, and thus it needs to be hydrolyzed into smaller polypeptides and amino acids. The hydrolyzed collagen can be well absorbed and utilized by the body, the absorption rate can reach 100 percent, and the absorption of other proteins in food can be promoted. Research proves that the collagen I hydrolysate can be specifically enriched in skin and utilized after being orally absorbed, and the edible collagen can inhibit harmful changes of skin moisture content reduction, epidermal cell proliferation, collagen content reduction and the like caused by ultraviolet radiation. In recent years, the collagen from marine aquatic products has excellent characteristics of low antigenicity, low irritability and the like, is not influenced by livestock and poultry diseases such as avian influenza and religion, and gradually replaces the traditional pig, cattle and sheep as a good raw material for extracting the collagen.
The eel is widely distributed in coastal areas of China, and has high edible and medicinal values. Although the eel breeding industry in China is very luxuriant, the eel processing technology is very weak, the processing rate is low, the product is single, and wastes such as fishbone, fishskin, fishhead, viscera and the like generated in the actual production and processing process cause a great deal of resource waste. Wherein the eel skin can be used as a good source for extracting collagen, and can improve the added value of eel.
The existing extraction methods of collagen mainly comprise an acid method, an enzyme method, an alkaline method, a hot water method and a salt method, and have the advantages and the disadvantages. The single collagen extraction method cannot meet the production requirements, and the safety and the biological activity of the obtained collagen peptide are in need of examination. Therefore, the invention provides the method for extracting the eel skin collagen by the acid-enzyme method, the obtained collagen product has high purity, the collagen structure is kept complete, the collagen peptide obtained by the in vitro digestion model hydrolysis has high safety, has good repairing and improving effects on skin photoaging injury, and provides a new idea for the development and utilization of the eel skin.
Disclosure of Invention
Aiming at the defects of the prior art, the invention provides a method for extracting collagen by combining an acid method and an enzyme method, and the collagen peptide with the skin improvement effect on photoaging is obtained by digesting eel skin collagen through an in-vitro digestion model.
In order to achieve the purpose, the invention adopts the following technical scheme:
a collagen peptide having a photoaging-ameliorating effect, which is prepared by a method comprising the steps of:
(1) raw material treatment: cutting eel skin into pieces with size of about 1cm2Adding the fragments into ice water, and cleaning by using a magnetic stirrer until the solution is clear;
(2) removing non-collagen, namely soaking the minced eel skin in 0.1mol/L NaOH solution for 48 hours according to the feed-liquid ratio of 1:10 g/mL, replacing the NaOH solution every 4 ~ 12 hours in the soaking process, and then washing the eel skin with distilled water until the washing liquid is neutral;
(3) degreasing, namely soaking the eel skin for 48 hours by using a butanol solution with the volume concentration of 10% according to the material-liquid ratio of 1:10 g/mL, replacing the butanol solution every 4 ~ 12 hours in the soaking process, and after soaking, washing the eel skin by using distilled water again until the washing liquid has no alcohol smell and no layering exists after standing;
(4) and (3) extraction: soaking the eel skin treated in the step (3) in 0.5mol/L acetic acid solution according to the material-liquid ratio of 1:10-30 g/mL for 18-30 h, continuously stirring by using a magnetic stirrer, after soaking, centrifuging, taking supernatant, storing in a refrigerator at 4 ℃, soaking the obtained precipitate in 0.5mol/L acetic acid solution according to the material-liquid ratio of 1:10-30 g/mL for 18-30 h, after soaking, centrifuging, taking supernatant, combining the supernatants obtained in two times, and adjusting the pH value to be neutral; then soaking the rest precipitate into 0.5mol/L acetic acid solution according to the material-liquid ratio of 1:10-30 g/mL, adding pepsin according to the amount of 20U/g, continuously stirring and soaking for 18-30 h, centrifuging to obtain supernatant, and adjusting the pH to be neutral;
(5) salting out: mixing the extracted supernatants, slowly adding NaCl and continuously stirring until the final concentration of NaCl reaches 2.6mol/L, centrifuging, and taking a precipitate;
(6) dialyzing, namely re-dissolving the precipitate obtained by centrifugation in 0.5mol/L acetic acid solution, dialyzing for 24 ~ 48h in 0.1mol/L acetic acid solution, and dialyzing for 24 ~ 48h with distilled water, wherein the dialysate is replaced every 4 ~ 12h during dialysis;
(7) freeze-drying: after dialysis, freeze-drying the solution in the dialysis bag to obtain eel skin collagen;
(8) digestion: simulating the digestion environment of the gastrointestinal tract of a human body, establishing an in-vitro digestion model to digest eel skin collagen, heating the mixed solution at 90 ℃ for 10 min to stop digestion, centrifuging at 4 ℃ for 20 min under 12000 g to obtain a collagen peptide mixed solution, performing ultrafiltration by using an ultrafiltration membrane with the molecular weight cutoff of 3000Da, and freeze-drying to obtain the collagen peptide with the small molecular weight.
The centrifugation in step (4) was carried out at 15000g for 15 min.
The centrifugation in step (5) was carried out at 15000g for 15 ~ 30 min.
Step (1) ~ (6) was all done at 4 ℃.
The digestion in the step (8) is specifically to treat the eel skin collagen by respectively taking artificial saliva, artificial gastric juice and artificial intestinal juice as digestive juice at 37 +/-2 ℃ according to the digestion process of food in the oral cavity, the stomach and the small intestine of a human body; wherein 50mL of artificial saliva, 100mL of artificial gastric juice and 150mL of artificial intestinal juice are used for every 3g of eel skin collagen.
The invention has the advantages and positive effects that:
1. the invention combines the acid method and the enzyme method to extract the collagen, can greatly extract the collagen from the eel skin, and has the extraction rate of more than 80 percent and the purity of more than 85 percent;
2. the invention obtains the collagen peptide by simulating the complete digestion process of the human body and digesting the collagen, and the obtained product is safer
3. The collagen peptide produced by the method has obvious antioxidant effect, has excellent improvement effect on skin collagen and water loss and other damages caused by photoaging, is beneficial to delaying aging and has great commercial production value.
Drawings
FIG. 1 is an SDS-PAGE gel of the collagen obtained in example 1;
FIG. 2 is a graph showing an ultraviolet absorption spectrum of collagen obtained in example 1;
FIG. 3 is a Fourier transform infrared absorption spectrum of collagen obtained in example 1;
FIG. 4 is a graph of the effect of different treatments on the organ index of mice;
FIG. 5 is a graph of the effect of different treatments on skin moisture content in photoaged mice;
FIG. 6 is a graph of the effect of different treatments on hydroxyproline content in the skin of photoaged mice;
FIG. 7 is a graph of the effect of different treatments on antioxidant activity in mouse skin;
FIG. 8 is a graph of the effect of different treatments on MDA levels in mouse skin;
FIG. 9 is a graph of the morphological changes in the skin tissue of the back of mice after different treatments.
Detailed Description
In order to make the present invention more comprehensible, the technical solutions of the present invention are further described below with reference to specific embodiments, but the present invention is not limited thereto.
Example 1
A collagen peptide having a photoaging-ameliorating effect, which is prepared by a method comprising the steps of:
(1) raw material treatment: scraping residual fish meat from eel skin, and cutting into pieces with size of about 1cm2Adding the fragments into ice water, repeatedly stirring and cleaning by using a magnetic stirrer, and replacing the ice water until the solution becomes clear;
(2) removal of non-collagenous proteins: soaking the minced eel skin in 0.1mol/L NaOH solution for 48h according to the material-liquid ratio of 1:10 g/mL, and replacing the NaOH solution every 12h in the soaking process (after the first eel skin soaking is swelled, the eel skin is minced again to improve the soaking effect); then, washing the eel skin with distilled water until the washing liquid is neutral;
(3) degreasing: soaking eel skin for 48 hours again by using a butanol solution with the volume concentration of 10% according to the feed-liquid ratio of 1:10 g/mL, and replacing the butanol solution every 12 hours in the soaking process; after soaking, washing the eel skin with distilled water again until the washing liquid has no alcohol smell and no layering exists after standing;
(4) and (3) extraction: soaking the eel skin treated in the step (3) in 0.5mol/L acetic acid solution for 24h according to the material-liquid ratio of 1:10 g/mL, continuously stirring by using a magnetic stirrer during the soaking, centrifuging for 15min under the condition of 15000g after the soaking is finished, taking the supernatant, storing at 4 ℃, soaking the obtained precipitate in 0.5mol/L acetic acid solution for 24h according to the material-liquid ratio of 1:10 g/mL, continuously stirring by using a magnetic stirrer during the soaking, centrifuging for 15min under the condition of 15000g after the soaking is finished, taking the supernatant, combining the supernatants obtained in two times, and adjusting the pH to be neutral; then immersing the residual precipitate after centrifugation into 0.5mol/L acetic acid solution according to the material-liquid ratio of 1:10 g/mL, adding pepsin according to the amount of 20U/g, continuously stirring for 24h, centrifuging for 15min under the condition of 15000g, taking supernatant, and adjusting the pH value to be neutral;
(5) salting out, namely combining the supernatant obtained by extraction, slowly adding NaCl and continuously stirring until the final concentration of the NaCl reaches 2.6mol/L, centrifuging at 15000g for 15 ~ 30min, and taking a precipitate;
(6) dialyzing, namely re-dissolving the precipitate obtained by centrifugation in 0.5mol/L acetic acid solution, dialyzing for 24 ~ 48h in 0.1mol/L acetic acid solution, and dialyzing for 24 ~ 48h with distilled water, wherein the dialysate is replaced every 6h during dialysis;
(7) freeze-drying: after dialysis, freeze-drying the solution in the dialysis bag to obtain eel skin collagen;
(8) digestion: establishing an in-vitro digestion model according to the digestion process of food in oral cavity, stomach and small intestine of a human body, wherein the in-vitro digestion model is specifically that 3g of collagen is firstly put into a conical flask, and 50mL of artificial saliva is added for full mixing; then adding 100mL of artificial gastric juice into the mixed solution twice, keeping the pH value of the mixed solution between 2 and 3, and then placing the mixed solution in a constant temperature oscillator to continuously oscillate (55 rpm, 37 ℃) for reaction for 2 hours; and finally, adding 150mL of artificial intestinal juice into the mixed solution, simultaneously adding sodium bicarbonate to adjust the pH value of a digestion system to 6-7, shaking for 2-4 h (55 rpm, 37 ℃), heating the mixed solution at 90 ℃ for 10 min to stop digestion, centrifuging for 20 min at 4 ℃ and 12000 g to obtain a collagen peptide mixed solution, performing ultrafiltration by using an ultrafiltration membrane with the molecular weight cutoff of 3000Da to obtain collagen peptide with the molecular weight of 3000Da, and performing freeze drying to obtain collagen peptide powder with the small molecular weight, wherein the collagen peptide powder is named as ESCP-I.
Step (1) ~ (6) was all done at 4 ℃.
Example 2
The soaking time in acetic acid in the step (4) was changed to 18 hours, and the rest of the operation was the same as that of example 1.
Example 3
The soaking time in acetic acid in the step (4) is changed to 30 h, and the rest of the operation is the same as that of the example 1.
Example 4
The feed-liquid ratio in step (4) was changed to 1:20, and the rest of the procedure was the same as in example 1.
Example 5
The feed-liquid ratio in step (4) was modified to 1:30, and the rest of the operation was the same as in example 1.
Comparative example 1
In step (4), only the pretreated eel skin was subjected to acid treatment twice without adding pepsin for further treatment, and the rest of the procedure was the same as in example 1.
Comparative example 2
The step (4) is modified to only be treated by pepsin, namely, the eel skin treated in the step (3) is soaked in acetic acid solution containing 2.5 percent of pepsin at 37 ℃ for 28 h according to the feed-liquid ratio of 1:45 g/mL, then the eel skin is centrifuged for 15min under the condition of 15000g, the pH of the supernatant is adjusted to be neutral, and the rest operations are the same as the operation of the example 1.
Comparative example 3
The step (4) is modified to be the extraction of collagen by a hot water method, namely the feed-liquid ratio of the eel skin to the water is 1:17 g/mL, the temperature is 80 ℃, the reaction time is 9 h, and the rest operations are the same as the example 1.
Comparative example 4
And (3) ultrafiltering the digested collagen peptide mixed solution obtained in the step (8) by using ultrafiltration membranes with molecular weight cut-off of 5000Da and 3000Da in sequence to obtain collagen peptide with molecular weight of 3000Da-5000Da, freeze-drying to obtain collagen peptide powder with medium molecular weight, and naming the collagen peptide powder as ESCP-II, wherein the rest operations are the same as those in the example 1.
Comparative example 5
And (4) ultrafiltering the digested collagen peptide mixed solution obtained in the step (8) by using an ultrafiltration membrane with the molecular weight cutoff of 5000Da to obtain collagen peptide with the molecular weight of more than 5000Da, and freeze-drying to obtain high-molecular-weight collagen peptide powder which is named as ESCP-III.
1. Identification of collagen
As a result of SDS-PAGE gel electrophoresis of the eel skin collagen sample obtained in example 1, the sample was characterized by type I collagen having 2. alpha. chains and one. beta. chain, as shown in FIG. 1.
The ultraviolet spectrum analysis of the sample obtained in example 1 showed that the obtained eel skin collagen has an obvious absorption peak at 227 nm, which is similar to the characteristic absorption peak of type i collagen at 226 nm, and further determines the similarity between the eel skin collagen and the type i collagen, as shown in fig. 2. And the sample has almost no absorption peak at 280 nm, which shows that the aromatic amino acid content in the sample is lower, and the prepared collagen is proved to have higher purity.
Fourier infrared spectroscopy analysis of the samples showed that the samples showed similar low and high structure to type I collagen as shown in FIG. 3.
In conclusion, the obtained samples all accord with the typical characteristics of the type I collagen, and the extracted samples are proved to be the collagen.
2. Determination of collagen content
Hydroxyproline is a characteristic amino acid of collagen, so that the content of collagen can be determined by identifying hydroxyproline in the eel skin collagen samples obtained in examples 1 to 5 and comparative examples 1 to 3, and the extraction rate and purity of collagen can be calculated, and the measurement results are shown in table 1 (for hydroxyproline content measurement method, reference is made to GBT9695.23-2008 meat and meat product hydroxyproline content measurement).
TABLE 1 comparison of collagen yields for examples 1-5 and comparative examples 1-3
3. Identification and sensory evaluation of collagen peptides
The mixed collagen peptide prepared after digestion in example 1 was subjected to SDS-PAGE gel electrophoresis analysis, Fourier infrared spectroscopy and amino acid composition analysis. The electrophoresis result shows that the collagen is completely enzymolyzed into polypeptide less than 10KDa, and has the potential of being absorbed by human body; fourier infrared spectrum results prove that the obtained collagen peptide has a specific absorption peak of collagen and is really a collagen product; the collagen peptide mainly contains glycine and also conforms to the typical characteristics of collagen.
The color, smell and shape of the collagen peptide with small molecular weight obtained in the examples and the comparative examples are subjected to sensory evaluation by randomly inviting 12 volunteers, the score of each evaluation index is 1-5 points from low to high, the average of each evaluation index is taken for statistics, (two significant figures are reserved for the result), wherein the overall score is good when the overall score is greater than 12, and is excellent when the overall score is greater than 13. The results are shown in Table 2. The results in table 2 prove that the obtained collagen peptide has good sensory quality and is easy to be accepted by consumers;
TABLE 2 collagen peptide sensory evaluation results
In conclusion, the collagen peptide prepared by the method has good quality and is suitable for industrial production.
4. In vitro antioxidant activity of collagen peptides between different molecular weight regions
Through DPPH.cleaning experiment,. OH cleaning experiment, O2•-The scavenging test measures the antioxidant activity of the collagen peptides obtained in example 1 and comparative examples 4 and 5 in different molecular weight ranges.
1) DPPH. scavenging Capacity
TABLE 3 eel skin collagen peptide DPPH scavenging power IC50
As can be seen from Table 3, IC with DPPH scavenging action by ESCP-I50At the lowest level, the collagen peptide with small molecular weight has strong DPPH scavenging capacity and can effectively interrupt the chain reaction of free radicals.
2) OH scavenging ability
TABLE 4 Anguillar Japonica skin collagen peptide OH scavenging IC50
As can be seen from Table 4, the ESCP-I has the highest OH-scavenging ability among the eel skin collagen peptides of different molecular weights, which indicates that the OH-scavenging ability of the collagen peptides is related to the molecular weight, and the smaller the molecular weight, the greater the scavenging ability.
3）O2 •-Cleaning ability
TABLE 5 Anguillar Japonica skin collagen peptide O2 -Scavenging force IC50
As can be seen from Table 5, ESCP-I showed better O than the other two molecular weight collagen peptides2 -The effect of scavenging.
In conclusion, the collagen peptide with the small molecular weight of less than 3000Da has the best antioxidant activity.
5. Improving effect of different collagen peptides on mouse skin photoaging
Adopting ultraviolet induced light aging mouse experiment, namely carrying out back unhairing on an experimental mouse and carrying out ultraviolet irradiation treatment by using an ultraviolet irradiation light source consisting of 1 UVA (peak value 340 nm) of 40W and 1 UVB (peak value 308nm) of 40W; experimental mice were grouped as follows:
i: blank group: no treatment is carried out;
II: model group: depilating, irradiating with ultraviolet rays, and perfusing stomach with physiological saline;
III: positive control group: depilating, irradiating with ultraviolet rays, and perfusing with 1000 mg/kg.d Vc;
IV: eel skin collagen group: performing depilation treatment, irradiating by ultraviolet rays, and performing intragastric administration by 1000 mg/kg. d collagen;
v: eel skin collagen peptide low dose group: unhairing treatment, ultraviolet irradiation, and gavage of 200 mg/kg.d sample;
VI: the dose groups of the eel skin collagen peptide are as follows: unhairing treatment, ultraviolet irradiation, and gavage of 500 mg/kg.d sample;
VII: eel skin collagen peptide high dose group: unhairing treatment, ultraviolet irradiation, and gavage of 1000 mg/kg.d sample;
VIII: commercial collagen peptide group: depilatory treatment, ultraviolet irradiation, 1000 mg/kg.d commercial collagen peptide gavage.
(the collagen peptide used is a low molecular weight collagen peptide with a molecular weight of less than 3000 Da).
And (3) test results:
1) effect of eel skin collagen peptide on mouse growth and body weight
The change in body weight of the mice during the experiment is shown in table 6. In the whole experiment process, the body weights of all groups of mice have no obvious difference and are slowly increased, which shows that the ultraviolet dose selected in the experiment does not exceed the standard, the eel skin collagen peptide has no toxic action on the mice, and the safety is high.
TABLE 6 change in body weight during mouse experiments
2) Influence of eel skin collagen peptide on mouse organ index
As shown in figure 4, the influence of long-term ultraviolet on the mouse liver is most obvious, compared with a blank group, the liver index of a model group is obviously reduced, each dosage group has a certain repairing effect on the mouse liver, wherein the repairing effect of the mouse liver by a high dosage group is most obvious, compared with the model group, the repairing effect is obviously enhanced, and the effect is superior to that of a commercial control group, which shows that the eel skin collagen peptide has an obvious improving effect on the improvement of the mouse immunocompetence, and the body can be protected from the influence of ultraviolet irradiation.
3) Influence of eel skin collagen peptide on water content of mouse skin
As shown in fig. 5, the moisture content of the skin was significantly reduced in the model group mice compared to the blank group. In the treatment group, compared with the model group, the skin moisture content of mice in the medium and high dose groups and the commercial control group is obviously increased, which shows that the eel skin collagen peptide can inhibit the loss of water and even can increase the skin moisture content, and the effect of the eel skin collagen peptide in the high dose is slightly better than that of the commercial collagen peptide.
4) Influence of eel skin collagen peptide on hydroxyproline content of mouse skin
As shown in fig. 6, compared with the model group mice, the hydroxyproline content in the skin of the blank group mice was significantly reduced, and the collagen content in each of the other groups was increased to some extent, wherein the collagen content in the high dose group was increased by 26.6%, which was significantly increased, indicating that the collagen and the collagen peptide could supplement the skin collagen loss caused by ultraviolet irradiation, and the effect of the eel skin collagen peptide was superior to that of the collagen and the commercial collagen peptide.
5) Influence of collagen peptide on antioxidant activity and Malondialdehyde (MDA) content in skin of mouse
As shown in fig. 7, the activity of antioxidant enzymes was significantly reduced in the model group compared to the blank group. The collagen group has little influence on the antioxidase, and the collagen peptide can effectively inhibit the activity reduction of the antioxidase.
As shown in fig. 8, the model group has a much higher MDA content than other groups, and the experimental group is not significantly different from the blank group, which indicates that the collagen peptide can effectively maintain the antioxidant balance of the body, and the collagen peptide of the high-dose group has a more significant effect than other experimental groups.
6) Influence of eel skin collagen peptide on mouse skin tissue morphology
Morphological observation of skin tissue is shown in fig. 9. The result shows that the collagen and the collagen peptide have obvious protective effect on the collagen fibers of the skin of the mouse, and can effectively improve the damage of the collagen fibers of the skin of the mouse caused by ultraviolet irradiation, so that the arrangement and distribution of elastic fibers of the mouse tend to be normal, and the skin is promoted to be elastic. Meanwhile, the injury repair effect of the eel skin collagen peptide on the mouse skin under the ultraviolet irradiation is far stronger than that of the commercial collagen peptide.
In conclusion, the eel skin collagen peptide has a certain protection effect on the photoaging of mice, can effectively relieve various physiological dysfunctions of the mice caused by ultraviolet irradiation, and has a function effect obviously higher than that of collagen and commercial collagen peptide.
The above description is only a preferred embodiment of the present invention, and all equivalent changes and modifications made in accordance with the claims of the present invention should be covered by the present invention.
Claims (10)
1. A method for producing a collagen peptide having a photoaging-ameliorating effect, comprising the steps of:
(1) raw material treatment: cutting eel skin into 1cm2Adding the fragments into ice water, and cleaning by using a magnetic stirrer until the solution is clear;
(2) removal of non-collagenous proteins: soaking the minced eel skin in NaOH solution for 48h, and then washing the eel skin with distilled water until the washing liquid is neutral;
(3) degreasing: soaking eel skin with butanol solution for 48 h; after soaking, washing the eel skin with distilled water again until the washing liquid has no alcohol smell and no layering exists after standing;
(4) and (3) extraction: immersing the eel skin treated in the step (3) in an acetic acid solution, continuously stirring by using a magnetic stirrer during the process, centrifuging to obtain a supernatant after the immersion is finished, immersing the obtained precipitate in the acetic acid solution again, merging the two supernatants after the centrifugation, and adjusting the pH value to be neutral; soaking the obtained residual precipitate in acetic acid solution, adding pepsin, stirring, centrifuging to obtain supernatant, and adjusting pH to neutral;
(5) salting out: mixing the extracted supernatants, slowly adding NaCl and continuously stirring until the final concentration of NaCl reaches 2.6mol/L, centrifuging, and taking a precipitate;
(6) and (3) dialysis: re-dissolving the precipitate obtained by centrifugation in 0.5mol/L acetic acid solution, dialyzing in 0.1mol/L acetic acid solution, and dialyzing with distilled water;
(7) freeze-drying: after dialysis, freeze-drying the solution in the dialysis bag to obtain eel skin collagen;
(8) digestion: simulating the human gastrointestinal tract digestion environment to establish an in-vitro digestion model to digest eel skin collagen, heating the mixed solution at 90 ℃ for 10 min to stop digestion, centrifuging at 4 ℃ and 12000 g for 20 min to obtain a collagen peptide mixed solution, performing fractionation by using an ultrafiltration membrane, and freeze-drying to obtain the collagen peptide with small molecular weight.
2. The method for preparing a collagen peptide having photoaging improving effect according to claim 1, wherein the concentration of NaOH solution used in step (2) is 0.1mol/L, the ratio of eel skin to NaOH solution is 1:10 g/mL, and the NaOH solution is replaced every 4 ~ 12h during the soaking process.
3. The method for preparing a collagen peptide having photoaging improving effect as claimed in claim 1, wherein the butanol solution used in step (3) has a volume concentration of 10%, the ratio of eel skin to butanol solution is 1:10 g/mL, and the butanol solution is replaced every 4 ~ 12h during the soaking process.
4. The method for preparing a collagen peptide having photoaging improving effect according to claim 1, wherein the concentration of the acetic acid solution used in step (4) is 0.5 mol/L; during each soaking, the material-liquid ratio of the material to the acetic acid solution is 1:10-30 g/mL, and the soaking time is 18-30 h; the amount of pepsin used is 20U/g; the centrifugation was carried out at 15000g for 15 min.
5. The method for preparing a collagen peptide having photoaging-improving effect according to claim 1, wherein the centrifugation in step (5) is carried out at 15000g for 15 ~ 30 min.
6. The method for preparing a collagen peptide having photoaging-improving effect of claim 1, wherein the dialysis time in step (6) is 24 ~ 48h, and the dialysis solution is changed every 4 ~ 12 h.
7. The method for preparing a collagen peptide having photoaging-improving effect according to claim 1, wherein the step (1) ~ (6) is performed at 4 ℃.
8. The method for preparing a collagen peptide having photoaging-improving effect according to claim 1, wherein the digestion in step (8) is performed by treating eel skin collagen with artificial saliva, artificial gastric juice and artificial intestinal juice as digestive juice at 37 ± 2 ℃ according to the digestion process of food in human mouth, stomach and small intestine.
9. The method for preparing a collagen peptide having photoaging-improving effect according to claim 1, wherein the ultrafiltration membrane used in step (8) has a molecular weight cut-off of 3000 Da.
10. A collagen peptide having photoaging-ameliorating effect obtained by the method of claim 1.
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