Method for improving gel property of mutton myofibrillar protein under low-salt condition

Abstract

The invention relates to the technical field of meat product processing, in particular to a method for improving the gel property of mutton myofibrillar protein under a low-salt condition. The invention provides a method for improving mutton myofibrillar protein gel characteristics. The method sequentially comprises the following steps: soaking Tan mutton with purified water, extracting myofibrillar protein with a phosphate buffer solution, adjusting the protein concentration with a protein dilution buffer solution, standing in a magnetic field environment, and heating to induce gel. The Tan mutton myofibrillar protein gel treated by the method disclosed by the invention has better gel strength and water-retaining property, can effectively improve the quality of low-salt mutton products, realizes reduction of texture characteristics of high-quality mutton outside an original place, and has a good application prospect.

Description

Technical Field

[0001] The invention relates to the technical field of meat product processing, in particular to a method for improving the gel properties of mutton myofibrillar protein under low-salt conditions. Background Art

[0002] Tan sheep is a special breed of sheep in Yanchi County, Ningxia Hui Autonomous Region, my country. Tan sheep meat is tender and fresh in taste. Products such as hand-pulled mutton, mutton sauce, and mutton pie processed from Tan sheep meat have been widely loved by consumers.

[0003] As an important ingredient in meat processing, salt has an impact on the texture characteristics of meat products. Sodium chloride in salt can promote the dissolution and cross-linking of mutton myofibrillar protein, thereby forming a stable gel state, improving the water retention of the product, and improving the taste of the product. However, excessive intake of salt will increase the risk of cardiovascular and cerebrovascular diseases, hypertension and other diseases in the human body, and has important potential risks to the health of consumers. Under low-salt conditions, the dissolution of mutton myofibrillar protein and the formation of gel network structure will be inhibited, affecting the properties of mutton myofibrillar protein gel, resulting in product texture deterioration, and then affecting the taste of the product. Therefore, how to solve the problem of texture deterioration and instability of mutton products under low-salt conditions has become a difficult problem that needs to be solved urgently in industrial development. The present invention aims to solve the problem of protein gel properties deterioration and instability caused by reducing the amount of salt added during the processing of low-salt mutton products, and provide a method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, improve the texture characteristics of low-salt mutton products, and be used for product research and development and production. Summary of the invention

[0004] The purpose of the present invention is to provide a method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, so as to solve the problem of deterioration and instability of the gel properties of mutton products under low-salt conditions, achieve the improvement of the gel properties and texture quality of low-salt mutton products, and has broad application prospects.

[0005] Specifically, the technical solution of the present invention is as follows: In a first aspect, the present invention provides a method for improving the gel properties of mutton myofibrillar protein, comprising the steps of soaking mutton in purified water, extracting myofibrillar protein using a phosphate buffer solution, adjusting the protein concentration using a protein dilution buffer, and standing and heating in a magnetic field environment to induce gel; wherein the phosphate buffer solution is composed of the following raw materials in mass fractions: 1000 parts of water, 4-8 parts of NaCl, 5-7 parts of disodium hydrogen phosphate, 0.4-0.7 parts of sodium dihydrogen phosphate, and 0.0004-0.005 parts of strontium chloride.

[0006] Preferably, the amount of the phosphate buffer solution added is 4-8 times the mass of the mutton after soaking.

[0007] Preferably, the phosphate buffer solution is composed of the following raw materials in mass fraction: 1000 parts of water, 5-6 parts of NaCl, 5.5-6.5 parts of disodium hydrogen phosphate and 0.5-0.6 parts of sodium dihydrogen phosphate, and 0.001-0.002 parts of strontium chloride; the amount of the phosphate buffer solution added is 5-6 times the mass of the soaked mutton.

[0008] Preferably, the protein dilution buffer is composed of the following raw materials by mass: 1000 parts of water, 30-45 parts of NaCl, 5-7 parts of disodium hydrogen phosphate and 0.4-0.7 parts of sodium dihydrogen phosphate, 0.0004-0.005 parts of strontium chloride, and 0.0002-0.001 parts of zinc chloride.

[0009] Preferably, the protein concentration is adjusted to 30-50 mg / mL using protein dilution buffer.

[0010] Preferably, the protein dilution buffer is composed of the following raw materials by mass: 1000 parts of water, 34-38 parts of NaCl, 5.5-6.5 parts of disodium hydrogen phosphate and 0.5-0.6 parts of sodium dihydrogen phosphate, 0.001-0.002 parts of strontium chloride, and 0.0005-0.0008 parts of zinc chloride; the protein dilution buffer is used to adjust the protein concentration to 40-45 mg / mL.

[0011] Preferably, the total organic carbon of the purified water does not exceed 0.50 mg / L, the ammonia does not exceed 0.00003%, the conductivity does not exceed 3.6 μs / cm at 10°C, does not exceed 4.3 μs / cm at 20°C, and does not exceed 5.1 μs / cm at 25°C.

[0012] Preferably, the time for soaking the mutton in purified water is 12-48 hours, the temperature is 0-4°C, and the water is changed every 6-8 hours.

[0013] Preferably, the amount of purified water added is 1-3 times the mass of the beach mutton.

[0014] Preferably, the magnetic field strength is 1-5 mT, the temperature in the magnetic field is 0-4° C., and the time is 0.5-2 h.

[0015] Preferably, the method of heating to induce gelation comprises: increasing the temperature gradually from 25 to 85°C at a heating rate of 1±0.2°C / min, keeping the temperature for 10±2min, rapidly cooling to room temperature in an ice water bath, and standing at 4±2°C for 6-24h.

[0016] In a second aspect, the present invention provides the use of the aforementioned method for improving the gel properties of mutton myofibrillar protein in improving the gel properties of mutton myofibrillar protein under low-salt conditions, wherein the low-salt conditions refer to a sodium chloride concentration lower than 0.4 mol / L.

[0017] Beneficial effects: The present invention provides a method for improving the gel properties of mutton myofibrillar protein, which comprises the steps of soaking mutton in purified water, extracting myofibrillar protein using a phosphate buffer solution, adjusting the protein concentration using a protein dilution buffer, and standing and heating in a magnetic field environment to induce gelation. The mutton myofibrillar protein gel treated by the method of the present invention has better gel strength and water retention, can effectively improve the quality of low-salt mutton products, and realize the restoration of high-quality mutton texture characteristics outside the place of origin, and has good application prospects. DETAILED DESCRIPTION

[0018] The present invention provides a processing method for improving the gel properties of mutton myofibrillar protein under low-salt conditions. Specifically, myofibrillar protein is extracted from beach mutton in Yanchi County, Ningxia as raw material, and the gel properties of beach mutton myofibrillar protein under low-salt conditions are improved through soaking treatment, extraction optimization and magnetic field treatment, thereby achieving the restoration of the texture properties of high-quality mutton outside the place of origin.

[0019] In a more specific embodiment provided by the present invention, the processing method comprises the following steps: (1) Soak the mutton in purified water; (2) Extract myofibrillar protein using phosphate buffer solution and adjust the protein concentration to between 30-50 mg / mL using protein dilution buffer; (3) Standing in a magnetic field environment; (4) Heat to prepare thermally induced gel.

[0020] Preferably, in the above method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the requirements for the purified water are: total organic carbon not exceeding 0.50 mg / L, ammonia not exceeding 0.00003%, conductivity not exceeding 3.6 μs / cm at 10°C, not exceeding 4.3 μs / cm at 20°C, and not exceeding 5.1 μs / cm at 25°C.

[0021] Preferably, in the above method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the soaking time in step (1) is 12-48 hours, the soaking temperature is 0-4°C, and the water is changed every 6-8 hours.

[0022] Preferably, the amount of purified water added is 1-3 times the mass of the Tan mutton.

[0023] The present invention uses purified water to solve the problem of metal ions in ordinary tap water migrating into the meat during the soaking process, thereby causing changes in the quality of mutton, and solves the problem of differences in product quality caused by differences in water quality in different regions, which is conducive to the standardization and promotion of the method.

[0024] Further preferably, in the above-mentioned method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the temperature of the purified water immersion is 0-4°C, the time is 12-24h, the water is changed 3-4 times, and the amount of purified water added is 1.5-2 times the mass of the blanched mutton.

[0025] Preferably, in the above-mentioned method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the phosphate buffer solution contains, by mass, 1000 parts of water, 4-8 parts of NaCl, 5-7 parts of disodium hydrogen phosphate and 0.4-0.7 parts of sodium dihydrogen phosphate, and 0.0004-0.005 parts of strontium chloride.

[0026] Preferably, the amount of the phosphate buffer solution added is 4-8 times the mass of the mutton after soaking.

[0027] Further preferably, in the above-mentioned method for improving the gel properties of mutton myofibrillar protein under low salt conditions, the phosphate buffer solution comprises 1000 parts of water, 5-6 parts of NaCl, 5.5-6.5 parts of disodium hydrogen phosphate and 0.5-0.6 parts of sodium dihydrogen phosphate, and 0.001-0.002 parts of strontium chloride, by mass, so that the pH value of the buffer solution reaches 7.0-7.5, thereby being away from the isoelectric point of myofibrillar protein, preventing the aggregation of myofibrillar protein, and at the same time, strontium ions can be ionically bonded with myofibrillar protein, changing the secondary and tertiary structures of myofibrillar protein, increasing the solubility and stability of the protein, and promoting the stability of the myofibrillar protein gel structure. The amount of the phosphate buffer solution added is 5-6 times the mass of the soaked mutton.

[0028] Preferably, in the above-mentioned method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the protein dilution buffer in step (2) contains, by weight, 1000 parts of water, 30-45 parts of NaCl, 5-7 parts of disodium hydrogen phosphate and 0.4-0.7 parts of sodium dihydrogen phosphate, 0.0004-0.005 parts of strontium chloride, and 0.0002-0.001 parts of zinc chloride.

[0029] Further preferably, in the above-mentioned method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the protein dilution buffer in step (2) contains, by weight, 1000 parts of water, 34-38 parts of NaCl, 5.5-6.5 parts of disodium hydrogen phosphate and 0.5-0.6 parts of sodium dihydrogen phosphate, 0.001-0.002 parts of strontium chloride, and 0.0005-0.0008 parts of zinc chloride.

[0030] In a more specific embodiment provided by the present invention, step (2) comprises: removing fat and connective tissue from the hind leg of lamb, blending, adding 5±1 times the volume of phosphate buffer solution, homogenizing at high speed in an ice water bath, homogenizing at 12000±1000 r / min for 1min±20s, centrifuging at 5000±500 g for 10±2 min at 4±2°C, discarding the supernatant, taking the precipitate, repeating the above operation 4±1 times, filtering the homogenate through four layers of gauze for the last time and centrifuging, and the obtained white precipitate is myofibrillar protein. The protein concentration is adjusted to 40±5 mg / mL using protein dilution buffer.

[0031] On the basis of the above-mentioned use of purified water soaking, buffer solution extraction and protein dilution buffer to adjust the protein concentration, in order to better improve the properties of low-salt mutton myofibrillar protein gel, the present invention further combines magnetic field treatment, and through treatment with a certain intensity, time and temperature, the water molecules are arranged regularly, which plays an important role in the formation of a good network structure of myofibrillar protein gel and the improvement of gel properties. Experiments have shown that purified water soaking, buffer solution extraction and concentration adjustment combined with magnetic field treatment can significantly improve the properties of mutton myofibrillar protein gel under low-salt conditions, and achieve quality improvement of low-salt mutton products.

[0032] Preferably, in the above method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the magnetic field strength in step (3) is 1-5 mT, the temperature is 0-4°C, the standing time is 0.5-2 h, and the gel is prepared immediately after completion.

[0033] Further preferably, in the above method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the magnetic field strength in step (3) is 2-3 mT, the temperature is 0-4°C, the standing time is 0.5-1.5 h, and the gel is prepared immediately after completion.

[0034] Preferably, in the above-mentioned method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, the preparation method of the heat-induced gel in step (4) is: gradient heating from 25 to 85 °C, the heating rate is 1 °C / min, and the temperature is kept for 10 minutes. After the preparation is completed, the gel is quickly moved into an ice water bath, cooled to room temperature, and then placed at 4 °C overnight.

[0035] In the present invention, the low salt condition refers to a sodium chloride concentration lower than 0.4 mol / L.

[0036] The method for improving the properties of mutton myofibrillar protein gel under low-salt conditions provided by the present invention can not only effectively improve the properties of mutton myofibrillar protein gel, but also is easy to operate, can effectively improve the quality of low-salt mutton products, and has good application effect.

[0037] The above method provided by the present invention can be used for the research and development and production of low-salt meat products. Those skilled in the art can combine the above preferred schemes to obtain a better embodiment of the present invention.

[0038] 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.

[0039] The endpoints and any values ​​of the ranges disclosed in this specification 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 considered as specifically disclosed in this article.

[0040] In the description of this specification, the description with reference to the terms "one embodiment", "some embodiments", "specific implementations", or "some specific implementations" etc. means that the specific features, structures, materials or characteristics described in conjunction with the embodiment or example are included in at least one embodiment or example of the embodiment of the present invention. In this specification, the schematic representations of the above terms do not necessarily refer to the same embodiment or example. Moreover, the specific features, structures, materials or characteristics described may be combined in any one or more embodiments or examples in a suitable manner. In addition, those skilled in the art may combine and combine the different embodiments or examples described in this specification and the features of the different embodiments or examples, without contradiction.

[0041] In the examples provided in this specification, if no specific techniques or conditions are specified, the techniques or conditions described in the literature in this field or the product instructions are used. If the manufacturer of the reagents or instruments used is not specified, they are all conventional products that can be purchased through regular channels.

[0042] Example 1

[0043] This embodiment provides a method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, and the specific steps are as follows: (1) Soaking of mutton: Select fresh mutton hind leg meat, wash it with purified water, and then soak it in purified water at 0-4°C for 24 hours, changing the water 4 times in the middle; (2) Extraction of myofibrillar protein: Remove the fat and connective tissue from the hind leg of the lamb, mince, add 5 times the volume of phosphate buffer solution, which contains 1000 parts of water, 6 parts of NaCl, 5.8 parts of disodium hydrogen phosphate and 0.52 parts of sodium dihydrogen phosphate, and 0.001 parts of strontium chloride, homogenize at high speed in an ice water bath, homogenize at 12000 r / min for 1 min, centrifuge at 5000 g for 10 min at 4°C, discard the supernatant, take the precipitate, repeat the above operation 4 times, and filter the homogenate through four layers of gauze for the last time and centrifuge. The white precipitate obtained is myofibrillar protein. The protein concentration is adjusted to 40 mg / mL using protein dilution buffer, which contains 1000 parts of water, 35 parts of NaCl, 5.8 parts of disodium hydrogen phosphate and 0.52 parts of sodium dihydrogen phosphate, 0.001 parts of strontium chloride, and 0.002 parts of zinc chloride.

[0044] (3) Magnetic field treatment: Place the diluted myofibrillar protein solution in a static magnetic field with a magnetic field strength of 3 mT and a temperature of 0-4°C for 1 h. After completion, prepare the gel immediately.

[0045] (4) Preparation of protein gel: Heat-induced gel was prepared by water bath heating with a gradient temperature of 25-85°C at a heating rate of 1°C / min. The temperature was kept warm for 10 min and refrigerated overnight to measure the gel strength and water retention of the protein.

[0046] Example 2

[0047] This embodiment provides a method for improving the gel properties of mutton myofibrillar protein under low-salt conditions, and the specific steps are as follows: (1) Soaking of mutton: Select fresh mutton hind leg meat, wash it with purified water, and then soak it in purified water at 0-4°C for 18 hours, changing the water three times in the middle; (2) Extraction of myofibrillar protein: Remove the fat and connective tissue from the hind leg of the lamb, mince, add 5 times the volume of phosphate buffer solution, including 1000 parts of water, 5 parts of NaCl, 6.5 parts of disodium hydrogen phosphate and 0.55 parts of sodium dihydrogen phosphate, 0.002 parts of strontium chloride, homogenize at high speed in an ice water bath, homogenize at 12000 r / min for 1 min, centrifuge at 5000 g for 10 min at 4°C, discard the supernatant, take the precipitate, repeat the above operation 4 times, and filter the homogenate through four layers of gauze for the last time and centrifuge. The white precipitate obtained is myofibrillar protein. The protein concentration is adjusted to 45 mg / mL using protein dilution buffer, which contains 1000 parts of water, 30 parts of NaCl, 6.5 parts of disodium hydrogen phosphate and 0.55 parts of sodium dihydrogen phosphate, 0.002 parts of strontium chloride, and 0.003 parts of zinc chloride.

[0048] (3) Magnetic field treatment: Place the diluted myofibrillar protein solution in a static magnetic field with a magnetic field strength of 2 mT, a temperature of 0-4°C, and a standing time of 0.5 h. After completion, gel preparation is carried out immediately.

[0049] (4) Preparation of protein gel: Heat-induced gel was prepared by water bath heating with a gradient temperature of 25-85°C at a heating rate of 1°C / min. The temperature was kept warm for 10 min and refrigerated overnight to measure the gel strength and water retention of the protein.

[0050] Comparative Example 1

[0051] The method for preparing mutton myofibrillar protein gel in this comparative example is different from that in Example 1, the mutton is soaked in tap water.

[0052] Comparative Example 2

[0053] The only difference between the method for preparing mutton myofibrillar protein gel in this comparative example and that in Example 1 is that both the phosphate buffer solution and the protein dilution buffer only contain 1000 parts of water and 60 parts of NaCl.

[0054] Comparative Example 3

[0055] The only difference between the method for preparing mutton myofibrillar protein gel in this comparative example and that in Example 1 is that the protein dilution buffer contains only 1000 parts of water, 45 parts of NaCl, 5.8 parts of disodium hydrogen phosphate and 0.52 parts of sodium dihydrogen phosphate.

[0056] Comparative Example 4

[0057] The method for preparing mutton myofibrillar protein gel in this comparative example is different from that in Example 1 in that the protein gel is directly prepared without using magnetic field treatment.

[0058] Comparative Example 5

[0059] The method for preparing mutton myofibrillar protein gel in this comparative example is different from that in Example 1, the phosphate buffer solution contains only 1000 parts of water and 6 parts of NaCl, and the protein gel is directly prepared without magnetic field treatment.

[0060] Test example

[0061] In this test example, the mutton myofibrillar protein gels prepared in Examples 1-2 and Comparative Examples 1-5 were tested to detect the gel strength and water retention of the protein. The test results are shown in Table 1.

[0062]

[0063] As can be seen from Table 1, the gel strength and water retention of the mutton myofibrillar protein prepared by the method of the present invention are both good. Comparative Example 1 did not use purified water to soak the mutton, but instead used tap water to soak it, which resulted in changes in the types and contents of metal ions in the mutton, reducing the strength and water retention of the protein gel. The phosphate buffer solution and protein dilution buffer used in Comparative Example 2 only contained sodium chloride, and the pH value of the solution was close to the isoelectric point of the protein. The protein aggregated, resulting in reduced strength and water retention of the protein gel. The protein dilution buffer used in Comparative Example 3 did not add strontium chloride and zinc chloride, and the cross-linking effect of the protein was poor, resulting in reduced strength and water retention of the protein gel. Comparative Example 4 did not use magnetic field treatment to directly prepare the protein gel, and the water molecules in the protein solution were arranged in a disordered manner, resulting in the inability of the protein gel and water to form a stable structure, affecting the strength and water retention of the protein gel. The phosphate buffer solution used in Comparative Example 5 contains only 1000 parts of water and 6 parts of NaCl. At the same time, the protein gel is directly prepared without magnetic field treatment. It lacks a variety of zinc ions and strontium ions, and no magnetic field treatment is used, which makes it difficult for the protein and water molecules to form a stable gel state. The gel strength and water retention are not as good as those in the embodiment.

[0064] 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 improving the gel properties of mutton myofibrillar protein, characterized in that: The method comprises the steps of soaking mutton in purified water, extracting myofibrillar protein in phosphate buffer solution, adjusting protein concentration in protein dilution buffer solution, standing in a magnetic field environment and heating to induce gelation; wherein the phosphate buffer solution is composed of the following raw materials in mass fractions: 1000 parts of water, 4-8 parts of NaCl, 5-7 parts of disodium hydrogen phosphate, 0.4-0.7 parts of sodium dihydrogen phosphate, and 0.0004-0.005 parts of strontium chloride.

2. The method for improving the gel properties of mutton myofibrillar protein according to claim 1, characterized in that: The amount of the phosphate buffer solution added is 4-8 times the mass of the mutton after soaking.

3. The method for improving the gel properties of mutton myofibrillar protein according to claim 1 or 2, characterized in that: The phosphate buffer solution is composed of the following raw materials in mass fraction: 1000 parts of water, 5-6 parts of NaCl, 5.5-6.5 parts of disodium hydrogen phosphate and 0.5-0.6 parts of sodium dihydrogen phosphate, and 0.001-0.002 parts of strontium chloride; the added amount of the phosphate buffer solution is 5-6 times the mass of the soaked mutton.

4. The method for improving the gel properties of mutton myofibrillar protein according to any one of claims 1 to 3, characterized in that: The protein dilution buffer is composed of the following raw materials in mass fractions: 1000 parts of water, 30-45 parts of NaCl, 5-7 parts of disodium hydrogen phosphate and 0.4-0.7 parts of sodium dihydrogen phosphate, 0.0004-0.005 parts of strontium chloride, and 0.0002-0.001 parts of zinc chloride.

5. The method for improving the gel properties of mutton myofibrillar protein according to any one of claims 1 to 4, characterized in that: Adjust the protein concentration to 30-50 mg / mL using protein dilution buffer.

6. The method for improving the gel properties of mutton myofibrillar protein according to any one of claims 1 to 5, characterized in that: The protein dilution buffer is composed of the following raw materials by mass: 1000 parts of water, 34-38 parts of NaCl, 5.5-6.5 parts of disodium hydrogen phosphate and 0.5-0.6 parts of sodium dihydrogen phosphate, 0.001-0.002 parts of strontium chloride, and 0.0005-0.0008 parts of zinc chloride; the protein dilution buffer is used to adjust the protein concentration to 40-45 mg / mL.

7. The method for improving the gel properties of mutton myofibrillar protein according to any one of claims 1 to 6, characterized in that: The total organic carbon of the purified water does not exceed 0.50 mg / L, the ammonia does not exceed 0.00003%, the conductivity does not exceed 3.6 μs / cm at 10°C, does not exceed 4.3 μs / cm at 20°C, and does not exceed 5.1 μs / cm at 25°C; And / or, soak the mutton in purified water for 12-48 hours at a temperature of 0-4°C, and change the water every 6-8 hours; And / or, the amount of purified water added is 1-3 times the mass of the beach mutton.

8. The method for improving the gel properties of mutton myofibrillar protein according to any one of claims 1 to 7, characterized in that: The magnetic field strength is 1-5 mT, the temperature in the magnetic field is 0-4°C, and the time is 0.5-2 h.

9. The method for improving the gel properties of mutton myofibrillar protein according to any one of claims 1 to 8, characterized in that: The method of heating to induce gelation includes: increasing the temperature gradually from 25 to 85°C at a heating rate of 1±0.2°C / min, keeping the temperature for 10±2min, rapidly cooling to room temperature in an ice water bath, and standing at 4±2°C for 6-24h.

10. Use of the method for improving the gel properties of mutton myofibrillar protein according to any one of claims 1 to 9 in improving the gel properties of mutton myofibrillar protein under low-salt conditions, wherein the low-salt conditions refer to sodium chloride concentrations lower than 0.4 mol / L.

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