Salty taste enhancing peptide as well as screening method, application and product thereof

Abstract

The invention discloses a salty taste enhancing peptide as well as a screening method, application and a product thereof, and belongs to the technical field of food seasonings. The salty taste enhancing peptide is screened from soybean protein and is combined with TMC4 receptor protein, and the salty taste enhancing peptide is composed of one of the following peptides: the amino acid sequence is DIF, and the molecular weight is 393.47 Da; the amino acid sequence is QPR, and the molecular weight is 399.48 Da; the amino acid sequence is MMR, and the molecular weight is 436.62 Da; the amino acid sequence is DPIY, and the molecular weight is 506.60 Da. Four peptide fragments including DIF, QPR, MMR and DPIY with potential salty taste enhancing effects are screened according to molecular docking results, and the molecular weights of the four peptide fragments are smaller than 1000Da. Sensory evaluation and electronic tongue analysis show that the four peptide fragments all have a good salty taste enhancing effect and can be applied to the field of food seasonings, and the purpose of reducing salt but not reducing salty taste is achieved. The invention provides a theoretical basis for discovering new salty taste enhancing peptide resources in soybeans and developing nutritional and healthy salty taste enhancing peptides.

Description

Technical Field

[0001] The present invention relates to the technical field of food seasonings, and in particular to a salty taste enhancing peptide screened from soybean protein and capable of docking with a salty taste receptor TMC4, a screening method thereof, an application thereof, and a product containing the salty taste enhancing peptide. Background Art

[0002] Salt (NaCl) is an important source of saltiness in daily diet, giving food a pleasant flavor. However, excessive intake can cause hypertension, cardiovascular and other related diseases. Therefore, without changing the original sensory quality of food, finding a way to "reduce salt without reducing saltiness" has received widespread attention around the world, and the development of salt substitutes has become a research hotspot. As a salt substitute, salty peptides and salt-increasing peptides have attracted much attention due to their natural safety, wide sources, low taste threshold, and rich nutrition. At present, traditional salty peptide research is mainly prepared from natural foods through biosynthesis, fermentation, hydrolysis, enzymatic hydrolysis, Maillard reaction and other methods. Although this method is relatively mature, it still has certain limitations in terms of efficiency, cost and quality. Therefore, it is urgent to explore a scientific and effective screening method.

[0003] Compared with traditional peptide preparation and identification methods, virtual screening technology accurately screens out ideal bioactive compounds through computer simulation and prediction of interactions between biomolecules. The method of integrating computer technology with traditional methods significantly improves the screening efficiency. TMC4 receptor protein is a voltage-dependent chloride ion channel discovered for the first time. It has been proved to be involved in the perception of high-concentration salty taste through mouse experiments and exhibits high-salt effect at low salt concentrations. Therefore, as a new salt receptor, it provides a new way for us to explore salty taste enhancing peptides in the future. Soy protein is mainly composed of β-conglycinin (7S) and globulin (11S), accounting for 80-90% of the total soy protein. Soy protein produces a large number of short peptides after enzymatic hydrolysis. The peptides have been identified to be related to nutritional functions such as lipid-lowering, blood sugar-lowering, and anti-oxidation. However, at present, there are few studies on the use of virtual screening technology to screen salty taste enhancing peptides from soy protein. Therefore, this study used virtual screening technology combined with sensory evaluation to identify and screen salty taste enhancing peptides.

[0004] Based on this, the present invention aims to screen out novel salty taste enhancing peptides from soy protein using virtual screening technology, providing a new strategy for achieving “salt reduction” without “salt reduction”. Summary of the invention

[0005] In view of this, the present invention provides a salty taste enhancing peptide and a screening method, application and product thereof.

[0006] In order to achieve the above object, the present invention adopts the following technical solution:

[0007] The present invention provides a salty taste enhancing peptide, which is screened from soybean protein and binds to TMC4 receptor protein. The salty taste enhancing peptide is composed of one of the following peptides:

[0008] The amino acid sequence is DIF, and the molecular weight is 393.47Da;

[0009] The amino acid sequence is QPR, and the molecular weight is 399.48Da;

[0010] The amino acid sequence is MMR, and the molecular weight is 436.62Da;

[0011] The amino acid sequence is DPIY and the molecular weight is 506.60Da.

[0012] Furthermore, in the salty taste enhancing peptide, the peptide segment with the amino acid sequence of DIF undergoes molecular docking with the receptor TMC4, and the main binding sites are Ala158, Gln279, Thr280, His293, Ala283, Glu286, Ala584 and Ser585.

[0013] Furthermore, in the salty taste enhancing peptide, the peptide segment with the amino acid sequence of QPR can be docked with the salty taste enhancing peptide TMC4 receptor based on molecular docking, and the main binding sites are Ala283, His293, Glu319, Glu323, Ala584 and Ser585.

[0014] Furthermore, in the salty taste enhancing peptide, the peptide segment with the amino acid sequence of MMR can be docked with the salty taste enhancing peptide TMC4 receptor based on molecular docking, and the main binding sites are Gln279, Glu286, His293, Glu319, Arg583, Ser585 and Asn588.

[0015] Furthermore, in the salty taste enhancing peptide, the peptide segment with the amino acid sequence DPIY can be docked with the salty taste enhancing peptide TMC4 receptor based on molecular docking, and the main binding sites are Ala158, Ala283, Glu286, His293, Glu319, Val322, Thr581, Phe582, Arg583, Ala584 and Ser585.

[0016] Furthermore, the saltiness value of the peptide segment with the amino acid sequence of DIF is 3.24;

[0017] and / or, the saltiness value of the peptide segment having the amino acid sequence of QPR is 3.79;

[0018] and / or, the saltiness value of the peptide segment having the amino acid sequence of MMR is 4.00;

[0019] And / or, the saltiness value of the peptide segment with the amino acid sequence of DPIY is 3.97.

[0020] The present invention provides a method for screening salty taste enhancing peptides, characterized in that the steps are as follows:

[0021] (1) Construct a TMC4 receptor protein model using the trRosetta online server and evaluate its reliability;

[0022] The reliability evaluation is as follows: according to the Ramachandran diagram, the proportion of amino acid residues falling in the allowed region and the maximum allowed region in the entire protein is required to be higher than 90%;

[0023] (2) computer simulation of enzymatic hydrolysis of soy protein isolate to obtain enzymatic peptide segments with sequence lengths of 3-10;

[0024] (3) predicting the biological activity of the enzymatic peptides, screening out peptides with potential biological activity, predicting their physicochemical properties, and screening out non-toxic and water-soluble peptides;

[0025] Among them, the screening criteria for the biological activity prediction are: prediction score>0.5;

[0026] The screening criteria for toxicity prediction are: NonToxin;

[0027] The screening criteria for water solubility prediction are: Good water solubility;

[0028] (4) molecular docking the TMC4 receptor protein model with the non-toxic, water-soluble peptide segment of step (3) to form a receptor protein and small molecule ligand complex;

[0029] Among them, the TMC4 receptor protein needs to remove water molecules and add hydrogen atoms under the CHARMM force field environment;

[0030] The active position coordinates of the molecular docking are: X=-59.1, Y=77, Z=72.4, and the radius is 20;

[0031] The molecular docking selects the largest cavity in the TMC4 receptor protein as the docking pocket;

[0032] (5) Screening peptides with potential salt-increasing effects based on the molecular docking results and synthesizing the peptides by solid-phase synthesis;

[0033] Wherein, the screening: selecting peptides with low energy values ​​in CDOCKER energy;

[0034] (6) The synthesized peptides are subjected to sensory evaluation and electronic tongue analysis to obtain the above-mentioned salty taste enhancing peptides.

[0035] The invention provides an application of a salty taste enhancing peptide in the preparation of condiments and foods.

[0036] The invention provides a product containing the salty taste enhancing peptide selected from soybean protein.

[0037] Compared with the prior art, the beneficial effects achieved by the present invention are as follows: the present invention screened out four peptide segments, DIF, QPR, MMR and DPIY, with a molecular weight less than 1000Da from the protein in soy protein, and sensory evaluation and electronic tongue analysis showed that the four peptide segments all had a good saltiness-enhancing effect. The four saltiness-enhancing peptides can be applied to food seasonings to achieve the purpose of "reducing salt" without "reducing saltiness". BRIEF DESCRIPTION OF THE DRAWINGS

[0038] In order to more clearly illustrate the embodiments of the present invention or the technical solutions in the prior art, the drawings required for use in the embodiments or the description of the prior art will be briefly introduced below. Obviously, the drawings described below are only embodiments of the present invention. For ordinary technicians in this field, other drawings can be obtained based on the provided drawings without paying creative work.

[0039] Figure 1 The evaluation diagram of the TMC4 receptor protein model of the embodiment of the present invention, wherein (A) is the TMC4 receptor protein model, (B) is the Ramachandran diagram, (C) is the transmembrane channel region, and (D) is the Verify 3D diagram;

[0040] Figure 2 The statistical results of the amino acid sites of the peptide segments of the present invention and the TMC4 receptor protein docking;

[0041] Figure 3 The 2D and 3D interaction diagrams of the peptide DIF of the embodiment of the present invention and the TMC4 receptor protein model molecule docking, wherein A represents the 3D view of the peptide and the TMC4 receptor binding surface groove; B represents the 3D view of the peptide and the TMC4 receptor docking; C represents the 2D view of the peptide and the TMC4 receptor docking;

[0042] Figure 4 The 2D and 3D interaction diagrams of the peptide QPR of the present invention and the TMC4 receptor protein model molecule docking, wherein A represents the 3D view of the peptide and the TMC4 receptor binding surface groove; B represents the 3D view of the peptide and the TMC4 receptor docking; C represents the 2D view of the peptide and the TMC4 receptor docking;

[0043] Figure 5The 2D and 3D interaction diagrams of the peptide MMR of the embodiment of the present invention and the TMC4 receptor protein model molecule docking, wherein A represents the 3D view of the peptide and the TMC4 receptor binding surface groove; B represents the 3D view of the peptide and the TMC4 receptor docking; C represents the 2D view of the peptide and the TMC4 receptor docking;

[0044] Figure 6 The 2D and 3D interaction diagrams of the peptide DPIY of the embodiment of the present invention and the TMC4 receptor protein model molecule docking, wherein A represents the 3D view of the peptide and the TMC4 receptor binding surface groove; B represents the 3D view of the peptide and the TMC4 receptor docking; C represents the 2D view of the peptide and the TMC4 receptor docking;

[0045] Figure 7 This is a diagram of sensory evaluation results of an embodiment of the present invention;

[0046] Figure 8 This is a result diagram of electronic tongue analysis according to an embodiment of the present invention;

[0047] Fig. 9 This is a diagram of the salinity value analysis results of an embodiment of the present invention. DETAILED DESCRIPTION

[0048] The following will be combined with the drawings in the embodiments of the present invention to clearly and completely describe the technical solutions in the embodiments of the present invention. Obviously, the described embodiments are only part of the embodiments of the present invention, not all of the embodiments. Based on the embodiments of the present invention, all other embodiments obtained by ordinary technicians in this field without creative work are within the scope of protection of the present invention.

[0049] The drugs required for the present invention are conventional experimental drugs, which are purchased from commercial channels; the experimental methods not mentioned are conventional experimental methods and will not be described in detail here.

[0050] Example 1

[0051] Construction of TMC4 receptor protein model

[0052] The amino acid sequence of TMC4 (NP_001138775) was obtained from the NCBI database, and the NCBIBLAST tool was used to search for the amino acid sequence of TMC4 with a homology of less than 30%. Therefore, the trRosetta online server was used to construct the TMC4 salty taste receptor protein model using the AI ​​de novo folding algorithm. The final 3D model is as follows Figure 1 (A).

[0053] Reliability evaluation of TMC4 receptor protein model

[0054] The constructed TMC4 salty taste receptor model was evaluated using the residual percentage of the Ramachandran plot and ERRAT in SEVES v6.0. Figure 1 As shown in (B), about 92.7% of the amino acid residues are located in the largest allowed region, 6.7% of the amino acid residues are located in other allowed regions, only 0.2% of the amino acid residues are located in the unallowed region, and 0.5% of the residues are located in the prohibited region. This shows that the model constructed by the AI ​​de novo folding algorithm has high reliability and can be used for subsequent research. The transmembrane domain of TMC4 was predicted using the DeepTMHMM online tool. Figure 1 As shown in (C), there are 10 transmembrane regions in the protein structure of the invention. The ERRAT analysis results are as follows Figure 1 As shown in (D), the Overall quality factor is 98.102. The above results show that the TMC4 receptor protein model constructed by the present invention can be used for subsequent experiments.

[0055] Computer simulation of enzymatic hydrolysis of soybean protein

[0056] The soybean 7s globulin protein sequence (β-conglycinin α (alpha-subunit), α' (alpha prime subunit) and β (beta-subunit) subunits, with accession numbers BAB64304.1, BAB64303.1, BAB64306.1, respectively) was obtained from the NCBI GenBank database. The protein sequence obtained above was virtually hydrolyzed using alkaline protease (EC3.4.21.62) and trypsin (EC3.4.21.4) in the "ENZYME (S) ACTION" program in BIOPEP-UWM, and a total of 208 peptides were hydrolyzed. Peptides with sequence lengths of 2-10 were selected from them, and their biological activity was predicted using the Peptide Ranker website. After entering the amino acid sequence of each peptide, there will be a corresponding biological activity score. The higher the score, the greater the biological activity of the peptide. Generally, a biological activity score of not less than 0.5 can be considered as an active peptide. A total of 33 peptides with potential biological activity were screened, and the results are shown in Table 1. The online website Innovagen was used to analyze the solubility of peptides in water. The website divides the water solubility of peptides into two types: "Goodwater solubility" and "Poorwater solubility". The online website ToxinPred was used to predict the toxicity of active peptides. The final results are shown in Table 2. All 13 peptides were non-toxic and well soluble in water.

[0057] Table 1 PeptideRanker prediction scores of potential bioactive peptides

[0058]

[0059] Table 2 Predicted toxicity and physicochemical properties of 13 peptides

[0060]

[0061] Molecular docking

[0062] In order to gain a deeper understanding of the interaction mechanism between the 13 potential salt-enhanced peptides screened from soybean protein and the TMC4 receptor protein model, the TMC4 receptor was added to the DS software, and the solvent water molecules were removed and hydrogen atoms were added under the CHARMM force field environment. The constructed peptides were docked into the active cavity of the TMC4 structure using CDOCKER of the Discovery Studio software. The active position of the docking was: X=-59.1, Y=77, Z=72.4, the radius was 30, and the other parameters were the default values. The CDOCKER molecular docking results showed that all 13 potential salt-enhanced peptides were able to bind to the TMC4 cavity pocket and form a stable complex. Figure 2 The interaction of 13 potential salt-enhanced peptides with the binding sites around the TMC4 subunit was shown, with a total of 19 binding sites. Dipeptides (MR, PR, GR, and EF) mainly bind to the TMC4 receptor through Arg294, Glu319, Glu323, Arg583, and Ser585, among which Glu319 appears most frequently. Glu286, His293, Glu319, Ala584, and Ser585 are the main binding sites of tripeptides (MMR, PGR, DIF, DDF, QPR, and PGS) with the receptor, among which Ser585 forms multiple hydrogen bonds with the ligand. The pentapeptide (NPQPR) and octapeptide (PHHADADF) mainly bind through hydrogen bonds with Ala283, Arg294, Ala286, Arg294, and Arg583. Glu286, His293, Glu319, and Ser585 appear more frequently during the docking process and are potential key receptor binding sites. The docking results of 14 potential salt-enhancing peptides with TMC4 are shown in Table 3. Generally, lower CDOCKER energy values ​​indicate that the peptide has stronger ability to bind to the TMC4 receptor, higher affinity, and may have higher flavor intensity. Therefore, based on the molecular docking results of peptide-TMC4 and the structure of amino acids, DIF, QPR, MMR and DPIY were selected for subsequent research on salty taste enhancing peptides.

[0063] Table 3 Molecular docking results of potential salt-enhanced peptides and TMC4 receptor protein

[0064]

[0065] Interaction mechanism of molecular docking

[0066] The interaction between the four peptides and TMC4 salty taste receptor protein Figure 3 As shown, the tripeptide DIF mainly interacts through hydrogen bonds and hydrophobic interactions, among which Thr280, Ala283, and Ser585 bind with carbon-hydrogen bonds, form hydrogen bonds with Gln279, and interact with Ala158, His293, and Ala584 in the receptor through hydrophobic interactions. Figure 4 As shown in Figure 2, QPR mainly interacts with Ala283, His293, Ala584, and Ser585 amino acid residues through hydrogen bonds. Figure 5 As shown, the interaction between MMR and TMC4 receptor protein mainly forms hydrogen bonds with the receptor through Glu319, Glu286, Ser584, Asn588 and Gln279. In addition to forming hydrogen bonds with the ligand, Glu286 and Glu319 also have electrostatic interactions. Figure 6 As shown, the interaction between the ligand DPIY and the receptor protein of TMC4 is mainly based on hydrogen bonds and hydrophobic interactions. It forms hydrogen bonds with His293, Thr581, Ala584 and Ser585, and Ala158, Ala283, Val322, Glu319, Arg583 and Phe582 interact with the receptor through hydrophobic interactions. In the above docking process, we can invent that conventional hydrogen bonds, carbon-hydrogen bonds, electrostatic interactions and hydrophobic interactions are the main forces that stabilize the binding of ligands to receptors, among which hydrogen bonds and hydrophobic interactions are the main factors.

[0067] Solid phase peptide synthesis

[0068] Nanjing Peptide Valley Biotechnology Co., Ltd. was commissioned to synthesize peptides through solid phase synthesis.

[0069] Sensory evaluation

[0070] The sensory evaluation panel consisted of 12 laboratory members to ensure sufficient sample size and statistically significant results. To ensure the breadth and representativeness of the results, there were 8 females and 4 males aged between 20 and 30 years. The sensory evaluation panel members were in good physical condition, had good taste and no bad habits. They were trained in sensory training according to ISO 8586-1:2012 to enable them to judge the concentration of five basic flavor solutions. The flavor reference solutions were prepared as follows: 0.08% (w / v) quinine sulfate solution (bitter), 0.08% (w / v) citric acid solution (sour), 0.40% (w / v) sodium chloride solution (salty), 0.35% (w / v) monosodium glutamate solution (fresh), 1.00% (w / v) sucrose solution (sweet). These samples were sensory evaluated on a scale of 0-10, with 0 representing no taste and 10 representing the strongest taste. Five sample solutions of flavor intensity were prepared, with the salt content of 0.4% (w / v) NaCl solution as 5 points. For every 0.1% (w / v) increase or decrease in concentration, the saltiness score increased or decreased by 2 points. Panelists were asked to rinse their mouths with 30-40 ml of ultrapure water for 5 minutes between testing two different samples. The synthetic peptides were dissolved in 0.4% (w / v) sodium chloride solution to prepare a 0.02% (w / v) solution, and then different panelists scored and recorded the five flavors in turn. The results showed that all four peptides had a salt-enhancing effect, such as Figure 4 As shown in the figure, MMR has the most significant salt-enhancing effect. However, since the results of sensory evaluation are greatly affected by subjective factors, they cannot be used as the final conclusion and need to be further verified using an electronic tongue.

[0071] Electronic tongue analysis

[0072] Dissolve the four synthetic peptides DIF, QPR, MMR, and DPIY in deionized water. After the solution is completely dissolved, pour it into a beaker dedicated to the electronic tongue to identify the taste characteristics of the synthetic peptides. Using 0.4% (w / w) sodium chloride solution as a control, the four peptides were added to 0.4% (w / v) sodium chloride solution to prepare 0.02% (w / v) solutions to compare the saltiness of the peptides. The results are as follows: Figure 5 As shown. It can be seen that saltiness is the main factor affecting the overall flavor of the peptide, followed by freshness, while sourness has the weakest response (p<0.05). The significant difference in acidity compared with sodium chloride solution may be related to the composition of solubility. In terms of increasing the saltiness level, MMR and DPIY have the most significant effects, while DIF has the worst effect. All solutions show obvious umami and have a certain synergistic effect with saltiness and umami. The saltiness enhancement effect of the four peptides is shown in Figure 6As shown. Generally, when the electronic tongue shows a high negative response value to a substance, it indicates that the electronic tongue is relatively less sensitive to the flavor or chemical or has weaker flavor attributes. Compared with 0.4% sodium chloride solution, the saltiness value of each peptide solution at a concentration of 0.02% (w / w) was negative, indicating that the four peptides themselves had no salty taste. However, when mixed with 0.4% sodium chloride solution, the four peptide solutions at a concentration of 0.02% (w / w) all showed significant salt enhancement effects, among which MMR had the strongest salt enhancement ability, increasing by 40.35%, followed by DPIY (39.30%) and QPR (32.98%), while DIF (13.68%) had the worst salt enhancement effect (p<0.05). The results of the salinity value are basically consistent with the above molecular docking results. The lower the docking energy of the peptide binding to the TMC4 receptor, the more stable the conformation of the complex and the stronger the salt enhancement effect. This is basically consistent with the results of sensory evaluation analysis. Therefore, it can be proved that DIF, QPR, MMR and DPIY have significant saltiness-enhancing effects and can be used as new saltiness-enhancing peptides in soy protein.

[0073] The specific embodiments described above further illustrate the objectives, technical solutions and beneficial effects of the present invention in detail. It should be understood that the above description is only a specific embodiment of the present invention and is not intended to limit the present invention. Any modifications, equivalent substitutions, improvements, etc. made within the spirit and principles of the present invention should be included in the scope of protection of the present invention.

Claims

1. A salty taste enhancing peptide, characterized in that: The salty taste enhancing peptide is screened from soybean protein and binds to TMC4 receptor protein. The salty taste enhancing peptide is composed of one of the following peptides: The amino acid sequence is DIF, and the molecular weight is 393.47Da; The amino acid sequence is QPR, and the molecular weight is 399.48Da; The amino acid sequence is MMR, and the molecular weight is 436.62Da; The amino acid sequence is DPIY and the molecular weight is 506.60Da.

2. A salty taste enhancing peptide according to claim 1, characterized in that: In the salty taste enhancing peptide, the peptide segment with the amino acid sequence of DIF is molecularly docked with the receptor TMC4, and the main binding sites are Ala158, Gln279, Thr280, His293, Ala283, Glu286, Ala584 and Ser585.

3. A salty taste enhancing peptide according to claim 1, characterized in that: In the salty taste enhancing peptide, the peptide segment with the amino acid sequence of QPR is molecularly docked with the receptor TMC4, and the main binding sites are Ala283, His293, Glu319, Glu323, Ala584 and Ser585.

4. A salty taste enhancing peptide according to claim 1, characterized in that: In the salty taste enhancing peptide, the peptide segment with the amino acid sequence of MMR undergoes molecular docking with the receptor TMC4, and the main binding sites are Gln279, Glu286, His293, Glu319, Arg583, Ser585 and Asn588.

5. A salty taste enhancing peptide according to claim 1, characterized in that: In the salty taste enhancing peptide, the peptide segment with the amino acid sequence of DPIY is molecularly docked with the receptor TMC4, and the main binding sites are Ala158, Ala283, Glu286, His293, Glu319, Thr581, Phe582, Val322, Arg583, Ala584 and Ser585.

6. A salty taste enhancing peptide according to claim 1, characterized in that: The saltiness value of the peptide segment with the amino acid sequence of DIF is 3.24; and / or, the saltiness value of the peptide segment having the amino acid sequence of QPR is 3.79; and / or, the saltiness value of the peptide segment having the amino acid sequence of MMR is 4.00; And / or, the saltiness value of the peptide segment with the amino acid sequence of DPIY is 3.

97.

7. A method for screening salty taste enhancing peptides, characterized in that: Here are the steps: (1) Construct a TMC4 receptor protein model using the trRosetta online server and evaluate its reliability; The reliability evaluation is as follows: according to the Ramachandran diagram, the proportion of amino acid residues falling in the allowed region and the maximum allowed region in the entire protein is required to be higher than 90%; (2) Computer simulation of enzymatic hydrolysis of soy protein isolate to obtain enzymatic peptides with a sequence length of 3-10; (3) predicting the biological activity of the enzymatic peptides, screening out peptides with potential biological activity, predicting their physicochemical properties, and screening out non-toxic and water-soluble peptides; Among them, the screening criteria for the biological activity prediction are: prediction score>0.5; The screening criteria for toxicity prediction are: NonToxin; The screening criteria for water solubility prediction are: Good water solubility; (4) molecular docking the TMC4 receptor protein model with the non-toxic, water-soluble peptide segment of step (3) to form a receptor protein and small molecule ligand complex; Among them, the TMC4 receptor protein needs to remove water molecules and add hydrogen atoms under the CHARMM force field environment; The active position coordinates of the molecular docking are: X=-59.1, Y=77, Z=72.4, and the radius is 20; The molecular docking selects the largest cavity in the TMC4 receptor protein as the docking pocket; (5) Screening peptides with potential salt-increasing effects based on the molecular docking results and synthesizing the peptides by solid-phase synthesis; Wherein, the screening: selecting peptides with low energy values ​​in CDOCKER energy; (6) Performing sensory evaluation and electronic tongue analysis on the synthesized peptide segments to obtain the salty taste enhancing peptide according to any one of claims 1 to 6.

8. Use of the salty taste enhancing peptide according to any one of claims 1 to 5 in preparing condiments and foods.

9. A product containing the salty taste enhancing peptide selected from soy protein isolate according to any one of claims 1 to 5.

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