Method for reducing salt dosage of myofibrillar protein gel
By adding seaweed polysaccharides to myofibrillar protein gel, the problem of decreased gel performance in low-salt meat products was solved, achieving efficient salt substitution and improved gel properties, and making it suitable for existing meat product production lines.
Patent Information
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Filing Date
- 2026-01-12
- Publication Date
- 2026-03-31
AI Technical Summary
Existing technologies for reducing salt use in meat products often lead to a decrease in the solubility and gel properties of myofibrillar proteins, and potassium salt substitutes bring unpleasant flavors. Additives increase costs and have limited effects, making it difficult to maintain the texture and water-holding capacity of meat products under low-salt conditions.
By using seaweed polysaccharides such as red algae polysaccharide or laver polysaccharide, and adding them during the extraction and dissolution of myofibrillar proteins, a dense gel network is formed, reducing the amount of salt used while improving gel strength and water retention.
While reducing the amount of salt used by one-third, it significantly improves the gel strength, water retention and freeze-thaw stability of myofibril protein gel, and the process is simple and does not require complicated processing, making it suitable for existing meat product production lines.
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Abstract
Description
Technical Field
[0001] This invention relates to the technical field of food processing, and specifically to a method for reducing the amount of salt used in myofibrillar protein gel. Background Technology
[0002] Meat and meat products, as important sources of protein in the human diet, are experiencing increasing consumer demand. Meat products, especially reconstituted meat products, occupy a significant position in the consumer market due to their ease of processing and product standardization. Myofibrillar protein (MP), mainly composed of thick and thin filaments made up of myosin and actin, is a major structural and functional protein in meat products, accounting for approximately 55% to 65% of the total muscle protein content. Its solubility and gelation properties directly determine the texture, water-holding capacity, and final sensory quality of the product.
[0003] MP (polysaccharide) is a salt-soluble protein that typically requires a neutral salt solution (such as 0.47M~0.68M NaCl) to fully dissolve and form a dense three-dimensional gel network. This makes table salt (NaCl) an indispensable functional ingredient in meat processing. In the meat industry, adding sodium chloride (NaCl) is a common practice to improve the technical and sensory properties of meat products. However, excessive salt intake is significantly associated with the risk of various chronic diseases such as hypertension, cardiovascular disease, and diabetes. With increasing health awareness, consumers' demand for low-sodium meat products is becoming increasingly urgent. Current salt reduction technologies mainly face the following bottlenecks: First, simply reducing the salt concentration leads to a sharp decline in MP solubility and gel performance, resulting in deterioration of product quality; second, the use of potassium salts such as potassium chloride (KCl) and carrageenan (containing potassium) as salt substitutes often results in unpleasant flavors (such as metallic and bitter tastes), affecting acceptability; third, the addition of polysaccharide additives such as carboxymethyl cellulose and carrageenan often requires complex processing conditions or high dosages, increasing costs and limiting their improvement effects.
[0004] Therefore, in order to balance the quality and health demands of meat products, there is an urgent need to develop a highly efficient, clean, and non-complex process-assisted natural polysaccharide solution to effectively enhance the gelling properties and other application characteristics of functional ingredients (MPs) under low-salt conditions, thus overcoming key technical challenges in the meat industry. This will not only help promote the healthier transformation of the meat products industry but also provide an important direction for the innovative application of functional ingredients in the food system. Summary of the Invention
[0005] The present invention aims to at least partially solve one of the technical problems in the above-mentioned technology, namely, to provide a method for reducing the amount of salt used in myofibrillar protein gel. This method improves the solubility of myofibrillar protein by adding seaweed polysaccharides, thereby partially replacing the salt in myofibrillar protein gel meat products, while ensuring the textural properties and economic benefits (cooking yield and freeze-thaw yield) of the protein gel.
[0006] Therefore, this invention proposes a method for reducing the amount of salt used in myofibrillar protein gel, which includes the following steps: Step 1: Extract myofibrillar protein from animal muscle using phosphate buffer solution and sodium chloride solution; Step 2: Dissolve the myofibrillar protein in sodium chloride solution and add seaweed polysaccharide; Step 3: Homogenize and mix the myofibrillar protein and seaweed polysaccharide from Step 2, and remove air bubbles to obtain a mixed sol; Step 4: The mixed sol is cooked to form a thermally conductive gel, and then stabilized at 4°C for 12 h to obtain myofibrillar protein gel.
[0007] According to the present invention, a method for reducing salt usage in myofibrillar protein gel preparation utilizes seaweed polysaccharides, directly reducing salt usage by one-third, precisely aligning with current health-conscious dietary trends. Furthermore, the gel strength of the protein gel is increased by 10%, and water retention and freeze-thaw stability are significantly improved. The seaweed polysaccharides used in this method are derived from natural seaweed, are unmodified, and offer advantages in both safety and label cleanliness. The addition amount is low (only 0.25%~0.75%), with widely available raw materials, demonstrating good economic viability and potential for large-scale application. This technology is simple, requiring no modification to existing production lines or the introduction of complex processing steps, and can be seamlessly integrated into traditional meat product production processes. It is suitable for existing meat product production lines, providing the industry with a practical and feasible high-quality salt reduction path.
[0008] Optionally, in step 1, the preparation of the myofibrillar protein includes: mixing and stirring animal muscle tissue with phosphate buffer solution, centrifuging to remove the supernatant, retaining the precipitate, and repeating this operation 2 to 4 times; then mixing the precipitate with sodium chloride solution, filtering, and centrifuging to obtain myofibrillar protein.
[0009] Furthermore, the mass-to-volume ratio of the animal muscle tissue to the phosphate buffer solution is 1:3 to 1:5; the concentration of the phosphate buffer solution is 0.08 M to 0.12 M; and the concentration of the sodium chloride solution is 0.08 M to 0.12 M.
[0010] Optionally, the seaweed polysaccharide is red algae polysaccharide or laver polysaccharide.
[0011] Optionally, in step 3, the concentration of myofibrillar protein in the mixed sol is 20 mg / mL to 40 mg / mL, and the amount of seaweed polysaccharide used is 0.25% to 0.75% of the myofibrillar protein mass.
[0012] Optionally, in step 3, the air bubbles are removed by centrifugation at 1500 rpm / min to 2500 rpm / min for 1 min to 3 min.
[0013] Optionally, in step 4, the steaming time is 25 min to 35 min, and the steaming temperature is 60℃ to 100℃.
[0014] In another aspect, the present invention also provides a myofibrillar protein gel prepared by the above method, wherein the amount of salt used in the myofibrillar protein gel is reduced by 1 / 3.
[0015] Additional aspects and advantages of the invention will be set forth in part in the description which follows, and in part will be obvious from the description, or may be learned by practice of the invention. Attached Figure Description
[0016] Figure 1 The effect of different concentrations of seaweed polysaccharides on the solubility of the examples and comparative examples; Figure 2 The effect of different salt ion concentrations on the solubility of the examples and comparative examples; Figure 3 The effect of different concentrations of seaweed polysaccharides on the gel strength of the examples and comparative examples; Figure 4 The effect of different salt ion concentrations on the gel strength of the examples and comparative examples; Figure 5 The effect of different concentrations of seaweed polysaccharides on the cooking yield of the examples and comparative examples; Figure 6 The effect of different salt ion concentrations on the cooking yield of the examples and comparative examples; Figure 7 The freeze-thaw yields of different concentrations of seaweed polysaccharides in the examples and comparative examples; Figure 8 The freeze-thaw yields of the examples and comparative examples are shown for different salt ion concentrations. Figure 9 The particle size of the examples and comparative examples is shown for different concentrations of seaweed polysaccharides; Figure 10 The particle size of the examples and comparative examples is shown for different salt ion concentrations. Detailed Implementation
[0017] The technical solution of the present invention is illustrated below through specific examples. It should be understood that the one or more method steps mentioned in the present invention do not preclude the existence of other method steps before or after the combined steps, or the insertion of other method steps between these explicitly mentioned steps; it should also be understood that these embodiments are for illustrative purposes only and are not intended to limit the scope of the present invention. Furthermore, unless otherwise stated, the numbering of each method step is merely a convenient tool for identifying each method step, and not for limiting the order of the method steps or defining the scope of the present invention. Changes or adjustments to their relative relationships, without substantially altering the technical content, should also be considered within the scope of the present invention.
[0018] To better understand the above technical solutions, exemplary embodiments of the present invention are described in more detail below. While exemplary embodiments of the present invention are shown, it should be understood that the present invention can be implemented in various forms and should not be limited to the embodiments set forth herein. Rather, these embodiments are provided to enable a more thorough understanding of the present invention and to fully convey the scope of the invention to those skilled in the art.
[0019] This application is based on the inventors' considerations regarding the following: In the production of animal myofibrillar protein gel meat products, the complete dissolution of myofibrillar proteins and the formation of a dense gel network typically require a salt concentration of 2% to 3% (0.47M to 0.68M). However, considering human health and meeting the demand for low-salt diets, reducing the salt content of meat products is essential. As anionic hydrophilic seaweed polysaccharides, *Rhododendron simsii* and *Porphyra yezoensis* polysaccharides, with their unique structural characteristics, can improve the solubility of myofibrillar proteins, enhance their interaction and cross-linking, improve the protein gel network structure, and enhance the water-holding capacity of the gel. The improvement in the texture and water-holding capacity of myofibrillar protein gels by *Rhododendron simsii* and *Porphyra yezoensis* polysaccharides can reduce the amount of salt used.
[0020] Therefore, this application proposes to use seaweed polysaccharides to prepare myofibrillar protein gel.
[0021] The preparation of polysaccharides from Rhododendron molle and Porphyra is as follows: Dry *Porphyra yezoensis* or *Porphyra yezoensis* at 60℃, pulverize using a pulverizer, and pass through a 100-mesh sieve to obtain *Porphyra yezoensis* powder or *Porphyra yezoensis* powder. Add 5-6 times the mass of anhydrous ethanol to the *Porphyra yezoensis* powder or *Porphyra yezoensis* powder, heat and stir at 55℃ and 800 rpm for 30 min, filter, and collect the decolorized *Porphyra yezoensis* powder or *Porphyra yezoensis* powder. Add 30-35 times the mass of distilled water to the *Porphyra yezoensis* powder or *Porphyra yezoensis* powder, maintain the temperature at 90℃ for 2 h, centrifuge at 4000 rpm for 10 min, and collect the supernatant of *Porphyra yezoensis* or *Porphyra yezoensis* polysaccharide. Concentrate the polysaccharide supernatant using a rotary evaporator at 50℃-60℃, reducing the volume of the polysaccharide concentrate to 1 / 3-1 / 4 of the original supernatant volume. Add 3 times the volume of anhydrous ethanol to the polysaccharide concentrate, resulting in a final ethanol concentration of 75%, and precipitate the polysaccharide overnight. Centrifuge at 4000 rpm for 10 min and collect the polysaccharide precipitate to obtain *Porphyra yezoensis* polysaccharide or *Porphyra yezoensis* polysaccharide.
[0022] The test materials used in this invention are all common commercial products, which can be purchased on the market or prepared by known methods.
[0023] The present invention will now be described with reference to specific embodiments. It should be noted that these embodiments are merely descriptive and do not limit the present invention in any way. Example 1 Step 1: Add 0.1M phosphate buffer solution (4 times the weight of pork) to the pork, break it up and disperse it. Centrifuge to remove the supernatant, retain the precipitate, and repeat 3 times. Add 0.1M NaCl solution (4 times the weight of pork) to the precipitate, centrifuge to retain the precipitate, and repeat twice to obtain myofibrillar protein.
[0024] Step 2: Dissolve the myofibrillar protein obtained in Step 1 in 0.6 M sodium chloride solution, and add 0.25%~0.75% of the myofibrillar protein content of red algae polysaccharide, while adjusting the myofibrillar protein concentration to 40 mg / mL. To dissolve 1000 g of extracted myofibrillar protein (protein content of 100 mg / mL), approximately 53 g of sodium chloride is required.
[0025] Step 3: Homogenize the myofibrillar protein and red algae polysaccharide from Step 2 at 10,000 rpm to 14,000 rpm for 10 min using a food processor to ensure thorough mixing. Dispense the mixture into sampling cups, centrifuge at 2,000 rpm for 2 min to remove air bubbles, and obtain a mixed sol. Step 4: Place the mixed sol after removing bubbles in Step 3 at 80°C and cook for 30 min, then stabilize at 4°C for 12 h to obtain myofibrillar protein gel.
[0026] Example 2 The processing method in this embodiment is roughly the same as that in embodiment 1, except that the red algae polysaccharide in step 2 is replaced with laver polysaccharide.
[0027] Example 3 Step 1: Add 0.1M phosphate buffer solution (4 times the weight of pork) to the pork, break it up and disperse it. Centrifuge to remove the supernatant, retain the precipitate, and repeat 3 times. Add 0.1M NaCl solution (4 times the weight of pork) to the precipitate, centrifuge to retain the precipitate, and repeat twice to obtain myofibrillar protein.
[0028] Step 2: Dissolve the myofibrillar protein obtained in Step 1 in 0.4 M~0.8 M sodium chloride solution, and add 0.25%~0.75% of the myofibrillar protein content of red algae polysaccharide, while adjusting the myofibrillar protein concentration to 40 mg / mL. To dissolve 1000 g of extracted myofibrillar protein (protein content of 100 mg / mL), approximately 35 g~70 g of sodium chloride is required.
[0029] Step 3: Homogenize the myofibrillar protein and red algae polysaccharide from Step 2 at 10,000 rpm to 14,000 rpm for 10 min using a food processor to ensure thorough mixing. Dispense the mixture into sampling cups, centrifuge at 2,000 rpm for 2 min to remove air bubbles, and obtain a mixed sol. Step 4: Place the mixed sol after removing bubbles in Step 3 at 80°C and cook for 30 min, then stabilize at 4°C for 12 h to obtain myofibrillar protein gel.
[0030] Example 4 The processing method in this embodiment is roughly the same as that in embodiment 3, except that the red algae polysaccharide in step 2 is replaced with laver polysaccharide.
[0031] Comparative Example 1 Step 1: Add 0.1M phosphate buffer solution (4 times the weight of pork) to the pork, break it up and disperse it. Centrifuge to remove the supernatant, retain the precipitate, and repeat 3 times. Add 0.1M NaCl solution (4 times the weight of pork) to the precipitate, centrifuge to retain the precipitate, and repeat twice to obtain myofibrillar protein.
[0032] Step 2: Dissolve the myofibrillar protein obtained in Step 1 with 0.6 M sodium chloride solution to adjust the concentration of myofibrillar protein to 40 mg / mL. To dissolve 1000 g of extracted myofibrillar protein (protein content of 100 mg / mL), approximately 53 g of sodium chloride is required.
[0033] Step 3: Homogenize the myofibrillar protein from Step 2 at 10,000 rpm to 14,000 rpm for 10 minutes using a food processor. Dispense the mixture into sampling cups, centrifuge at 2,000 rpm for 2 minutes to remove air bubbles, and obtain myofibrillar protein sol. Step 4: Place the myofibrillar protein sol after removing bubbles in Step 3 in 80℃ and cook for 30 min, then stabilize it in 4℃ for 12 h to obtain myofibrillar protein gel.
[0034] Comparative Example 2 Step 1: Add 0.1M phosphate buffer solution (4 times the weight of pork) to the pork, break it up and disperse it. Centrifuge to remove the supernatant, retain the precipitate, and repeat 3 times. Add 0.1M NaCl solution (4 times the weight of pork) to the precipitate, centrifuge to retain the precipitate, and repeat twice to obtain myofibrillar protein.
[0035] Step 2: Dissolve the myofibrillar protein obtained in Step 1 in 0.4 M to 0.8 M sodium chloride solution to adjust the concentration of myofibrillar protein to 40 mg / mL. If you need to dissolve 1000 g of extracted myofibrillar protein (protein content of 100 mg / mL), you will need 35 g to 70 g of sodium chloride.
[0036] Step 3: Homogenize the myofibrillar protein from Step 2 at 10,000 rpm to 14,000 rpm for 10 min using a food processor. Dispense the mixture into sampling cups, centrifuge at 2,000 rpm for 2 min to remove air bubbles, and obtain myofibrillar protein sol. Step 4: Place the myofibrillar protein sol after removing bubbles in Step 3 in 80℃ and cook for 30 min, then stabilize it in 4℃ for 12 h to obtain myofibrillar protein gel.
[0037] Test case The properties of the pork myofibrillar protein gels obtained in Examples 1-4 and Comparative Examples 1-2 were determined.
[0038] (1) Determination of solubility Uninduced myofibrillar proteolytic samples were adjusted to a protein concentration of 1 mg / mL using the corresponding salt solution (0.2M, 0.4M, 0.6M, 0.8M, or 1M sodium chloride solution), centrifuged at 5000 g / min for 15 min, and the protein content in the supernatant was determined using a BCA kit. Protein solubility (%) was defined as the solubility of protein in the supernatant compared to the initial solution.
[0039] The results are as follows Figure 1 and Figure 2 As shown, 0.25%~0.75% of Rhodophyta polysaccharide and 0.25%~1% of Porphyra polysaccharide can significantly improve the solubility of myofibrillar protein gel.
[0040] (2) Determination of gel strength The gel strength of the gel samples was determined using a texture analyzer. The texture analyzer parameters were set as follows: test mode was compression mode; compression distance was 12 mm; initial speed was 2 mm / s; test speed was 1 mm / s; post-test speed was 2 mm / s; trigger force was 3 g, and the maximum sustained force was the gel strength.
[0041] The results are as follows Figure 3 and Figure 4 As shown, both *Rhododendron simsii* polysaccharides and *Porphyra yezoensis* polysaccharides significantly improved the gel strength of myofibrillar protein gels at concentrations ranging from 0.25% to 1%, with the best effects observed at concentrations of 0.5% to 0.75%. Furthermore, the effect of *Porphyra yezoensis* polysaccharides was significantly greater than that of *Rhododendron simsii* polysaccharides. Except for the 0.2 M concentration, which resulted in severe gel dehydration due to poor myofibrillar protein solubility, the gel strength of the myofibrillar protein gel gradually increased with increasing salt ion concentration (0.4 M to 1 M). All polysaccharides improved the gel strength of the myofibrillar protein gel, but the effect was not significant.
[0042] (3) Determination of cooking yield The cooking yield is the ratio of the mass change of the sample before and after heat-induced treatment, calculated using the formula.
[0043] Where M1 represents the mass of the protein sol sample and M2 represents the mass of the gel sample after cooking. Each experiment was repeated 4 times.
[0044] The results are as follows Figure 5 and Figure 6 As shown, 0.75%–1% of *Rhododendron simsii* polysaccharide and 0.25%–0.75% of *Porphyra yezoensis* polysaccharide significantly improved the cooking yield of myofibrillar protein gel, with 0.75% polysaccharide showing the best effect. The cooking yield of myofibrillar protein gel gradually increased with increasing salt ion concentration (0.2M–1M). Specifically, at a salt ion concentration of 0.6M, 0.5% of *Rhododendron simsii* polysaccharide and *Porphyra yezoensis* polysaccharide significantly improved the cooking yield of myofibrillar protein gel, while the effect of polysaccharides was not significant at other salt ion concentrations.
[0045] (4) Determination of freeze-thaw yield Cut the gel sample into small pieces M1 (approximately 3g), and... After being stored at 20°C for 24 hours, all samples were completely thawed at 4°C for 12 hours, which was designated as one freeze-thaw cycle. After three freeze-thaw cycles, the freeze-thaw yield of the gel was evaluated by centrifugation. The gel was then wrapped in three layers of absorbent paper, centrifuged at 4000 rpm for 15 minutes, and weighed again after centrifugation; the mass was recorded as M2.
[0046]
[0047] Where M1 represents the mass of the gel sample after cooking before centrifugation, and M2 represents the mass of the gel sample after centrifugation. Each experiment is repeated 3 times.
[0048] The results are as follows Figure 7 and Figure 8 As shown, 0.5%–1% of *Rhododendron simsii* polysaccharide and 0.25%–1% of *Porphyra yezoensis* polysaccharide significantly improved the freeze-thaw yield of myofibrillar protein gel. The freeze-thaw yield of myofibrillar protein gel increased with increasing salt ion concentration, but there was no significant difference between the 0.2M and 0.4M groups, or between the 0.8M and 1M groups. Compared to the blank control group, the 0.6M *Rhododendron simsii* polysaccharide, *Porphyra yezoensis* polysaccharide, and 1M *Rhododendron simsii* polysaccharide all improved the freeze-thaw yield of myofibrillar protein gel.
[0049] (5) Particle size determination Uninduced myofibrillar protein sol samples were adjusted to a protein concentration of 0.2 mg / mL using appropriate salt solutions (0.2 M, 0.4 M, 0.6 M, 0.8 M, or 1 M sodium chloride solution), and MP suspensions were prepared at 80 °C. The particle size of the myofibrillar protein suspension was determined using a nanoparticle size analyzer (NS-90Z, Zhuhai Omec Co., Ltd.). The thermal equilibrium time was 60 s, the target temperature was 25 °C, and the medium was water (refractive index 1.333). Each sample was scanned three times, and the PDI was controlled to be below 1.
[0050] The results are as follows Figure 9 and Figure 10 As shown, the addition of polysaccharides from *Rhodophyta rubrum* and *Porphyra yezoensis* both increased the particle size of myofibrillar proteins (MPs), possibly because polysaccharides (DPs) promoted MP aggregation. However, excessively large particles (0.25%, 0.75%, and 1%) may affect the uniformity of the protein gel, resulting in a less fine gel. With increasing salt ion concentration (0.2M~1M), the particle size gradually decreased due to increased myofibrillar protein solubility. At salt ion concentrations greater than or equal to 0.6M, the effect of salt ion concentration changes on myofibrillar protein particle size was not significant, consistent with the solubility results. When the salt ion concentration was ≤0.4M, polysaccharides reduced the myofibrillar protein particle size. At salt ion concentrations greater than or equal to 0.8M, the addition of polysaccharides had no significant effect on the myofibrillar protein particle size.
[0051] (6) Data Analysis Each experiment was repeated at least three times, and results are expressed as mean ± standard deviation. SPSS Statistics 27 and Excel software were used to analyze the experimental data. Duncan's multiple comparisons were used to compare the significance of data points. The detection limit was 0.05, and P < 0.05 was considered statistically significant.
[0052] Combination Figures 1-10 Compared to the blank control group (0.6 M salt ions), the optimal embodiment (0.75% laver polysaccharide and 0.6 M salt ions) showed an approximately 10% increase in gel strength. The 0.6 M group also showed an approximately 10% increase in gel strength compared to the 0.4 M group, meaning that the addition of 0.75% laver polysaccharide could reduce the amount of salt used by 0.2 M. MP is a salt-soluble protein, and its complete dissolution and formation of a dense gel network typically require a salt concentration of 2%-3% (0.47M~0.68M). In the meat industry, a 0.6M salt concentration is the most commonly used, meaning that the addition of 0.75% laver polysaccharide could reduce salt usage by one-third.
[0053] In summary, according to embodiments of the present invention, by utilizing the hydrophilic anionic properties of red algae polysaccharides and laver polysaccharides, the solubility of MP is improved through intermolecular interactions, and the protein cross-linking and gel network structure are enhanced, thereby reducing the amount of salt used by 1 / 3 while improving gel strength, water retention and freeze-thaw stability.
[0054] In the description of this specification, the references to terms such as "one embodiment," "some embodiments," "example," "specific example," or "some examples," etc., indicate that a specific feature, structure, material, or characteristic described in connection with that embodiment or example is included in at least one embodiment or example of the invention. The illustrative expressions of the above terms in this specification should not be construed as necessarily referring to the same embodiment or example. Furthermore, the specific features, structures, materials, or characteristics described may be combined in any suitable manner in one or more embodiments or examples. In addition, those skilled in the art can combine and integrate the different embodiments or examples described in this specification.
[0055] Although embodiments of the present invention have been shown and described above, it is understood that the above embodiments are exemplary and should not be construed as limiting the present invention. Those skilled in the art can make changes, modifications, substitutions and variations to the above embodiments within the scope of the present invention.
Claims
1. A method for reducing the amount of salt used in myofibrillar protein gel, characterized in that, Includes the following steps: Step 1: Extract myofibrillar protein from animal muscle using phosphate buffer solution and sodium chloride solution; Step 2: Dissolve the myofibrillar protein in sodium chloride solution and add seaweed polysaccharide; Step 3: Homogenize and mix the myofibrillar protein and seaweed polysaccharide from Step 2, and remove air bubbles to obtain a mixed sol; Step 4: The mixed sol is cooked to form a thermally conductive gel, and then stabilized at 4°C for 12 h to obtain myofibrillar protein gel.
2. The method as described in claim 1, characterized in that, In step 1, the preparation of the myofibrillar protein includes: mixing and stirring animal muscle tissue with phosphate buffer solution, centrifuging to remove the supernatant, retaining the precipitate, and repeating this operation 2 to 4 times; then mixing the precipitate with sodium chloride solution, filtering, and centrifuging to obtain myofibrillar protein.
3. The method as described in claim 2, characterized in that, The mass-to-volume ratio of the animal muscle tissue to the phosphate buffer solution is 1:3 to 1:5; the concentration of the phosphate buffer solution is 0.08 M to 0.12 M; and the concentration of the sodium chloride solution is 0.08 M to 0.12 M.
4. The method as described in claim 1, characterized in that, The seaweed polysaccharide is either red algae polysaccharide or laver polysaccharide.
5. The method as described in claim 1, characterized in that, In step 3, the concentration of myofibrillar protein in the mixed sol is 20 mg / mL to 40 mg / mL, and the amount of seaweed polysaccharide used is 0.25% to 0.75% of the myofibrillar protein mass.
6. The method as described in claim 1, characterized in that, In step 3, the air bubbles are removed by centrifugation at 1500 rpm / min to 2500 rpm / min for 1 min to 3 min.
7. The method as described in claim 1, characterized in that, In step 4, the steaming time is 25 min to 35 min, and the steaming temperature is 60℃ to 100℃.
8. The myofibrillar protein gel prepared by the method according to any one of claims 1-7, characterized in that, The amount of salt used in the myofibrillar protein gel is reduced by 1 / 3.