Albumin peptide for increasing immunity and resisting allergy and preparation method thereof

Abstract

A method for preparing an albumin peptide that enhances immunity and combats allergies, relating to the field of small molecule active peptides, is disclosed. The method includes: dissolving egg white powder in pure water, adjusting the pH, and allowing the mixture to settle and precipitate ovalbumin; dissolving the ovalbumin precipitate in pure water, adjusting the pH and temperature, and then adding a complex protease for enzymatic hydrolysis; after hydrolysis, heating the solution to inactivate the enzyme; centrifuging the enzyme-inactivated solution and desalting the supernatant; separating the desalted solution using a membrane device and collecting the permeate; concentrating and drying the permeate to obtain the small molecule albumin peptide. This invention provides an albumin peptide that enhances immunity and combats allergies, its preparation method, and the anti-allergic active peptide Ala-Leu-Ala-Met, which not only eliminates the allergenicity of ovalbumin but also possesses anti-allergic activity, showing promising application prospects and significant implications for the further application of ovalbumin-related products in the food and pharmaceutical fields.

Description

Technical Field

[0001] This invention relates to the field of small molecule bioactive peptide technology, and in particular to an albumin peptide that enhances the body's immunity and has anti-allergic properties, and its preparation method. Background Technology

[0002] Ovalbumin is the main protein in egg white, accounting for about 65% of its composition. It contains all the essential amino acids required by the human body, and its amino acid composition closely resembles that of the human body, giving it a biological value of over 95, making it one of the most ideal high-quality proteins in food. Due to its excellent gelling, foaming, and emulsifying properties, ovalbumin is widely used in the traditional food industry. Furthermore, it possesses various biological activities, such as protecting the liver, enhancing immunity, anti-oxidation, and promoting brain development.

[0003] However, ovalbumin also presents an allergenic risk. Egg allergy is a common immediate-type food allergy, frequently occurring in children, and can cause significant harm, triggering not only a range of skin conditions but also respiratory and gastrointestinal dysfunction. Studies have shown that ovalbumin is one of the main allergens in eggs, capable of binding to IgE in human serum and triggering an immune response.

[0004] Studies have found that enzymatic hydrolysis can significantly reduce the sensitizing properties of large protein molecules, and some peptides obtained from enzymatic hydrolysis even possess anti-allergic activity. Anti-allergic peptides are a class of small-molecule peptides with significant anti-allergic activity, offering advantages such as better efficacy, fewer side effects, and higher safety compared to traditional anti-allergy drugs. Several studies have reported on anti-allergic peptides from different sources, such as soybean peptides, wheat peptides, oyster peptides, and salmon skin collagen peptides. Furthermore, related patents have also been reported, such as Chinese patent CN110452287A, which discloses an anti-allergic peptide and its preparation method. This patent mainly uses Atlantic salmon viscera to prepare anti-allergic peptides, and includes the following steps: Preparation of enzymatic hydrolysis products from Atlantic salmon viscera: 12% substrate is mixed in distilled water (w / v) and pepsin, then the pH is adjusted to 2.0 using 1M HCl, and the mixture is kept at 37 ℃ for 8 hours to release the anti-allergic peptides. Pepsin is then inactivated by heating at 100 ℃ for 15 minutes. After cooling, the mixture is filtered through a 0.45 μm filter membrane to remove unhydrolyzed proteins. Chinese patent CN110638681A discloses a method for preparing mussel anti-allergy peptides and their application in cosmetics, which mainly includes the following steps: pretreatment, homogenization, ultra-high pressure extraction, subcritical extraction, enzymatic hydrolysis, ultrafiltration, vacuum concentration and drying.

[0005] Currently, there are no reported studies on the preparation of anti-allergy peptides using ovalbumin. Therefore, the preparation of an albumin peptide that enhances the body's immunity and possesses anti-allergy activity through enzymatic hydrolysis is of great significance for the further application of ovalbumin in the food and pharmaceutical fields. Summary of the Invention

[0006] The purpose of this invention is to provide an albumin peptide that enhances the body's immunity and has anti-allergic properties, as well as a method for preparing the same, to fill the gap in the preparation of anti-allergic peptides from ovalbumin.

[0007] The technical solution adopted by this invention to solve the technical problem is as follows:

[0008] This invention provides a method for preparing albumin peptides that enhance immunity and have anti-allergic properties, which specifically includes the following steps:

[0009] Step S1: Extraction of ovalbumin;

[0010] Add egg white powder to pure water and stir to dissolve. After adjusting the pH, let it stand to precipitate ovalbumin.

[0011] Step S2: Enzymatic hydrolysis;

[0012] Take the ovalbumin precipitate, add it to pure water and stir to dissolve. After adjusting the pH and temperature, add the complex protease for enzymatic hydrolysis. After the enzymatic hydrolysis is completed, heat the solution to inactivate the enzyme.

[0013] Step S3: Desalination;

[0014] Centrifuge the enzyme-inactivated liquid and take the clear liquid for desalting treatment;

[0015] Step S4: Separation;

[0016] The desalinated feed solution is separated using a membrane device, and the permeate is collected.

[0017] Step S5: Drying;

[0018] The separated permeate was concentrated and dried to obtain small molecule albumin peptides.

[0019] Preferably, in step S1, egg white powder is added to 5-10 times its weight of pure water and stirred to dissolve. After adjusting the pH of the solution to 4.3-4.7, it is allowed to stand for 0.5-2 hours to precipitate egg white protein.

[0020] Preferably, in step S2, ovalbumin precipitate is added to 5-20 times its mass of pure water and stirred to dissolve. The pH of the solution is adjusted to 6-10 and the temperature to 40-60℃. 0.3-1% of a complex protease is added for enzymatic hydrolysis for 3-6 hours.

[0021] More preferably, the complex protease is composed of alkaline protease, chymotrypsin, and fig protease, and the mass ratio of alkaline protease, chymotrypsin, and fig protease is (3-5):(1-2):(0-2).

[0022] Preferably, in step S2, after enzymatic hydrolysis, the liquid is heated to 80-90℃ for 10-15 minutes to inactivate the enzyme.

[0023] This invention provides an albumin peptide that enhances the body's immunity and has anti-allergic properties, prepared by the aforementioned method.

[0024] Preferably, the albumin peptide contains an anti-allergic active peptide segment, and the amino acid sequence of the anti-allergic active peptide segment is Ala-Leu-Ala-Met.

[0025] The present invention also provides an anti-allergic active peptide obtained by preparing an albumin peptide that enhances the body's immunity and has anti-allergic properties.

[0026] Preferably, the amino acid sequence of the anti-allergic active peptide is Ala-Leu-Ala-Met.

[0027] The beneficial effects of this invention are:

[0028] 1. This invention provides an albumin peptide that enhances the body's immunity and has anti-allergic properties. This albumin peptide exhibits significant physiological activity, along with excellent immune-enhancing and anti-allergic effects.

[0029] 2. This invention provides a method for preparing albumin peptides that enhance immunity and have anti-allergic properties. This method is simple to operate and has relatively mild reaction conditions, making it suitable for large-scale production of albumin peptides.

[0030] 3. This invention provides an anti-allergic active peptide obtained from albumin peptides. The amino acid sequence of this anti-allergic active peptide is Ala-Leu-Ala-Met. This anti-allergic active peptide is a novel small molecule peptide derived from ovalbumin with high anti-allergic activity.

[0031] 4. The present invention provides an albumin peptide that enhances the body's immunity and has anti-allergic properties, a method for preparing the peptide, and the anti-allergic active peptide Ala-Leu-Ala-Met. This not only eliminates the sensitization of ovalbumin but also possesses anti-allergic activity, showing promising application prospects. It is of great significance for the further application of ovalbumin-related products in the food and pharmaceutical fields. Attached Figure Description

[0032] Figure 1 The dose-response curve shows the inhibitory effect of the albumin peptide prepared in Example 1 on hyaluronidase.

[0033] Figure 2 The dose-response curve shows the inhibitory effect of the albumin peptide prepared in Example 2 on hyaluronidase.

[0034] Figure 3 This is the dose-response curve of the inhibitory effect of the anti-allergic active peptide Ala-Leu-Ala-Met on hyaluronidase. Detailed Implementation

[0035] In a first aspect, the present invention provides an albumin peptide that enhances the body's immunity and has anti-allergic properties.

[0036] The present invention provides an albumin peptide that enhances the body's immunity and has anti-allergic properties, which uses small molecule albumin peptide as the active ingredient.

[0037] This invention provides an albumin peptide that enhances the body's immunity and has anti-allergic properties, exhibiting immune-enhancing activity.

[0038] The present invention provides an albumin peptide that enhances the body's immunity and has anti-allergic properties. It contains anti-allergic active peptide segments and therefore has anti-allergic activity.

[0039] Specifically, the amino acid sequence of the anti-allergic active peptide is Ala-Leu-Ala-Met.

[0040] Secondly, the present invention provides a method for preparing albumin peptides that enhance the body's immunity and have anti-allergic properties.

[0041] This invention provides a method for preparing albumin peptides that enhance immunity and have anti-allergic properties. The specific implementation process is as follows:

[0042] Step S1: Extraction of ovalbumin;

[0043] Take egg white powder, add 5-10 times its weight of pure water and stir slowly to dissolve. Adjust the pH of the solution to 4.3-4.7 (preferably 4.5) and let it stand for 0.5-2 hours to precipitate egg white protein.

[0044] Preferably, commercially available egg white powder products with a protein content of ≥80% are used.

[0045] Step S2: Enzymatic hydrolysis;

[0046] Take the ovalbumin precipitate obtained above, add 5-20 times the mass of pure water and stir to dissolve. Adjust the pH of the solution to 6-10 and the temperature to 40-60℃. Add 0.3-1% of compound protease for enzymatic hydrolysis for 3-6 hours. After enzymatic hydrolysis, heat the solution to 80-90℃ (preferably 90℃) for 10-15 minutes (preferably 15 minutes) to inactivate the enzyme.

[0047] Preferably, the complex protease is mainly composed of alkaline protease, chymotrypsin and fig protease, and the mass ratio of alkaline protease, chymotrypsin and fig protease is (3-5):(1-2):(0-2).

[0048] Step S3: Desalination;

[0049] Centrifuge the enzyme-inactivated solution (6000-10000 rpm, 10 min), collect the supernatant, and desalinate it using an electrodialysis device (10-20 mA / cm², conductivity 200-300 μS / cm).

[0050] Step S4: Separation;

[0051] The desalted feed solution is separated by a membrane device with a molecular weight cutoff of 1000-2000 Da (preferably 1000 Da), and the permeate is collected.

[0052] Step S5: Drying;

[0053] The separated permeate is concentrated, spray-dried, or freeze-dried to obtain small molecule albumin peptides.

[0054] Thirdly, the present invention provides an anti-allergic active peptide.

[0055] The present invention provides an anti-allergic active peptide with the amino acid sequence Ala-Leu-Ala-Met.

[0056] The present invention provides an anti-allergic active peptide that can be synthesized by biotechnology. The anti-allergic active peptide Ala-Leu-Ala-Met has been tested and found to have extremely strong anti-allergic activity, which is superior to albumin peptides of the same concentration.

[0057] The technical solutions of the present invention will be clearly and completely described below with reference to the embodiments of the present invention. Obviously, the described embodiments are only some embodiments of the present invention, and not all embodiments. Based on the embodiments of the present invention, all other embodiments obtained by those of ordinary skill in the art without creative effort are within the scope of protection of the present invention.

[0058] Example 1: Preparation of an albumin peptide that enhances immunity and has anti-allergic properties

[0059] Dissolve 500g of egg white powder in 10 times its weight of pure water by slow stirring. Adjust the pH of the solution to 4.5 and let it stand for 2 hours to precipitate ovalbumin. Take the ovalbumin precipitate obtained above, add 15 times its weight of pure water again, stir to dissolve, adjust the pH of the solution to 9.0, and set the temperature to 50℃. Add 0.5% of a complex protease (alkaline protease, chymotrypsin, and fig protease in a mass ratio of 4:2:1) and enzymatically hydrolyze for 5 hours. After enzymatic hydrolysis, heat the solution to 90℃ for 15 minutes to inactivate the enzyme. Centrifuge the enzyme-inactivated solution (10000 rpm, 10 minutes), collect the supernatant, and desalt it using an electrodialysis device (20 mA / cm², conductivity 250 μS / cm). Separate the desalted solution using a membrane device with a molecular weight cutoff of 1000 Da and collect the permeate. Concentrate the separated permeate, spray dry, or freeze dry to obtain small molecule albumin peptides.

[0060] Example 2: Preparation of an albumin peptide that enhances immunity and has anti-allergic properties

[0061] Dissolve 500g of egg white powder in 10 times its weight of pure water by slow stirring. Adjust the pH of the solution to 4.5 and let it stand for 1.5 hours to precipitate ovalbumin. Take the ovalbumin precipitate obtained above, add 20 times its weight of pure water again, stir to dissolve, adjust the pH of the solution to 8.0, and set the temperature to 45℃. Add 1% of a complex protease (alkaline protease, chymotrypsin, and fig protease in a mass ratio of 3:3:2) and enzymatically hydrolyze for 4 hours. After enzymatic hydrolysis, heat the solution to 90℃ for 15 minutes to inactivate the enzyme. Centrifuge the enzyme-inactivated solution (8000 rpm, 10 minutes), collect the supernatant, and desalt it using an electrodialysis device (15mA / cm², conductivity 300μS / cm). Separate the desalted solution using a membrane device with a molecular weight cutoff of 1000Da and collect the permeate. Concentrate the separated permeate, spray dry, or freeze dry to obtain small molecule albumin peptides.

[0062] Experimental Example 1: The albumin peptide prepared in Example 1 was used as the test sample to test the amino acid composition of the albumin peptide.

[0063] The amino acid composition of the albumin peptide prepared in Example 1 was tested, and the amino acid composition of the albumin peptide is shown in Table 1. The albumin peptide prepared in Example 1 contains 18 hydrolyzed amino acids, and the total content of the 18 hydrolyzed amino acids is 86.64 g / 100 g. Among them, the content of the 8 essential amino acids for adults is 30.11 g / 100 g, indicating that it has an important material basis for promoting the recovery or enhancement of immune function.

[0064] Table 1. Amino acid composition test results of the albumin peptides prepared in Example 1.

[0065]

[0066] Experimental Example 2 used the albumin peptide prepared in Example 1 as the test sample to test the molecular weight distribution of the albumin peptide.

[0067] The molecular weight distribution of the albumin peptides prepared in Example 1 was tested, and the results are shown in Table 2. Of the albumin peptides prepared in Example 1, 93.58% had a molecular weight below 1000 Da, with 58.18% falling between 189 and 500 Da. This indicates that the hydrolysis process of the present invention has a good effect, hydrolyzing large protein molecules into oligopeptides, providing a structural basis for their immune-enhancing and anti-allergic activities. Compared to proteins, oligopeptides exhibit stronger advantages in absorption efficiency, bioavailability, and physiological activity due to their unique structure and function.

[0068] Table 2. Molecular weight distribution of albumin peptides prepared in Example 1

[0069]

[0070] Experimental Example 3 used the albumin peptide prepared in Example 1 as the test sample to test its immune-enhancing activity.

[0071] Experimental animals: female mice, weighing 18-22g, 10 mice per group.

[0072] Dosage grouping and administration time of test samples:

[0073] The recommended oral dose of albumin peptide for humans is 5g / day, which translates to a dose of 0.0833g / kg body weight (bw) for an adult with a standard weight of 60kg. The experiment included three dose groups (low-dose, medium-dose, and high-dose) and one negative control group (physiological saline). The three dose groups were administered the test sample by gavage for 30 days, while the negative control group was administered physiological saline by gavage for 30 days. Mice in the low-dose group were fed a standard dose of 0.416g / kg bw, the medium-dose group at 0.833g / kg bw, and the high-dose group at 2.499g / kg bw, approximately 5, 10, and 30 times the recommended oral dose for humans (0.0833g / kg bw), respectively.

[0074] The test items and methods are as follows:

[0075] 1. Determination of body weight and organ / body weight ratio: Mice were sacrificed 30 days after the experiment, and the thymus and spleen were weighed to determine the ratio of thymus to body weight and the ratio of spleen to body weight.

[0076] 2. Cellular immune function assay: ConA-induced mouse spleen lymphocyte transformation assay (MTT method).

[0077] Spleens from mice in each group were placed in culture dishes containing 5 mL of sterile PBS. Fat and connective tissue were removed, and the cells were washed twice with PBS. A single-cell suspension was prepared by grinding, centrifugation at 1500 r / min for 5 min, and the supernatant was discarded. Cells were resuspended in 5 mL of RPMI 1640 medium, centrifuged at 1500 r / min for 5 min, and washed twice. The cell concentration was adjusted to 2 × 10⁶ cells / mL using RPMI 1640 medium. 6 Cells / mL; 100 μL cell suspension (2 × 10⁻⁶) 5 Add 100 μL of ConA solution (final concentration 5 μg / mL) to each well and incubate at 37℃ in a 5% CO2 incubator for 48 h. Four h before the end of the culture, add 20 μL of MTT solution (5 mg / mL) to each well and continue incubation for another 4 h. Carefully aspirate the supernatant from each well and add 150 μL of DMSO to each well. Place the well on a shaker and shake at low speed for 10 min to fully dissolve the formazan crystals. Measure the absorbance (OD value) of each well at 570 nm using a microplate reader.

[0078] 3. Humoral immune function test: serum hemolysin test (half-hemolysis value);

[0079] Mouse serum from each group was diluted with PBS at ratios of 1:5, 1:10, and 1:20, respectively. Guinea pig serum was diluted with PBS at a ratio of 1:10 and used as complement. In 96-well plates, the following solutions were prepared: experimental groups (low-dose, medium-dose, and high-dose groups): 100 μL diluted serum + 50 μL 5% sheep red blood cell (SRBC) suspension + 50 μL complement; positive control group (total hemolysis): 100 μL diluted serum + 50 μL 5% SRBC suspension + 50 μL distilled water (to replace complement and completely hemolyze SRBCs); Negative control group 1 (without complement): 100 μL diluted serum + 50 μL 5% SRBC suspension + 50 μL PBS; Negative control group 2 (complement inactivated): 100 μL diluted serum + 50 μL 5% SRBC suspension + 50 μL complement inactivated at 56℃; Blank control group: 100 μL diluent + 50 μL 5% SRBC suspension + 50 μL complement; Incubate the wells in a 37℃ CO2 incubator for 30 minutes, then immediately place them on ice to stop the reaction. Add 20 μL of 0.1% glacial acetic acid to each well (to fix unlysed cells) and let stand for 5 minutes; Centrifuge at 3000 r / min for 10 minutes, transfer 100 μL of supernatant to a new 96-well plate, and measure the absorbance (OD value) at 540 nm using a microplate reader. Hemolysis rate of each group = (OD value of experimental group - OD value of blank control group) / (OD value of total hemolysis - OD value of blank control group) * 100%, and the half-maximum hemolysis value (HCV) of each group. 50() represents the dilution factor of mouse serum when the hemolysis rate is 50%, calculated by plotting the hemolysis curve.

[0080] The test results are as follows:

[0081] 1. Effects of albumin peptides on mouse body weight and organ / body weight ratio;

[0082] The effects of albumin peptide on mouse body weight and organ / body weight ratio are shown in Table 3. There were no significant differences in body weight and organ / body weight ratio between the different dose groups and the negative control group, indicating that different doses of albumin peptide had no effect on mouse body weight and immune organ / body weight ratio.

[0083] Table 3. Effects of albumin peptides prepared in Example 1 on mouse body weight and organ / body weight ratio ( ±S)

[0084]

[0085] 2. Effects of albumin peptides on mouse cellular immune function;

[0086] The effects of albumin peptide on mouse cellular immune function are shown in Table 4. All dose groups significantly improved the proliferation capacity of mouse spleen lymphocytes, and the proliferation capacity of spleen lymphocytes showed a continuous upward trend with the increase of dose, indicating that albumin peptide has a significant enhancing effect on mouse cellular immune function.

[0087] Table 4. Effects of albumin peptides prepared in Example 1 on ConA-induced proliferation of mouse spleen lymphocytes ( ±S)

[0088]

[0089] 3. Effects of albumin peptides on humoral immune function in mice;

[0090] The effects of albumin peptide on humoral immune function in mice are shown in Table 5. Each dose group significantly increased serum hemolysin in mice, indicating that albumin peptide has a significant enhancing effect on humoral immune function in mice.

[0091] Table 5. Effect of albumin peptides prepared in Example 1 on the half-hemolytic value in mice ( ±S)

[0092]

[0093] According to the "Methods for Testing and Evaluation of Functions of Health Foods (2023 Edition)," which helps in determining immunity enhancement, a positive result in any two of the four aspects—cellular immune function, humoral immune function, mononuclear-macrophage function, and NK cell activity—indicates that the tested sample has an effect in enhancing immunity. Therefore, it can be determined that the albumin peptide prepared in this invention possesses immune-enhancing activity.

[0094] Experimental Example 4 used the albumin peptide prepared in Example 2 as the test sample to test its immune-enhancing activity.

[0095] The experimental method was the same as in Example 3, and the results are shown in the table below. The albumin peptide prepared in Example 2 showed the same immune-enhancing effect as the albumin peptide prepared in Example 1.

[0096] Table 6. Effects of albumin peptides prepared in Example 2 on mouse body weight and organ / body weight ratio ( ±S)

[0097]

[0098] Table 7. Effects of albumin peptides prepared in Example 2 on ConA-induced proliferation of mouse spleen lymphocytes ( ±S)

[0099]

[0100] Table 8. Effect of albumin peptides prepared in Example 2 on the half-hemolytic value in mice ( ±S)

[0101]

[0102] Experimental Example 5 used the albumin peptides prepared in Examples 1 and 2 as test samples to test their anti-allergic activity.

[0103] The hyaluronidase inhibition assay is one of the main in vitro methods for evaluating the anti-allergic activity of substances. By measuring the inhibition rate of a substance on hyaluronidase activity, the strength of its anti-allergic activity can be evaluated. The greater the inhibition rate, the stronger the anti-allergic activity of the substance.

[0104] The experimental method is as follows:

[0105] 0.1 mL of 0.25 mmol / L CaCl2 solution was added, followed by hyaluronidase solution (50 mg hyaluronidase dissolved in 20 mL of 0.1 mol / L acetate buffer, pH 4.01), and incubated at 37 °C for 20 min. Then, 0.5 mL of albumin peptide solutions of different concentrations (20, 40, 60, 80, 100 mg / mL) were added, and the mixture was incubated at 37 °C for 20 min. Next, 0.6 mL of 0.6 mg / mL sodium hyaluronate solution was added, and the mixture was incubated at 37 °C for 20 min. Then, 1 mL of 0.4 mol / L NaOH solution was added, and the mixture was rapidly cooled on ice water for 15 min. Finally, 0.2 mL of boric acid was added, and the mixture was incubated in a boiling water bath for 3 min, immediately cooled on ice water for 5 min, and then 3 mL of P-DAB reagent was added. The mixture was incubated at 37 °C for 20 min, and the color was developed. The OD value was measured at 585 nm.

[0106] The specific formula for calculating anti-allergic activity is as follows:

[0107]

[0108] In the formula, A is the OD value of the control solution (enzyme + buffer + substrate);

[0109] B represents the OD value of the control blank solution (buffer solution + buffer solution + substrate);

[0110] C represents the OD value of the sample (enzyme + albumin peptide solution + substrate);

[0111] D represents the OD value of the blank control sample (buffer solution + albumin peptide solution + substrate).

[0112] Experimental results are as follows Figure 1 and Figure 2 As shown, within the experimental concentration range, the inhibition rate of albumin peptide against hyaluronidase increases with increasing concentration, indicating that the albumin peptide prepared in this invention has good anti-allergic activity.

[0113] Experimental Example 6: Preparation and Anti-allergic Activity Test of the Anti-allergic Active Peptide Ala-Leu-Ala-Met

[0114] 1. Preparation of the anti-allergic active peptide Ala-Leu-Ala-Met;

[0115] The albumin peptide prepared in Example 1 was subjected to peptide sequence identification and relative abundance analysis using LC-MS / MS technology. A peptide with high anti-allergic activity was screened out, with the amino acid sequence Ala-Leu-Ala-Met. This amino acid sequence was found to be a new active peptide by searching the online databases BIOPEP and EROP-Moscow.

[0116] 2. Anti-allergic activity test of the anti-allergic active peptide Ala-Leu-Ala-Met;

[0117] A peptide with the amino acid sequence Ala-Leu-Ala-Met was synthesized using biotechnology, with a purity of 99.31%. Different concentrations (20 mg / mL, 40 mg / mL, 60 mg / mL, 80 mg / mL, and 100 mg / mL) of the synthesized peptide were prepared, and its anti-allergic activity was determined.

[0118] Experimental results are as follows Figure 3 As shown, within the experimental concentration range, the inhibition rate of the Ala-Leu-Ala-Met active peptide against hyaluronidase increased with increasing concentration, and was related to... Figure 1 Compared with the results shown, the Ala-Leu-Ala-Met active peptide fragment showed a significantly higher inhibition rate of hyaluronidase than albumin peptide of the same concentration, indicating that the active Ala-Leu-Ala-Met peptide fragment has extremely strong anti-allergic activity and is superior to albumin peptide of the same concentration.

[0119] This invention discloses an albumin peptide that enhances the body's immunity and has anti-allergic properties, as well as a method for its preparation. Those skilled in the art can refer to the content of this document and appropriately modify the process parameters to achieve the desired result. It is particularly important to note that all similar substitutions and modifications are obvious to those skilled in the art and are considered to be included in this invention. The product of this invention has been described through preferred embodiments, and those skilled in the art can clearly modify or appropriately change and combine the product described herein without departing from the content, spirit, and scope of this invention to realize and apply the technology of this invention.

Claims

1. An anti-allergic active peptide fragment, characterized in that, Ala-Leu-Ala-Met.

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