Method for preparing meat-derived anti-inflammatory peptide and application of meat-derived anti-inflammatory peptide

Abstract

The invention relates to a method for preparing meat-derived anti-inflammatory peptide and application of the meat-derived anti-inflammatory peptide. The method comprises the following steps: preparing an enzymatic hydrolysate by taking a dry-cured meat product as a substrate, mixing the enzymatic hydrolysate with a metal ion compound, and then carrying out multi-enzyme catalysis, metal ions in the metal ion compound comprise calcium ions, magnesium ions and zinc ions in a molar ratio of (2.0-3.0): (1.0-2.0): (0.8-1.2); the dry-cured meat product contains endogenous terminal peptidase, and the protein degradation index of the dry-cured meat product is not lower than 12; and the endogenous terminal peptidase comprises alanyl aminopeptidase, arginyl aminopeptidase, leucyl aminopeptidase, dipeptidase I and dipeptidase IV. A metal ion compound required by endogenous terminal peptidase is added into the enzymatic hydrolysate of the dry-cured meat product, the enzyme activity of multi-enzyme co-catalysis is regulated and controlled, polypeptide is promoted to be subjected to enzymolysis into small peptides, the content of the anti-inflammatory peptide is increased by regulating and controlling the activity of the endogenous terminal peptidase, and the prepared meat-derived anti-inflammatory peptide is beneficial supplement for daily dietary bioactive substance intake.

Description

Technical Field

[0001] The invention relates to the field of food biotechnology, and in particular to a method for preparing meat-derived anti-inflammatory peptides and application thereof. Background Art

[0002] In recent years, health problems caused by unbalanced daily dietary nutrition structure have become increasingly prominent and have become one of the main causes affecting health. The intake of foodborne bioactive substances can compensate for the health problems caused by unbalanced dietary structure to a certain extent, and the market prospects are broad. The degree of protein degradation of dry-cured meat products is high, thus generating rich peptides and amino acids, and they are important foods rich in natural bioactive peptides. As functional fragments in proteins, bioactive peptides can only exert their biological activity after being released. The biological activity of peptides depends on the amino acid composition and spatial arrangement, and the formation and accumulation of peptides are closely related to the cleavage sites of endogenous proteases. In muscle endogenous proteases, terminal peptidases such as dipeptidases and aminopeptidases act on the terminal peptide bonds of peptide chains, selectively hydrolyze peptides composed of amino acids at specific sites or specific side chains, and form small peptides or free amino acids. However, the formation of active peptides in dry-cured meat products is a complex biocatalytic process, which is difficult to achieve directional regulation. How to achieve directional regulation and enrichment of bioactive peptides is a key technology for improving meat processing and nutritional health attributes.

[0003] At present, researchers mostly use heat treatment, high voltage field, microwave, ultrasound or electrical stimulation to change the interaction, structure and hydrophobicity of protein molecules, thereby affecting the hydrolysis and release of polypeptides. The biological activity of polypeptides is closely related to the composition of terminal amino acids. Among terminal peptidases, dipeptidases and aminopeptidases are metalloenzymes, and their activity is regulated by metal ions. However, there are few reports on methods for preparing food-derived bioactive peptides by regulating endogenous enzyme activity, especially terminal peptidases, without exogenous addition of protease hydrolysis. Bioactive peptides are a class of polypeptides that play important physiological roles, including antioxidant, anti-inflammatory, cholesterol-lowering, blood pressure-lowering, anti-cardiovascular sclerosis, and immune regulation. Studies have reported that platelet-activating factor acetylhydrolase (PAFAH) is a clinical research marker for many inflammatory diseases. For example, angiography shows that PAFAH is significantly increased in patients with coronary artery disease, which is a predictive indicator of coronary heart disease and can indicate the risk of atherosclerosis. Therefore, PAFAH inhibitory activity is one of the evaluation indicators of anti-inflammatory effects. Currently, there have been many reports on the research of food-derived bioactive peptides focusing on anti-oxidation, lowering blood pressure, etc., and the research on anti-inflammatory biological activity urgently needs in-depth study. Summary of the invention

[0004] In order to solve the above technical problems, the present invention provides a method for preparing meat-derived anti-inflammatory peptides and application thereof.

[0005] In a first aspect, the present invention provides a method for preparing meat-derived anti-inflammatory peptides, comprising: preparing an enzymatic hydrolysate using a dry-cured meat product as a substrate, mixing the enzymatic hydrolysate with a metal ion complex, and then performing multi-enzyme catalysis; the metal ions in the metal ion complex include calcium ions, magnesium ions and zinc ions in a molar ratio of (2.0-3.0): (1.0-2.0): (0.8-1.2); the dry-cured meat product contains endogenous terminal peptidase, and the protein degradation index of the dry-cured meat product is not less than 12; the endogenous terminal peptidase includes alanyl aminopeptidase, arginyl aminopeptidase, leucyl aminopeptidase, dipeptidase I and dipeptidase IV.

[0006] The present invention prepares an enzymatic solution from a dry-cured meat product containing endogenous terminal peptidases (alanyl aminopeptidase, arginyl aminopeptidase, leucyl aminopeptidase, dipeptidase I and dipeptidase IV), adds a metal ion complex required by the endogenous terminal peptidase to the solution, and regulates the enzyme activity of multi-enzyme co-catalysis, thereby promoting further enzymatic hydrolysis of polypeptides into small peptides, and preparing meat-derived anti-inflammatory peptides. Many inflammatory diseases are related to changes in the activity of PAFAH. PAFAH can be used as a clinical research marker for many inflammatory diseases, and PAFAH activity inhibition is an important evaluation indicator of anti-inflammatory effects. The present invention can effectively increase the content of anti-inflammatory peptides and improve the inhibitory effect of PAFAH by regulating the activity of terminal peptidases. The meat-derived anti-inflammatory peptides prepared by the present invention are a beneficial supplement to the intake of daily dietary bioactive substances.

[0007] Preferably, the metal ions in the metal ion complex are calcium ions, magnesium ions and zinc ions in a molar ratio of (2.0-2.8): (1.0-1.8): (0.8-1.0). By adopting an optimized ratio, the activity of dipeptidase and aminopeptidase can be better promoted, thereby making the small peptide enrichment effect better. After tests including PAFAH inhibitory activity, when the metal ion complex adopts a preferred ratio of calcium ions, magnesium ions and zinc ions, the anti-inflammatory activity can be further greatly improved.

[0008] Preferably, the metal ion complex consists of calcium chloride, magnesium chloride and zinc chloride.

[0009] More preferably, the molar ratio of calcium ion, magnesium ion and zinc ion is (2.0-2.5):1.0:(0.8-1.0). The synergistic effect of specific metal ions in the preferred ratio has a better comprehensive effect. More preferably, it is 2.0:1.0:0.8.

[0010] Further preferably, in the enzyme catalytic system after the enzymatic hydrolysate and the metal ion complex are mixed, the total concentration of the metal ion complex is 2-10 mM (based on the multi-enzyme catalytic reaction system, the solvent is the buffer solution).

[0011] Further preferably, in the enzymatic hydrolyzate, the concentrations of calcium ions, magnesium ions and zinc ions are 3-9 mM, for example, 3 mM, 4 mM, 5 mM, 6 mM, 7 mM, 8 mM, etc. and any values ​​therebetween.

[0012] Preferably, the preparation of the enzymatic hydrolysate comprises: removing fat and fascia from the dry-cured meat product, mixing the obtained muscle tissue of the dry-cured meat product with a phosphate buffer solution and then crushing at high speed.

[0013] Further preferably, the mass volume ratio of the dry-cured meat product muscle tissue to the phosphate buffer solution is (30-80): (615-630) g / mL, and the pH of the phosphate buffer solution is 5.5-6.0; and / or the temperature of the high-speed mashing is 0-5°C and the rotation speed is 3500-7500 r / min.

[0014] Further preferably, the present invention prepares the enzymatic hydrolysate after the dry-cured meat product is pounded at low temperature and high speed; preferably, the homogenization is performed at 0-4°C at a speed of 6000-9000 r / min for 30±5s, 2-3 times, and each time interval is 30±5s. The present invention better maintains the activity of endogenous enzymes by preparing under low temperature conditions.

[0015] Preferably, the multi-enzyme catalysis temperature is 45-55°C, the pH is 5.5-6.0, and the time is 6-12h.

[0016] It is further preferred that the protein degradation index of the dry-cured meat product is 12-31; and / or the dry-cured meat product is a scrap in the process of trimming dry-cured meat products; and / or the dry-cured meat product includes dry-cured pork neck. In the present invention, the terminal peptidase in the scraps in the process of trimming the dry-cured meat product has residual enzyme activity, and the present invention does not limit the specific size of the enzyme activity. In the preparation process of the meat-derived anti-inflammatory peptide provided by the present invention, the multi-enzyme catalysis used in the processing process is regulated by the above-mentioned regulation method, and the protein degradation index of the scraps of the dry-cured meat product is preferably 12-31. For example, the protein degradation index is 12, 15, 18, 31, etc. and any value therebetween. In the present invention, dry-cured meat products include but are not limited to dry-cured pork neck.

[0017] Preferably, the multi-enzyme is a terminal peptidase; the terminal peptidase includes an aminopeptidase and / or a dipeptidase.

[0018] Further preferably, the terminal peptidase is from one or more of alanyl aminopeptidase (AAPep), arginyl aminopeptidase (RAPep), leucyl aminopeptidase (LAPep), dipeptidase I (Dipep I), dipeptidase IV (Dipep IV); preferably, the terminal peptidase includes alanyl aminopeptidase, arginyl aminopeptidase, leucyl aminopeptidase, dipeptidase I and dipeptidase IV.

[0019] The present invention found that among the endogenous terminal peptidases, arginine aminopeptidase (RAPep), alanyl aminopeptidase (AAPep), leucyl aminopeptidase (LAPep), dipeptidase I (Dipep I) and dipeptidase IV (Dipep IV) maintained good catalytic activity, which helped to promote the hydrolysis of the terminal amino acids and dipeptides of polypeptides, and further regulated the amino acid composition and spatial structure of polypeptides by changing the terminal amino acid composition of polypeptides, thereby improving the biological activity of polypeptides.

[0020] In the present invention, the regulation method adopts raw material preparation and pretreatment, collects the scraps in the process of finishing dry-cured meat products, prepares an enzymatic solution after low-temperature and high-speed crushing, adds the metal ion complex required by the endogenous terminal peptidase to the enzymatic solution, and then carries out multi-enzyme co-catalysis, regulates the enzyme activity of multiple enzymes, regulates the multi-enzyme co-catalysis process, thereby promoting the further enzymatic hydrolysis of polypeptides into small peptides, and preparing meat-derived (bioactive) anti-inflammatory peptides.

[0021] Preferably, the method further comprises the steps of separating and purifying the enzymatic hydrolysate and collecting components with a molecular weight of 500-1500Da; preferably, the small peptides obtained by multi-enzyme catalysis are separated and purified by ultrafiltration, gel chromatography, etc., and components with a molecular weight of 500-1500Da are collected. In the present invention, the meat-derived anti-inflammatory peptide prepared by regulating multi-enzyme co-catalysis is a component with a molecular weight of 500-1500Da, which has good anti-inflammatory activity, namely, platelet activating factor acetylhydrolase (PAFAH) inhibitory activity.

[0022] In a second aspect, the present invention provides a meat-derived anti-inflammatory peptide prepared by the above-mentioned method for preparing a meat-derived anti-inflammatory peptide; preferably, the meat-derived anti-inflammatory peptide is a dry-cured meat-derived bioactive peptide.

[0023] In a third aspect, the present invention provides a method for preparing the above-mentioned meat-derived anti-inflammatory peptide or the use of the above-mentioned meat-derived anti-inflammatory peptide in preparing food containing food-derived anti-inflammatory peptide.

[0024] The beneficial effect of the present invention is at least that: the present invention innovatively uses a specific metal ion complex and catalytic environment regulation to improve the endogenous terminal peptidase activity, and further promotes the directional enrichment of small peptides in dry-cured meat products. The method for preparing meat-derived biological anti-inflammatory peptides by multi-enzyme co-catalysis provided by the present invention can effectively improve the biological activity and nutritional characteristics of the leftover materials of dry-cured meat production, and is a beneficial supplement to food-derived biologically active substances. BRIEF DESCRIPTION OF THE DRAWINGS

[0025] In order to more clearly illustrate the technical solutions in the present invention or the prior art, the following briefly introduces the drawings required for use in the embodiments or the description of the prior art. Obviously, the drawings described below are some embodiments of the present invention. For ordinary technicians in this field, other drawings can be obtained based on these drawings without paying creative work.

[0026] Figure 1 The enzyme activity of the terminal peptidase in the regulated polypeptide sample provided in the embodiment of the present invention.

[0027] Figure 2 The peptide content in the regulated polypeptide sample provided in the embodiment of the present invention.

[0028] Figure 3 The total free amino acids in the regulated polypeptide sample provided in the embodiment of the present invention.

[0029] Figure 4 This is a comparison chart of the anti-inflammatory activities of components with different molecular weights provided in Example 1 of the present invention.

[0030] Figure 5 This is the anti-inflammatory activity of the regulated polypeptide sample provided in the embodiments of the present invention. DETAILED DESCRIPTION

[0031] In order to make the purpose, technical solution and advantages of the present invention clearer, the technical solution of the present invention will be described clearly and completely below. Obviously, the described embodiments are part of the embodiments of the present invention, not all of the embodiments. Based on the embodiments of the present invention, all other embodiments obtained by ordinary technicians in this field without creative work are within the scope of protection of the present invention.

[0032] The endpoints and any values ​​of the ranges disclosed in the present invention are not limited to the precise ranges or values, and these ranges or values ​​should be understood to include values ​​close to these ranges or values. For numerical ranges, the endpoint values ​​of each range, the endpoint values ​​of each range and the individual point values, and the individual point values ​​can be combined with each other to obtain one or more new numerical ranges, which should be regarded as specifically disclosed in the present invention.

[0033] If no specific technology or conditions are specified in the examples of the present invention, the technology or conditions described in the literature in the field or the product instructions are used. If the manufacturer of the devices, instruments, reagents, etc. is not specified, they are all conventional products that can be purchased through regular channels. The experimental reagents and raw materials involved are all commercially available, and the reagents are all analytically pure products.

[0034] Example 1 This example uses a method for regulating multi-enzyme co-catalysis to prepare meat-derived anti-inflammatory peptides, as follows: The metal ion complex is composed of calcium chloride, magnesium chloride and zinc chloride in a molar ratio of 2.0:1.0:0.8. The molar concentration of the metal ion complex in the enzyme catalysis system is 5 mM. The incubation temperature is 45° C. and the pH is 5.5.

[0035] The leftovers of dry cured meat products were selected to prepare polypeptide hydrolysates, and the endogenous terminal peptidases including alanyl aminopeptidase, arginyl aminopeptidase, leucyl aminopeptidase, dipeptidase I and dipeptidase IV had residual enzyme activities, and the protein degradation index was 14.

[0036] The multi-enzyme catalytic regulation and preparation technology provided in this embodiment includes the following process: 1) Collect the trimmings of dry-cured meat products (dry-cured pork neck meat), remove fat and fascia, mince and weigh 50 g of muscle, add 625 mL of phosphate buffer solution (pH 5.5), and use a high-speed tissue pounder at 6000 r / min at 4 °C for 30 s each time, 3 times, with 30 s interval in between, to prepare the enzymatic hydrolyzate.

[0037] 2) Add the metal ion complex required by endogenous terminal peptidase to the enzymatic hydrolysis solution. The incubation temperature for terminal peptidase multi-enzyme co-catalyzed polypeptide hydrolysis is 45°C, pH 5.5, magnetic stirring is 150 r / min, and the incubation time is 8 h.

[0038] The activities of various terminal peptidases, including AAPep, RAPep, LAPep, Dipep I and Dipep IV, were measured in the peptide hydrolysate samples. The determination method was based on the method described by Wang et al. (Elucidation of potential relationshipbetween endogenous proteases and key flavor substances in dry-cured porkcoppa. Food Science and Human Wellness, 2024). The activity of terminal peptidase was determined as follows: 25 mL of enzymatic hydrolysate was centrifuged (20000×g, 20min) and the supernatant was taken to 25 mL for use as terminal peptidase extract.

[0039] The reaction solution system for the determination of aminopeptidase activity is a phosphate buffer containing fluorescent substrate (containing 0.33% of 30% Brij-35, 1mM DTT), including AAPep (pH 7.0, 5mM CaCl2, 250μM Ala-AMC), RAPep (pH 6.5, 150mM NaCl, 250μM Arg-AMC), and LAPep (pH 6.5, 5mM MgCl2, 250μM Leu-AMC). The determination conditions are as follows: take 25μL of enzyme extract (when determining RAPep, add 10μL of 1mM E-64), add 125μL of reaction solution, incubate at 37℃ for 30min, add 500μL of anhydrous ethanol to terminate the reaction, centrifuge (10000×g, 10min), take the supernatant and place it in a microplate reader to measure the fluorescence value (fluorescence excitation wavelength is 360nm, emission wavelength is 440nm).

[0040] The reaction solution systems for dipeptidase activity assay are: Dipep I reaction solution is pH 6.0 citric acid buffer, containing 0.5mM DTT and 0.5mM Gly-Arg-AMC; Dipep IV reaction solution is pH 8.0 Tris-HCl buffer, containing 0.5mM DTT, 0.25mM Gly-Pro-AMC. The assay conditions are: take 25μL enzyme extract, add 125μL reaction solution, incubate at 37℃ for 20min, add 500μL anhydrous ethanol to terminate the reaction, centrifuge (10000×g, 10min), take the supernatant and place it in a microplate reader to measure the fluorescence value (fluorescence excitation wavelength is 380nm, emission wavelength is 440nm).

[0041] The activity unit (U) of telopeptidase was defined as the amount of enzyme required to generate 1 μmol AMC per gram of protein per minute at 37°C.

[0042] 3) In the peptide separation and purification process, add phosphate extract (0.02M, 4-5 times volume) to the enzymatic hydrolyzate to extract crude peptides, centrifuge (12000×g, 30min) to collect the supernatant, then add anhydrous ethanol (3-5 times volume) for protein precipitation, let stand overnight and centrifuge to collect the filtrate. The filtrate was concentrated by rotary evaporator, then separated by ultrafiltration tube (3kDa), and the components with molecular weight less than 3kDa were collected for freeze-drying. The freeze-dried sample was further separated by dextran chromatography (Sephadex G-15, ultrapure water elution, flow rate of 1mL / min, A220nm), and the components with molecular weight of 500-1500Da were collected and freeze-dried.

[0043] Peptide content, total free amino acid content, and anti-inflammatory activity were determined.

[0044] Example 2 The present embodiment provides a meat-derived anti-inflammatory peptide prepared by regulating multi-enzyme co-catalysis and a method thereof, using the same method as Example 1, except that the metal ion complex is composed of calcium chloride, magnesium chloride, and zinc chloride, with a molar ratio of 3.0:1.0:1.0 and a molar concentration of 5 mM.

[0045] Example 3 The present embodiment provides a meat-derived anti-inflammatory peptide prepared by regulating multi-enzyme co-catalysis and a method thereof, using the same method as Example 1, except that the metal ion complex is composed of calcium chloride, magnesium chloride, and zinc chloride, with a molar ratio of 4.0:1.0:1.2 and a molar concentration of 5 mM.

[0046] Example 4 The present embodiment provides a meat-derived anti-inflammatory peptide prepared by regulating multi-enzyme co-catalysis and a method thereof. The method is the same as the method in Example 1, except that the metal ion complex is composed of calcium chloride, magnesium chloride, zinc chloride, and sodium chloride, the molar ratio of which is 2:1:1:2, and the molar concentration is 5 mM.

[0047] Comparative Example 1 This comparative example provides a meat-derived bioactive peptide prepared by regulating multi-enzyme co-catalysis and a method thereof, the method is the same as the method in Example 1, the difference being that no metal ion complex is used and 100% calcium chloride is used.

[0048] Comparative Example 2 This comparative example provides a meat-derived bioactive peptide prepared by regulating multi-enzyme co-catalysis and a method thereof, the method is the same as the method in Example 1, except that no metal ion complex is used, and 100% zinc chloride is used.

[0049] Comparative Example 3 This comparative example provides a meat-derived bioactive peptide prepared by regulating multi-enzyme co-catalysis and a method thereof, the method is the same as the method in Example 1, the difference being that no metal ion complex is used and 100% sodium chloride is used.

[0050] Comparative Example 4 This comparative example provides a meat-derived bioactive peptide prepared by regulating multi-enzyme co-catalysis and a method thereof, the method is the same as the method in Example 1, except that the metal ion complex uses magnesium chloride and zinc chloride in a molar ratio of 1.0:2.0.

[0051] Comparative Example 5 This comparative example provides a meat-derived bioactive peptide prepared by regulating multi-enzyme co-catalysis and a method thereof, the method is the same as the method in Example 1, except that no metal ion complex is added in step 2).

[0052] Experimental Example 1 This experimental example provides enzyme activity analysis and comparison of the terminal peptidase regulation methods of each embodiment and each comparative example, including AAPep, RAPep, LAPep, Dipep I and Dipep IV. The test method of this experimental example is specifically described in the enzyme activity determination method described in Example 1.

[0053] The changes of enzyme activities among different groups Figure 1 As shown, the activities of AAPep and Dipep I in the terminal peptidases of Examples 1-3 are significantly better than the activities of the two enzymes in the comparative example.

[0054] Experimental Example 2 In this experimental example, the polypeptide content and free amino acid content of the polypeptide enzymatic hydrolysis degree of the embodiment and the comparative example were analyzed and compared, and the determination method was referred to the method described in the literature Zhang et al. (Purification and identification ofantioxidative peptides from dry-cured Xuanwei ham. Food Chemistry, 2016).

[0055] The peptide content and free fatty acid content are key indicators for evaluating the further hydrolysis of the peptide. The changes in peptide extraction rate, peptide content, and free amino acid content of different examples and comparative examples are shown in Figure 2. Figure 2-3 As shown, compared with the results of Comparative Examples 1-5, the peptide extraction rate, polypeptide content, and the content of free amino acids generated in Examples 1-4 are higher. Combined with the changes in the terminal peptidase activity of Examples 1-4, the results show that the polypeptides in the samples prepared in Examples 1-4 are further hydrolyzed by terminal peptidase, releasing more small peptides and free amino acids, thereby promoting further enrichment of small peptides.

[0056] Experimental Example 3 This experimental example analyzes and compares the anti-inflammatory effects of polypeptides of different molecular weight components in Example 1, and the enzymatic hydrolyzed polypeptide samples of Examples 1-4 and Comparative Examples 1-5, and the PAFAH kit (Cayman Chemical Company) is used for determination.

[0057] PAFAH activity is associated with many inflammatory diseases and is a research marker for many inflammatory diseases. For example, PAFAH activity changes in the plasma of patients with inflammatory diseases. Therefore, the PAFAH inhibition rate is an important indicator for evaluating the anti-inflammatory effect of bioactive peptides, that is, the PAFAH inhibition rate is positively correlated with the anti-inflammatory effect of bioactive peptides. Figure 4The results shown in the figure show that the anti-inflammatory effects of polypeptide components with different molecular weights are significantly different. Components with molecular weights > 3kDa do not show anti-inflammatory effects, while components with molecular weights < 3kDa begin to show certain anti-inflammatory effects. In contrast, components with molecular weights between 500-1500Da have the best anti-inflammatory effects. Furthermore, Figure 5 The results show that the PAFAH inhibition rate of the embodiment of the present invention is significantly improved, that is, the anti-inflammatory effect of the small peptide is improved, indicating that by regulating the activity of the terminal peptidase, the anti-inflammatory effect of the small peptide produced after the enzymatic hydrolysis sample is better. Figure 1-5 The test results show that the embodiments of the present invention achieve excellent comprehensive effects, with embodiment 1 having the best effect.

[0058] Finally, it should be noted that the above embodiments are only used to illustrate the technical solutions of the present invention, rather than to limit it. Although the present invention has been described in detail with reference to the aforementioned embodiments, those skilled in the art should understand that they can still modify the technical solutions described in the aforementioned embodiments, or make equivalent replacements for some of the technical features therein. However, these modifications or replacements do not deviate the essence of the corresponding technical solutions from the spirit and scope of the technical solutions of the embodiments of the present invention.

Claims

1. A method for preparing meat-derived anti-inflammatory peptides, characterized in that: include: The enzymatic hydrolysate is prepared by using the dry cured meat product as a substrate, the enzymatic hydrolysate is mixed with a metal ion complex, and then multi-enzyme catalysis is performed; The metal ions in the metal ion complex include calcium ions, magnesium ions and zinc ions in a molar ratio of (2.0-3.0): (1.0-2.0): (0.8-1.2); the dry-cured meat product contains endogenous terminal peptidase, and the protein degradation index of the dry-cured meat product is not less than 12; the endogenous terminal peptidase includes alanyl aminopeptidase, arginyl aminopeptidase, leucyl aminopeptidase, dipeptidase I and dipeptidase IV.

2. The method for preparing meat-derived anti-inflammatory peptides according to claim 1, characterized in that: The molar ratio of the calcium ion, the magnesium ion and the zinc ion is (2.0-2.8): (1.0-1.8): (0.8-1.0); and / or the metal ion complex consists of calcium chloride, magnesium chloride and zinc chloride.

3. The method for preparing meat-derived anti-inflammatory peptides according to claim 2, characterized in that: In the enzyme catalysis system after the enzymatic hydrolysate and the metal ion complex are mixed, the total concentration of the metal ion complex is 2-10 mM.

4. The method for preparing meat-derived anti-inflammatory peptides according to claim 1, characterized in that: The preparation of the enzymatic hydrolysate comprises: removing fat and fascia from the dry-cured meat product, mixing the obtained muscle tissue of the dry-cured meat product with a phosphate buffer solution, and then pounding the mixture at a high speed.

5. The method for preparing meat-derived anti-inflammatory peptides according to claim 4, characterized in that: The mass volume ratio of the dry-cured meat product muscle tissue to the phosphate buffer solution is (30-80): (615-630) g / mL, and the pH of the phosphate buffer solution is 5.5-6.0; and / or the temperature of the high-speed mashing is 0-5° C., and the rotation speed is 3500-7500 r / min.

6. The method for preparing meat-derived anti-inflammatory peptides according to claim 1, characterized in that: The multi-enzyme catalysis is carried out at a temperature of 45-55° C., a pH of 5.5-6.0, and a time of 6-12 hours.

7. The method for preparing meat-derived anti-inflammatory peptides according to claim 1, characterized in that: The protein degradation index of the dry-cured meat product is 12-31; and / or the dry-cured meat product is a leftover from the trimming process of dry-cured meat products; and / or the dry-cured meat product comprises dry-cured pork neck.

8. The method for preparing meat-derived anti-inflammatory peptides according to any one of claims 1 to 7, characterized in that: The method also includes the steps of separating and purifying the enzymatic hydrolysis products and collecting components with a molecular weight of 500-1500Da.

9. A meat-derived anti-inflammatory peptide, characterized in that: The meat-derived anti-inflammatory peptide is prepared by the method for preparing the meat-derived anti-inflammatory peptide according to any one of claims 1 to 8.

10. The method for preparing a meat-derived anti-inflammatory peptide according to any one of claims 1 to 8 or use of the meat-derived anti-inflammatory peptide according to claim 9 in preparing a food containing a food-derived anti-inflammatory peptide.

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