Preparation method and application of myofibrillar protein hydrogel

Abstract

The invention provides a preparation method of myofibrillar protein hydrogel, which comprises the following steps: uniformly dispersing myofibrillar protein in water to obtain a myofibrillar protein suspension, mixing the myofibrillar protein suspension with L-lysine to obtain a mixed solution A, mixing the mixed solution A with a glucan aqueous solution to carry out glycosylation reaction to obtain a mixed solution B, putting the mixed solution B into an ice-water bath to cool, and carrying out freeze-drying to obtain the myofibrillar protein hydrogel. And storing at 4 DEG C to obtain the myofibrillar protein hydrogel. The invention further provides application of the myofibrillar protein hydrogel in preparation of protein beverages and nasal feeding nutrient solutions. The method for preparing the myofibrillar protein hydrogel with higher lysine content and excellent dispersity and storage stability at lower production cost under the condition that professional large-scale instruments and equipment are not needed is used for preparing protein beverages and nasal feeding nutrient solutions.

Description

Technical Field

[0001] The invention belongs to the technical field of protein processing, and particularly relates to a preparation method of a myofibrillar protein hydrogel and application thereof. Background Art

[0002] Lysine, an essential amino acid and also known as the "first limiting amino acid," plays an irreplaceable role in human growth and development, protein synthesis, and immune function. However, this amino acid is scarce in grains and plant-based foods, making meat a crucial source of lysine. However, traditional meat products have a relatively tough texture, and their primary protein (myofibrillar protein) is insoluble in water and lacks a stable and uniform dispersion. This is particularly problematic for the elderly, infants, and children, especially those with dysphagia. The World Health Organization (WHO) has included dysphagia in the 10th edition of the International Classification of Diseases. Dou Zulin et al. reported at the 7th European Dysphagia Conference and the First World Dysphagia Forum that the prevalence of dysphagia in the elderly is as high as 11.4% to 33.7%. Against this backdrop, the development of an easy-to-swallow, fluid-like myofibrillar protein hydrogel has promising practical applications and commercial prospects. Summary of the Invention

[0003] The technical problem to be solved by the present invention is to address the deficiencies of the above-mentioned prior art and provide a method for preparing a myofibrillar protein hydrogel and its application. This method does not require professional large-scale instruments and equipment and can prepare a myofibrillar protein hydrogel with a high lysine content, excellent dispersibility and storage stability at a low production cost. The hydrogel can be used for the preparation of protein beverages and nasogastric nutrient solutions.

[0004] In order to solve the above technical problems, the technical solution adopted by the present invention is: a method for preparing myofibrillar protein hydrogel, the method comprising: S1. Evenly dispersing myofibrillar protein in water to obtain a myofibrillar protein suspension; S2, mixing the myofibrillar protein suspension obtained in S1 with L-lysine, and stirring to obtain a mixed solution A; S3, mixing the mixed solution A obtained in S2 and the dextran aqueous solution, stirring in a water bath at a temperature of 37° C. for saccharification reaction to obtain a mixed solution B; S4, placing the mixed solution B obtained in S3 into an ice water bath to cool down to obtain a sol; S5. Storing the sol obtained in S4 at 4° C. to obtain a myofibrillar protein hydrogel.

[0005] Preferably, the concentration of the myofibrillar protein suspension in S1 is 20 mg / mL.

[0006] Preferably, the mass of the L-lysine in 2 is 5% of the mass of the myofibrillar protein in the myofibrillar protein suspension.

[0007] Preferably, the concentration of the dextran aqueous solution in S3 is 20 mg / mL, and the molecular weight of the dextran in the dextran aqueous solution is 70 kDa.

[0008] Preferably, the volume ratio of the mixed solution A and the dextran aqueous solution in S3 is 1:1.

[0009] Preferably, the glycosylation reaction time in S3 is 8 hours.

[0010] The present invention also provides the use of the myofibrillar protein hydrogel prepared by the above preparation method. The myofibrillar protein hydrogel is used for the preparation of protein beverages and nasogastric feeding nutrient solutions.

[0011] Compared with the prior art, the present invention has the following advantages: The preparation method of the present invention combines the methods of exogenous addition of amino acids and glycosylation to prepare myofibrillar protein hydrogels without the need for large-scale professional instruments and equipment. The addition of lysine expands the closed secondary and tertiary structures of meat proteins by binding to acidic residues and aromatic residues on the protein, exposing more glycosylation sites for subsequent reactions. The introduction of sugar molecules with a large number of hydrophilic hydroxyl groups increases the affinity of meat proteins with water. Lysine induces the oxidation of active sulfhydryl groups between myofibrillar proteins to form disulfide bonds by changing the pH value without the need to add any additional cross-linking agents. The formed hydrogel has the characteristics of high lysine content, good stability and dispersibility, uniform structure, high solubility and low turbidity. As a new type of meat product, this product can be formulated into various flavors to become a protein beverage that is easy for daily consumers to carry, or it can be used as a carrier of nutrients for nutritional supplements for the elderly, infants, and patients with dysphagia. It also has the potential to be used as a nasogastric nutrient solution for patients who have lost the ability to swallow.

[0012] The present invention will be further described in detail below with reference to the accompanying drawings and embodiments. BRIEF DESCRIPTION OF THE DRAWINGS

[0013] Figure 1 Graphs showing the effects of different preparation methods on the (A) microstructure, (B) particle size distribution, (C) average particle size, and (D, E) sample appearance before (D) and after (E) storage for 14 days of myofibrillar protein hydrogels in Example 1 and Comparative Examples 1-4 of the present invention.

[0014] Figure 2Graph showing the effects of different preparation methods on (A) solubility, (B) turbidity, (C) potential, and (D) pH of myofibrillar protein hydrogels in Example 1 and Comparative Examples 1-4 of the present invention.

[0015] Figure 3 Graphs showing the effects of different preparation methods on (A) frequency scanning results and (B) apparent viscosity measurement results of myofibrillar protein hydrogels in Example 1 and Comparative Examples 1-4 of the present invention. DETAILED DESCRIPTION

[0016] Example 1 The preparation method of the myofibrillar protein hydrogel of this embodiment is as follows: S1. Disperse myofibrillar protein uniformly in water to obtain a myofibrillar protein suspension with a concentration of 20 mg / mL; S2. The myofibrillar protein suspension obtained in S1 is mixed with L-lysine, and the mixture is stirred at a speed of 200 r / min for 30 min to obtain a mixed solution A; the mass of the L-lysine is 5% of the mass of the myofibrillar protein in the myofibrillar protein suspension; S3. Mix the mixed solution A obtained in S2 with a 20 mg / mL aqueous solution of dextran, seal the top end to isolate oxygen, and stir in a water bath at 37°C for glycosylation reaction for 8 h to obtain a mixed solution B; the molecular weight of dextran is 70 kDa; S4, placing the mixed solution B obtained in S3 in an ice water bath and cooling it to 0-4°C to terminate the glycosylation reaction and obtain a sol; S5. Store the sol obtained in S4 at 4° C. overnight to obtain a myofibrillar protein hydrogel.

[0017] The myofibrillar protein hydrogel prepared in this example was subjected to three replicate measurements. The results showed that the L-lysine content per 100g of protein was 11.73±0.76 g, the protein solubility was 64.57±0.93%, the turbidity was 0.02±0.00, the viscosity was significantly increased, and a shear-thinning structure was observed. No obvious stratification was observed after storage at 4°C for 14 days.

[0018] Comparative Example 1 The preparation method of the myofibrillar protein hydrogel in this comparative example is different from that in Example 1 in that steps S2, S3, and S4 are not performed, i.e., exogenous amino acid addition, glycosylation treatment, and termination reaction are not performed. The rest of the preparation method is consistent with the preparation method of the myofibrillar protein hydrogel in Example 1.

[0019] Comparative Example 2 The method for preparing the myofibrillar protein hydrogel in this comparative example differs from that in Example 1 in that the glycosylation treatment and termination reaction in step S3 are not performed. The rest of the preparation method is the same as that in Example 1.

[0020] Comparative Example 3 The method for preparing the myofibrillar protein hydrogel in this comparative example is different from that in Example 1 in that step S2 of adding exogenous amino acids is not performed. The rest of the preparation method is the same as that in Example 1.

[0021] Comparative Example 4 The preparation method of myofibrillar protein hydrogel in this comparative example, S1. Disperse myofibrillar protein uniformly in water to obtain a myofibrillar protein suspension with a concentration of 20 mg / mL; S2. Mix the 20 mg / mL myofibrillar protein suspension mixed solution A obtained in S1 and the 20 mg / mL dextran aqueous solution, seal the top end to isolate oxygen, and stir in a water bath at 37°C for glycosylation reaction for 8 h to obtain a mixed solution A; the molecular weight of the dextran is 70 kDa; S3, mixing the mixed solution A obtained in S2 and L-lysine, and stirring at a speed of 200 r / min for 30 min to obtain a mixed solution B; the mass of the L-lysine is 5% of the mass of the myofibrillar protein in the mixed solution A; S4, placing the mixed solution B obtained in S3 in an ice water bath and cooling it to 0-4°C to terminate the glycosylation reaction and obtain a sol; S5. Store the sol obtained in S4 at 4° C. overnight to obtain a myofibrillar protein hydrogel.

[0022] Example 2 This example is a test experiment of the myofibrillar protein hydrogel prepared in Example 1 and Comparative Examples 1-4. Three parallel measurements were performed each time, and the data results are expressed as mean ± standard deviation.

[0023] Experiment 1 The myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 were diluted to 2 mg / mL with deionized water. The hydrogels were centrifuged at 4000 g and 4°C for 10 min in a refrigerated centrifuge. The protein concentrations before and after centrifugation were determined using the BCA assay. The final solubility results were calculated using the following formula: Solubility (%) = supernatant protein concentration / stock solution protein concentration × 100 like Figure 2As shown in (A), the solubility of native myofibrillar protein in Comparative Example 1 is very low (2.49%). This is primarily due to the fact that myosin, the major protein in myofibrillar protein, possesses periodically distributed tails with clusters of varying electrostatic charge, which causes the protein to spontaneously aggregate into bipolar helical filaments in a low-salt environment. The solubility of myofibrillar protein in Comparative Examples 2 and 3 significantly increased, reaching 15.91% and 33.60%, respectively. This improvement is likely due to the addition of L-lysine, which significantly weakens the intermolecular forces between proteins, modulates charge characteristics, and promotes a more dispersed protein structure. The hydrophilic groups of the polysaccharide molecules introduced during the glycosylation process reduce the surface hydrophobicity of the protein, weakening intermolecular hydrogen bonds, leading to unfolding of the secondary structure and inhibiting subsequent sedimentation and aggregation. It is worth noting that the combination of the two methods further significantly improved solubility, with Example 1 significantly outperforming Comparative Example 4, with a solubility of 64.57±0.93%. Lysine can unfold the protein structure and convert the α-helical structure into other structures, thereby exposing internal protein groups on the protein surface. Therefore, we hypothesize that this "exposure" and attachment of lysine residues to proteins increases the number of amino acid sites available for glycosylation, thereby improving glycosylation efficiency.

[0024] Experiment 2 The myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 were diluted to 1 mg / mL with deionized water. The absorbance of the sample at 600 nm was measured using a spectrophotometer as the turbidity of the sample. Figure 2 (A, B), the turbidities of Comparative Examples 1-4 and Example 1 were 0.89±0.01, 0.01±0.00, 0.76±0.00, 0.14±0.00, and 0.02±0.00, respectively, and the solubilities were 2.49±0.04%, 15.91±0.46%, 33.60±0.53%, 55.03±1.50%, and 64.57±0.93%, respectively. Solubility and turbidity generally exhibited a negative correlation, with Comparative Example 2 and Example 1 showing particularly low turbidities of 0.01 and 0.02, respectively. This is primarily due to the fact that lysine unwinds the double helix structure of myosin, causing myosin to lose its self-assembled rod-like structure. Glycosylation also slightly reduces turbidity, as the polyhydroxy sugar molecules incorporated into the protein enhance its hydrophilicity. The improved solubility and turbidity result in a more uniform product appearance, facilitating future formulation and development of this product without significantly impacting consumer sensory perception.

[0025] Experiment 3 The myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 were placed in sample appearance bottles, and the appearance of the samples was observed after standing for 5 minutes. The appearance of the samples was observed after standing in a cold storage at 4°C in the dark for 14 days. Figure 1 As shown in Figures (D and E), corresponding to the turbidity results, after 14 days of storage in a 4°C refrigerator, varying degrees of stratification were observed. Comparative Example 1 showed almost complete migration to the bottom of the bottle, demonstrating the instability of the myofibrillar protein solution. Migration levels were reduced to varying degrees in Comparative Examples 2-4 and Example 1, with Example 1 showing virtually no visible migration. This demonstrates that the treatment method of the present invention significantly enhances the storage stability of the protein, ensuring that the product does not experience spontaneous aggregation during storage, which could affect its shelf life.

[0026] Experiment 4 The myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 were diluted to 0.1 mg / ml solution, and the micron-level particle size was measured using a laser particle size analyzer. Figure 1 As shown in (B, C), in a low ionic strength solution, the periodically distributed charge clusters in the myosin tail attract each other and induce self-assembly. Therefore, Comparative Example 1 has the largest average particle size (d 4，3 ), reaching 79.84±1.63 μm. The particle size distribution is bimodal, in which the large particle peak is attributed to the self-assembled aggregates of myosin, and the low particle peak is due to the oligomers and monomeric substances in myosin. In contrast, the average volume diameter of Comparative Example 2 is significantly reduced to 55.49±3.45 μm, and the large particle peak in the particle size distribution is significantly shifted toward the small particle peak, indicating that the addition of lysine promotes the dissociation of myosin filamentous aggregates into soluble myosin oligomers. At the same time, we found that the particle size distribution of Comparative Example 2, Comparative Example 4, and Example 1 is significantly wider, mainly because the alkaline solution can promote the breaking of some non-covalent bonds in the protein and induce protein swelling. In contrast, the unfolding and expansion of the protein structure caused by lysine interactions exposed more glucan grafting sites and promoted subsequent glycosylation reactions, resulting in the smallest particle size in Example 1, 43.91±0.36 μm, significantly lower than the 47.52±0.49 μm and 53.88±0.92 μm of Comparative Examples 3 and 4, respectively. A smaller particle size contributes to a more delicate and uniform product taste and facilitates digestion and utilization.

[0027] Experiment 5 The myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 were diluted to 0.1 mg / ml solution, and the micron-scale particle size and Zeta-potential were measured using a laser particle size analyzer and a particle size potential analyzer, respectively. Figure 2(C), due to deprotonation, the potentials of all groups are negative. The potentials of Comparative Examples 2 and 3 are -8±0.87 mV and -9.98±0.20 mV, respectively. The absolute potential is higher than -6.1 mV of Comparative Example 1, because lysine causes the pH value to deviate further from the isoelectric point of myosin. On the other hand, because the Ɛ-amino group of lysine can capture protons from the acidic residues of myosin, deprotonation is further deepened. The change in potential of Comparative Example 3 is mainly attributed to the consumption of lysine in the glycosylation reaction, which leads to a decrease in the number of positively charged amino acids on the protein surface, thereby increasing the absolute potential value. Example 1 has the highest absolute negative potential, at -15.25±0.59 mV, which is better than -12.68±0.75 mV of Comparative Example 4. This is because lysine reacts with the acidic residues on myosin, isolating protons and enhancing its deprotonation by changing the pH value. Simultaneously, lysine induces the unfolding of the secondary and tertiary structures of myosin to stretch and expose more sites for subsequent glycosylation reactions, which contributes to the increase of negative charge under their combined processing.

[0028] Generally speaking, an increase in the absolute value of the zeta potential leads to increased electrostatic repulsion between proteins, making the system more stable. Furthermore, an increase in the potential disrupts the electrostatic repulsion-dependent aggregation of myosin tails, a potential mechanism for the stabilization of myofibrillar hydrogels.

[0029] Experiment 6 1 mL of each of the myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 was mixed with a dye solution containing 1.0 g / L Nile blue, shaken, and allowed to stand for 30 minutes. 5 μL of the dyed sample was dropped onto a glass slide with a coverslip. The microscopic morphology and distribution of the protein sample was observed using a confocal laser scanning microscope with a 40x objective lens, and photos of typical fluorescence images were taken. Figure 1 (A) In Comparative Example 1, numerous intact filamentous structures are visible. In Comparative Example 2, the individual myosin particles are significantly smaller in size than in Comparative Example 1, but their volume is significantly expanded, confirming hydrogel formation. Comparative Example 3 has the smallest particle size. Compared to Comparative Example 3, the increase in particle size caused by swelling in Comparative Example 4 outweighs the decrease in particle size caused by induced protein unfolding. The image of Example 1 is significantly more uniform and looser.

[0030] Experiment 7 3 mL of each of the myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 was injected into a hydrolysis tube, 10 mL of 6 M hydrochloric acid solution was added, mixed evenly, and the hydrolysis tube was placed in an electric blower thermostat at 110 ° C ± 1 ° C for 22 hours. After hydrolysis, it was taken out and cooled to room temperature. The hydrolyzate was filtered into a 25 mL volumetric flask, the hydrolysis tube was completely rinsed with a small amount of deionized water, fixed and shaken. 0.5 mL of the filtrate was pipetted into a 15 mL test tube, dried with nitrogen, and made up to 10 ml with 0.02 M hydrochloric acid solution, shaken evenly, and after passing through a 0.22 μM microporous membrane, the amino acid content was determined using a LA8080 fully automatic amino acid analyzer.

[0031] Table 1 Amino acid content of myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 (g / 100g) Note: Lowercase letters indicate significant differences at the p < 0.05 level.

[0032] As shown in Table 1, Comparative Example 2 shows significant differences in lysine and arginine levels compared to Comparative Example 1. This can be attributed to the ability of lysine to alter the solution pH, promoting the covalent attachment of cysteines in myofibrillar proteins, leading to disulfide bond formation and subsequent conversion to cystine. Although lysine may react with acidic and aromatic amino acid residues, results from amino acid hydrolysis indicate that this effect is not significant or has no substantial impact on the amino acid structure, thus remaining detectable. In Comparative Example 3, in addition to contributing the ε-amino group of lysine, the indole group of tryptophan, the imidazole group of histidine, the guanidine group of arginine, and the free amino group at the N-terminus of the protein were also observed to participate in this reaction. Cysteine ​​may participate in sulfhydryl conversion during glycosylation. Furthermore, the levels of valine, isoleucine, and tyrosine decreased significantly during glycosylation, although the specific reaction mechanism is unclear. Furthermore, the levels of other amino acids decreased slightly, but without statistical significance, indicating that glycosylation is not limited to specific amino acids. The amino acid profile of Example 1 is significantly different from that of Comparative Example 4, indicating that the preparation order plays an important role in the processing process. The higher lysine content of the amino acid is more beneficial as a nutritional supplement, and has a positive impact on human growth and development, protein synthesis, and immune function.

[0033] Experiment 8 The pH of the myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 was measured using an automatic pH meter. Figure 2As shown in Figure 2 (D), the pH values ​​of Example 1 and Comparative Examples 1-4 were 5.71±0.02, 7.81±0.02, 5.84±0.04, 7.53±0.03, and 7.61±0.02, respectively. The native myofibrillar protein in Comparative Example 1 was slightly acidic, while the pH values ​​of Comparative Examples 2, 4, and Example 1, which added alkaline lysine, were significantly improved. In Comparative Example 3, glycosylation had almost no significant effect on the pH value. Overall, although the pH value of the present invention has changed, it remains within a suitable range for consumption as a product and does not significantly affect sensory perception or digestion and absorption.

[0034] Experiment 8 The myofibrillar protein hydrogels prepared by different processes in Example 1 and Comparative Examples 1-4 were subjected to frequency sweep and apparent viscosity measurement using a rheological analyzer. The specific parameters are as follows: Frequency Sweep: The storage modulus (G') and loss modulus (G") were correlated with angular frequency (μ) in the range of 1-100 rad / s at 25°C. A 10% amplitude strain was applied to ensure that all dynamic measurements were performed within the linear viscoelastic range.

[0035] Apparent viscosity: 1-100 s -1 The apparent viscosity was measured at a shear rate of 1.

[0036] like Figure 3 (B) The apparent viscosity of all samples decreased with increasing shear rate, indicating shear-thinning behavior characteristic of non-Newtonian fluids. However, the apparent viscosity of Comparative Example 3 was significantly lower than that of Comparative Example 1, and this decrease was less pronounced due to the weakened interaction between the myosin tail and head caused by glycosylation. Lysine increased the apparent viscosity of the samples regardless of the addition method. This effect is primarily attributed to the pH shift caused by the basic amino acid, which leads to disulfide crosslinking and ultimately hydrogel formation. In terms of viscosity, the ratio for Comparative Example 4 was significantly lower than that for Example 1. This observation suggests that steric hindrance from the initial glycosylation reaction affected the subsequent lysine reaction. According to Stokes' law, increased viscosity helps reduce the sedimentation rate of the samples, which is one of the factors that enabled Comparative Example 2 and Example 1 to remain suspended for extended periods. However, when considering protein precipitation, factors such as electrostatic repulsion between particles and particle size must be considered. Therefore, the sedimentation effect and viscosity results are not entirely consistent. The products developed in this invention are slightly viscous and can be loaded with small particles such as fruit pulp and crushed oats. They serve as a basis for the development of various flavor products.

[0037] In the dynamic oscillation experiment, G' and G" represent the elasticity and viscosity of the protein, respectively. The frequency scan results of each sample treated with each method are shown in Figure 2. Figure 3(A) is shown. For each sample, both G' and G'' gradually increase with ω, indicating a small amount of frequency dependence. G' of all treatment groups always exceeds G', indicating the presence of viscoelastic dispersion behavior. Specifically, the G' values ​​of Comparative Example 2 and Example 1 show parallel changes over the entire range, and they are classified as weak gels, mainly due to the cross-linking of disulfide bonds inducing the formation of weak gels. In addition, the G' and G'' values ​​of Comparative Example 3 are significantly lower than those of Comparative Example 1, while the G' and G'' values ​​of Example 1 are significantly lower than those of Comparative Example 2, which confirms that the interaction between proteins is inhibited after the Maillard reaction. The G' value of Comparative Example 4 is significantly higher than that of Comparative Example 3 but significantly lower than that of Example 1, which is mainly attributed to the steric hindrance of glucan after glycosylation inhibiting the subsequent disulfide bond cross-linking induced by lysine.

[0038] The method prepares a myofibrillar protein hydrogel with a high lysine content, excellent dispersibility and storage stability at a low production cost without the need for specialized large-scale instruments and equipment. The myofibrillar protein hydrogel prepared by the invention is used for the preparation of protein beverages and nasogastric nutrient solutions.

[0039] The above description is only a preferred embodiment of the present invention and does not limit the present invention in any way. Any simple modification, change and equivalent variation made to the above embodiment based on the essence of the invention technology shall still fall within the scope of protection of the technical solution of the present invention.

Claims

1. A method for preparing a myofibrillar protein hydrogel, characterized in that: The method is: S1. Evenly dispersing myofibrillar protein in water to obtain a myofibrillar protein suspension; S2, mixing the myofibrillar protein suspension obtained in S1 with L-lysine, and stirring to obtain a mixed solution A; S3, mixing the mixed solution A obtained in S2 and the dextran aqueous solution, stirring in a water bath at a temperature of 37° C. for saccharification reaction to obtain a mixed solution B; S4, placing the mixed solution B obtained in S3 into an ice water bath to cool down to obtain a sol; S5. Storing the sol obtained in S4 at 4° C. to obtain a myofibrillar protein hydrogel.

2. The method for preparing a myofibrillar protein hydrogel according to claim 1, wherein: The concentration of the myofibrillar protein suspension described in S1 is 20 mg / mL.

3. The method for preparing a myofibrillar protein hydrogel according to claim 1, wherein: The mass of the L-lysine in S2 is 5% of the mass of the myofibrillar protein in the myofibrillar protein suspension.

4. The method for preparing a myofibrillar protein hydrogel according to claim 1, wherein: The concentration of the dextran aqueous solution in S3 is 20 mg / mL, and the molecular weight of the dextran in the dextran aqueous solution is 70 kDa.

5. The method for preparing a myofibrillar protein hydrogel according to claim 1, wherein: The volume ratio of the mixed solution A and the dextran aqueous solution in S3 is 1:

1.

6. The method for preparing a myofibrillar protein hydrogel according to claim 1, wherein: The glycosylation reaction time in S3 is 8 h.

7. An application of the myofibrillar protein hydrogel prepared by the preparation method according to any one of claims 1 to 6, characterized in that: The myofibrillar protein hydrogel is used for preparing protein beverages and nasogastric nutrient solutions.

Images