Antioxidant salmon collagen peptide and preparation method thereof

Abstract

The invention discloses antioxidant salmon collagen peptide and a preparation method thereof, and belongs to the technical field of processing of salmon collagen peptide. The preparation method comprises the following steps: firstly, carrying out enzymolysis on the salmon material by using phospholipase A2, hydrolyzing abundant membrane phospholipids in the salmon material, destroying fat cell structures and releasing wrapped triglyceride, then carrying out secondary enzymolysis by using aspergillus oryzae lipase, hydrolyzing macromolecular lipids into free fatty acids which are easily dissolved in supercritical carbon dioxide, and carrying out secondary enzymolysis by using aspergillus oryzae lipase. The degreased salmon material is obtained by means of supercritical carbon dioxide extraction, the lipid removal rate is greatly increased, and the antioxidant salmon collagen peptide which is small in molecular weight and high in oxidation resistance is obtained through subsequent collagen extraction and enzymolysis.

Description

Technical Field

[0001] The present invention relates to the technical field of processing of salmon collagen peptides, and particularly relates to a preparation method of antioxidant salmon collagen peptides. Background Art

[0002] With the increasing demand for functional foods and health ingredients, marine bioactive peptides have attracted much attention due to their high nutritional value and physiological functions. Salmon is rich in collagen, and its enzymatic hydrolysis product - salmon collagen peptides (Salmon Collagen Peptides, SCP) has characteristics such as easy absorption and low allergenicity. However, its natural antioxidant capacity is limited and it is difficult to meet the demand for efficient free radical scavenging.

[0003] Traditional methods for enhancing antioxidant activity include: enzymatic hydrolysis optimization: selectively hydrolyzing through alkaline protease, trypsin, etc. to release antioxidant peptide segments containing specific amino acids (such as histidine, tyrosine); physical modification: such as ultrasonic treatment or high-pressure homogenization to expose active groups; chemical cross-linking: binding with polyphenolic substances (such as tea polyphenols), but often facing problems such as low binding rate or poor stability.

[0004] However, these methods have defects such as easily destroying the protein structure and resulting in loss of product activity. Summary of the Invention

[0005] The main object of the present invention is to provide an antioxidant salmon collagen peptide and its preparation method, so as to solve the technical problems in the prior art that the preparation of salmon collagen peptides easily destroys their structure and has poor antioxidant properties.

[0006] To achieve the above object, the present invention provides a preparation method of antioxidant salmon collagen peptides, comprising the following steps: S10: Break the salmon material into a slurry, add phospholipase A2 for the first enzymatic hydrolysis, then add Aspergillus oryzae lipase for the second enzymatic hydrolysis, inactivate the enzyme activity and dry to a water content of less than 10%, and then place it in a supercritical extraction kettle to obtain defatted salmon material through supercritical CO2 extraction; S20: Mix and stir the defatted salmon material, acetic acid solution and pepsin, then add NaCl solution for salting out, then centrifuge to obtain a precipitate, dissolve the precipitate with acetic acid and then perform dialysis and the first spray drying to obtain salmon collagen; S30: Dissolve the salmon collagen to obtain a salmon collagen solution, add alkaline protease to the salmon collagen solution for the third enzymatic hydrolysis, inactivate the enzyme activity and then perform dialysis and the second spray drying to obtain salmon collagen peptides.

[0007] In some embodiments of the present invention, the addition amount of phospholipase A2 is 1% - 2% of the mass of the salmon feed.

[0008] In some embodiments of the present invention, the addition amount of Aspergillus oryzae lipase is 1% - 2% of the mass of the salmon feed.

[0009] In some embodiments of the present invention, the temperature of the first enzymatic hydrolysis is 35°C - 45°C; the temperature of the second enzymatic hydrolysis is 40°C - 50°C.

[0010] In some embodiments of the present invention, the extraction process includes a first stage and a second stage. The pressure in the first stage is 15 MPa - 20 MPa, and the temperature is 35°C - 40°C; the pressure in the second stage is 30 MPa - 35 MPa, and the temperature is 50°C - 55°C.

[0011] In some embodiments of the present invention, the flow rate of the supercritical CO2 is 40 - 60 g / min.

[0012] In some embodiments of the present invention, the supercritical CO2 contains citric acid.

[0013] In some embodiments of the present invention, the addition amount of pepsin is 1% - 2% of the mass of the defatted salmon feed.

[0014] In some embodiments of the present invention, after dissolving the salmon collagen to obtain a salmon collagen solution, the salmon collagen solution is irradiated with UV.

[0015] The present invention also provides a salmon collagen peptide, which is prepared by the preparation method of the antioxidant salmon collagen peptide as described above.

[0016] The beneficial effects that the present invention can achieve: In the steps of processing the salmon feed in the present invention, first, phospholipase A2 and Aspergillus oryzae lipase are used for stepwise enzymatic hydrolysis to selectively hydrolyze triglycerides and phospholipids, and then combined with supercritical CO2 extraction to achieve deep degreasing, while also retaining the integrity of the salmon collagen, thereby ensuring the antioxidant property of the subsequent salmon collagen peptide. Then, pepsin is selected for enzymatic hydrolysis under acidic conditions, and combined with salting - out and dialysis techniques to extract high - purity salmon collagen, avoiding the problems that the traditional acid - base method for extracting collagen easily destroys the protein structure and the antioxidant performance of the subsequent collagen peptide. Then, alkaline protease is used to hydrolyze the salmon collagen to obtain an antioxidant salmon collagen peptide with good antioxidant performance and a relatively small molecular weight. Description of the Drawings

[0017] To more clearly illustrate the technical solutions in the embodiments of the present invention or the prior art, the following briefly introduces the drawings required for the description of the embodiments or the prior art. Obviously, the drawings in the following description are only some embodiments of the present invention. For those of ordinary skill in the art, without creative efforts, other drawings can be obtained based on the structures shown in these drawings.

[0018] Figure 1 It is a schematic diagram of the preparation process of an antioxidant salmon collagen peptide of the present invention.

[0019] The realization of the object of the present invention, functional features and advantages will be further described in conjunction with the embodiments with reference to the drawings. Specific embodiments

[0020] It should be understood that the specific embodiments described herein are only used to explain the present invention and are not used to limit the present invention.

[0021] The following will clearly and completely describe the technical solutions in the embodiments of the present invention with reference to the drawings in the embodiments of the present invention. Obviously, the described embodiments are only some embodiments of the present invention, rather than all embodiments. Based on the embodiments of the present invention, all other embodiments obtained by those of ordinary skill in the art without creative efforts belong to the scope of protection of the present invention.

[0022] In the present invention, descriptions such as "first" and "second" are only for descriptive purposes and cannot be understood as indicating or implying their relative importance or implicitly indicating the quantity of the indicated technical features. Thus, features defined with "first" and "second" may explicitly or implicitly include at least one of such features. In addition, the technical solutions between the various embodiments can be combined with each other, but it must be based on the fact that those of ordinary skill in the art can implement them. When the combination of technical solutions results in contradictions or cannot be implemented, it should be considered that such a combination of technical solutions does not exist and is not within the scope of protection required by the present invention.

[0023] The present invention provides a method for preparing an antioxidant salmon collagen peptide and a salmon collagen peptide. Refer to Figure 1 , and the preparation method includes the following steps: S10: Break the salmon material into a slurry, add phospholipase A2 for the first enzymatic hydrolysis, then add Aspergillus oryzae lipase for the second enzymatic hydrolysis, inactivate the enzyme activity and dry it to a moisture content of less than 10%, and then place it in a supercritical extraction kettle to obtain defatted salmon material through supercritical CO2 extraction; S20: Mix and stir the defatted salmon material, acetic acid solution and pepsin, then add NaCl solution for salting out, followed by centrifugation to obtain a precipitate. Dissolve the precipitate with acetic acid, then perform dialysis and first spray drying to obtain salmon collagen; S30: Dissolve the salmon collagen to obtain a salmon collagen solution, add alkaline protease to the salmon collagen solution for the third enzymatic hydrolysis, inactivate the enzyme activity, then perform dialysis and second spray drying to obtain salmon collagen peptides.

[0024] In the steps of processing the salmon material in the present invention, first, phospholipase A2 and Aspergillus oryzae lipase are used for stepwise enzymatic hydrolysis to selectively hydrolyze triglycerides and phospholipids, and then combined with supercritical CO2 extraction to achieve deep degreasing. At the same time, the integrity of salmon collagen can be retained, thus ensuring the antioxidant property of salmon collagen peptides. Then, pepsin is selected for enzymatic hydrolysis under acidic conditions, and combined with salting out and dialysis techniques to extract high-purity salmon collagen, avoiding the problem that traditional acid-base methods for protein extraction easily damage the protein structure and antioxidant properties. Then, alkaline protease is used to hydrolyze salmon protein to obtain antioxidant salmon collagen peptides with better antioxidant properties and smaller molecular weights.

[0025] Lipid substances in the salmon material usually have long-chain structures and ester bonds, which will reduce their compatibility with supercritical carbon dioxide. Therefore, before supercritical extraction, phospholipase A2 is used for the first enzymatic hydrolysis. Phospholipase A2 can hydrolyze the abundant membrane phospholipids in the salmon material, destroy the fat cell structure, release the encapsulated triglycerides, improve the enzymatic hydrolysis efficiency of triglycerides in the second enzymatic hydrolysis, and hydrolyze triglycerides into free fatty acids. Free fatty acids have smaller molecular weights and low polarity, and the carboxyl groups therein can form hydrogen bonds with the weak polarity of CO2, enhancing the solubility of lipid substances in CO2 and making them more easily extracted by supercritical carbon dioxide, thereby achieving the effect of improving the removal of lipids, while retaining the structural integrity of proteins and ensuring the antioxidant activity of the subsequent prepared salmon collagen peptides.

[0026] In step S10, smashing the salmon material into a slurry can not only improve the enzymatic hydrolysis effect of lipase, but also increase the contact area with supercritical CO2 during the subsequent supercritical CO2 extraction process, improve the removal rate of impurities such as lipid substances and fishy smell substances, obtain salmon protein with higher purity, retain its structural integrity, and retain the antioxidant activity of the final product salmon collagen peptides.

[0027] In some embodiments, the temperature of the first enzymatic hydrolysis is 35°C to 45°C, the time of the first enzymatic hydrolysis is 2 h to 3 h, the pH of the first enzymatic hydrolysis is 6 to 8, the temperature of the second enzymatic hydrolysis is 40°C to 50°C, the time of the second enzymatic hydrolysis is 1 h to 2 h, and the pH of the second enzymatic hydrolysis is 7 to 8. By performing two enzymatic hydrolysis treatments, the present invention shortens the enzymatic hydrolysis time and can solve the generation of bitter peptide taste caused by the long enzymatic hydrolysis time. In this embodiment, the pH can be adjusted by adding a phosphate buffer solution.

[0028] In some embodiments, the addition amount of Aspergillus oryzae lipase is 1% to 2% of the mass of the salmon material, which can be 1%, 1.5%, 2%, etc., and the addition amount of phospholipase A2 is 1% to 2% of the mass of the salmon material, which can be 1%, 1.5%, 2%, etc.

[0029] In some embodiments, the method for inactivating enzymes in step S10 includes the pulse method, and the pulsed intense light range is 1 J / cm 2 ~5 J / cm 2 , which is beneficial to retaining the heat-sensitive antioxidant components in the salmon collagen peptide and facilitating some hydrophobic peptide segments, thereby ensuring the antioxidant performance of the product.

[0030] In some embodiments, the salmon material includes at least one of salmon meat, salmon bones, and salmon skin.

[0031] In some embodiments, after the salmon material is pulped, it can also be rinsed with a 1% NaCl solution by mass concentration to reduce the inhibition of enzyme activity by hemoglobin.

[0032] In some embodiments, the extraction process includes a first stage and a second stage. In the first stage, the pressure is 15 MPa to 20 MPa and the temperature is 35°C to 40°C, which is beneficial to removing free lipids. In the second stage, the pressure is 30 MPa to 35 MPa and the temperature is 50°C to 55°C, which can effectively extract bound lipids. By combining the first stage of low temperature and low pressure and the second stage of high temperature and high pressure, the removal effect of lipid substances in the salmon material can be improved, and at the same time, the structural integrity of salmon collagen can be retained, thereby ensuring the antioxidant performance of the final product, salmon collagen peptide.

[0033] In some embodiments, the extraction time of the first stage is 1 h to 2 h, and the extraction time of the second stage is 1 h to 2 h.

[0034] In some embodiments, the flow rate of supercritical CO2 is 40 g / min to 60 g / min.

[0035] In some embodiments, a trace amount of citric acid is added to supercritical CO2 to control the pH of CO2 to be 3-4, which can inhibit the crosslinking of lipid oxidation products and proteins, reduce protein carbonylation, thereby improving the extraction effect of protein peptides and enhancing the antioxidant performance of the product salmon collagen peptide.

[0036] In some embodiments, before performing the operation of step S20, the defatted salmon material is subjected to plasma treatment. The conditions of the plasma treatment are as follows: the power of the plasma treatment is 50 w - 100 w, and the time of the plasma treatment is 2 min - 5 min. This can loosen the collagen fiber structure of the defatted salmon material, improve the permeability of pepsin in step S20, reduce the amount of enzyme used, or increase the extraction rate of salmon collagen under the condition of the same amount of enzyme used, thereby strengthening the extraction of salmon collagen peptide and enhancing the antioxidant property of the final product.

[0037] In the present invention, the function of step S20 is to extract collagen from the salmon material.

[0038] In some embodiments, in the step of mixing the defatted salmon material, acetic acid solution, and pepsin, the material-liquid ratio of the defatted salmon material to the acetic acid solution is 100 g / 1 L, and the addition amount of pepsin is 1% - 2% of the mass of the defatted salmon material.

[0039] In some embodiments, the stirring temperature is 4°C, and the stirring time is 40 h - 50 h.

[0040] In some embodiments, the concentration of the NaCl solution for salting out is 2.5 M - 3 M.

[0041] In some embodiments, the centrifugation speed is 10000 - 15000, and the centrifugation time is 20 min - 30 min.

[0042] In some embodiments, the concentration of acetic acid used to dissolve the precipitate is 0.1 M - 0.2 M.

[0043] In some embodiments, during the dialysis process, the molecular cut-off is 3 kDa - 3.5 kDa, and the dialysis time is 60 h - 72 h, so as to achieve the purpose of removing impurities.

[0044] In the present invention, step S30 mainly enzymatically hydrolyzes the extracted collagen to obtain collagen peptides.

[0045] In some embodiments, the salmon collagen can be dissolved in an acetic acid solution with a concentration of 0.1 M - 0.2 M to obtain a salmon collagen solution, and the mass concentration of the salmon collagen solution can be 10 g - 20 g / 100 ml.

[0046] In some embodiments, the addition amount of alkaline protease is 4% - 5% of the mass of salmon collagen.

[0047] In some embodiments, the enzymatic hydrolysis temperature for the third enzymatic hydrolysis is 50°C - 55°C, and the enzymatic hydrolysis time is 2h - 3h.

[0048] In some embodiments, during the dialysis process, the molecular cut-off is 3 kDa - 3.5 kDa, and the dialysis time is 40h - 72h, so as to achieve the purpose of removing impurities.

[0049] In some embodiments, the method for inactivating enzymes in step S30 includes the pulse method, and the pulsed intense light range is 1 J / cm 2 ~5 J / cm 2 . It is beneficial to retain the heat-sensitive antioxidant components in the salmon collagen peptide, facilitate some hydrophobic peptide segments, and thus ensure the antioxidant performance of the product.

[0050] In some embodiments, after dissolving salmon collagen to obtain a salmon collagen solution, the salmon collagen solution is irradiated with UV. Pretreating the salmon collagen solution with UV irradiation is beneficial to inducing protein oxidative folding, exposing hidden antioxidant groups, enhancing the release of antioxidant active peptides by subsequent enzymatic hydrolysis, and thus improving the antioxidant performance of the final product, salmon collagen peptide.

[0051] In some embodiments, the wavelength of the UV irradiation is 254 nm, which is beneficial to exposing hidden protein disulfide bonds and aromatic amino acids and enhancing the release of antioxidant active peptides.

[0052] In some embodiments, the intensity of the UV irradiation is 10 mW / cm 2 ~15 mW / cm 2 .

[0053] In some embodiments, the time of the UV irradiation is 5 min - 10 min.

[0054] In some embodiments, during the UV irradiation process, it is carried out at a frequency of irradiating for 2 min and pausing for 1 min, so that the temperature of the salmon collagen solution ≤ 40°C to prevent overheating from damaging the protein structure.

[0055] In some embodiments, the distance between the irradiation lamp tube and the salmon collagen solution is 10 cm - 15 cm to prevent the protein structure from being damaged due to excessive temperature.

[0056] In some embodiments, after completing the UV irradiation treatment, the salmon collagen solution is transferred to a light-proof container and stirred to dissipate heat.

[0057] The technical solutions of the present invention will be further described in detail below in conjunction with specific embodiments. It should be understood that the following specific embodiments are only used to explain the present invention and are not used to limit the present invention.

[0058] Example 1 The preparation method of antioxidant salmon collagen peptide in Example 1 is as follows: S10: Break the salmon material into a slurry, add phospholipase A2 according to 1% of the mass of the salmon material, adjust the pH to 6 - 8, and perform the first enzymatic hydrolysis at 40°C for 3 h. Then, add Aspergillus oryzae lipase according to 2% of the mass of the salmon material, adjust the pH to 7 - 8, and perform the second enzymatic hydrolysis at 45°C for 1 h. Then, use pulsed light with an intensity of 5 J / cm 2 to inactivate the enzyme activity, and dry it to a water content of less than 10%. Then, place it in a supercritical extraction kettle and obtain defatted salmon material through supercritical CO2 extraction. The conditions for supercritical extraction are as follows: In the first stage, control the pressure at 20 MPa and the temperature at 35°C. After extracting for 1 h, adjust to the second stage. In the second stage, control the pressure at 30 MPa and the temperature at 55°C, and the extraction time is 2 h. Control the flow rate of CO2 at 60 g / min throughout the process, and add a small amount of citric acid to CO2 to control the pH of the input supercritical CO2 at 3 - 4.

[0059] S20: Dissolve the defatted salmon material with a 0.1 M acetic acid solution to obtain a defatted salmon material solution with a concentration of 100 g / 1 L, add pepsin according to 1% of the mass of the salmon material, stir at 4°C for 50 h, then add a 3 M NaCl solution for salting out, and then centrifuge at a speed of 15000 for 20 min to obtain a precipitate. Dissolve the precipitate with a 0.1 M acetic acid solution and then perform dialysis for 72 h. The molecular weight intercepted by dialysis is 3.5 kDa. Then, perform spray drying to obtain salmon collagen.

[0060] S30: Dissolve the salmon collagen with a 1 M acetic acid solution to obtain a salmon collagen solution with a mass concentration of 10 g / 100 ml, add alkaline protease according to 4% of the mass of the salmon collagen, perform the third enzymatic hydrolysis at 50°C for 2 h, then use pulsed light with an intensity of 5 J / cm 2 to inactivate the enzyme activity, then perform dialysis for 50 h, the intercepted molecular weight is 3 kDa, and then perform spray drying to obtain salmon collagen peptide.

[0061] Example 2 Example 2 prepares antioxidant salmon collagen peptide with reference to the preparation method of Example 1. The difference is that the addition amount of phospholipase A2 is 2%.

[0062] Example 3 Example 3: Refer to the preparation method of Example 1 to prepare antioxidant salmon collagen peptide, except that the addition amount of Aspergillus oryzae lipase is 1%.

[0063] Example 4 Example 4: Refer to the preparation method of Example 1 to prepare antioxidant salmon collagen peptide, except that the addition amount of pepsin is 2% of the mass of defatted salmon material.

[0064] Example 5 Example 5: Refer to the preparation method of Example 1 to prepare antioxidant salmon collagen peptide, except that citric acid is not added in step S10 to adjust the pH of supercritical CO2.

[0065] Example 6 Example 6: Refer to the preparation method of Example 1 to prepare antioxidant salmon collagen peptide, except that in step S10, after obtaining defatted salmon material by supercritical CO2 extraction, the defatted salmon material is treated with plasma equipment, with a power of 100 w and a time of 2 min.

[0066] Example 7 Example 7: Refer to the preparation method of Example 1 to prepare antioxidant salmon collagen peptide, except that in step S30, after dissolving salmon collagen with a 1 M acetic acid solution to obtain a salmon collagen solution, the salmon collagen solution is irradiated with UV. The irradiation lamp tube is 10 cm away from the salmon collagen solution, the irradiation wavelength is 254 nm, and the irradiation intensity is 10 mW / cm 2 , the irradiation time is 8 min, and the irradiation frequency is to pause for 1 min every 2 min of irradiation to ensure that the temperature of the salmon collagen solution ≤ 40 °C.

[0067] Comparative Example 1 Comparative Example 1: Refer to the preparation method of Example 1 to prepare antioxidant salmon collagen peptide, except that phospholipase A2 is not added in step S10 for the first enzymatic hydrolysis.

[0068] Comparative Example 2 Comparative Example 2: Refer to the preparation method of Example 1 to prepare antioxidant salmon collagen peptide, except that Aspergillus oryzae lipase is not added in step S10 for the second enzymatic hydrolysis.

[0069] Performance Test Antioxidant performance test: The salmon collagen peptides prepared in Examples 1 to 5 and Comparative Examples 1 to 2 were formulated into a sample aqueous solution of 10 mg / ml. In a 96-well plate, 200 μL of the sample solution was added and mixed with an equal volume of 0.1 mmol / L DPPH ethanol solution. After reacting for 30 min at room temperature in the dark, the absorbance of the reaction solution at 517 nm was measured.

[0070] A control group was set up: the DPPH ethanol solution in each group was replaced with absolute ethanol as the corresponding control group.

[0071] A blank group was set up: the sample aqueous solution in each group was replaced with deionized water as the corresponding blank group.

[0072] A solvent group was set up: a mixed solution of absolute ethanol and deionized water in equal volume was used as the solvent group.

[0073] The absorbance of each reaction solution was measured respectively. The calculation formula for the DPPH free radical scavenging rate is as follows: DPPH free radical scavenging rate (%) = 1 - (A0 - A2 / A1 - A3) × 100%; Among them, the experimental group was A0, the blank group was A1, the control group was A2, and the solvent group was A3.

[0074] Table 1

[0075] As can be seen from Table 1, the antioxidant salmon collagen peptides prepared by the method of the present invention have good antioxidant performance. Moreover, after the defatted salmon material was treated with plasma in Example 6 and the salmon collagen solution was irradiated in Example 7, the antioxidant performance of the salmon collagen peptides can be effectively improved.

[0076] The above are only the preferred embodiments of the present invention, and do not limit the patent scope of the present invention. Any equivalent structure or equivalent process transformation made by using the specification and drawings of the present invention, or directly or indirectly applied in other related technical fields, shall be equally included in the patent protection scope of the present invention.

Claims

1. A preparation method of antioxidant salmon collagen peptide, characterized in that, It includes the following steps: S10: Break the salmon material into a slurry, add phospholipase A2 for the first enzymatic hydrolysis, then add Aspergillus oryzae lipase for the second enzymatic hydrolysis. After inactivating the enzyme activity, dry it to a water content of less than 10%, and then place it in a supercritical extraction kettle. Obtain defatted salmon material through supercritical CO2 extraction; S20: Mix and stir the defatted salmon material, acetic acid solution and pepsin, then add NaCl solution for salting out, and then centrifuge to obtain a precipitate. Dissolve the precipitate with acetic acid and then perform dialysis and the first spray drying to obtain salmon collagen; S30: Dissolve the salmon collagen to obtain a salmon collagen solution, add alkaline protease to the salmon collagen solution for the third enzymatic hydrolysis. After inactivating the enzyme activity, perform dialysis and the second spray drying to obtain salmon collagen peptides.

2. The preparation method of the antioxidant salmon collagen peptide according to claim 1, wherein The addition amount of the phospholipase A2 is 1% - 2% of the mass of the salmon material.

3. The preparation method of the antioxidant salmon collagen peptide according to claim 1, wherein, The addition amount of the Aspergillus oryzae lipase is 1% - 2% of the mass of the salmon material.

4. The preparation method of the antioxidant salmon collagen peptide according to claim 1, characterized in that, The temperature of the first enzymatic hydrolysis is 35°C - 45°C; the temperature of the second enzymatic hydrolysis is 40°C - 50°C.

5. The preparation method of the antioxidant salmon collagen peptide according to claim 1, characterized in that, The extraction process includes a first stage and a second stage. The pressure in the first stage is 15MPa - 20MPa, and the temperature is 35°C - 40°C; the pressure in the second stage is 30MPa - 35MPa, and the temperature is 50°C - 55°C.

6. The preparation method of the antioxidant salmon collagen peptide according to claim 1, characterized in that, The flow rate of the supercritical CO2 is 40g / min - 60g / min.

7. The preparation method of the antioxidant salmon collagen peptide according to claim 1, wherein, The supercritical CO2 contains citric acid.

8. The preparation method of the antioxidant salmon collagen peptide according to claim 1, characterized in that, The addition amount of the pepsin is 1% - 2% of the mass of the defatted salmon material.

9. The preparation method of the antioxidant salmon collagen peptide according to claim 1, characterized in that, After dissolving the salmon collagen to obtain a salmon collagen solution, irradiate the salmon collagen solution with UV irradiation.

10. A salmon collagen peptide, characterized in that, The salmon collagen peptides are prepared by using the preparation method of the antioxidant salmon collagen peptides according to any one of claims 1 to 9.

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