Preparation method and application of small molecule peptide in peanut meal

Abstract

The invention relates to a preparation method and application of small molecule peptide in peanut meal, and belongs to the technical field of preparation of plant small molecule peptide. The preparation method comprises the steps of enzymolysis extraction, high-speed counter-current chromatography separation, purification after enzymolysis and the like. The peanut meal small molecule peptide prepared by the method has a better anti-oxidation effect, and when the peanut meal small molecule peptide is added into edible oil, the oxidation and rancidity conditions in the storage process of the edible oil can be obviously reduced, the stability of the edible oil is improved, and the shelf life is prolonged.

Description

Technical Field

[0001] The invention belongs to the technical field of preparation of plant small molecule peptides, and relates to a preparation method of small molecule peptides in peanut meal and application thereof. Background Art

[0002] Oils and fats are an important source of nutrients in human daily life, and their quality and safety have always been the focus of attention. However, oils and fats contain a large amount of polyunsaturated fatty acids, which are easily affected by external factors, resulting in quality deterioration and the production of carcinogenic aldehydes and ketones, which pose a risk to human health. Therefore, it is important to take a series of measures to inhibit lipid oxidation in edible oil production, storage, and sales. Antioxidants can interact with peroxides produced by unsaturated fatty acids under certain conditions, blocking the pathway of oil oxidation and deterioration, and therefore play a key role in improving oil stability and extending shelf life.

[0003] Peanut protein is a high-quality source of plant protein, containing a variety of essential amino acids and having high nutritional value. Moderate enzymatic hydrolysis can improve the functional properties of peanut protein, convert it into products with certain functional characteristics, give full play to the nutrition and function of peanut protein, and increase the utilization rate of protein. After hydrolysis, peanut protein not only has a strong ability to scavenge free radicals, chelate metal ions, inhibit lipid oxidation and delay aging, but also has the characteristics of safety and no toxic side effects compared with synthetic antioxidants. It has been reported in the literature that peanut protein peptide can improve the emulsification stability and oxidation stability of walnut milk, and improve the quality and storage stability of walnut milk.

[0004] However, there is no research or report on the effect of small molecule peptides in peanut meal on the stability of edible oil in the prior art. Summary of the invention

[0005] The main purpose of the present invention is to provide a method for preparing small molecule peptides in peanut meal and the effect of the peptides on improving the stability of edible oil.

[0006] The present invention adopts the following technical solutions to achieve the above purpose: A method for preparing small molecule peptides from peanut meal comprises the following steps: Step 1, dispersing peanut meal powder into water to prepare a suspension, adding citric acid to adjust the pH value of the suspension to 4.5, adding cellulase, and performing enzymolysis at 30-35° C. for 1-1.5 hours; then adjusting the pH value of the enzymolysis solution to 6.0 with sodium bicarbonate, adding flavor protease, performing enzymolysis at 50-55° C. for 2-2.5 hours, filtering, and obtaining an extract; Step 2, concentrating the extract obtained in step 1, and separating by high-speed countercurrent chromatography to obtain a primary product; Step 3, dispersing the primary product obtained in step 2 into an aqueous solution containing ficin, papain, and nattokinase, adjusting the pH to 6.0, performing enzymolysis at 40-45° C. for 1-1.5 hours, heating to inactivate the enzyme, cooling, adding ethanol, and adjusting the alcohol content to 30%, 50%, and 70% in sequence, standing for 20-30 minutes after each adjustment of the alcohol content, and centrifuging to obtain a precipitate; Step 4, after re-dissolving the precipitate obtained in step 3, loading it on a dextran gel column, eluting it with deionized water, testing the eluate, collecting the eluate containing peptides with a molecular weight of 500-1200 Da, concentrating it, and drying it to obtain the target peanut meal small molecule peptide.

[0007] Furthermore, in step 1, the material-liquid ratio of peanut meal to water is 1:(5-8) in kg / L.

[0008] Furthermore, the amount of cellulase added in step 1 is 0.4-0.5% of the mass of the peanut meal.

[0009] Furthermore, the amount of flavor protease added in step 1 is 0.2-0.3% of the mass of peanut meal.

[0010] Furthermore, the solvent system in the high-speed countercurrent chromatography in step 2 is: n-butanol, acetonitrile and water in a volume ratio of 1:0.5:1:2 and a volume ratio of 3:1:3.

[0011] Furthermore, in step 2, the rotation speed of the high-speed countercurrent chromatography is 800 r / min, the flow rate of the mobile phase is 2 mL / min, the temperature is 25° C., the ultraviolet detection wavelength is 254 nm, and the retention value of the stationary phase is 50-60%.

[0012] Furthermore, the target fraction in the high-speed countercurrent chromatography in step 2 is the target peak fraction 70-110 minutes after injection.

[0013] Furthermore, the aqueous solution in step 3 contains 1.0 g / L of ficin, 2.5 g / L of papain, and 0.8 g / L of nattokinase.

[0014] Furthermore, in step 3, the material-to-liquid ratio of the initial product and the enzyme-containing aqueous solution is 1:(3-5) in kg / mL.

[0015] The present invention provides a specific use of the peanut meal small molecule peptide, that is, the peanut meal small molecule peptide can be added to edible oil to improve the stability of the edible oil.

[0016] The present invention has the following beneficial effects: The invention firstly adopts a method of enzymolysis of cellulase and flavor protease in sequence to extract protein peptides from peanut meal, and the enzymolysis method can improve the extraction rate of protein peptides; then a high-speed countercurrent chromatography method is used to preliminarily separate the protein peptides obtained by enzymolysis to obtain protein peptides of target fragments; the target protein peptides are enzymolyzed by using ficin, papain and nattokinase to decompose the macromolecular protein peptides into small molecular peptides; then, the protein peptides are purified by a dextran gel column to intercept the small molecular peptides of the target fragments.

[0017] The peanut meal small molecule peptide obtained by the method of the present invention has good antioxidant activity. When added to edible oil, it can significantly alleviate the oxidation and rancidity of the edible oil, improve the stability of the edible oil, and extend the shelf life of the edible oil. BRIEF DESCRIPTION OF THE DRAWINGS

[0018] Figure 1 : Changes in peroxide value of edible oils with different peanut meal peptides added; Figure 2 : Changes in acid value of edible oils with different peanut meal peptides added; Figure 3 : High speed countercurrent chromatogram described in Example 1; Figure 4 : High speed countercurrent chromatogram described in Comparative Example 2; Figure 5 : High speed countercurrent chromatogram described in Comparative Example 3. DETAILED DESCRIPTION

[0019] The present invention is further explained below in conjunction with specific examples. It should be understood that these examples are only used to illustrate the present invention and are not used to limit the scope of the present invention. After reading the present invention, modifications to various equivalent forms of the present invention by those skilled in the art all fall within the scope protected by the claims of this application. The enzymes used in the following embodiments are all commercially available products, which can be purchased from online or offline channels, wherein the flavor protease enzyme activity is 50000u / g, the fig protease enzyme activity is 100000u / g, the papain enzyme activity is 100000u / g, and the nattokinase enzyme activity is 20000U / g.

[0020] Example 1 Step 1, crushing peanut meal, passing through a 100-mesh sieve, and obtaining peanut meal powder for later use; dispersing 1 kg of peanut meal powder into 8 L of deionized water to prepare a suspension, adding citric acid to adjust the pH value of the suspension to 4.5, adding 5 g of cellulase, heating to 30° C., and keeping the temperature for enzymolysis for 1 hour; then adjusting the pH value of the enzymolysis solution to 6.0 with sodium bicarbonate, adding 3 g of flavor protease, heating to 55° C., keeping the temperature for enzymolysis for 2 hours, filtering, and obtaining an extract; Step 2, after concentrating the extract obtained in step 1, separate it by high speed countercurrent chromatography: The solvent system is n-butanol-acetonitrile-water with a volume ratio of 3:1:3, the upper phase is the stationary phase, and the lower phase is the mobile phase. The preparation method is as follows: n-butanol-acetonitrile-water is placed in a separatory funnel, and after shaking, the funnel is allowed to stand for stratification, the upper phase and the lower phase are separated, and ultrasonic degassing is performed respectively; the stationary phase is pumped into the pipeline of a high-speed countercurrent chromatograph, and after the stationary phase fills the pipeline, the forward rotation is started at 800r / min, the column temperature is 25°C, and the mobile phase is pumped in at a flow rate of 2mL / min. After the instrument reaches equilibrium, the ultraviolet detector is started, and the detection wavelength is 254nm. After the baseline is stable, the concentrated extract is injected from the injection valve, and the target peak fraction (70-110min) is collected. After reduced pressure concentration, the initial product is obtained; the retention value of the stationary phase is 53%; Step 3, dispersing the primary product obtained in step 2 into an aqueous solution containing 1.0 g / L of ficin, 2.5 g / L of papain, and 0.8 g / L of nattokinase according to a material-liquid ratio of 1:5, kg / L, adjusting the pH to 6.0, heating to 45°C, keeping the enzymolysis for 1 hour, heating to kill the enzyme, cooling, adding ethanol, and adjusting the alcohol content to 30%, 50%, and 70% in sequence, standing for 20 minutes after each adjustment of the alcohol content, centrifuging, and obtaining a precipitate; Step 4, after re-dissolving the precipitate obtained in step 3 with water, loading it on a Sephadex G-15 dextran gel column, eluting it with deionized water, testing the eluate, collecting the eluate containing peptides with a molecular weight of 500-1200 Da, concentrating it, and drying it to obtain the target peanut meal small molecule peptide.

[0021] Example 2 Step 1, crushing peanut meal, passing through a 100-mesh sieve, and obtaining peanut meal powder for later use; dispersing 1 kg of peanut meal powder into 5 L of deionized water to prepare a suspension, adding citric acid to adjust the pH value of the suspension to 5.0, adding 4 g of cellulase, heating to 35° C., and keeping the temperature for enzymolysis for 1.5 hours; then adjusting the pH value of the enzymolysis solution to 6.5 with sodium bicarbonate, adding 2 g of flavor protease, heating to 50° C., keeping the temperature for enzymolysis for 2.5 hours, filtering, and obtaining an extract; Step 2, after concentrating the extract obtained in step 1, separate it by high speed countercurrent chromatography: The solvent system is n-butanol-acetonitrile-water with a volume ratio of 3:1:3, the upper phase is the stationary phase, and the lower phase is the mobile phase. The preparation method is as follows: n-butanol-acetonitrile-water is placed in a separatory funnel, and after shaking, the funnel is allowed to stand for stratification, the upper phase and the lower phase are separated, and ultrasonic degassing is performed respectively; the stationary phase is pumped into the pipeline of a high-speed countercurrent chromatograph, and after the stationary phase fills the pipeline, the forward rotation is started at 800r / min, the column temperature is 25°C, and the mobile phase is pumped in at a flow rate of 2mL / min. After the instrument reaches equilibrium, the ultraviolet detector is started, and the detection wavelength is 254nm. After the baseline is stable, the concentrated extract is injected from the injection valve, and the target peak fraction (70-110min) is collected. After reduced pressure concentration, the initial product is obtained; the retention value of the stationary phase is 59%; Step 3, dispersing the primary product obtained in step 2 into an aqueous solution containing 0.5 g / L of ficin, 3.0 g / L of papain, and 1.2 g / L of nattokinase according to a material-liquid ratio of 1:3, kg / L, adjusting the pH to 6.0, heating to 40°C, keeping the enzymolysis for 1.5 hours, heating to kill the enzyme, cooling, adding ethanol, and adjusting the alcohol content to 30%, 50%, and 70% in sequence, standing for 30 minutes after each adjustment of the alcohol content, and centrifuging to obtain a precipitate; Step 4, after re-dissolving the precipitate obtained in step 3 with water, loading it on a Sephadex G-15 dextran gel column, eluting it with deionized water, testing the eluate, collecting the eluate containing peptides with a molecular weight of 500-1200 Da, concentrating it, and drying it to obtain the target peanut meal small molecule peptide.

[0022] Example 3 Step 1, crushing peanut meal, passing through a 100-mesh sieve, and obtaining peanut meal powder for later use; dispersing 1 kg of peanut meal powder into 6 L of deionized water to prepare a suspension, adding citric acid to adjust the pH value of the suspension to 5.0, adding 4.5 g of cellulase, heating to 35° C., and keeping the temperature for enzymolysis for 1 hour; then adjusting the pH value of the enzymolysis solution to 6.0 with sodium bicarbonate, adding 2.5 g of flavor protease, heating to 55° C., keeping the temperature for enzymolysis for 2 hours, filtering, and obtaining an extract; Step 2, after concentrating the extract obtained in step 1, separate it by high speed countercurrent chromatography: The solvent system is n-butanol-acetonitrile-water with a volume ratio of 3:1:3, the upper phase is the stationary phase, and the lower phase is the mobile phase. The preparation method is as follows: n-butanol-acetonitrile-water is placed in a separatory funnel, and after shaking, the funnel is allowed to stand for stratification, the upper phase and the lower phase are separated, and ultrasonic degassing is performed respectively; the stationary phase is pumped into the pipeline of a high-speed countercurrent chromatograph, and after the stationary phase fills the pipeline, the forward rotation is started at 800r / min, the column temperature is 25°C, and the mobile phase is pumped in at a flow rate of 2mL / min. After the instrument reaches equilibrium, the ultraviolet detector is started, and the detection wavelength is 254nm. After the baseline is stable, the concentrated extract is injected from the injection valve, and the target peak fraction (70-110min) is collected. After reduced pressure concentration, the initial product is obtained; the retention value of the stationary phase is 55%; Step 3, dispersing the primary product obtained in step 2 into an aqueous solution containing 0.8 g / L of ficin, 2.7 g / L of papain, and 1.0 g / L of nattokinase according to a material-liquid ratio of 1:4, kg / L, adjusting the pH to 6.0, heating to 45°C, keeping the enzymolysis for 1 hour, heating to kill the enzyme, cooling, adding ethanol, and adjusting the alcohol content to 30%, 50%, and 70% in sequence, standing for 20 minutes after each adjustment of the alcohol content, centrifuging, and obtaining a precipitate; Step 4, after re-dissolving the precipitate obtained in step 3 with water, loading it on a Sephadex G-15 dextran gel column, eluting it with deionized water, testing the eluate, collecting the eluate containing peptides with a molecular weight of 500-1200 Da, concentrating it, and drying it to obtain the target peanut meal small molecule peptide.

[0023] Comparative Example 1 Step 1, crushing peanut meal, passing through a 100-mesh sieve, and obtaining peanut meal powder for later use; dispersing 1 kg of peanut meal powder into 5 L of deionized water to prepare a suspension, adding citric acid to adjust the pH value of the suspension to 5.0, adding 4 g of cellulase, heating to 35° C., and keeping the temperature for enzymolysis for 1.5 hours; then adjusting the pH value of the enzymolysis solution to 6.5 with sodium bicarbonate, adding 2 g of flavor protease, heating to 50° C., keeping the temperature for enzymolysis for 2.5 hours, filtering, and obtaining an extract; Step 2, adding ethanol to the extract obtained in step 1, adjusting the alcohol content to 30%, 50%, and 70% in sequence, standing for 30 minutes after each adjustment of the alcohol content, centrifuging to obtain a precipitate, and drying to obtain peanut meal peptide.

[0024] Comparative Example 2 Step 1, crushing peanut meal, passing through a 100-mesh sieve, and obtaining peanut meal powder for later use; dispersing 1 kg of peanut meal powder into 5 L of deionized water to prepare a suspension, adding citric acid to adjust the pH value of the suspension to 5.0, adding 4 g of cellulase, heating to 35° C., and keeping the temperature for enzymolysis for 1.5 hours; then adjusting the pH value of the enzymolysis solution to 6.5 with sodium bicarbonate, adding 2 g of flavor protease, heating to 50° C., keeping the temperature for enzymolysis for 2.5 hours, filtering, and obtaining an extract; Step 2, after concentrating the extract obtained in step 1, separate it by high speed countercurrent chromatography: The solvent system is n-butanol-acetonitrile-water with a volume ratio of 3:1:3, the upper phase is the stationary phase, and the lower phase is the mobile phase. The preparation method is as follows: n-butanol-acetonitrile-water is placed in a separatory funnel, and after shaking, the funnel is allowed to stand for stratification, the upper phase and the lower phase are separated, and ultrasonic degassing is performed respectively; the stationary phase is pumped into the pipeline of a high-speed countercurrent chromatograph, and after the stationary phase fills the pipeline, the forward rotation is started at 800r / min, the column temperature is 25°C, and the mobile phase is pumped in at a flow rate of 2mL / min. After the instrument reaches equilibrium, the ultraviolet detector is started, and the detection wavelength is 254nm. After the baseline is stable, the concentrated extract is injected from the injection valve, and the fractions are collected (140-170min). After reduced pressure concentration, the initial product is obtained; the retention value of the stationary phase is 51%; Step 3, dispersing the primary product obtained in step 2 into an aqueous solution containing 0.5 g / L of ficin, 3.0 g / L of papain, and 1.2 g / L of nattokinase according to a material-liquid ratio of 1:3, kg / L, adjusting the pH to 6.0, heating to 40°C, keeping the enzymolysis for 1.5 hours, heating to kill the enzyme, cooling, adding ethanol, and adjusting the alcohol content to 30%, 50%, and 70% in sequence, standing for 30 minutes after each adjustment of the alcohol content, and centrifuging to obtain a precipitate; Step 4, after re-dissolving the precipitate obtained in step 3 with water, loading it on a Sephadex G-15 dextran gel column, eluting it with deionized water, testing the eluate, collecting the eluate containing peptides with a molecular weight of 500-1200 Da, concentrating it, and drying it to obtain the target peanut meal small molecule peptide.

[0025] Comparative Example 3 Step 1, crush the peanut meal, pass it through a 100-mesh sieve, and obtain peanut meal powder for later use; disperse 1 kg of peanut meal powder in 5 L of deionized water to prepare a suspension, adjust the pH value of the enzymatic solution to 6.5 with sodium bicarbonate, add 2 g of flavor protease, heat to 50° C., keep the temperature for enzymatic hydrolysis for 2.5 hours, filter, and obtain an extract; Step 2, after concentrating the extract obtained in step 1, separate it by high speed countercurrent chromatography: The solvent system is n-butanol-acetonitrile-water with a volume ratio of 3:1:3, the upper phase is the stationary phase, and the lower phase is the mobile phase. The preparation method is as follows: methyl tert-butyl ether-acetonitrile-water is placed in a separatory funnel, and after shaking, the mixture is allowed to stand for stratification, the upper phase and the lower phase are separated, and ultrasonic degassing is performed respectively; the stationary phase is pumped into the pipeline of a high-speed countercurrent chromatograph, and after the stationary phase fills the pipeline, the forward rotation is started at 800r / min, the column temperature is 25°C, and the mobile phase is pumped in at a flow rate of 2mL / min. After the instrument reaches equilibrium, the ultraviolet detector is started, and the detection wavelength is 254nm. After the baseline is stable, the concentrated extract is injected from the injection valve, and the target peak fraction (70-110min) is collected. After reduced pressure concentration, the initial product is obtained; the retention value of the stationary phase is 57%; Step 3, dispersing the initial product obtained in step 2 into an aqueous solution containing 1.2 g / L of nattokinase according to a material-liquid ratio of 1:3, kg / L, adjusting the pH to 6.0, heating to 40°C, keeping the enzymolysis for 1.5 hours, heating to kill the enzyme, cooling, adding ethanol, and adjusting the alcohol content to 30%, 50%, and 70% in sequence, standing for 30 minutes after each adjustment of the alcohol content, centrifuging, and obtaining a precipitate; Step 4, after re-dissolving the precipitate obtained in step 3 with water, loading it on a Sephadex G-15 dextran gel column, eluting it with deionized water, testing the eluate, collecting the eluate containing peptides with a molecular weight of 500-1200 Da, concentrating it, and drying it to obtain the target peanut meal small molecule peptide.

[0026] Effect of small molecule peptides from peanut meal on oxidative stability of edible oil Weigh 7 portions of freshly squeezed peanut oil, 500 mL each, and add the peanut meal peptides obtained in Examples 1 to 3 and Comparative Examples 1 to 3 to the edible oils, respectively. One group without addition is used as a blank control group. The oil samples are placed in a 60±2°C constant temperature box for 30 days, and samples are taken at 0, 5, 10, 20, and 30 hours for determination of physical and chemical indicators.

[0027] The peroxide value refers to the titration method (GB / T5009.227-2016 "Determination of Peroxide Value in Food" Method 1), and the acid value refers to the indicator titration method (GB5009.229-2016 "Determination of Acid Value in Food" Method 1).

[0028] The test results are as follows: Neutral fats in edible oils are broken down into glycerol and fatty acids. The unsaturated chains in fatty acids break to form peroxides. The higher the peroxide value, the more serious the oxidation of the oil. Figure 1The peroxide value of the blank group gradually increased with time. After adding the peanut meal peptide, the oxidation of the edible oil was alleviated, but the oxidation of Comparative Example 2 was basically not alleviated, which was not much different from the blank group. The oxidation of Comparative Example 1 and Comparative Example 3 was better than that of Comparative Example 2, but compared with Examples 1 to 3 of the present invention, the effect was poor. It can be seen that the peanut meal small molecule peptide prepared by the present invention has a good effect of inhibiting the oxidation and deterioration of edible oil.

[0029] Triglycerides in oils and fats will hydrolyze during heating to produce free fatty acids, causing rancidity. Free fatty acids continue to accumulate during the hydrolysis and rancidity process, which will accelerate the rancidity of oils and fats. The results are attached. Figure 2 In the blank group, the acid value in the edible oil increased continuously with the extension of time. After adding the peanut meal peptide, the rancidity was also alleviated, but consistent with the oxidation situation, the edible oil in Comparative Example 2 was basically not alleviated, and the alleviation in Comparative Example 1 and Comparative Example 3 was worse than that in Example 1-Example 3. It can be seen that the peanut meal small molecule peptide prepared by the present invention also has the effect of inhibiting the rancidity of edible oil.

Claims

1. A method for preparing small molecule peptides from peanut meal, characterized in that: The following steps are involved: Step 1, dispersing peanut meal powder into water to prepare a suspension, adding citric acid to adjust the pH value of the suspension to 4.5, adding cellulase, and performing enzymolysis at 30-35° C. for 1-1.5 hours; then adjusting the pH value of the enzymolysis solution to 6.0 with sodium bicarbonate, adding flavor protease, performing enzymolysis at 50-55° C. for 2-2.5 hours, filtering, and obtaining an extract; Step 2, concentrating the extract obtained in step 1, and separating by high-speed countercurrent chromatography to obtain a primary product; Step 3, dispersing the primary product obtained in step 2 into an aqueous solution containing ficin, papain, and nattokinase, adjusting the pH to 6.0, performing enzymolysis at 40-45° C. for 1-1.5 hours, heating to inactivate the enzyme, cooling, adding ethanol, and adjusting the alcohol content to 30%, 50%, and 70% in sequence, standing for 20-30 minutes after each adjustment of the alcohol content, and centrifuging to obtain a precipitate; Step 4, after re-dissolving the precipitate obtained in step 3, loading it on a dextran gel column, eluting it with deionized water, testing the eluate, collecting the eluate containing peptides with a molecular weight of 500-1200 Da, concentrating it, and drying it to obtain the target peanut meal small molecule peptide.

2. The preparation method according to claim 1, characterized in that In the step 1, the material-liquid ratio of peanut meal to water is 1:(5-8) in kg / L.

3. The preparation method according to claim 1, characterized in that: In the step 1, the amount of cellulase added is 0.4-0.5% of the mass of the peanut meal.

4. The preparation method according to claim 1, characterized in that: In the step 1, the amount of flavor protease added is 0.2-0.3% of the mass of the peanut meal.

5. The preparation method according to claim 1, characterized in that: The solvent system in the high-speed countercurrent chromatography in step 2 is: n-butanol, acetonitrile and water in a volume ratio of 1:0.5:1:2 and a volume ratio of 3:1:

3.

6. The preparation method according to claim 1, characterized in that: In the step 2, the rotation speed of the high-speed countercurrent chromatography is 800 r / min, the flow rate of the mobile phase is 2 mL / min, the temperature is 25° C., the ultraviolet detection wavelength is 254 nm, and the retention value of the stationary phase is 50-60%.

7. The preparation method according to claim 1, characterized in that: The target fraction in the high-speed countercurrent chromatography in step 2 is the target peak fraction 70-110 minutes after injection.

8. The preparation method according to claim 1, characterized in that: The aqueous solution in step 3 contains 1.0 g / L of ficin, 2.5 g / L of papain, and 0.8 g / L of nattokinase.

9. The preparation method according to claim 1, characterized in that: In the step 3, the material-liquid ratio of the initial product to the enzyme-containing aqueous solution is 1:(3-5) in kg / mL.

10. A use of a peanut meal small molecule peptide in improving the stability of edible oil, characterized in that: The peanut meal small molecule peptide is the peanut meal small molecule peptide prepared by the preparation method described in any one of claims 1-9.

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