Method for removing bitter taste of food by using myofibrillar protein and application of method

Abstract

The invention discloses a method for removing bitter taste of food by using myofibrillar protein, and belongs to the technical field of food processing. The problems that in the prior art, a chemical taste masking agent is left, and the physical debitterizing efficiency is low are solved. The method comprises the following steps: firstly, extracting myofibrillar protein from meat raw materials and preparing a solution; premixing the flavonoids bitter substances and the enzymolysis whey protein peptide according to the mass ratio of 1: (3-5) to form a compound; under the conditions that the temperature is 4-15 DEG C and the pH value is 6.5-7.8, carrying out single treatment on a myofibrillar protein solution and the compound under the pressure of 50-100 MPa; and carrying out vortex oscillation incubation on the homogeneous system for 10-30 minutes at the temperature of 4-10 DEG C and the speed of 200-500 rpm. According to the method, protein-peptide-bitter substance ternary complex assembly is induced through high pressure, bitter release is synergistically inhibited through the steric hindrance effect of myofibrillar protein and the molecular embedding effect of whey protein peptide, and the method can be applied to bitter inhibition of meat processed products, plant-based food and beverages.

Description

Technical Field

[0001] The present invention relates to the technical field of food processing, and more specifically, to a method and application of myofibrillar protein in removing bitterness from food. Background Art

[0002] In the field of food processing, especially in the plant-based food, beverage and meat products industries, the presence of bitter substances seriously affects the sensory quality and consumer acceptance of products. Flavonoids, as common bitter substances, are widely found in raw materials such as citrus fruits, tea, and spices. The bitterness problem they produce has always been a difficult problem that needs to be solved in the food industry. For example, in meat processing, the bitter flavonoid components contained in spices can cause flavor imbalance and reduce the market competitiveness of products.

[0003] At present, the commonly used bitterness removal methods in the industry include water washing, adding sweeteners, using flavor masking agents, etc., but all of them have obvious limitations. The water washing method is prone to cause the loss of nutrients and the destruction of flavor structure; sweeteners can only mask the bitterness, but do not fundamentally eliminate bitter substances, and may cause health concerns; flavor masking agents have problems such as short-lasting effects, complex formulas, and affecting the overall flavor of the product. These traditional methods are difficult to meet the modern food industry's demand for high-quality and healthy products. There is an urgent need to develop an efficient, natural bitterness removal technology that does not affect the original flavor and nutrients of the product. Summary of the invention

[0004] An object of the present invention is to provide a method for removing the bitterness of food by myofibrillar protein, comprising the following steps: S1. extracting myofibrillar protein from meat raw materials and preparing a myofibrillar protein solution; S2, premixing the flavonoid bitter substance and the enzymatic whey protein peptide with a molecular weight of 800-1000 Da at a mass ratio of 1:3-5 to form a complex; S3, treating the myofibrillar protein solution and the complex at a pressure of 50-100 MPa at 4-15°C and pH 6.5-7.8 for a single time; S4. After homogenization, the system was incubated with vortexing at 4-10°C and 200-500 rpm for 10-30 minutes.

[0005] Preferably, the method for preparing and extracting the myofibrillar protein solution comprises the following steps: A1. Cut the beef into chunks to obtain beef chunks; A2. Add separation buffer to the beef cubes at a mass volume ratio of 1:4 and mix thoroughly; A3, after homogenization, centrifuge at 4°C and 2000 g for 15 minutes and filter to obtain the precipitate; A4. Wash the obtained precipitate repeatedly with the separation buffer, centrifuge 2 - 3 times, and then wash and centrifuge 2 - 3 times with an NaCl solution at a mass - volume ratio of 1:8. A5. Before the last centrifugation, first filter with four - layer degreased gauze, then collect the paste - like solid obtained from the last centrifugation, and then redissolve and resuspend it with a 0.05 M sodium acetate complex solution containing 0.5 - 1.0 mM DTT and 0.1 M mannitol. The pH value of the sodium acetate solution is 6.8 - 7.0 to obtain a resuspended solution. A6. Add a 0.5 M calcium chelator EGTA solution at 5 - 8% of the volume of the separation buffer to the resuspended solution, vortex and mix well, and then let it stand for 10 minutes to obtain a myofibrillar protein solution.

[0006] Preferably, the separation buffer in steps A2 and A4 includes: 0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / L EGTA, 20 mmol / L Tris - HCl, 100 mmol / L KCl, and a 0.5% protease inhibitor mixture is added to the separation buffer. The protease inhibitor mixture includes at least one of EDTA, EGTA, and phenylmethylsulfonyl fluoride, and the pH value of the separation buffer is 7.0.

[0007] Preferably, after standing for 10 minutes in step A6, add mesoporous silica nanoparticles to the solution, with an addition amount of 0.5 - 1.5% of the solution mass, oscillate and adsorb at 25°C and 300 rpm for 15 minutes, and then remove the nanoparticles through a 0.22 μm microfiltration membrane.

[0008] Preferably, in the complex solution containing DTT in step A5, an antioxidant microcapsule is additionally added. Its core is lip - soluble tocopherol, and its shell is poly (lactic - co - glycolic acid). The particle size of the antioxidant microcapsule is 0.5 - 2 μm, and the addition amount is 1 - 3% of the volume of the complex solution.

[0009] Preferably, the enzymatically hydrolyzed whey protein peptide in step S2 needs to be phosphorylated, specifically: Dissolve the enzymatically hydrolyzed whey protein peptide in a 0.1 M phosphate buffer with a pH of 7.0, add a sodium tripolyphosphate - succinic anhydride complex at 5 - 8% of the mass of the enzymatically hydrolyzed whey protein peptide, react at 45°C for 30 minutes, dialyze to remove free phosphate ions, and then lyophilize.

[0010] Preferably, when premixing in step S2, cellulose nanocrystals are additionally added, with an addition amount of 0.5 - 1.0% of the mass of the enzymatically hydrolyzed whey protein peptide.

[0011] Preferably, the cellulose nanocrystals are coated before premixing, and the specific treatment method is: Disperse cellulose nanocrystals with a length of 200 - 400 nm and a diameter of 15 - 30 nm in a phosphate buffer solution with a pH of 7.0, and add poly(sulfobetaine) until the final concentration reaches 0.5 - 1.0 mg / m 2 the surface area of the whiskers. After ultrasonic treatment at 40 kHz for 10 minutes, centrifuge and collect to obtain a PSB~CNC complex with a neutral surface charge.

[0012] Provide an application of the described method in the inhibition of bitterness in meat processing, plant-based foods or beverages.

[0013] Preferably, when the food is an acidic beverage with a pH ≤ 5.0, before step S3, carboxymethylate the myofibrillar protein solution: mix the myofibrillar protein solution and chloroacetic acid at a mass ratio of 1:0.1 - 0.3, react at pH 8.5 and 40 °C for 1 hour to obtain a modified myofibrillar protein solution, and use the modified myofibrillar protein solution to replace the original myofibrillar protein solution.

[0014] The present invention has at least the following beneficial effects: First, compared with the water washing method, the method of adding sweeteners, and the method of using flavor masking agents, the present invention assembles a ternary complex of myofibrillar protein - whey peptide - bitter substance, and uses the steric hindrance effect of myofibrillar protein and the molecular encapsulation effect of whey protein peptide to fundamentally reduce the free state of bitter molecules, rather than simply masking bitterness. It can be widely applied to the inhibition of bitterness in meat processing products, plant-based foods and beverages.

[0015] Second, through electronic tongue analysis and principal component analysis, the present invention finds that after myofibrillar protein binds to isoquercitrin and astragalin, the bitterness score decreases and the taste characteristics of the sample change. This indicates that myofibrillar protein binds to flavonoid bitter substances and undergoes physicochemical interactions (such as hydrogen bonding, hydrophobic interaction, electrostatic interaction, etc.), reduces the free state of bitter molecules by forming a stable complex, affects the response of bitter substances in taste detection, and thus reduces the bitter perception, providing data support for the mechanism of bitterness removal.

[0016] Third, during the extraction process of myofibrillar protein, the present invention uses a separation buffer solution with a complex composition, and optimizes the steps by adding mesoporous silica nanoparticles, antioxidant microcapsules, phosphorylated enzymatically hydrolyzed whey protein peptides, etc., which can significantly improve the effect of bitterness removal.

[0017] Fourth, for acidic beverages with pH ≤ 5.0, the present invention carboxymethylates myofibrillar protein, achieving a 90% removal rate of isoquercitrin in the peony flower tea extract at pH 4.2, and reducing the bitterness score to 1.5 points. This proves that by optimizing the extraction conditions and post-treatment steps, the binding and removal ability of bitter substances can be further enhanced, expanding the applicability of the method in different food systems.

[0018] Other advantages, objectives, and features of the present invention will be partially reflected in the following description and partially understood by those skilled in the art through research and practice of the present invention. BRIEF DESCRIPTION OF THE DRAWINGS

[0019] Figure 1 It is the electronic tongue taste score chart of this myofibrillar protein, isoquercitrin, and astragalin; Figure 2 It is the electronic tongue PCA analysis result chart of myofibrillar protein, isoquercitrin, and astragalin. DETAILED DESCRIPTION OF THE INVENTION

[0020] The following further details the present invention with reference to the drawings, enabling those skilled in the art to implement it according to the description in the specification.

[0021] It should be noted that the experimental methods described in the following implementation examples are all conventional methods unless otherwise specified, and the reagents and materials can be obtained from commercial sources unless otherwise specified.

[0022] Chinese prickly ash is a common spice. Since the main bitter substances in Chinese prickly ash are flavonoids, isoquercitrin and astragalin were selected as representatives to observe the masking behavior of myofibrillar protein on the bitter substances in Chinese prickly ash.

[0023] <Example 1> A method for removing bitter substances in Chinese prickly ash includes the following steps: Extract myofibrillar protein according to the following method: After removing visible fat and fascia from bovine hind tendons, cut them into cubes with a size of 1 mm × 1 mm × 1 mm, add a separation buffer (0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / L EGTA, pH 7.0) at a mass-to-volume ratio of 1:4 (w / v), and mix well. After homogenization, centrifuge (4°C, 2000 g, 15 min), and repeat washing and centrifuging the obtained precipitate twice; Continue to wash the precipitate with a 0.1 mol / L NaCl solution at a mass-to-volume ratio of 1:8 (w / v) according to the above steps. After centrifuging twice, filter with four layers of degreased gauze, and the paste-like solid obtained by centrifuging again is myofibrillar protein; Prepare quercetin-3-O-glucoside and astragalin standard solutions at a concentration of 0.1 mg / mL respectively; Disperse myofibrillar protein in 50 mmol / L phosphate buffer (containing 0.6 mol / L NaCl) to obtain a myofibrillar protein dispersion. Take 9.9 mL of the myofibrillar protein dispersion and place it in a 15 mL centrifuge tube. Add 100 μL of 0.1 mg / mL quercetin-3-O-glucoside and astragalin standard solutions respectively to make their concentrations in the whole system 1 mg / L. After mixing, incubate at 4 °C for 12 h.

[0024] Use an electronic tongue to analyze the bitterness scores of the two incubated mixtures (quercetin-3-O-glucoside-protein, astragalin-protein), the myofibrillar protein dispersion, the quercetin-3-O-glucoside standard solution, and the astragalin standard solution, and conduct principal component analysis. Among them, 10 points means no bitterness, and 0 points means extremely bitter taste. The test results are as Figure 1 and Figure 2 shown; From Figure 1 it can be seen that compared with quercetin-3-O-glucoside and astragalin alone, the bitterness scores of quercetin-3-O-glucoside-protein and astragalin-myofibrillar protein complexes decrease. For example, the bitterness score of quercetin-3-O-glucoside is 7.5, and the bitterness score of quercetin-3-O-glucoside-myofibrillar protein drops to 6.6. The bitterness score of astragalin is 7.2, and the bitterness score of astragalin-protein complex is 6.6. This indicates that after myofibrillar protein binds to flavonoid bitter substances, it can effectively reduce their bitterness and has a good adsorption effect on flavonoid bitter substances, thus verifying the effectiveness of the method for removing bitterness using myofibrillar protein in this invention; From Figure 2 it can be judged that after myofibrillar protein binds to flavonoid bitter substances, the taste characteristics of the sample have changed significantly, further indicating that the binding of myofibrillar protein to flavonoid bitter substances has changed the taste characteristics of the system. This provides data support for the mechanism study of removing bitterness by myofibrillar protein, indicating that the binding of the two affects the response of bitter substances in taste detection, thereby reducing the perception of bitterness.

[0025] To investigate the effect of pH on the secondary structure of myofibrillar protein-bitter substances, the myofibrillar protein was aliquoted into 50 mL centrifuge tubes, and appropriate volumes of 50 mmol / L phosphate buffer (containing 0.6 mol / L NaCl) with pH values of 5.0, 5.5, 6.0, 6.5, and 7.0 were added respectively. After homogenizing and mixing, the pH of the myofibrillar protein dispersion was adjusted to the corresponding pH (±0.02) value of the phosphate buffer using 2 mol / L HCl or 2 mol / L NaOH. The MPs dispersions under 5 different pH conditions were stored in a 4°C refrigerator and used up within 48 hours. When measuring different experimental indicators, it was diluted to the corresponding protein concentration with 50 mmol / L phosphate buffer (containing 0.6 mol / L NaCl) at the corresponding pH, and isoquercetin and astragalin were added to make their final concentration 10 mg / L. The myofibrillar protein dispersion without adding bitter substances was used as the control group. The Fourier transform infrared spectroscopy was used to observe the binding strength between the myofibrillar protein and flavonoids. The test results are shown in Table 1: Table 1 Effect of pH on the secondary structure of myofibrillar protein-bitter substances Note: The data in the table are mean ± standard deviation. Different letters in the same pH and different treatment groups indicate significant differences ( P <0.05).

[0026] According to the data in Table 1, it can be seen that pH and the type of complex jointly regulate the secondary structure of myofibrillar protein. Binding flavonoids (especially astragalin) under neutral conditions can significantly enhance the stability of α-helix and reduce the disordered structure, thereby optimizing the adsorption efficiency of bitter molecules. The promoting effect of astragalin on α-helix is more significant under neutral conditions, while isoquercetin maintains structural adaptability in a wide pH range, which can provide targeted solutions for bitter inhibition in different food systems.

[0027] <Example 2> 1. Extraction of myofibrillar protein Raw material pretreatment: Take 500 g of fresh bovine hind tendon, thoroughly remove visible fat and connective tissue, and use a scalpel to cut the muscle into small pieces of 1 mm × 1 mm × 1 mm; Add 2000 mL of separation buffer to the meat chunks. The buffer contains 0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / L EGTA, 20 mmol / L Tris-HCl, 100 mmol / L KCl, with the pH adjusted to 7.0, and add 0.5% protease inhibitor mixture. The protease inhibitor mixture contains 0.3% EDTA, 0.1% PMSF, 0.1% EGTA. The meat chunks and the buffer are mixed strictly according to the mass-to-volume ratio of 1:4, homogenized at 20,000 rpm for 3 minutes at 4°C to obtain a homogenate. The homogenate is centrifuged at 4°C and 2000×g for 15 minutes, the supernatant is discarded, and the precipitate is retained; Resuspend the precipitate with the same separation buffer according to the mass-to-volume ratio of 1:4, and repeat the washing and centrifugation at 4°C and 2000×g for 2 times, 15 minutes each time. Subsequently, transfer the precipitate to be resuspended with 0.1 mol / L NaCl solution according to the mass-to-volume ratio of 1:8, and also repeat the washing and centrifugation at 4°C and 2000×g for 2 times; Before the last centrifugation, pre-filter the suspension through 4 layers of sterile absorbent cotton gauze, and then centrifuge the filtrate at 4°C and 2000×g for 15 minutes to collect the paste-like myofibrillar protein solid at the bottom of the centrifuge tube, 2. Preparation of myofibrillar protein solution Weigh 40 g of the paste-like protein solid, add 320 mL of the reconstitution solution. The reconstitution solution is 0.05 M sodium acetate solution containing 0.75 mM dithiothreitol (DTT), 0.1 M mannitol, and the pH value is adjusted to 6.9, and vortex and resuspend at 4°C for 30 minutes; Add 130 mL of 0.5 M EGTA solution to the resuspended solution. The addition amount is 6.5% of the original separation buffer volume of 2000 mL, vortex and mix for 5 minutes, and let it stand at room temperature for 10 minutes to finally obtain the myofibrillar protein solution; 3. Extraction of zanthoxylum flavonoids Take 100 g of dry zanthoxylum powder, add 700 mL of 70% ethanol solution, extract by ultrasonic at a frequency of 50 kHz for 30 minutes, filter by suction, then concentrate by rotary evaporation, and freeze-dry to obtain zanthoxylum flavonoid powder; 4. Formation of complex Weigh 125 mg of zanthoxylum flavonoid powder and 500 mg of enzymatically hydrolyzed whey protein peptide with a molecular weight of 1000 Da, mix them according to the mass ratio of 1:4, add 5 mL of deionized water, and vortex and mix at 25°C for 5 minutes to form a homogeneous complex suspension; Take 20 mL of myofibrillar protein solution and mix it with all the complex suspensions. Adjust the pH of the mixture to 7.2 with 0.1 M NaOH. Load the mixture into a high-pressure bag and process it once at 80 MPa hydrostatic pressure at 8 °C for 5 minutes of holding time. The output solution is processed by a homogenizer at a speed of 10,000 rpm for 1 minute, and then transferred to an oscillating incubator and vortexed at 6 °C and 350 rpm for 20 minutes.

[0028] <Example 3> 1. Extraction of myofibrillar protein Raw material pretreatment: Take 500 g of fresh bovine hind tendon meat, thoroughly remove visible fat and connective tissue, and use a scalpel to cut the muscle into small pieces of 1 mm × 1 mm × 1 mm; Add 2000 mL of separation buffer to the meat pieces. This buffer contains 0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / L EGTA, 20 mmol / L Tris-HCl, 100 mmol / L KCl, with the pH adjusted to 7.0, and add 0.5% protease inhibitor mixture. The protease inhibitor mixture contains 0.3% EDTA, 0.1% PMSF, 0.1% EGTA. The meat pieces and the buffer are strictly mixed at a mass-to-volume ratio of 1:4, homogenized at 20,000 rpm for 3 minutes at 4 °C to obtain a homogenate. The homogenate is centrifuged at 4 °C and 2000 × g for 15 minutes, and the supernatant is discarded, retaining the precipitate; Resuspend the precipitate with the same separation buffer at a mass-to-volume ratio of 1:4, and repeat the washing and centrifugation 2 times at 4 °C and 2000 × g, 15 minutes each time. Subsequently, transfer the precipitate to a 0.1 mol / L NaCl solution and resuspend it at a mass-to-volume ratio of 1:8, and also repeat the washing and centrifugation 2 times at 4 °C and 2000 × g; Before the last centrifugation, pre-filter the suspension through 4 layers of sterile absorbent cotton gauze, and then centrifuge the filtrate at 4 °C and 2000 × g for 15 minutes to collect the paste-like myofibrillar protein solid at the bottom of the centrifuge tube. 2. Preparation of myofibrillar protein solution Weigh 40 g of the paste-like protein solid and add 320 mL of a reconstitution solution, which is a 0.05 M sodium acetate solution containing 0.75 mM dithiothreitol (DTT), 0.1 M mannitol, with the pH adjusted to 6.9, and vortex and resuspend at 4 °C for 30 minutes; Add 130 mL of 0.5 M EGTA solution to the resuspended solution. The addition amount is 6.5% of the original separation buffer volume of 2000 mL, vortex and mix for 5 minutes, and let it stand at room temperature for 10 minutes; Subsequently, mesoporous silica nanoparticles were added to the solution at an addition amount of 1.0% of the solution mass, and the mixture was oscillated and adsorbed at 25 °C and 300 rpm for 15 minutes. Then, the nanoparticles were removed through a 0.22-μm microfiltration membrane, and finally, a myofibrillar protein solution was obtained. 3. Extraction of Zanthoxylum flavonoids 100 g of dried Zanthoxylum powder was taken and added to 700 mL of 70% ethanol solution. The mixture was ultrasonically extracted at a frequency of 50 kHz for 30 minutes, filtered by suction, and then concentrated by rotary evaporation and freeze-dried to obtain Zanthoxylum flavonoid powder. 4. Formation of the complex 125 mg of Zanthoxylum flavonoid powder and 500 mg of enzymatically hydrolyzed whey protein peptide with a molecular weight of 1000 Da were weighed and mixed at a mass ratio of 1:4. Then, 5 mL of deionized water was added, and the mixture was vortex-mixed at 25 °C for 5 minutes to form a homogeneous complex suspension. 20 mL of the myofibrillar protein solution was taken and mixed with all of the complex suspension. The pH of the mixture was adjusted to 7.2 with 0.1 M NaOH. The mixture was filled into a high-pressure bag and treated once at a hydrostatic pressure of 80 MPa at 8 °C for 5 minutes. The output solution was processed by a homogenizer at a rotation speed of 10,000 rpm for 1 minute, and then transferred to an oscillating incubator and vortex-oscillated at 6 °C and 350 rpm for 20 minutes.

[0029] <Example 4> 1. Extraction of myofibrillar protein Raw material pretreatment: 500 g of fresh bovine hind shank meat was taken, and visible fat and connective tissue were completely removed. The muscle was cut into small pieces of 1 mm × 1 mm × 1 mm using a scalpel. 2000 mL of separation buffer was added to the meat pieces. The buffer contained 0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / L EGTA, 20 mmol / L Tris-HCl, 100 mmol / L KCl, and the pH was adjusted to 7.0. A 0.5% protease inhibitor mixture was added, and the protease inhibitor mixture contained 0.3% EDTA, 0.1% PMSF, and 0.1% EGTA. The meat pieces and the buffer were strictly mixed at a mass-to-volume ratio of 1:4 and homogenized at 20,000 rpm for 3 minutes at 4 °C to obtain a homogenate. The homogenate was centrifuged at 4 °C and 2000 × g for 15 minutes, and the supernatant was discarded, and the precipitate was retained. The precipitate was resuspended with the same separation buffer at a mass-to-volume ratio of 1:4 and washed and centrifuged twice at 4 °C and 2000 × g for 15 minutes each time. Subsequently, the precipitate was resuspended with 0.1 mol / L NaCl solution at a mass-to-volume ratio of 1:8 and also washed and centrifuged twice under the same conditions of 4 °C and 2000 × g. Before the last centrifugation, the suspension was pre-filtered through four layers of sterile absorbent cotton gauze, and the filtrate was then centrifuged at 4 °C and 2000×g for 15 minutes. The paste-like myofibrillar protein solid at the bottom of the centrifuge tube was collected. 2. Preparation of myofibrillar protein solution Weigh 40 g of the paste-like protein solid and add 320 mL of the complex solution, which is a 0.05 M sodium acetate solution containing 0.75 mM dithiothreitol (DTT), 0.1 M mannitol. At the same time, add antioxidant microcapsules (with a lipid-soluble tocopherol core and a poly(lactic-co-glycolic acid) copolymer shell, with a particle size of 1 μm) accounting for 2% of the volume of the complex solution. Adjust the pH value to 6.9 and vortex and resuspend at 4 °C for 30 minutes. Add 160 mL of 0.5 M EGTA solution (the addition amount is 8% of the original separation buffer volume of 2000 mL) to the resuspended solution, vortex and mix for 5 minutes, and let it stand at room temperature for 10 minutes. After standing, add mesoporous silica nanoparticles to the solution, with an addition amount of 1.2% of the solution mass. Oscillate and adsorb at 25 °C and 300 rpm for 15 minutes, and then remove the nanoparticles through a 0.22 μm microfiltration membrane to obtain the myofibrillar protein solution. 3. Extraction of zanthoxylum flavonoids Take 100 g of dry zanthoxylum powder, add 700 mL of 70% ethanol solution, ultrasonically extract at a frequency of 50 kHz for 30 minutes, filter by suction, then rotary evaporate and concentrate, and freeze-dry to obtain zanthoxylum flavonoid powder. 4. Complex formation Weigh 125 mg of zanthoxylum flavonoid powder and 500 mg of enzymatically hydrolyzed whey protein peptide with a molecular weight of 1000 Da, mix them in a mass ratio of 1:4, add 5 mL of deionized water, and vortex and mix at 25 °C for 5 minutes to form a homogeneous complex suspension. Take 20 mL of the myofibrillar protein solution and mix it with all the complex suspension. Adjust the pH of the mixed solution to 7.2 with 0.1 M NaOH. Put the mixed solution into a high-pressure bag and treat it once at 80 MPa hydrostatic pressure at 8 °C for 5 minutes. The output solution is processed by a homogenizer at a rotation speed of 10,000 rpm for 1 minute, and then transferred to an oscillating incubator and vortex-oscillated at 6 °C and 350 rpm for 20 minutes.

[0030] <Example 5> 1. Extraction of myofibrillar protein Raw material pretreatment: Take 500 g of fresh bovine hind tendon meat, thoroughly remove visible fat and connective tissue, and use a scalpel to cut the muscle into small pieces of 1 mm × 1 mm × 1 mm. Add 2000 mL of separation buffer to the meat chunks. The buffer contains 0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / L EGTA, 20 mmol / L Tris-HCl, 100 mmol / L KCl, with the pH adjusted to 7.0, and add 0.5% protease inhibitor mixture. The protease inhibitor mixture contains 0.3% EDTA, 0.1% PMSF, 0.1% EGTA. The meat chunks and the buffer are mixed strictly according to the mass-to-volume ratio of 1:4, homogenized at 20,000 rpm for 3 minutes at 4°C to obtain a homogenate. The homogenate is centrifuged at 4°C and 2000×g for 15 minutes, the supernatant is discarded, and the precipitate is retained; Resuspend the precipitate with the same separation buffer according to the mass-to-volume ratio of 1:4, and repeat the washing and centrifugation at 4°C and 2000×g for 2 times, 15 minutes each time. Subsequently, transfer the precipitate to be resuspended with 0.1 mol / L NaCl solution according to the mass-to-volume ratio of 1:8, and also repeat the washing and centrifugation at 4°C and 2000×g for 2 times; Before the last centrifugation, pre-filter the suspension through 4 layers of sterile absorbent cotton gauze, and then centrifuge the filtrate at 4°C and 2000×g for 15 minutes to collect the paste-like myofibrillar protein solid at the bottom of the centrifuge tube, 2. Preparation of myofibrillar protein solution Weigh 40 g of the paste-like protein solid, add 320 mL of the reconstitution solution. The reconstitution solution is 0.05 M sodium acetate solution containing 0.75 mM dithiothreitol (DTT), 0.1 M mannitol, and at the same time add antioxidant microcapsules (with a lipid-soluble tocopherol core and a poly(lactic-co-glycolic acid) copolymer shell, particle size 1 μm) accounting for 2% of the volume of the reconstitution solution. Adjust the pH value to 6.9 and vortex and resuspend at 4°C for 30 minutes; Add 160 mL of 0.5 M EGTA solution (the addition amount is 8% of the original 2000 mL volume of the separation buffer) to the resuspended solution, vortex and mix for 5 minutes, and let it stand at room temperature for 10 minutes; After standing, add mesoporous silica nanoparticles to the solution, with the addition amount being 1.2% of the solution mass. Oscillate and adsorb at 25°C and 300 rpm for 15 minutes, and then remove the nanoparticles through a 0.22 μm microfiltration membrane to obtain the myofibrillar protein solution; 3. Extraction of zanthoxylum flavonoids Take 100 g of dry zanthoxylum powder, add 700 mL of 70% ethanol solution, extract by ultrasonic wave at a frequency of 50 kHz for 30 minutes, filter by suction, then concentrate by rotary evaporation, and freeze-dry to obtain zanthoxylum flavonoid powder; Weigh 500 mg of enzymatically hydrolyzed whey protein peptide with a molecular weight of 1000 Da, dissolve it in 0.1 M phosphate buffer with a pH of 7.0, add sodium tripolyphosphate-succinic anhydride complex accounting for 7% of the mass of the enzymatically hydrolyzed whey protein peptide, react at 45 °C for 30 minutes. After the reaction, use a dialysis bag to dialyze and remove free phosphate ions, and then freeze-dry after dialysis to obtain phosphorylated modified enzymatically hydrolyzed whey protein peptide; 4. Complex formation Weigh 125 mg of zanthoxylum flavone powder and 500 mg of phosphorylated modified enzymatically hydrolyzed whey protein peptide with a molecular weight of 1000 Da, mix them at a mass ratio of 1:4, add 5 mL of deionized water, and vortex mix at 25 °C for 5 minutes to form a homogeneous complex suspension; Take 20 mL of myofibrillar protein solution and mix it with all of the complex suspension. Adjust the pH of the mixture to 7.2 with 0.1 M NaOH. Transfer the mixture into a high-pressure bag and process it once at a hydrostatic pressure of 80 MPa at 8 °C for 5 minutes. The output liquid is processed by a homogenizer at a rotational speed of 10,000 rpm for 1 minute, and then transferred to an oscillating incubator and vortex oscillated at 6 °C and 350 rpm for 20 minutes.

[0031] <Example 6> 1. Extraction of myofibrillar protein Raw material pretreatment: Take 500 g of fresh bovine hind tendon meat, thoroughly remove visible fat and connective tissue, and use a scalpel to cut the muscle into small pieces of 1 mm×1 mm×1 mm; Add 2000 mL of separation buffer to the meat pieces. This buffer contains 0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / L EGTA, 20 mmol / L Tris-HCl, 100 mmol / L KCl, adjust the pH to 7.0, and add 0.5% protease inhibitor mixture. The protease inhibitor mixture contains 0.3% EDTA, 0.1% PMSF, 0.1% EGTA. The meat pieces and the buffer are strictly mixed at a mass-to-volume ratio of 1:4, homogenize at 20,000 rpm for 3 minutes at 4 °C to obtain a homogenate. The homogenate is centrifuged at 4 °C and 2000×g for 15 minutes, discard the supernatant, and retain the precipitate; Resuspend the precipitate with the same separation buffer at a mass-to-volume ratio of 1:4, and repeat the washing and centrifugation 2 times at 4 °C and 2000×g for 15 minutes each time. Subsequently, transfer the precipitate to a 0.1 mol / L NaCl solution and resuspend it at a mass-to-volume ratio of 1:8, and also repeat the washing and centrifugation 2 times at 4 °C and 2000×g; Before the last centrifugation, pre-filter the suspension through 4 layers of sterile degreased cotton gauze, and then centrifuge the filtrate at 4 °C and 2000×g for 15 minutes to collect the paste-like myofibrillar protein solid at the bottom of the centrifuge tube. 2. Preparation of Myofibrillar Protein Solution Weigh 40 g of paste-like protein solid and add 320 mL of a complex solution, which is a 0.05 M sodium acetate solution containing 0.75 mM dithiothreitol (DTT), 0.1 M mannitol. At the same time, add antioxidant microcapsules (with a lipid-soluble tocopherol core and a poly(lactic-co-glycolic acid) copolymer shell, particle size 1 μm) accounting for 2% of the volume of the complex solution. Adjust the pH value to 6.9 and vortex and resuspend at 4°C for 30 minutes; Add 160 mL of 0.5 M EGTA solution (the addition amount is 8% of the volume of the original separation buffer solution of 2000 mL) to the resuspended solution, vortex and mix for 5 minutes, and let it stand at room temperature for 10 minutes; After standing, add mesoporous silica nanoparticles to the solution, with an addition amount of 1.2% of the solution mass. Oscillate and adsorb at 25°C and 300 rpm for 15 minutes, and then remove the nanoparticles through a 0.22 μm microfiltration membrane to obtain the myofibrillar protein solution; 3. Extraction of Zanthoxylum bungeanum Flavonoids Take 100 g of dry Zanthoxylum bungeanum powder, add 700 mL of 70% ethanol solution, ultrasonically extract at a frequency of 50 kHz for 30 minutes, filter by suction, then rotary evaporate and concentrate, and freeze-dry to obtain Zanthoxylum bungeanum flavonoid powder; Weigh 500 mg of enzymatically hydrolyzed whey protein peptide with a molecular weight of 1000 Da, dissolve it in 0.1 M phosphate buffer with a pH of 7.0, add sodium tripolyphosphate-succinic anhydride complex accounting for 7% of the mass of the enzymatically hydrolyzed whey protein peptide, react at 45°C for 30 minutes. After the reaction, use a dialysis bag to dialyze and remove free phosphate ions, and then freeze-dry after dialysis to obtain phosphorylated modified enzymatically hydrolyzed whey protein peptide; Disperse cellulose nanocrystals with a length of 300 nm and a diameter of 20 nm in phosphate buffer with a pH of 7.0, add poly(sulfobetaine) to a final concentration of 0.8 mg / m 2 the surface area of the whiskers. After ultrasonic treatment at 40 kHz for 10 minutes, centrifuge at 10,000×g for 10 minutes, collect the precipitate to obtain a surface charge-neutral PSB-CNC complex; 4. Complex Formation Weigh 125 mg of Zanthoxylum bungeanum flavonoid powder, 500 mg of phosphorylated modified enzymatically hydrolyzed whey protein peptide with a molecular weight of 1000 Da, and 2.5 mg of PSB-CNC complex (0.5% of the mass of the enzymatically hydrolyzed whey protein peptide), mix them in a mass ratio of 1:4, add 5 mL of deionized water, and vortex and mix at 25°C for 5 minutes to form a homogeneous complex suspension; Take 20 mL of myofibrillar protein solution and mix it with all of the complex suspension. Adjust the pH of the mixture to 7.2 with 0.1 M NaOH. Load the mixture into a high-pressure bag and process it once at 80 MPa hydrostatic pressure at 8 °C for a holding time of 5 minutes. The output liquid is processed by a homogenizer at a speed of 10,000 rpm for 1 minute, and then transferred to an oscillating incubator and vortexed at 6 °C and 350 rpm for 20 minutes.

[0032] <Comparative Example 1> This method is the method of adding a sweetener, specifically: Add sucrose to Zanthoxylum bungeanum containing isoquercitrin, and the addition amount is 5% of the mass of Zanthoxylum bungeanum, and stir evenly.

[0033] <Comparative Example 2> The method is the method of using a flavor masking agent, specifically: Add β-cyclodextrin to Zanthoxylum bungeanum containing isoquercitrin, and the addition amount is 3% of the food mass, and stir evenly.

[0034] <Comparative Example 3> 1. Myofibrillar protein extraction Raw material pretreatment: Take 500 g of fresh bovine hind tendon meat, thoroughly remove visible fat and connective tissue, and use a scalpel to cut the muscle into small pieces of 1 mm × 1 mm × 1 mm; Add 2000 mL of separation buffer to the meat pieces. This buffer contains 0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / L EGTA, 20 mmol / L Tris-HCl, 100 mmol / L KCl, adjust the pH to 7.0, and add 0.5% protease inhibitor mixture. The protease inhibitor mixture contains 0.3% EDTA, 0.1% PMSF, 0.1% EGTA. The meat pieces and the buffer are strictly mixed at a mass-to-volume ratio of 1:4, homogenized at 20,000 rpm for 3 minutes at 4 °C to obtain a homogenate. The homogenate is centrifuged at 4 °C and 2000 × g for 15 minutes, discard the supernatant, and retain the precipitate; Resuspend the precipitate with the same separation buffer at a mass-to-volume ratio of 1:4, and repeat the washing and centrifugation at 4 °C and 2000 × g for 2 times, 15 minutes each time. Subsequently, transfer the precipitate to be resuspended with 0.1 mol / L NaCl solution at a mass-to-volume ratio of 1:8, and repeat the washing and centrifugation at 4 °C and 2000 × g for 2 times; Before the last centrifugation, pre-filter the suspension through 4 layers of sterile degreased cotton gauze, and then centrifuge the filtrate at 4 °C and 2000 × g for 15 minutes to collect the paste-like myofibrillar protein solid at the bottom of the centrifuge tube. 2. Preparation of myofibrillar protein solution Weigh 40 g of pasteurized protein solids and add 320 mL of a reconstitution solution, which is a 0.05 M sodium acetate solution containing 0.75 mM dithiothreitol (DTT), 0.1 M mannitol, and the pH is adjusted to 6.9. Vortex and resuspend at 4°C for 30 minutes; Add 130 mL of 0.5 M EGTA solution to the resuspended solution. The addition amount is 6.5% of the original separation buffer volume of 2000 mL. Vortex for 5 minutes and let stand at room temperature for 10 minutes to finally obtain a myofibrillar protein solution; 3. Extraction of Zanthoxylum flavonoids Take 100 g of dry Zanthoxylum powder, add 700 mL of 70% ethanol solution, extract by ultrasonic wave at a frequency of 50 kHz for 30 minutes, filter by suction, then concentrate by rotary evaporation and freeze-dry to obtain Zanthoxylum flavonoid powder; 4. Formation of the complex Weigh 125 mg of Zanthoxylum flavonoid powder and 500 mg of enzymatically hydrolyzed whey protein peptide with a molecular weight of 1000 Da, mix them in a mass ratio of 1:4, add 5 mL of deionized water, and vortex at 25°C for 5 minutes to form a homogeneous complex suspension; Adjust the pH of the mixture to 7.2 with 0.1 M NaOH. Transfer the mixture into a high-pressure bag and treat it once at 80 MPa hydrostatic pressure at 8°C for 5 minutes. The output liquid is processed by a homogenizer at a speed of 10,000 rpm for 1 minute, and then transferred to an oscillating incubator and vortexed at 6°C and 350 rpm for 20 minutes.

[0035] For the Zanthoxylum treated in Examples 2 - 7 and Comparative Examples 1 - 3, perform 10 bitterness score evaluations using an electronic tongue, and conduct a bitterness sensory score on the treated Zanthoxylum using a 10-point scale. Among them, 0 points means no bitterness, and 10 points means extremely bitter. Take the average value as the final sensory score.

[0036] Use high performance liquid chromatography (HPLC) to determine the residual amount of astragalin in the treated Zanthoxylum. Among them, the chromatographic conditions are as follows: C18 chromatographic column (250 mm × 4.6 mm, 5 μm), mobile phase is acetonitrile - 0.1% phosphoric acid aqueous solution (gradient elution), flow rate is 1.0 mL / min, detection wavelength is 280 nm, column temperature is 30°C, and injection volume is 20 μL.

[0037] The Zanthoxylum used in Examples 2 - 6 and Comparative Examples 1 - 2 is from the same batch of Zanthoxylum. After detection, the astragalin content in the Zanthoxylum flavonoid powder used before the experiment is about 2.15 mg / g for all, with little difference. The results of the sensory score and the residual amount and removal rate of astragalin in the treated Zanthoxylum flavonoid powder are shown in Table 2 below: Table 2 Sensory score results of each group, and the residual amount and removal rate of astragalin in the treated Zanthoxylum flavonoid powder According to the data in Table 2, among various bitter taste removal methods, in Example 6, myofibrillar protein was used to treat Chinese prickly ash. Compared with Examples 2-5, its bitter taste effect was more significant, indicating that the technical optimization significantly reduced the bitter taste perception. For Comparative Example 1 using the sweetener addition method and Comparative Example 2 using the flavor masking agent method, the removal rates were 52.56% and 54.42% respectively, and the sensory scores were 7.2 points and 6.1 points respectively. Compared with the methods in Examples 2-6, these two methods could only temporarily mask the bitter taste, could not fundamentally reduce the content of bitter substances, and had poor effects, indicating that the traditional bitter taste removal methods had relatively limited effects.

[0038] Compared with Example 2, in Comparative Example 3, the myofibrillar protein solution was not mixed with the complex suspension, and the Chinese prickly ash flavonoids only bound to the whey protein peptides, lacking the synergistic effect of myofibrillar protein. The removal efficiency of bitter substances decreased significantly, and it also proved that myofibrillar protein, as a bitter taste carrier, was irreplaceable.

[0039] Example 6 included the treatment method of phosphorylated peptide + PSB-CNC complex, with the lowest sensory score and a sharp reduction in the residual amount of astragalin, indicating that it precisely encapsulated bitter molecules through charge modification and nano-carriers. Comparing Example 4 with Example 3, the residual amount of astragalin decreased significantly, indicating that antioxidant protection reduced the bitter and astringent taste brought by oxidation by-products. The residual amount of astragalin in Example 3 decreased from 1.98 mg / g in Example 2 to 1.87 mg / g, verifying the effectiveness of mesoporous silica in adsorbing small molecule bitter components.

[0040] The myofibrillar protein-Chinese prickly ash flavonoid composite technology can efficiently regulate the bitter taste, and its effect increases progressively with the technological upgrade: basic extraction (Example 2) → nano-adsorption (Example 3) → antioxidant protection (Example 4) → peptide modification (Example 5) → composite nano-carrier (Example 6). Among them, the composite nano-carrier (Example 6) is the optimal solution: Enhance the binding force through phosphorylated peptide and provide a neutral carrier interface by PSB-CNC to achieve deep encapsulation of bitter molecules; Combined with high-pressure homogenization and low-temperature oscillation to promote the stable formation of the complex, and the bitter taste sensory score decreased by 71%; The traditional masking method only covers the taste bud perception (Comparative Examples 1-2), while this technology reduces the bioavailability of bitter substances through molecular encapsulation, achieving a leap from "masking" to "eliminating".

[0041] In summary, in terms of removing the bitterness of Chinese prickly ash, the myofibrillar protein treatment method adopted in Example 6 has the best comprehensive effect, providing an efficient and potentially applicable new approach to solve the problem of flavonoid bitter substances in food processing. Follow-up research can further explore the applicability of this method in different food systems.

[0042] <Example 7> Raw materials and reagents: Acidic beverage: commercially available peony flower tea extract (pH = 4.2, detected to contain 1.8 mg / L of isoquercitrin); Modified myofibrillar protein solution: 200 mL of the myofibrillar albumin solution extracted by the method of Example 6 was mixed with chloroacetic acid at a mass ratio of 1:0.2, the pH was adjusted to 8.5, and after reacting at 40 °C for 1 h, the residual chloroacetic acid was removed by dialysis to obtain the modified myofibrillar protein solution; According to the method of Example 6, 125 mg of commercially available peony flower tea extract, 500 mg of enzymatically hydrolyzed whey protein peptide phosphorylated modified with a molecular weight of 1000 Da, and 2.5 mg of PSB-CNC complex (0.5% of the mass of the enzymatically hydrolyzed whey protein peptide) were mixed at a mass ratio of 1:4, 5 mL of deionized water was added, and vortex mixed at 25 °C for 5 minutes to form a homogeneous complex suspension; Take 20 mL of the modified myofibrillar protein solution and mix it with all the complex suspensions, adjust the pH of the mixture to 7.2 with 0.1 M NaOH, put the mixture into a high-pressure bag, and under the condition of 8 °C, treat it once at a hydrostatic pressure of 80 MPa, the holding time is 5 minutes, the output liquid is treated by a homogenizer at a speed of 10,000 rpm for 1 minute, and then transferred to an oscillating incubator, and vortex oscillated at 6 °C and 350 rpm for 20 minutes.

[0043] Control group setting: Control group 1: Treat the peony flower tea extract according to the method of Example 6; Control group 2: Add 3.5% of β-cyclodextrin to the peony flower tea extract; Control group 3: Untreated peony flower tea extract.

[0044] Detect the residual amount of isoquercitrin in the treated solutions in Example 7 and Control groups 1-3, and calculate the removal rate. Conduct sensory scoring (10-point system, 0 points = no bitterness), astringency (10-point system, 10 points = no astringency), and smoothness of taste (10-point system, 10 points = full score for smooth taste) scoring for the treated solutions. Among them, the scoring was blindly evaluated by 10 sensory personnel and the average value was taken. The results are shown in Tables 3 and 4 below: Table 3 Residual amount and removal rate of isoquercitrin in the treated solutions of each group Table 4 Sensory evaluation results of each group The residual protein content in Example 7 was detected to be 0.18 mg / mL (detected by HPLC, meeting food-grade requirements).

[0045] According to the data in Table 3 and Table 4, it can be seen that in Example 7, the carboxymethylated modified myofibrillar protein solution was used for treatment, achieving a 90% debittering rate, which was significantly better than that of Control Group 1 (82.8%) and Control Group 2 (60%). This indicates that the carboxymethylation modification of myofibrillar protein enhances the charge stability in an acidic environment (pH 4.2) and improves the binding ability of bitter substances (isoquercetin). The bitterness score of Example 7 was only 1.5 (close to no bitterness), which was 88% lower than that of Control Group 3 (untreated group). The bitterness residue (score 2.6) of Control Group 1 (treated by the method of Example 6) was higher than that of Example 7 due to the lack of pH adaptability. The astringency score of Example 7 was 9.0 (basically eliminated) and the smoothness was 9.1, confirming that the modified myofibrillar protein and the PSB-CNC complex synergistically improved the taste.

[0046] The carboxymethylation modification of myofibrillar protein is the core innovation in the flavor improvement of acidic beverages. By enhancing the electro-negativity and steric hindrance of the protein, it realizes the efficient capture of bitter substances and the synergistic improvement of taste, providing a solution for functional acidic beverages (such as the extract of peony flower tea).

[0047] Although the embodiments of the present invention have been disclosed as above, they are not limited to the applications listed in the specification and embodiments. It can be fully applied to various fields suitable for the present invention. For those familiar with the field, additional modifications can be easily made. Therefore, without departing from the general concept defined by the claims and the equivalent scope, the present invention is not limited to the specific details and the examples shown and described herein.

[0048] Appendix Figure 2 The English annotations in Astragalin is astragalin, astragalin-MP is astragalin-myofibrillar protein, isoquercetin is isoquercetin, and isoquercetin-MP is isoquercetin-myofibrillar protein.

Claims

1. A method for removing bitterness from food by myofibrillar protein, characterized in that, It includes the following steps: S1. Extract myofibrillar protein from meat raw materials and prepare a myofibrillar protein solution; S2. Pre-mix flavonoid bitter substances with enzymatically hydrolyzed whey protein peptides with a molecular weight of 800 - 1000 Da at a mass ratio of 1:3 - 5 to form a complex; S3. Under the conditions of 4 - 15 °C and pH 6.5 - 7.8, subject the myofibrillar protein solution and the complex to a single treatment at a pressure of 50 - 100 MPa; S4. After homogenization, the system is vortex - oscillated and incubated at 4 - 10 °C and 200 - 500 rpm for 10 - 30 minutes.

2. The method for removing food bitterness by myofibrillar protein according to claim 1, wherein The preparation and extraction method of the myofibrillar protein solution includes the following steps: A1. Cut beef into pieces to obtain beef chunks; A2. Add a separation buffer to the beef chunks at a mass - to - volume ratio of 1:4 and mix well; A3. After homogenization, centrifuge at 4 °C and 2000 g for 15 minutes, and filter to obtain a precipitate; A4. Wash and centrifuge the obtained precipitate 2 - 3 times with the separation buffer, and then wash and centrifuge 2 - 3 times with a NaCl solution at a mass - to - volume ratio of 1:8; A5. Before the last centrifugation, first filter with 4 - layer degreased gauze, then collect the paste - like solid obtained from the last centrifugation, and then re - dissolve and resuspend it with a 0.05 M sodium acetate complex solution containing 0.5 - 1.0 mM DTT and 0.1 M mannitol. The pH value of the sodium acetate solution is 6.8 - 7.0; A6. Add a 0.5 M calcium chelator EGTA solution accounting for 5 - 8% of the volume of the separation buffer to the resuspended solution, vortex - mix and let stand for 10 minutes to obtain a myofibrillar protein solution.

3. The method for removing food bitterness by myofibrillar protein according to claim 2, characterized in that, The separation buffer in steps A2 and A4 includes: 0.1 mol / L NaCl, 10 mmol / L Na3PO4, 2 mmol / L MgCl2, 1 mmol / LEGTA, 20 mmol / L Tris - HCl, 100 mmol / L KCl, and a 0.5% protease inhibitor mixture is added to the separation buffer. The protease inhibitor mixture includes at least one of EDTA, EGTA, and phenylmethylsulfonyl fluoride, and the pH value of the separation buffer is 7.

0.

4. The method for removing food bitterness by myofibrillar protein according to claim 2, wherein After standing for 10 minutes in step A6, add mesoporous silica nanoparticles to the solution, with an addition amount of 0.5 - 1.5% of the solution mass, oscillate and adsorb at 25 °C and 300 rpm for 15 minutes, and then remove the nanoparticles through a 0.22 μm microfiltration membrane.

5. The method for removing bitterness from food by myofibrillar protein according to claim 2, wherein In the complex solution containing DTT in step A5, an antioxidant microcapsule is additionally added. Its core is lipophilic tocopherol, and its shell is poly (lactic - co - glycolic acid). The particle size of the antioxidant microcapsule is 0.5 - 2 μm, and the addition amount is 1 - 3% of the volume of the complex solution.

6. The method for removing food bitterness by myofibrillar protein according to claim 1, characterized in that, In step S2, the enzymatically hydrolyzed whey protein peptides need to be phosphorylated and modified. Specifically: Dissolve the enzymatically hydrolyzed whey protein peptides in a 0.1 M phosphate buffer with a pH of 7.0, add a sodium tripolyphosphate - succinic anhydride complex accounting for 5 - 8% of the mass of the enzymatically hydrolyzed whey protein peptides, react at 45 °C for 30 minutes, dialyze to remove free phosphate ions, and then lyophilize.

7. The method for removing food bitterness by myofibrillar protein as described in claim 1, characterized in that, During the premixing in step S2, cellulose nanowhiskers are additionally added, and the addition amount is 0.5-1.0% of the mass of the enzymatically hydrolyzed whey protein peptides.

8. The method for removing food bitterness by myofibrillar protein according to claim 7, characterized in that The cellulose nanowhiskers are coated before premixing, and the specific treatment method is as follows: Disperse cellulose nanocrystals with a length of 200 - 400 nm and a diameter of 15 - 30 nm in a phosphate buffer solution with a pH of 7.0, add poly(sulfobetaine) until the final concentration reaches 0.5 - 1.0 mg / m 2 the surface area of the whiskers, and after ultrasonic treatment at 40 kHz for 10 minutes, centrifuge and collect to obtain a PSB - CNC complex with a neutral surface charge.

9. Use of the method according to any one of claims 1 to 8 in the inhibition of bitterness in meat processing, plant-based foods or beverages.

10. Use of the method for removing food bitterness by myofibrillar protein according to claim 9, characterized in that, When the food is an acidic beverage with pH ≤ 5.0, before step S3, the myofibrillar protein solution is subjected to carboxymethylation modification: the myofibrillar protein solution and chloroacetic acid are mixed at a mass ratio of 1:0.1-0.3, reacted at pH 8.5 and 40 °C for 1 hour to obtain a modified myofibrillar protein solution, and the modified myofibrillar protein solution is used to replace the original myofibrillar protein solution.

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