Albumin anti-inflammatory peptide for improving muscle loss as well as preparation method and application of albumin anti-inflammatory peptide

Abstract

The invention relates to the technical field of active peptides, and particularly discloses an albumin anti-inflammatory peptide for improving muscle loss as well as a preparation method and application of the albumin anti-inflammatory peptide. The albumin anti-inflammatory peptide for improving muscle loss provided by the invention is prepared by mixing an NKVVR active peptide and an FDVFK active peptide, the amino acid sequence of the NKVVR active peptide is as follows: asparagine, lysine, valine, valine and arginine; the amino acid sequence of the FDVFK active peptide is as follows: phenylalanine, aspartic acid, valine, phenylalanine and lysine. The albumin anti-inflammatory peptide prepared by the invention can reduce individual inflammatory immune response, has good anti-inflammatory property, and can be applied to food for improving muscle loss or medicine for improving muscle loss.

Description

Technical Field

[0001] The present application relates to the technical field of active peptides, and in particular to an albumin anti-inflammatory peptide for improving muscle loss, and a preparation method and application thereof. Background Art

[0002] Muscle loss is a health issue that refers to the loss of muscle mass, volume, and function due to age, disease, or reduced physical activity. Since muscle is one of the main metabolic organs in the body, muscle loss also leads to a decrease in the basal metabolic rate, which can lead to weight gain and obesity.

[0003] Interleukin-6 (IL-6) and tumor necrosis factor-α (TNF-α) are cytokines that promote inflammatory responses. Human clinical data show that the concentrations of IL-6 and TNF-α increase in patients with some special diseases (such as cancer, AIDS, chronic obstructive pulmonary disease, etc.), those taking anticancer drugs, and the elderly, accompanied by increased muscle breakdown and consumption or increased muscle cell death. Studies have shown that the administration of IL-6 and TNF-α to increase the concentration of IL-6 and TNF-α in experimental animals can induce muscle cell damage (including imbalance of myosin metabolism, muscle cell apoptosis, etc.), leading to muscle loss or atrophy.

[0004] Anti-inflammatory substances refer to compounds or elements that have the property of reducing or inhibiting inflammatory responses. These substances can reduce inflammation through a variety of mechanisms, including but not limited to inhibiting the production of inflammatory mediators, preventing the activation and migration of inflammatory cells, and reducing the oxidative stress response of damaged tissues.

[0005] Therefore, obtaining anti-inflammatory substances that can improve muscle loss has good prospects and significance. Summary of the invention

[0006] In order to solve the above technical problems, the present application provides an albumin anti-inflammatory peptide for improving muscle loss, and a preparation method and application thereof.

[0007] In the first aspect, the present application provides an albumin anti-inflammatory peptide for improving muscle loss, which is composed of a mixture of NKVVR active peptide and FDVFK active peptide; The amino acid sequence of the NKVVR active peptide is shown in SEQ ID NO.1, which is: asparagine-lysine-valine-valine-arginine; the amino acid sequence of the FDVFK active peptide is shown in SEQ ID NO.2, which is: phenylalanine-aspartic acid-valine-phenylalanine-lysine.

[0008] Preferably, the albumin anti-inflammatory peptide for improving muscle loss is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 20-50:0.2-1.

[0009] Preferably, the albumin anti-inflammatory peptide for improving muscle loss is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 30-40:0.4-0.8.

[0010] In a specific embodiment, the albumin anti-inflammatory peptide for improving muscle loss is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 20:0.2, 20:0.4, 20:0.6, 20:0.8, 20:1, 30:0.2, 30:0.4, 30:0.6, 30:0.8, 30:1, 35:0.2, 35:0.4, 35:0.6, 35:0.8, 35:1, 40:0.2, 40:0.4, 40:0.6, 40:0.8, 40:1, 50:0.2, 50:0.4, 50:0.6, 50:0.8, and 50:1.

[0011] In a second aspect, the present application provides a method for preparing the above-mentioned albumin anti-inflammatory peptide for improving muscle loss, which is characterized in that it specifically includes the following steps in sequence: taking an albumin oligopeptide concentrate, adding physiological saline, adding flavor protease for enzymatic hydrolysis, boiling to inactivate the enzyme, and cooling to room temperature; then adding alkaline protease for enzymatic hydrolysis, boiling to inactivate the enzyme, and then cooling to room temperature to filter, ultrafilter, concentrate, vacuum dry, and screen and separate to obtain the albumin anti-inflammatory peptide.

[0012] The present application found in the research and experimental process that NKVVR active peptide and FDVFK active peptide have significant anti-inflammatory activity as albumin peptides, and the activity is closely related to the presence of their anti-inflammatory peptides. However, the preparation of albumin anti-inflammatory peptides is mainly carried out by enzymatic hydrolysis. Since factors such as the type of enzyme, hydrolysis conditions, and the molecular weight of the peptide affect the anti-inflammatory activity of the hydrolyzate, the output rate of effective anti-inflammatory peptides is not high. The applicant has greatly improved the output rate of NKVVR active peptide and FDVFK active peptide by optimizing the reaction conditions of the matching enzymatic hydrolysis.

[0013] Preferably, the preparation method of the albumin anti-inflammatory peptide for improving muscle loss specifically comprises the following steps in sequence: taking 1000 parts by weight of albumin oligopeptide concentrate, adding 8000-12000 parts by weight of physiological saline, adding 0.01-0.03 parts by weight of flavor protease, enzymolysis at 35-45°C for 3-5h, then boiling to inactivate the enzyme, and cooling to room temperature; then adding 0.004-0.008 parts by weight of alkaline protease, enzymolysis at 50-60°C for 2-4h, boiling to inactivate the enzyme, then cooling to room temperature, filtering, ultrafiltration, concentration, vacuum drying, screening and separation to obtain the albumin anti-inflammatory peptide.

[0014] Preferably, the amount of the flavor protease is 0.015-0.025 parts by weight.

[0015] In a specific embodiment, the amount of the flavor protease is 0.01, 0.015, 0.02, 0.025, or 0.03 parts by weight.

[0016] Preferably, before adding flavor protease, the pH is adjusted to 6.0-7.0.

[0017] In a specific embodiment, the pH is adjusted to 6.0, 6.5 or 7.0 before adding the flavor protease.

[0018] Preferably, the amount of alkaline protease used is 0.005-0.007 parts by weight.

[0019] In a specific embodiment, the amount of alkaline protease used is 0.004, 0.005, 0.006, 0.007, or 0.008 parts by weight.

[0020] Preferably, before adding alkaline protease, the pH is adjusted to 7.5-9.0.

[0021] In a specific embodiment, the pH is adjusted to 7.5, 8.0, 8.5, or 9.0 before adding alkaline protease.

[0022] In a third aspect, the present application provides the use of the above-mentioned albumin anti-inflammatory peptide in the preparation of food for improving muscle loss or medicine for improving muscle loss.

[0023] In summary, the technical solution of this application has the following effects: The albumin anti-inflammatory peptide composed of a mixture of NKVVR active peptide and FDVFK active peptide prepared by the technical solution of the present application has excellent anti-inflammatory properties.

[0024] The present application obtains NKVVR active peptide and FDVFK active peptide with high yield by optimizing the preparation method of anti-albumin anti-inflammatory peptide. DETAILED DESCRIPTION

[0025] The present application is further described in detail below in conjunction with examples, comparative examples and performance testing experiments. These examples should not be construed as limiting the scope of protection claimed in the present application. Example Example 1

[0026] Example 1 provides an albumin anti-inflammatory peptide for improving muscle loss.

[0027] The preparation method of albumin anti-inflammatory peptide in Example 1 is: Enzymatic hydrolysis: Take 1kg of albumin oligopeptide concentrate (10% protein content, sourced from Shaoxing Jiayun Biotechnology Co., Ltd.), add 10kg of physiological saline, adjust the pH to 6.5, add 0.02kg of flavor protease, perform enzymatic hydrolysis at 40°C for 4h, then boil to inactivate the enzyme, and cool to room temperature; then adjust the pH to 8.0, add 0.006kg of alkaline protease, perform enzymatic hydrolysis at 55°C for 3h, boil to inactivate the enzyme, and cool to room temperature.

[0028] Post-treatment after centrifugal filtration, ultrafiltration, concentration, and vacuum drying: The enzymatic hydrolyzate cooled to room temperature was centrifuged at 6000r / min for 15min to obtain the supernatant, which was filtered through a 0.45μm filter membrane and the filtrate was collected for the next step. The filtrate was separated with 10kDa, 5kDa, and 3kDa ultrafiltration membranes to collect polypeptides of different molecular weights (>10kDa, 5-10kDa, 3-5kDa, and <3kDa), and the polypeptide solutions of the four different molecular weights were vacuum freeze-dried and stored at -80°C.

[0029] Screening and separation: LC-MS / MS liquid mass analysis was performed on the peptide components with molecular weight less than 3kDa, and the peptide sequence was used to draw the 2D structure diagram of the peptide, and then the 3D structure diagram of the peptide was drawn and set as the structure with the minimum energy (pdkgt format). The x-ray crystal structure of inducible NO synthase (iNOS, PDB I:3e6t) was downloaded from the RCSBProteinDataBank database (PDB format), and the receptor iNOS was subjected to operations such as removal of water molecules, hydrogenation, and charge calculation using Autedocktools1.5.6 software. All peptides were docked with receptor proteins using BR.0.8 software. In general, the docking energy is less than 0. The smaller the value, the tighter the docking and the higher the anti-inflammatory potential. Therefore, the peptides were sorted according to the absolute value of the docking energy, and the top-ranked peptides were used to predict their possible biological activity values ​​using PeptideRanker.

[0030] Inducible nitric oxide synthase (iNQS) is a nervous system enzyme closely related to inflammatory response. When stimulated by various inflammatory conditions, LPS or cytokines induce a large amount of IQ8 expression, which in turn continuously produces NO, which may cause tissue damage at the site of inflammation. Controlling IOS is one of the important strategies to control inflammatory responses under various pathological conditions, and iNOS has become a key target for the treatment of inflammatory diseases. PRz software can simulate the docking of receptors with different ligands in batches, and judge the strength of their interaction by the docking energy to achieve virtual screening effects. The docking energy score can indicate the binding potential of the receptor and the ligand. Generally speaking, a lower score represents a stronger binding ability between the two. The peptides obtained by LC-MSIMS were simulated and scored, and the docking energy of the peptides was ≤-8.5kcalmo11, indicating that the binding force with INQS was relatively strong. The two peptides were compared with the BIQPER-UWM database, of which the NKVVR active peptide and the FDVFK active peptide were synthesized and verified as anti-inflammatory peptides.

[0031] In this example, NKVVR active peptide and FDVFK active peptide were obtained. Embodiment 2-7

[0032] Examples 2-7 each provide an albumin anti-inflammatory peptide.

[0033] The difference between the above embodiment and embodiment 1 is that the method of enzymatic hydrolysis of the albumin oligopeptide concentrate is different, as shown below.

[0034] In Example 2, 1 kg of albumin oligopeptide concentrate was taken, 10 kg of physiological saline was added, the pH was adjusted to 8.0, 0.02 kg of flavor protease was added, and enzymatic hydrolysis was carried out at 40°C for 4 hours, then the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature; then, the pH was adjusted to 6.5, 0.006 kg of alkaline protease was added, enzymatic hydrolysis was carried out at 55°C for 3 hours, the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature. In Example 3: 1 kg of albumin oligopeptide concentrate was taken, 10 kg of physiological saline was added, the pH was adjusted to 6.5, 0.02 kg of flavor protease was added, and enzymatic hydrolysis was carried out at 55°C for 4 hours, then the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature; then the pH was adjusted to 8.0, 0.006 kg of alkaline protease was added, enzymatic hydrolysis was carried out at 40°C for 3 hours, the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature.

[0035] In Example 4: 1 kg of albumin oligopeptide concentrate was taken, 10 kg of physiological saline was added, the pH was adjusted to 6.5, 0.01 kg of flavor protease was added, and enzymatic hydrolysis was carried out at 40°C for 4 hours, then the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature; then the pH was adjusted to 8.0, 0.008 kg of alkaline protease was added, enzymatic hydrolysis was carried out at 55°C for 3 hours, the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature.

[0036] In Example 5: 1 kg of albumin oligopeptide concentrate was taken, 10 kg of physiological saline was added, the pH was adjusted to 6.5, 0.03 kg of flavor protease was added, and enzymatic hydrolysis was carried out at 40°C for 4 hours, then the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature; then the pH was adjusted to 8.0, 0.004 kg of alkaline protease was added, enzymatic hydrolysis was carried out at 55°C for 3 hours, the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature.

[0037] In Example 6: 1 kg of albumin oligopeptide concentrate was taken, 10 kg of physiological saline was added, the pH was adjusted to 6.0, 0.015 kg of flavor protease was added, and enzymatic hydrolysis was carried out at 40°C for 4 hours, then the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature; then the pH was adjusted to 8.0, 0.007 kg of alkaline protease was added, enzymatic hydrolysis was carried out at 55°C for 3 hours, the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature.

[0038] In Example 7: 1 kg of albumin oligopeptide concentrate was taken, 10 kg of physiological saline was added, the pH was adjusted to 7.0, 0.025 kg of flavor protease was added, and enzymatic hydrolysis was carried out at 40°C for 4 hours, then the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature; then the pH was adjusted to 8.0, 0.005 kg of alkaline protease was added, enzymatic hydrolysis was carried out at 55°C for 3 hours, the enzyme activity was inactivated by boiling, and the temperature was lowered to room temperature.

[0039] The other process parameters in the above embodiment are the same as those in embodiment 1. Comparative Example

[0040] Comparative Examples 1-3 Comparative Examples 1-3 each provide an albumin anti-inflammatory peptide.

[0041] The difference between the comparative example and Example 1 is that the enzymatic hydrolysis method of the albumin oligopeptide concentrate is different, as shown below.

[0042] In Comparative Example 1: Enzymatic hydrolysis: Take 1 kg of albumin oligopeptide concentrate (10% protein content, sourced from Shaoxing Jiayun Biotechnology Co., Ltd.), add 10 kg of physiological saline, adjust the pH to 8.0, add 0.006 kg of alkaline protease, enzymolyze at 55 ° C for 3 hours, then boil to inactivate the enzyme, and cool to room temperature; then adjust the pH to 6.5, add 0.02 kg of flavor protease, enzymolyze at 40 ° C for 4 hours, boil to inactivate the enzyme, and cool to room temperature.

[0043] In Comparative Example 2: Enzymatic hydrolysis: Take 1 kg of albumin oligopeptide concentrate (10% protein content, sourced from Shaoxing Jiayun Biotechnology Co., Ltd.), add 10 kg of physiological saline, adjust the pH to 7.5, add 0.02 kg of flavor protease and 0.006 kg of alkaline protease, enzymatically hydrolyze at 55°C for 3 hours, boil to inactivate the enzyme, and cool to room temperature.

[0044] In Comparative Example 3: Enzymatic hydrolysis: Take 1 kg of albumin oligopeptide concentrate (10% protein content, sourced from Shaoxing Jiayun Biotechnology Co., Ltd.), add 10 kg of physiological saline, adjust the pH to 6.5, add 0.02 kg of pancreatic enzyme, enzymolyze at 40 ° C for 4 hours, then boil to inactivate the enzyme, and cool to room temperature; then adjust the pH to 8.0, add 0.006 kg of alkaline protease, enzymolyze at 55 ° C for 3 hours, boil to inactivate the enzyme, and cool to room temperature.

[0045] The remaining process parameters in the above comparative example are the same as those in Example 1. Performance testing

[0046] The output of the albumin anti-inflammatory peptides prepared in Examples 1-7 and Comparative Examples 1-3 was recorded. The results are shown in Table 1.

[0047] Table 1 Output of albumin anti-inflammatory peptides in Examples 1-7 and Comparative Examples 1-3

[0048] Combined with Table 1, by comparing the test results of Examples 1-7 with those of Comparative Examples 1-3, it can be seen that the technical solution of the present application first uses flavor protease to enzymatically hydrolyze the albumin oligopeptide concentrate, inactivates it, and then uses alkaline protease to enzymatically hydrolyze it. The quality of the prepared NKVVR active peptide and FDVFK active peptide is higher. Embodiment 8-15

[0049] Examples 8-15 each provide an albumin anti-inflammatory peptide.

[0050] The difference between the above examples is that the weight ratio between the NKVVR active peptide and the FDVFK active peptide is as follows: The NKVVR active peptide and the FDVFK active peptide in the above examples are derived from Example 1.

[0051] In Example 8: the albumin anti-inflammatory peptide is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 10:3.

[0052] In Example 9: the albumin anti-inflammatory peptide is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 60:0.1.

[0053] In Example 10: the albumin anti-inflammatory peptide is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 20:1.

[0054] In Example 11: the albumin anti-inflammatory peptide is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 50:0.2.

[0055] In Example 12: the albumin anti-inflammatory peptide is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 30:0.8.

[0056] In Example 13: the albumin anti-inflammatory peptide is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 40:0.4.

[0057] In Example 14: the albumin anti-inflammatory peptide is a NKVVR active peptide.

[0058] In Example 15: the albumin anti-inflammatory peptide is a DVFK active peptide. Performance testing

[0059] (1) Animal toxicity test Ordinary NIH mice (weight 20 g ± 1 g) were used as experimental mice, half of which were male and half were female.

[0060] The albumin anti-inflammatory peptide powder was dissolved in sterile water to prepare a 50 mg / mL albumin anti-inflammatory peptide sample solution, which was administered to mice at a dose of 1 ml / 10 g body weight. The mice were closely observed for 12 h and records were made, and the observation was continued for 7 days.

[0061] The experimental results showed that during the 7 days, there was no death of the mice, their behavior was active, their food intake was normal, their fur was shiny and not loose or dirty, they were not addicted to saliva, there was no abnormal secretion in their eyes, mouth, nose, ears and perianal area, and there was no broken tail or rotten toes. Then 3 mice were selected from each group of experimental mice and killed. It was observed with the naked eye that no abnormal changes were found in the important organs of the experimental mice, such as the heart, liver, lungs, stomach and thymus, indicating that the albumin anti-inflammatory peptide powder had no acute toxicity.

[0062] (2) Evaluation of the anti-inflammatory properties of albumin anti-inflammatory peptides The albumin anti-inflammatory peptide powder was dissolved in sterile water to prepare a 50 mg / mL albumin anti-inflammatory peptide sample solution.

[0063] In order to confirm whether albumin anti-inflammatory peptide powder can reduce the inflammatory response of cells, the changes in cytokine gene expression in cells during inflammation were measured.

[0064] Mouse macrophage RAW264.7 cell line was used, and lipopolysaccharide (LPS; Sigma-Aldrich, #L2630), the main component of the cell wall of Gram-negative bacteria, was used as a substance that causes an inflammatory response. Cells were cultured in DMEM (Lonza, #BE12-604F) containing 10% FBS and 1% penicillin-streptomycin at 37°C and 5% CO2.

[0065] The cells were cultured at 2.5 × 10 5The cells were seeded in a 96-well plate at a density of cells / well. After 24 hours, the prepared cells were treated with the albumin anti-inflammatory peptide sample solution. After incubation at 37°C for 45 minutes, they were treated with 200 ng / mL of LPS to induce inflammation. After incubation at 37°C for 8 hours, the cells without culture medium were treated with TRIzolTM (Invitrogen, #15596018) to lyse the cells. RNA was obtained by the given experimental method, and cDNA was generated using reverse transcriptase (Promega, #M1705). Subsequently, SYBR Green (Enzynomics, RT530) and mouse primers for each inflammatory cytokine gene (TNFα, IL-6 and IL-1β) were used to measure the cytokine expression level. At the same time, cells not treated with the albumin anti-inflammatory peptide sample solution were used as a blank control group.

[0066] The inhibition rates of cytokines (TNFα, IL-6 and IL-1β) were calculated based on the experimental group and the blank control group.

[0067] Test results: as shown in Table 2.

[0068] Table 2 Results of application performance test of albumin anti-inflammatory peptides in Examples 8-15

[0069] Combined with the test results of Examples 8-15 in Table 2, it can be seen that when the cells were treated with the albumin anti-inflammatory peptide prepared in the present application, the inflammatory cytokines (TNFα, IL-6 and IL-1β) were reduced compared with the blank control group; this shows that the albumin anti-inflammatory peptide prepared in the present application can reduce the inflammatory immune response of individuals, has good anti-inflammatory properties, and can be used in foods for improving muscle loss or drugs for improving muscle loss.

[0070] Although the present invention has been described in detail above with general descriptions and specific embodiments, it is obvious to those skilled in the art that some modifications or improvements may be made thereto based on the present invention. Therefore, these modifications or improvements made without departing from the spirit of the present invention all fall within the scope of protection claimed by the present invention.

Claims

1. An albumin anti-inflammatory peptide for improving muscle loss, characterized in that: It is composed of a mixture of NKVVR active peptide and FDVFK active peptide; The amino acid sequence of the NKVVR active peptide is shown in SEQ ID NO.1, which is: asparagine-lysine-valine-valine-arginine; the amino acid sequence of the FDVFK active peptide is shown in SEQ ID NO.2, which is: phenylalanine-aspartic acid-valine-phenylalanine-lysine.

2. The albumin anti-inflammatory peptide for improving muscle loss according to claim 1, characterized in that: By weight ratio of 20-50: 0.2-1 NKVVR active peptide and DVFK active peptide are mixed.

3. The albumin anti-inflammatory peptide for improving muscle loss according to claim 1, characterized in that: The invention is composed of a mixture of NKVVR active peptide and DVFK active peptide in a weight ratio of 30-40:0.4-0.

8.

4. The method for preparing the albumin anti-inflammatory peptide for improving muscle loss according to any one of claims 1 to 3, characterized in that: Specifically, the method comprises the following steps in sequence: taking albumin oligopeptide concentrate, adding physiological saline, adding flavor protease for enzymolysis, boiling to inactivate the enzyme, and cooling to room temperature; then adding alkaline protease for enzymolysis, boiling to inactivate the enzyme, and then cooling to room temperature to filter, ultrafilter, concentrate, vacuum dry, and screen and separate to obtain albumin anti-inflammatory peptides.

5. The method for preparing the albumin anti-inflammatory peptide for improving muscle loss according to claim 4, characterized in that: Specifically, the following steps are sequentially performed: taking 1000 parts by weight of albumin oligopeptide concentrate, adding 8000-12000 parts by weight of physiological saline, adding 0.01-0.03 parts by weight of flavor protease, enzymolysis at 35-45° C. for 3-5 hours, then boiling to inactivate the enzyme, and cooling to room temperature; Then, 0.004-0.008 parts by weight of alkaline protease is added, and enzymolysis is carried out at 50-60° C. for 2-4 hours, and the enzyme activity is inactivated by boiling. Then, the mixture is cooled to room temperature, filtered, ultrafiltered, concentrated, vacuum dried, and screened to separate the albumin anti-inflammatory peptide.

6. The method for preparing the albumin anti-inflammatory peptide for improving muscle loss according to claim 5, characterized in that: The amount of the flavor protease used is 0.015-0.025 parts by weight.

7. The method for preparing the albumin anti-inflammatory peptide for improving muscle loss according to claim 5, characterized in that: Before adding flavor protease, adjust the pH to 6.0-7.

0.

8. The method for preparing the albumin anti-inflammatory peptide for improving muscle loss according to claim 5, characterized in that: The amount of alkaline protease used is 0.005-0.007 parts by weight.

9. The method for preparing the albumin anti-inflammatory peptide for improving muscle loss according to claim 5, characterized in that: Before adding alkaline protease, adjust the pH to 7.5-9.

0.

10. Use of the albumin anti-inflammatory peptide according to any one of claims 1 to 3 in the preparation of food or medicine for improving muscle loss.

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