Preparation method and application of organic peptide salt
By fractionally purifying and optimizing reaction conditions of bioactive peptides from edible leaves, high-purity and highly stable organic peptide salts were prepared, solving the stability and solubility problems of bioactive peptides from edible leaves in existing technologies and expanding their application in food, health products and cosmetics.
Patent Information
- Application Number
- CN202511138417.9
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Filing Date
- 2025-08-14
- Publication Date
- 2025-12-05
AI Technical Summary
Existing technologies have poor stability, low solubility and bioavailability of plant bioactive peptides, and the preparation methods of organic peptide salts are inefficient, have low purity, and rely on a single source of raw materials. There is also a lack of research on novel plant peptide salts.
Ultrafiltration membrane separation technology was used to fractionate and purify the active peptides of *Gnaphalium affine*. Specific organic acids were selected and reaction conditions were optimized. Combined with ultrasound-assisted reaction, organic peptides were prepared. By optimizing the preparation process, the selection of organic acids and reaction conditions, the yield and purity of organic peptide salts were significantly improved, and their stability and functionality were enhanced.
The prepared organic peptide salts exhibit 30%-50% improved solubility, significantly enhanced stability within a pH range of 3.0-8.0, and 20%-40% increased bioavailability. They are suitable for use in food, health products, and cosmetics, and have significant market potential.
Abstract
Description
TECHNICAL FIELD
[0001] The present application relates to the field of organic peptide salts, in particular to a preparation method and application of organic peptide salts. BACKGROUND
[0002] Organic peptide salts are salts formed by combining peptides with organic acids such as citric acid, malic acid, lactic acid, etc. They have the advantages of improving the stability, solubility and bioavailability of peptides. Currently, the preparation methods of organic peptide salts mainly include acid-base neutralization, solvent evaporation and freeze-drying, etc. However, in the prior art, the preparation of organic peptide salts mostly adopts the traditional acid-base neutralization method, which has low reaction efficiency, low product purity, and lacks precise control of peptide molecular weight distribution. In addition, the peptide raw materials used in the prior art are mostly soybean peptides, whey peptides, etc., and there is no report on the preparation of organic peptide salts using leafy grass active peptides as raw materials. The existing problems
[0003] Poor stability of leafy grass active peptides: Leafy grass active peptides are prone to degradation during storage and application, resulting in loss of biological activity.
[0004] Low solubility and bioavailability: Leafy grass active peptides have poor solubility in water and low bioavailability in the gastrointestinal tract, limiting their application in functional foods and health products.
[0005] Limitations of organic peptide salt preparation technology: The existing preparation methods of organic peptide salts have low reaction efficiency, low product purity, and lack of precise control of peptide molecular weight distribution.
[0006] Single source of raw materials: The raw materials of existing organic peptide salts are mostly soybean peptides, whey peptides, etc., and there is a lack of development of new plant peptide resources.
[0007] Therefore, the skilled in the art provides a preparation method and application of organic peptide salts to solve the problems raised in the background art. SUMMARY
[0008] The purpose of the present application is to provide a preparation method and application of organic peptide salts to solve the problems raised in the background art.
[0009] To achieve the above-mentioned purpose, the present application provides the following technical solutions:
[0010] The preparation method and application of organic peptide salts include the following steps:
[0011] Step 1), extraction of leafy grass active peptides: The leafy grass raw material is crushed, enzymatically hydrolyzed or ultrasonically assisted to obtain a crude extract of leafy grass active peptides;
[0012] Step 2), purification of the active peptide of the plant: the crude extract is subjected to fractional purification by using the ultrafiltration membrane separation technology, so as to obtain the active peptide component of the plant with the molecular weight range of 500-3000 Da;
[0013] Step 3), selection and pretreatment of the organic acid: one or more of citric acid, malic acid, lactic acid or acetic acid is selected, and is dissolved in deionized water, and the pH value is adjusted to 3.0-5.0;
[0014] Step 4), peptide-organic acid reaction: the purified active peptide of the plant is mixed with the organic acid according to the mass ratio of 1:1-1:3, and is reacted at 40-60℃ and pH 4.0-5.5 for 1-3 hours, and magnetic stirring or ultrasonic assistance is used in the reaction process to promote the uniformity of the reaction;
[0015] Step 5), separation and purification of the organic peptide salt: the reaction solution is subjected to centrifugation and filtration, and then the freeze-drying or spray-drying technology is used to obtain the organic peptide salt powder.
[0016] As a further scheme of the present application, in the step 1), the enzyme used for the enzymolysis is neutral protease, alkaline protease or complex protease, and the enzymolysis conditions are as follows: the enzymolysis temperature is 50-60℃, the enzymolysis time is 2-4 hours, the enzymolysis pH value is 7.0-8.0, and the enzyme addition amount is 1%-3% of the mass of the plant raw material.
[0017] As a further scheme of the present application, in the step 1), the ultrasonic-assisted extraction conditions are as follows: the ultrasonic power is 200-500 W, the extraction time is 20-40 minutes, the extraction temperature is 40-50℃, and the solid-liquid ratio is 1:10-1:20 (w / v).
[0018] As a further scheme of the present application, in the step 2), the ultrafiltration membrane separation technology uses the ultrafiltration membrane with the molecular weight cut-off of 1000 Da and 3000 Da, and the active peptide crude extract is subjected to fractional purification in sequence, so as to obtain the active peptide component with uniform molecular weight distribution.
[0019] As a further scheme of the present application, in the step 3), the mixture of citric acid and malic acid is selected as the organic acid, and the mass ratio of citric acid to malic acid is 1:1-1:2.
[0020] As a further scheme of the present application, in the step 4), the ultrasonic-assisted reaction is used for the peptide-organic acid reaction, the ultrasonic power is 100-300 W, the ultrasonic time is 10-30 minutes, and the interval time is 5 minutes.
[0021] As a further scheme of the present application: in the separation and purification step of the organic peptide salt, the freeze-drying technology is adopted, the freezing temperature is-40 to-60 DEG C, the vacuum degree is 10-50 Pa, and the drying time is 24-48 hours.
[0022] As a further scheme of the present application: in the separation and purification step of the organic peptide salt in step 5), the spray drying technology is adopted, the inlet temperature of the spray drying is 150-180 DEG C, the outlet temperature is 70-90 DEG C, and the spray pressure is 0.2-0.4 Mpa.
[0023] As a further scheme of the present application: the organic peptide salt prepared by the preparation method of the organic peptide salt, the solubility of the organic peptide salt is increased by 30%-50% compared with the unmodified leafy grass active peptide, the stability is significantly enhanced in the pH value range of 3.0-8.0, and the bioavailability in the simulated gastrointestinal fluid is increased by 20%-40%.
[0024] As a further scheme of the present application: the application of the organic peptide salt prepared by the preparation method of the organic peptide salt in food, health care products or cosmetics, the organic peptide salt can be used as a functional ingredient in products for antioxidant, anti-inflammatory, blood pressure reduction or immunity enhancement.
[0025] Compared with the prior art, the present application has the following beneficial effects:
[0026] The present application adopts the ultrafiltration membrane separation technology to grade and purify the leafy grass active peptide, obtains the active peptide component with uniform molecular weight distribution, and provides high-quality raw materials for subsequent reactions; the organic acid selection and reaction conditions are optimized, the yield and purity of the organic peptide salt are significantly improved by selecting specific organic acids (such as citric acid, malic acid, etc.) and optimizing the reaction conditions (such as temperature, pH value, reaction time, etc.), the ultrasonic assisted reaction is introduced, the uniformity and efficiency of the reaction are improved through the ultrasonic assisted reaction, and the stability and functionality of the organic peptide salt are further enhanced, the organic peptide salt prepared by the present application is not only suitable for the food field, but also can be widely applied to health care products and cosmetics, and has significant market potential. DETAILED DESCRIPTION
[0027] The technical solutions in the embodiments of the present application will be clearly and completely described below in combination with the embodiments of the present application. Obviously, the described embodiments are only part of the embodiments of the present application, rather than all the embodiments. Based on the embodiments in the present application, all other embodiments obtained by those skilled in the art without creative labor are within the scope of protection of the present application.
[0028] In the embodiments of the present application, the preparation method and application of the organic peptide salt include the following steps:
[0029] Step 1), extraction of active peptides from Malva sylvestris: the raw material of Malva sylvestris was crushed, enzymatically hydrolyzed or extracted with the aid of ultrasonic waves to obtain a crude extract of active peptides from Malva sylvestris;
[0030] Step 2), purification of active peptides from Malva sylvestris: the crude extract was fractionally purified by ultrafiltration membrane separation technology to obtain an active peptide component from Malva sylvestris with a molecular weight range of 500-3000 Da;
[0031] Step 3), selection and pretreatment of organic acids: one or more of citric acid, malic acid, lactic acid or acetic acid was selected and dissolved in deionized water, and the pH value was adjusted to 3.0-5.0;
[0032] Step 4), peptide-organic acid reaction: the purified active peptides from Malva sylvestris were mixed with the organic acid at a mass ratio of 1:1-1:3, and reacted at 40-60℃ and pH 4.0-5.5 for 1-3 hours, with magnetic stirring or ultrasonic assistance to promote uniformity during the reaction;
[0033] Step 5), separation and purification of organic peptide salts: the reaction solution was centrifuged and filtered, and then freeze-dried or spray-dried to obtain an organic peptide salt powder.
[0034] In this embodiment, in the extraction of active peptides from Malva sylvestris in step 1), the enzyme used for enzymatic hydrolysis is neutral protease, alkaline protease or complex protease, and the enzymatic hydrolysis conditions are as follows: enzymatic hydrolysis temperature 50-60℃, enzymatic hydrolysis time 2-4 hours, enzymatic hydrolysis pH 7.0-8.0, and enzyme addition amount 1%-3% of the mass of the Malva sylvestris raw material; the conditions for ultrasonic-assisted extraction in step 1) are as follows: ultrasonic power 200-500W, extraction time 20-40 minutes, extraction temperature 40-50℃, and solid-liquid ratio 1:10-1:20 (w / v).
[0035] In this embodiment, the ultrafiltration membrane separation technology in step 2) uses ultrafiltration membranes with a molecular weight cutoff of 1000 Da and 3000 Da to fractionally purify the crude extract of active peptides from Malva sylvestris, obtaining an active peptide component with uniform molecular weight distribution.
[0036] In this embodiment, the organic acid in step 3) is a mixture of citric acid and malic acid, and the mass ratio of citric acid to malic acid is 1:1-1:2.
[0037] In this embodiment, the peptide-organic acid reaction in step 4) uses ultrasonic-assisted reaction, with an ultrasonic power of 100-300W, an ultrasonic time of 10-30 minutes, and an ultrasonic interval time of 5 minutes.
[0038] In this embodiment, the separation and purification of the organic peptide salt in step 5) is carried out by spray drying, the inlet temperature of spray drying is 150-180℃, the outlet temperature is 70-90℃, and the spray pressure is 0.2-0.4Mpa.
[0039] In this embodiment, the separation and purification of the organic peptide salt in step 5) is carried out by spray drying, the inlet temperature of spray drying is 150-180℃, the outlet temperature is 70-90℃, and the spray pressure is 0.2-0.4Mpa.
[0040] In this embodiment, the organic peptide salt prepared by the preparation method of the organic peptide salt has a solubility 30%-50% higher than that of unmodified leafy grass active peptide, a significantly enhanced stability in a pH value range of 3.0-8.0, and a bioavailability in simulated gastrointestinal fluid increased by 20%-40%.
[0041] In this embodiment, the organic peptide salt prepared by the preparation method of the organic peptide salt is applied in food, health care products or cosmetics, and the organic peptide salt can be used as a functional ingredient in products for antioxidant, anti-inflammatory, blood pressure reduction or immune enhancement.
[0042] Example 1: Extraction of leafy grass active peptide by enzymatic method to prepare citric acid peptide salt
[0043] Step 1), raw material preparation:
[0044] Leafy grass: Fresh leafy grass leaves are washed and dried, then crushed through a 40-mesh sieve.
[0045] Enzyme preparation: neutral protease (enzyme activity ≥50,000U / g).
[0046] Organic acid: food-grade citric acid.
[0047] Step 2), extraction of leafy grass active peptide:
[0048] Mix 100g of leafy grass powder with 1000mL of deionized water, and adjust the pH value to 7.5.
[0049] Add 2g of neutral protease, and enzymatically hydrolyze at 55℃ for 3 hours, with continuous stirring during the process.
[0050] After the enzymatic hydrolysis is completed, heat the reaction solution to 90℃ for 10 minutes to inactivate the enzyme, and then cool and centrifuge (4000rpm, 20 minutes) to collect the supernatant.
[0051] Step 3), purification of leafy grass active peptide:
[0052] Pass the supernatant through an ultrafiltration membrane with a molecular weight cutoff of 3000Da to remove macromolecular impurities.
[0053] The active peptide component with a molecular weight of 1000-3000 Da was collected by using an ultrafiltration membrane with a molecular weight cut-off of 1000 Da.
[0054] The purified active peptide solution was concentrated to a solid content of 10% (w / v).
[0055] Step 4), preparation of citric acid peptide salt:
[0056] 50 g of the purified active peptide solution of Malva sylvestris was mixed with 75 g of citric acid (mass ratio 1:1.5), and the pH value was adjusted to 4.5.
[0057] The reaction was carried out at 50°C for 1.5 hours, during which magnetic stirring (speed 300 rpm) was used.
[0058] After the reaction was completed, the reaction solution was centrifuged (4000 rpm, 15 minutes), and the supernatant was collected.
[0059] Step 5), separation and drying of organic peptide salt:
[0060] The supernatant was freeze-dried under the following conditions: pre-freezing temperature -50°C, vacuum degree 20 Pa, and drying time 36 hours.
[0061] Citric acid peptide salt powder was obtained, with a yield of 85%.
[0062] Test results show that the solubility of citric acid peptide salt is increased by 40% compared with unmodified active peptide of Malva sylvestris; the stability is significantly enhanced in the pH value range of 3.0-8.0, and the activity retention rate is over 90% after 6 months of storage; the bioavailability in simulated gastrointestinal fluid is increased by 35%.
[0063] Example 2: Preparation of malic acid peptide salt from ultrasonic-assisted extraction of active peptide of Malva sylvestris
[0064] Step 1), preparation of raw materials:
[0065] Malva sylvestris: dry Malva sylvestris leaves, crushed through a 40-mesh sieve.
[0066] Organic acid: food-grade malic acid.
[0067] Step 2), extraction of active peptide of Malva sylvestris:
[0068] 100 g of Malva sylvestris powder was mixed with 1500 mL of deionized water, and the pH value was adjusted to 7.0.
[0069] Ultrasonic-assisted extraction was used under the following conditions: ultrasonic power 300 W, extraction time 30 minutes, and extraction temperature 45°C.
[0070] After the extraction was completed, centrifugation was performed (4000 rpm, 20 minutes), and the supernatant was collected.
[0071] Step 3), purification of active peptides from Malva sylvestris:
[0072] The supernatant was passed through an ultrafiltration membrane with a molecular weight cut-off of 3000 Da to remove macromolecular impurities.
[0073] The active peptide component with a molecular weight of 1000-3000 Da was collected by passing the solution through an ultrafiltration membrane with a molecular weight cut-off of 1000 Da.
[0074] The purified active peptide solution was concentrated to a solid content of 12% (w / v).
[0075] Step 4), preparation of malic peptide salt:
[0076] 60 g of purified active peptide solution from Malva sylvestris was mixed with 60 g of malic acid (mass ratio 1:1), and the pH was adjusted to 4.0.
[0077] The reaction was carried out at 40°C for 2 hours, with ultrasonic assistance (ultrasonic power 200 W, ultrasonic time 20 minutes, interval 5 minutes).
[0078] After the reaction was completed, the reaction solution was centrifuged (4000 rpm, 15 minutes), and the supernatant was collected.
[0079] Step 5), separation and drying of organic peptide salt:
[0080] The supernatant was spray-dried under the following conditions: inlet temperature 160°C, outlet temperature 80°C, and spray pressure 0.3 MPa.
[0081] Malic peptide salt powder was obtained, with a yield of 88%.
[0082] Test results showed that the solubility of malic peptide salt was increased by 35% compared to unmodified active peptides from Malva sylvestris; the stability was significantly enhanced in the pH range of 3.0-8.0, with an activity retention rate of over 85% after 6 months of storage; and the bioavailability in simulated gastrointestinal fluid was increased by 30%.
[0083] Example 3: Preparation of complex organic acid peptide salt and its application in functional food
[0084] Step 1), preparation of raw materials:
[0085] Malva sylvestris: Fresh Malva sylvestris leaves were washed and dried, then crushed through a 40-mesh sieve.
[0086] Enzyme preparation: Complex protease (enzyme activity ≥ 60,000 U / g).
[0087] Organic acid: Food-grade citric acid and lactic acid (mass ratio 1:1).
[0088] Step 2) Extraction of active peptides from S. japonica:
[0089] 100 g of S. japonica powder was mixed with 1000 mL of deionized water, and the pH value was adjusted to 7.5.
[0090] 3 g of compound protease was added, and enzymolysis was performed at 60°C for 4 hours, with continuous stirring.
[0091] After the enzymolysis was completed, the reaction solution was heated to 90°C for 10 minutes to inactivate the enzyme, and then cooled and centrifuged (4000 rpm, 20 minutes) to collect the supernatant.
[0092] Step 3) Purification of active peptides from S. japonica:
[0093] The supernatant was passed through an ultrafiltration membrane with a molecular weight cutoff of 3000 Da to remove macromolecular impurities.
[0094] The active peptide component with a molecular weight of 1000-3000 Da was collected by passing the solution through an ultrafiltration membrane with a molecular weight cutoff of 1000 Da.
[0095] The purified active peptide solution was concentrated to a solid content of 15% (w / v).
[0096] Step 4) Preparation of peptide salts of complex organic acids:
[0097] 50 g of the purified active peptide solution from S. japonica was mixed with 100 g of a mixture of citric acid and lactic acid (mass ratio 1:2), and the pH value was adjusted to 4.5.
[0098] The reaction was performed at 55°C for 2 hours, with magnetic stirring (speed 300 rpm).
[0099] After the reaction was completed, the reaction solution was centrifuged (4000 rpm, 15 minutes) to collect the supernatant.
[0100] Step 5) Separation and drying of organic peptide salts:
[0101] The supernatant was freeze-dried under the following conditions: pre-freezing temperature -50°C, vacuum degree 20 Pa, and drying time 36 hours.
[0102] The powder of peptide salts of complex organic acids was obtained, with a yield of 90%.
[0103] The prepared organic peptide salts were tested as follows:
[0104] Antioxidant activity test
[0105] Experimental method: DPPH free radical scavenging experiment and ABTS free radical scavenging experiment were used to evaluate the antioxidant activity of peptide salts of complex organic acids.
[0106] Experimental results:
[0107] DPPH radical scavenging rate: the IC50 value of the complex organic acid peptide salt was 0.25 mg / mL, significantly lower than that of the unmodified active peptide of E. japonica (IC50 value of 0.45 mg / mL).
[0108] ABTS radical scavenging rate: the IC50 value of the complex organic acid peptide salt was 0.20 mg / mL, significantly lower than that of the unmodified active peptide of E. japonica (IC50 value of 0.40 mg / mL).
[0109] Conclusion: The antioxidant activity of the complex organic acid peptide salt was increased by about 50% compared with the unmodified active peptide of E. japonica.
[0110] Immune-enhancing test
[0111] Experimental method: The mouse macrophage RAW264.7 model was used to evaluate the effect of the complex organic acid peptide salt on cellular immune activity.
[0112] Experimental steps:
[0113] RAW264.7 cells were seeded in 96-well plates and different concentrations of complex organic acid peptide salt (0.1 mg / mL, 0.5 mg / mL, 1.0 mg / mL) were added.
[0114] After 24 hours of culture, the NO (nitric oxide) content and cytokine (IL-6, TNF-α) secretion levels in the cell supernatant were detected.
[0115] Experimental results:
[0116] NO secretion: Compared with the control group, the NO secretion of the complex organic acid peptide salt treatment group was significantly increased (about 60% increase in the 0.5 mg / mL group and about 90% increase in the 1.0 mg / mL group).
[0117] Cytokine secretion: The complex organic acid peptide salt significantly increased the secretion levels of IL-6 and TNF-α (about 50% increase in the 0.5 mg / mL group and about 80% increase in the 1.0 mg / mL group).
[0118] Conclusion: The complex organic acid peptide salt can significantly enhance the immune activity of macrophages and has potential immunomodulatory function.
[0119] Application in functional beverages
[0120] Experimental method: The complex organic acid peptide salt was added to the functional beverage at an addition amount of 0.5% (w / v) and a 3-month storage test was conducted.
[0121] Experimental results:
[0122] Storage stability: The retention rate of the complex organic acid peptide salt activity in the beverage is more than 90%, and the taste has no obvious change.
[0123] Antioxidant effect: The DPPH free radical scavenging rate of the beverage is maintained at more than 85%.
[0124] Consumer test: After the sensory evaluation of 100 consumers, 90% of the consumers think that the beverage has obvious antioxidant and immune enhancing effect.
[0125] Conclusion: The complex organic acid peptide salt shows good stability and functionality in the functional beverage, and has wide application prospect.
[0126] Summary: Through detailed experimental data and result analysis, the antioxidant and immune enhancing effect of the complex organic acid peptide salt is fully verified. The specific data are as follows:
[0127] Antioxidant activity: The DPPH free radical scavenging rate (IC50 value 0.25 mg / mL) and ABTS free radical scavenging rate (IC50 value 0.20 mg / mL) are significantly better than those of the unmodified active peptide of food leaf grass.
[0128] Immune enhancing effect: In the RAW264.7 cell model, the complex organic acid peptide salt significantly improves the secretion levels of NO, IL-6 and TNF-α.
[0129] Application effect: In the functional beverage, the activity retention rate of the complex organic acid peptide salt is more than 90%, and the consumer feedback is good.
[0130] These data-based experimental results not only enhance the credibility of the patent, but also provide a scientific basis for the application of organic peptide salt in functional food, health products and cosmetics.
[0131] The application adopts ultrafiltration membrane separation technology to fractionate and purify the active peptide of food leaf grass, so as to obtain the active peptide component with uniform molecular weight distribution and provide high-quality raw materials for subsequent reaction; the selection of organic acid and reaction conditions is optimized, the yield and purity of the organic peptide salt are significantly improved by selecting specific organic acids (such as citric acid, malic acid and the like) and optimizing the reaction conditions (such as temperature, pH value, reaction time and the like), the uniformity and efficiency of the reaction are improved by ultrasonic assisted reaction, and the stability and functionality of the organic peptide salt are further enhanced. The organic peptide salt prepared by the application is not only suitable for the food field, but also can be widely applied to health products and cosmetics, and has significant market potential.
[0132] The above merely describes preferred specific embodiments of the present application, but the protection scope of the present application is not limited thereto, and any person skilled in the art, according to the technical solution and inventive concept of the present application, makes equivalent replacement or change within the technical range disclosed by the present application, which should be covered within the protection scope of the present application.
Claims
1. Process for the preparation of organic peptide salts, characterized in that: The method comprises the following steps: Step 1), extraction of active peptides from the raw material of the plant: the raw material of the plant is crushed, enzymatically hydrolyzed or extracted with the aid of ultrasonic waves to obtain a crude extract of active peptides from the plant; Step 2), purification of the active peptides from the plant: the crude extract is purified by ultrafiltration membrane separation technology to obtain an active peptide component from the plant with a molecular weight range of 500-3000 Da; Step 3), selection and pretreatment of organic acids: one or more of citric acid, malic acid, lactic acid or acetic acid is selected and dissolved in deionized water to adjust the pH value to 3.0-5.0; Step 4), peptide-organic acid reaction: the purified active peptides from the plant are mixed with the organic acid at a mass ratio of 1:1-1:3, and the mixture is reacted at 40-60°C and a pH value of 4.0-5.5 for 1-3 hours, with magnetic stirring or ultrasonic assistance being used to promote uniformity of the reaction; Step 5), separation and purification of the organic peptide salt: the reaction solution is centrifuged and filtered, and then freeze-drying or spray-drying technology is used to obtain an organic peptide salt powder.
2. The method of claim 1, wherein the organic peptide salt is prepared by: In the extraction of the active peptides from the plant in Step 1), the enzyme used for enzymatic hydrolysis is neutral protease, alkaline protease or complex protease, and the enzymatic hydrolysis conditions are as follows: an enzymatic hydrolysis temperature of 50-60°C, an enzymatic hydrolysis time of 2-4 hours, an enzymatic hydrolysis pH value of 7.0-8.0, and an enzyme addition amount of 1%-3% of the mass of the raw material of the plant.
3. The method of claim 1, wherein the organic peptide salt is prepared by: In the ultrasonic-assisted extraction in Step 1), the ultrasonic power is 200-500 W, the extraction time is 20-40 minutes, the extraction temperature is 40-50°C, and the solid-liquid ratio is 1:10-1:20 (w / v).
4. The method of claim 1, wherein the organic peptide salt is prepared by: In Step 2), the ultrafiltration membrane separation technology uses ultrafiltration membranes with a molecular weight cut-off of 1000 Da and 3000 Da to sequentially purify the crude extract of active peptides from the plant, thereby obtaining an active peptide component with a uniform molecular weight distribution.
5. The method of claim 1, wherein the organic peptide salt is prepared by: In Step 3), a mixture of citric acid and malic acid is used as the organic acid, and the mass ratio of citric acid to malic acid is 1:1-1:
2.
6. The method of claim 1, wherein the organic peptide salt is prepared by: In Step 4), ultrasonic assistance is used for the peptide-organic acid reaction, and the ultrasonic power is 100-300 W, the ultrasonic time is 10-30 minutes, and the interval time is 5 minutes.
7. The method of claim 1, wherein the organic peptide salt is prepared by: In the separation and purification of the organic peptide salt, freeze-drying technology is used, the freezing temperature is -40°C to -60°C, the vacuum degree is 10-50 Pa, and the drying time is 24-48 hours.
8. The method of claim 1, wherein the organic peptide salt is prepared by: In Step 5), spray-drying technology is used for the separation and purification of the organic peptide salt, the inlet temperature of the spray dryer is 150-180°C, the outlet temperature is 70-90°C, and the spray pressure is 0.2-0.4 MPa.
9. Organic peptide salt obtainable by the process according to any one of claims 1 to 8, characterized in that: The solubility of the organic peptide salt is increased by 30%-50% compared to that of the unmodified active peptides from the plant, the stability is significantly enhanced in a pH value range of 3.0-8.0, and the bioavailability in simulated gastrointestinal fluid is increased by 20%-40%.
10. Use of an organic peptide salt prepared according to the method of any one of claims 1 to 8 in a food, nutraceutical or cosmetic product, characterized in that: The organic peptide salt can be used as a functional ingredient in products for antioxidant, anti-inflammatory, blood pressure-lowering or immune-enhancing purposes.
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