Salty peptide as well as composition and application thereof
By developing new salty peptides and compositions that can bind to the salty receptor SCNN1A, the problem that existing salty peptides are not widely used in the low-salt food field is solved, and the significant salty gain effect and food flavor maintenance are achieved under low sodium conditions.
Patent Information
- Application Number
- CN202510031954.7
- Authority / Receiving Office
- CN · China
- Patent Type
- Applications(China)
- Current Assignee / Owner
- Filing Date
- 2025-01-09
- Publication Date
- 2025-05-30
- Estimated Expiration
- Not applicable · inactive patent
AI Technical Summary
The existing salty peptides are not widely used in the fields of low-salt foods, food industry and pet food, and cannot effectively meet consumers' needs for healthy diets and low-salt products.
A new salty peptide and composition are developed to provide significant salty gain by combining with the salty receptor SCNN1A and applied in foods in the form of a salty seasoning.
This salty peptide can provide a salty taste similar to traditional edible salt under low sodium conditions, helping to reduce sodium intake, maintain food flavor, and improve food market competitiveness.
Smart Images
Figure CN120058871A_ABST
Abstract
Description
Technical Field
[0001] The present invention belongs to the technical field of protein active peptides, and particularly relates to salty peptides, their compositions and applications. Background Art
[0002] As a green and healthy salt substitute that can not only provide saltiness but also supplement essential amino acids for the human body, salty peptides have broad application prospects and development potential in the food industry. Salty peptides themselves have salty characteristics, and their saltiness is soft, delicate, mellow and rich, superior to salt and amino acid salty agents. When the mass concentration of the peptide substrate is certain, its saltiness evaluation value may be equal to or even higher than that of the same concentration of sodium chloride aqueous solution. With the increasing attention of consumers to healthy diets and the growing demand for low-salt products, since salty peptides can effectively reduce the sodium salt content in foods without reducing the original flavor of the foods, salty peptides are increasingly favored by consumers.
[0003] However, the current applications of existing salty peptides are still not extensive in fields such as low-salt foods, the food industry, and pet foods. With the improvement of consumers' health awareness, a low-salt diet has gradually become a trend. While maintaining health, low-salt foods also need to meet the demand for rich taste. Salty peptides have great potential in this field and can effectively enhance the taste of foods, enabling them to provide a rich taste experience even when the salt content is reduced. In the food industry, the demand for salt is mainly reflected in aspects such as anti-corrosion, flavoring, and improving the taste of foods. With the implementation of healthy diets, many food processing enterprises have started to reduce the use of salt in foods and search for suitable substitutes. Salty peptides can provide salt substitutes without increasing sodium, which is an important direction for the future development of the food industry. In the field of pet foods, with the increasing number of pet health problems, the ingredients of pet foods are gradually developing towards low-salt, low-fat, high-protein, etc. As a low-sodium and highly effective saltiness enhancer, salty peptides can make pet foods provide palatability while reducing the potential impact on pet health.
[0004] Although there are already many research results on salty peptides at present, in order to meet the needs of fields such as low-salt foods, the food industry, and pet foods, more types of salty peptides need to be developed. These new salty peptides not only need to have good saltiness perception intensity, but also need to be optimized in terms of production cost, stability, adaptability, etc., in order to promote the popularization of healthier foods and dietary patterns. Summary of the Invention
[0005] To overcome the deficiencies of the above-mentioned prior art, the purpose of the present invention is to provide salty peptides, their compositions and applications, which have the characteristics of significant saltiness enhancement effect, contributing to reducing sodium intake, and maintaining the flavor of foods.
[0006] To achieve the above purpose, the technical solution adopted by the present invention is:
[0007] A salty peptide has a salty taste and can bind to the salty taste receptor SCNN1A. The amino acid sequence of the salty peptide is any one of SEQ ID NO.1 to SEQ ID NO.25.
[0008] A salty peptide composition, which comprises at least two kinds of salty peptides with amino acid sequences as shown in SEQ ID NO.1 to SEQ ID NO.25.
[0009] A salt substitute seasoning, by mass percentage, comprises 55% - 70% of main ingredients, 25% - 35% of auxiliary ingredients and 1% - 6% of salty peptides, and the balance is spices.
[0010] Among them, the main ingredients are one or more of sodium glutamate, yeast extract, oyster sauce, fish sauce, edible salt and 5'-inosinic acid disodium; the auxiliary ingredients are one or more of glutinous rice flour, sodium alginate, xanthan gum, glucose, konjac powder, polyglutamic acid, soy protein, wheat starch, low methoxyl pectin, potato starch, pea starch, rice starch, pectin, erythritol, beet root powder, tapioca starch, adzuki bean powder, calcium stearate, sorghum powder, soy isoflavone and corn cellulose; the salty peptide is at least one of the salty peptides with amino acid sequences as shown in SEQ ID NO.1 to SEQ ID NO.25.
[0011] A food, which contains an additive, and the additive is the salty peptide described in claim 1 or the salty peptide composition described in claim 2 or the salt substitute seasoning described in claim 3.
[0012] Use of the described salty peptide or the described salty peptide composition or the described salt substitute seasoning in food preparation.
[0013] The food is a low-salt food. Low-salt foods specifically refer to those with the sodium content in every 100 grams of solid food or every 100 milliliters of liquid food strictly controlled within a low level not exceeding 120 milligrams, which are designed to meet the nutritional needs of special groups such as infants, the elderly, cardiovascular disease patients, etc. and the healthy diet standards for pets, aiming to effectively reduce the risk of excessive sodium intake, thereby maintaining the health status of these specific target groups.
[0014] The food is a seasoning.
[0015] The seasoning is a low-sodium food additive for compound seasoning powder, seasoning sauce and liquid seasoning.
[0016] The low-salt food is food for infants and the elderly, nutritional dietary food for cardiovascular patients or pet food.
[0017] A method for increasing the saltiness of food, which comprises adding a salty peptide, a salty peptide composition or a salt substitute seasoning to the food.
[0018] Compared with the prior art, the present invention has the following beneficial effects:
[0019] The salty peptide provided by the present invention is found to be able to bind to the salty receptor SCNN1A through molecular docking and has a specific salty threshold; through sensory evaluation, it is proved that a lower concentration of this salty peptide has a saltiness similar to that of traditional edible salt and provides a significant salty enhancement effect under low-sodium conditions. Therefore, this salty peptide can be added to food as a seasoning to replace part of the edible salt, thereby reducing sodium intake, which is of great significance for controlling hypertension and preventing cardiovascular diseases. While reducing the use of edible salt, it can help maintain the flavor of food, make low-salt food taste closer to full-salt food in terms of taste, and improve the acceptance of consumers. In low-salt food, it helps to improve the overall flavor balance of food, enhance the quality of food, and make the product more competitive in the market. In addition, for specific populations that need to limit their salt intake, such as hypertensive patients, the elderly, etc., low-salt food with salty peptides can meet their special needs for a healthy diet and contribute to promoting the food industry to develop in a healthier and more sustainable direction. Description of the Drawings
[0020] Figure 1 It is the mass spectrometry result diagram of SEQ ID NO.1.
[0021] Figure 2 It is the mass spectrometry result diagram of SEQ ID NO.2.
[0022] Figure 3 It is the mass spectrometry result diagram of SEQ ID NO.3.
[0023] Figure 4 It is the mass spectrometry result diagram of SEQ ID NO.4.
[0024] Figure 5 It is the mass spectrometry result diagram of SEQ ID NO.5.
[0025] Figure 6 It is the mass spectrometry result diagram of SEQ ID NO.6.
[0026] Figure 7 It is the mass spectrometry result diagram of SEQ ID NO.7.
[0027] Figure 8 It is the mass spectrometry result diagram of SEQ ID NO.8.
[0028] Figure 9 It is the mass spectrometry result diagram of SEQ ID NO.9.
[0029] Figure 10 It is the mass spectrometry result diagram of SEQ ID NO.10.
[0030] Figure 11 It is the mass spectrometry result diagram of SEQ ID NO.11.
[0031] Figure 12 It is the mass spectrometry result diagram of SEQ ID NO.12.
[0032] Figure 13 It is the mass spectrometry result diagram of SEQ ID NO.13.
[0033] Figure 14 It is the mass spectrometry result diagram of SEQ ID NO.14.
[0034] Figure 15 It is the mass spectrometry result diagram of SEQ ID NO.15.
[0035] Figure 16 It is the mass spectrometry result diagram of SEQ ID NO.16.
[0036] Figure 17 It is the mass spectrometry result diagram of SEQ ID NO.17.
[0037] Figure 18 It is the mass spectrometry result diagram of SEQ ID NO.18.
[0038] Figure 19 It is the mass spectrometry result diagram of SEQ ID NO.19.
[0039] Figure 20 It is the mass spectrometry result diagram of SEQ ID NO.20.
[0040] Figure 21 It is the mass spectrometry result diagram of SEQ ID NO.21.
[0041] Figure 22 It is the mass spectrometry result diagram of SEQ ID NO.22.
[0042] Figure 23 It is the mass spectrometry result diagram of SEQ ID NO.23.
[0043] Figure 24 It is the mass spectrometry result diagram of SEQ ID NO.24.
[0044] Figure 25 It is the docking diagram of SEQ ID NO.1 and SCNN1A.
[0045] Figure 26 It is the docking diagram of SEQ ID NO.1 and SCNN1A.
[0046] Figure 27 It is the docking diagram of SEQ ID NO.2 and SCNN1A.
[0047] Figure 28 It is the docking diagram of SEQ ID NO.3 and SCNN1A.
[0048] Figure 29 It is the docking diagram of SEQ ID NO.4 and SCNN1A.
[0049] Figure 30 It is the docking diagram of SEQ ID NO.5 and SCNN1A.
[0050] Figure 31 It is the docking diagram of SEQ ID NO.6 and SCNN1A.
[0051] Figure 32 It is the docking diagram of SEQ ID NO.7 and SCNN1A.
[0052] Figure 33 It is the docking diagram of SEQ ID NO.8 and SCNN1A.
[0053] Figure 34 It is the docking diagram of SEQ ID NO.9 and SCNN1A;
[0054] Figure 35 It is the docking diagram of SEQ ID NO.10 and SCNN1A.
[0055] Figure 36 It is the docking diagram of SEQ ID NO.11 and SCNN1A.
[0056] Figure 37 It is the docking diagram of SEQ ID NO.12 and SCNN1A.
[0057] Figure 38 It is the docking diagram of SEQ ID NO.13 and SCNN1A.
[0058] Figure 39 It is the docking diagram of SEQ ID NO.14 and SCNN1A.
[0059] Figure 40 It is the docking diagram of SEQ ID NO.15 and SCNN1A.
[0060] Figure 41 It is the docking diagram of SEQ ID NO.16 and SCNN1A.
[0061] Figure 42 It is the docking diagram of SEQ ID NO.17 and SCNN1A.
[0062] Figure 43 It is the docking diagram of SEQ ID NO.18 and SCNN1A.
[0063] Figure 44 It is the docking diagram of SEQ ID NO.19 and SCNN1A.
[0064] Figure 45 It is the docking diagram of SEQ ID NO.20 and SCNN1A.
[0065] Figure 46 It is the docking diagram of SEQ ID NO.21 and SCNN1A.
[0066] Figure 47 It is the docking diagram of SEQ ID NO.22 and SCNN1A.
[0067] Figure 48 It is the docking diagram of SEQ ID NO.23 and SCNN1A.
[0068] Figure 49 It is the docking diagram of SEQ ID NO.24 and SCNN1A.
[0069] Figure 50 It is the docking diagram of SEQ ID NO.25 and SCNN1A.
[0070] Figure 51 It is the surface force analysis diagram of the interaction between SCNN1A and the SEQ ID NO.1 salty peptide.
[0071] Figure 52 It is the surface force analysis diagram of the interaction between SCNN1A and the SEQ ID NO.2 salty peptide.
[0072] Figure 53 It is the surface force analysis diagram of the interaction between SCNN1A and the SEQ ID NO.3 salty peptide.
[0073] Figure 54 It is the surface force analysis diagram of the interaction between SCNN1A and the SEQ ID NO.4 salty peptide.
[0074] Figure 55 It is the surface force analysis diagram of the interaction between SCNN1A and the SEQ ID NO.5 salty peptide.
[0075] Figure 56 It is the surface force analysis diagram of the interaction between SCNN1A and the SEQ ID NO.6 salty peptide.
[0076] Figure 57 It is the surface force analysis diagram of the interaction between SCNN1A and the SEQ ID NO.7 salty peptide.
[0077] Figure 58 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 8.
[0078] Figure 59 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 9.
[0079] Figure 60 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 10.
[0080] Figure 61 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 11.
[0081] Figure 62 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 12.
[0082] Figure 63 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 13.
[0083] Figure 64 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 14.
[0084] Figure 65 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 15.
[0085] Figure 66 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 16.
[0086] Figure 67 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 17.
[0087] Figure 68 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 18.
[0088] Figure 69 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 19.
[0089] Figure 70 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO. 20.
[0090] Figure 71It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO.21.
[0091] Figure 72 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO.22.
[0092] Figure 73 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO.23.
[0093] Figure 74 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO.24.
[0094] Figure 75 It is a surface force analysis diagram of the interaction between SCNN1A and the salt-taste peptide of SEQ ID NO.25.
[0095] Figure 76 It is a salt-taste threshold enhancement diagram of the salt-taste peptides of SEQ ID NO.1 to SEQ ID NO.25 and NaCl.
[0096] Figure 77 It is a salt-taste enhancement effect diagram of the salt-taste peptides of SEQ ID NO.1 to SEQ ID NO.25. Detailed implementation manners
[0097] To enable those skilled in the art to understand the features and effects of the present invention, the following provides a general description and definition only for the terms and expressions mentioned in the specification and claims. Unless otherwise specified, all technical and scientific terms used herein shall have the ordinary meanings understood by those skilled in the art for the present invention. In case of conflict, the definitions in this specification shall prevail.
[0098] The present invention will be further described below in conjunction with specific embodiments. It should be understood that these embodiments are only used to illustrate the present invention and not to limit the scope of the present invention. In addition, it should be understood that after reading the content taught by the present invention, those skilled in the art can make various changes or modifications to the present invention, and these equivalent forms also fall within the scope defined by the appended claims of this application.
[0099] The following embodiments use conventional instruments and equipment in the art. The experimental methods without specific conditions noted in the following embodiments are usually carried out under conventional conditions or according to the conditions recommended by the manufacturers. Various raw materials used in the following embodiments are all commercially available products unless otherwise stated, and their specifications are the conventional specifications in the art.
[0100] It should be noted that the salty peptides involved in this article are not limited to being extracted by the extraction methods given in the following examples, and can also be obtained by artificial synthesis according to the amino acid sequences of the salty peptides given in the examples.
[0101] Example 1
[0102] A salty peptide, having a salty taste and capable of binding to the salty receptor SCNN1A, and the amino acid sequence of the salty peptide is SEQ ID NO.1.
[0103] Example 2
[0104] A salty peptide, having a salty taste and capable of binding to the salty receptor SCNN1A, and the amino acid sequence of the salty peptide is SEQ ID NO.13.
[0105] Example 3
[0106] A salty peptide, having a salty taste and capable of binding to the salty receptor SCNN1A, and the amino acid sequence of the salty peptide is SEQ ID NO.25.
[0107] Example 4
[0108] A salty peptide composition, the salty peptide composition comprising amino acid sequences SEQ ID NO.1 to SEQ ID NO.2.
[0109] Example 5
[0110] A salty peptide composition, the salty peptide composition comprising amino acid sequences SEQ ID NO.8 to SEQ ID NO.10.
[0111] Example 6
[0112] A salty peptide composition, the salty peptide composition comprising amino acid sequences SEQ ID NO.15 to SEQ ID NO.16.
[0113] Example 7
[0114] A salt substitute seasoning, by mass percentage, comprising 55% of main ingredient, 25% of auxiliary ingredient and 1% of salty peptide, and the balance is spices;
[0115] Wherein, the main ingredient is sodium glutamate; the auxiliary ingredient is glutinous rice flour; and the salty peptide is amino acid sequence SEQ ID NO.1.
[0116] Example 8
[0117] A salt substitute seasoning, by mass percentage, comprising 63% of main ingredient, 30% of auxiliary ingredient and 3.5% of salty peptide, and the balance is spices;
[0118] Among them, the main ingredient is fish sauce, and the auxiliary ingredient is pea starch; the salty peptide has an amino acid sequence such as SEQ ID NO. 113.
[0119] Example 9
[0120] A salt substitute seasoning, by mass percentage, includes 70% of the main ingredient, 35% of the auxiliary ingredient, and 6% of the salty peptide, with the balance being spices;
[0121] Among them, the main ingredient is disodium 5'-ribonucleotide, the auxiliary ingredient is corn cellulose; the salty peptide has an amino acid sequence such as SEQ ID NO. 25.
[0122] Example 10
[0123] A food, the food contains an additive, and the additive is a salty peptide. The food is a low-salt food. Low-salt foods specifically refer to those in which the sodium content in every 100 grams of solid food or every 100 milliliters of liquid food is strictly controlled within a low level not exceeding 120 milligrams. It is designed to meet the nutritional needs of special groups such as infants, the elderly, and cardiovascular disease patients, as well as the healthy diet standards for pets, aiming to effectively reduce the risk of excessive sodium intake and thus maintain the health status of these specific target groups.
[0124] Example 11
[0125] A food, the food contains an additive, and the additive is a salty peptide composition. The food is a seasoning.
[0126] Example 12
[0127] A food, the food contains an additive, and the additive is a salt substitute seasoning. The low-salt food is food for infants and the elderly, nutritional diet food for cardiovascular patients, or pet food.
[0128] Extraction of salty peptide in Example 13
[0129] Making mushroom soup: Take 69.6 g of mushrooms, wash and blanch for 5 min, add 1 g each of scallions and ginger, add high soup according to a liquid-to-material ratio of 2.5:1 (the high soup is prepared by taking 1.6 kg of pig leg bones, washing, cutting into pieces, putting them into cold water together with 10 g of scallions, 10 g of ginger, and 10 g of cooking wine, blanching for 30 min, skimming off the floating foam, then fishing them out, washing to remove the blood, frying the pig leg bones for 10 min, then adding 4 L of water, 10 g of scallions, 10 g of ginger, and 5 g of salt and boiling for 4 h), boil at 74 °C for 1.5 h, and take out of the pot and cool.
[0130] Making mushroom and chicken soup: Take 60 g of chicken pieces and 9.6 g of mushrooms, blanch them separately for 5 min, add 1 g each of scallions and ginger, add pure water according to a liquid-to-material ratio of 2.5:1, boil at 74 °C for 1.5 h, and take out of the pot and cool.
[0131] Separate the cooled shiitake mushroom soup and shiitake mushroom chicken soup, centrifuge to collect the supernatant, and remove impurities and solid particles. Filter the supernatant using an ultrafiltration membrane or other filtration techniques to remove macromolecules and microparticles. Finally, take an appropriate amount of the sample and desalt it through a C18 desalting column, and analyze the sample by LC-MS / MS equipped with an online nano-spray ion source.
[0132] Example 14 Identification of Salty Peptides
[0133] Perform sequence identification on the polypeptide obtained in Step 1 by mass spectrometry, and the mass spectrometry results are as Figures 1 to 25As shown, the amino acid sequences of the extracted polypeptides are as shown in SEQ ID NO.1 to SEQ ID NO.25 in Table 1, specifically: Ala-Ala-Glu-Lys-Ala-Gly-Tyr-Asn-Leu-Asp-Ser-Gln-Thr-Ala-Asp-Lys-Ile-Ser-Asn-Ala-Val-Ser-Glu-Gly-Leu-Gly-Lys-Phe-Gly-Gly-Lys-Trp, Lys-Asp-Leu-Val-Gln-Asp-Leu-Tyr-Leu-Lys-Glu-Ile-Lys-Gly-Tyr-Lys-Ala-Pro-Pro-Val-Ala-Lys-Asp-Ala-His-Val-Gly-Val-Val-Lys, Asn-Pro-Val-Thr-Ile-Val-Glu-Asp-Gly-Ala-Ser-Ser-Gly-Leu-Gln-Thr-Leu-Pro-Tyr-Gly-Arg-Ile-Leu, Ser-Gln-Lys-Ser-Thr-Thr-Gln-Lys-Ala-Gly-Asp-Ala-Leu-Ser-Ser-Asn-Ser-Asn-Glu-Asn-Glu-Asp-Ser-Leu-Leu-Thr-Lys-Ala-Gln-Asn-Ala-Ile-Gly-Leu-Gly-Asn-Ser-Gly-Asn-Ser-Arg, Ala-Pro-Ile-Thr-Leu-Gly-Ser-Pro-Pro-Gln-Glu-Phe-Lys-Val-Ile-Leu-Asp-Thr-Gly-Ser-Ser-Asn, Gly-Phe-Phe-His-His-Glu-Ser-Asp-Glu-Ala-Gln-Ala-Tyr-Asp-Gln-Val-Val-Asn-Ala-Pro-His-Lys-Ala-Glu, Gly-Phe-Phe-His-His-Glu-Ser-Asp-Glu-Ala-Gln-Ala-Tyr-Asp-Gln-Val-Val-Asn-Ala-Pro-His, Gly-Leu-Phe-Ser-Asp-Asp-Ser-Asp-Gln-Ala-Gln-Ala-Trp-Asp-Gln-Val-Asn-Asn-Ala-Pro-His-Lys-Ala-Glu-Leu-Ser-His-Glu,Ser-Thr-Ser-Gln-Glu-Ala-Glu-Ala-Ala-Ile-Ala-Ala-Leu-His-Glu-Gln-Glu-Leu-Asp-Gly-Arg-Leu-Ile-Lys, Gly-Leu-Phe-Ser-Asp-Asp-Ser-Asp-Gln-Ala-Gln-Ala-Trp-Asp-Gln-Val-Asn-Asn-Ala-Pro-His, Asp-Arg-Met-Val-Glu-Thr-Lys-Gly-Leu-Asp-Phe-Val-Asp-Lys-Glu-Lys-Ala-Lys-His-Gln, Asp-Arg-Ile-Val-Glu-Thr-Lys-Gly-Leu-Asp-Phe-Ile-Asp-Lys-Glu-Lys-Ala-Gln-Tyr-His, Glu-Thr-Lys-Gly-Leu-Asp-Phe-Ile-Asp-Lys-Glu-Lys-Ala-Gln, Ala-Lys-Lys-Gln-Leu-Glu-Ala-Gln-Phe, Ala-Thr-Phe-Ala-Gly-Gly-Phe-Ile-Asp-Arg, Ile-Gly-Leu-Gly-Asn-Ser-Gly-Asn-Ser-Arg, Lys-Lys-Gln-Leu-Glu-Ala-Gln-Phe, Ser-Gly-Pro-Pro-Gly-Pro-Ala-Gly-Pro-Arg, Gly-Arg-Pro-Gly-Leu-Pro-Gly-Pro-Ala, Pro-Gly-Gln-Pro-Gly-Ser-Pro-Gly-Pro-Ala-Gly-Lys-Glu-Gly, Ala-Ala-Phe-Ser-Gly-Ala-Phe-Val-Asp-Arg, Ala-Pro-Val-Pro-Pro-Lys-Thr-Leu-Ser-Ala-Ala, Gly-Leu-Ala-Gly-Pro-Gln-Gly-Pro-Arg, Ser-Val-Arg-Pro-Gly-Pro-Gly-Ser-Pro and Gly-Ala-Phe-Gly-Pro-Arg-Gly-Leu-Ala-Gly-Pro-Gln.,
[0134] Table 1 Identification Results of Salty Peptide Compositions
[0135]
[0136] Example 15 Evaluation of the Salty Taste Characteristics of Salty Peptides
[0137] The extracted taste peptides were verified and evaluated through sensory evaluation to ensure that they had the required taste effect and purity.
[0138] The AlphaFold2 software was used to establish a model of the salty taste receptor SCNN1A and the polypeptide extracted in the first step. The pdb files of the salty taste receptor SCNN1A and the extracted polypeptide were selected, and molecular docking was performed through Discovery Studio 2019. The docking results are as Figures 26 to 75 shown.
[0139] From Figures 26 to 50 it can be observed the specific binding position and binding angle of the extracted polypeptide on the receptor protein. The 3D map can show the amino acid residues and binding sites of the extracted polypeptide; from the analysis of the 3D map, the active sites of SCNN1A are mainly Arg438, Ala643, Gln239, Trp59, Arg50, Tyr51, Pro58, and Val56. Among them, the ones with the highest frequency are Ala643, Arg438, Trp59, and Arg50. Thus, it can be known that these active sites are the key binding sites. The 2D map can show the types of the key molecular bonds and the distances between molecules.
[0140] Figures 51 to 75 is the result of the interaction between the extracted polypeptide and the receptor protein. From the color depth in the figure, it can be seen that the ones with more obvious color depth comparison are the key interaction forces, and the main interactions between the extracted polypeptide and the SCNN1A receptor protein are aromatic interaction, hydrophobicity, and hydrogen bond interaction.
[0141] The above results indicate that the extracted polypeptides all belong to salty peptides.
[0142] Example 16 Sensory Evaluation of Salty Peptides
[0143] Ten volunteers (5 males and 5 females, aged between 23 and 26 years) without taste disorders and without a history of taste disorders were recruited and trained in advance to taste the basic salty taste, namely NaCl. To avoid the influence of the previous sample on the next sample, the group members were required to rinse their mouths with 50 mL of pure water between two samples.
[0144] The quantitative descriptive analysis method was used to conduct a sensory evaluation of the extracted salty peptides. According to the amino acid sequences shown in SEQ ID NO.1~SEQ ID NO.25 in Table 1, 25 corresponding salty peptides were synthesized respectively. Then the 25 salty peptides were fully dissolved in ultrapure water to prepare test solutions with a concentration of 2 mg / mL. Then they were respectively filled into sterilized bottles (each bottle was randomly numbered with three digits), denoted as P1~P25. At the same time, NaCl was made into a solution with a concentration of 2 mg / mL as the salty control solution for the next sensory evaluation.
[0145] The panelists were required to hold the test solution / salty control solution in their mouths for 10 s and then describe the taste of the sample, such as saltiness, and score its intensity. After scoring, rinse the mouth with 50 mL of pure water and wait for at least 1 min. After the taste in the mouth dissipated, then taste and score the next group of solutions. Finally, calculate the average value according to the scoring results.
[0146] The scoring results of each group are as Figure 76 shown. The 25 extracted salty peptides have the characteristics of enhancing the saltiness of food and can be used as seasonings (base materials and auxiliary materials) in the food field, which can meet the sensory needs while ensuring nutritional safety.
[0147] Example 17 Application of Salty Peptides
[0148] A salt substitute seasoning, by mass percentage, includes 55%~70% of main materials, 25%~35% of auxiliary materials, 1%~6% of salty peptides, and the balance is spices;
[0149] Among them, the main materials are one or more of sodium glutamate, yeast extract, oyster sauce, fish sauce, edible salt, and 5'-ribonucleotide disodium; the auxiliary materials are one or more of starch, glutinous rice flour, sodium alginate, xanthan gum, glucose, konjac powder, polyglutamic acid, soy protein, wheat starch, low-methoxyl pectin, potato starch, pea starch, rice starch, pectin, erythritol, beet root powder, tapioca starch, adzuki bean powder, calcium stearate, sorghum powder, soy isoflavone, and corn cellulose; the salty peptides are one or more of the polypeptides with amino acid sequences shown in SEQ ID NO.1~SEQ ID NO.25.
[0150] By adding different contents (1%, 2%, 3%, 4%, 5%, and 6%) of salty peptides to the salt substitute seasoning, the influence of the addition amount of the salty peptide composition on the salty effect was explored, as follows:
[0151] 1), A salt substitute seasoning, by mass percentage, includes 35% edible salt, 30% fish sauce, 15% glutinous rice flour, 18% pectin, 1% salty peptide, and 1% spice. The salty peptide is obtained by mixing 25 kinds of salty peptides shown in SEQ ID NO.1 to SEQ ID NO.25 in equal proportions.
[0152] 2), A salt substitute seasoning, by mass percentage, includes 35% edible salt, 30% fish sauce, 15% glutinous rice flour, 17% pectin, 2% salty peptide, and 1% spice. The salty peptide is obtained by mixing 25 kinds of salty peptides shown in SEQ ID NO.1 to SEQ ID NO.25 in equal proportions.
[0153] 3), A salt substitute seasoning, by mass percentage, includes 35% edible salt, 30% fish sauce, 15% glutinous rice flour, 16% pectin, 3% salty peptide, and 1% spice. The salty peptide is obtained by mixing 25 kinds of salty peptides shown in SEQ ID NO.1 to SEQ ID NO.25 in equal proportions.
[0154] 4), A salt substitute seasoning, by mass percentage, includes 35% edible salt, 30% fish sauce, 15% glutinous rice flour, 15% pectin, 4% salty peptide, and 1% spice. The salty peptide is obtained by mixing 25 kinds of salty peptides shown in SEQ ID NO.1 to SEQ ID NO.25 in equal proportions.
[0155] 5), A salt substitute seasoning, by mass percentage, includes 35% edible salt, 30% fish sauce, 15% glutinous rice flour, 14% pectin, 5% salty peptide, and 1% spice. The salty peptide is obtained by mixing 25 kinds of salty peptides shown in SEQ ID NO.1 to SEQ ID NO.25 in equal proportions.
[0156] 6), A salt substitute seasoning, by mass percentage, includes 35% edible salt, 30% fish sauce, 14% glutinous rice flour, 14% pectin, 6% salty peptide, and 1% spice. The salty peptide is obtained by mixing 25 kinds of salty peptides shown in SEQ ID NO.1 to SEQ ID NO.25 in equal proportions.
[0157] Meanwhile, a seasoning formed by 35% edible salt, 30% fish sauce, 14% glutinous rice flour, 14% pectin, and 1% spice is used as a control, and the salt substitute seasonings of each group are scored according to the aforementioned sensory evaluation method of the salty peptide.
[0158] The scoring results of each group are as Figure 77As shown, with the increase in the content of the salty peptide composition, the salty effect of the salt substitute seasoning is enhanced, indicating that the extracted salty peptides have an obvious synergistic effect on the salt substitute seasoning.
[0159] The above content is only to illustrate the technical idea of the present invention and cannot be used to limit the protection scope of the present invention. Any modifications made on the basis of the technical solution according to the technical idea proposed by the present invention fall within the protection scope of the claims of the present invention.
Claims
1. A salty peptide, characterized in that The salty peptide can bind to the salty taste receptor SCNN1A, and the amino acid sequence of the salty taste peptide is any one of SEQ ID NO.1 to SEQ ID NO.
25.
2. A salty peptide composition, characterized in that: The salty peptides include at least two of the salty peptides shown in the amino acid sequences SEQ ID NO.1 to SEQ ID NO.
25.
3. A salt substitute seasoning, characterized in that: In terms of mass percentage, it includes 55% to 70% of main ingredients, 25% to 35% of auxiliary ingredients and 1% to 6% of salty peptides, and the remainder is spices; The main ingredients are one or more of monosodium glutamate, yeast extract, oyster sauce, fish sauce, edible salt and disodium 5'-ribonucleotide; the auxiliary ingredients are one or more of glutinous rice flour, sodium alginate, xanthan gum, glucose, konjac flour, polyglutamic acid, soy protein, wheat starch, low methoxyl pectin, potato starch, pea starch, rice starch, pectin, erythritol, beetroot powder, cassava starch, red bean powder, calcium stearate, sorghum powder, soy isoflavones and corn cellulose; and the salty peptide is at least one of the salty peptides shown in the amino acid sequences SEQ ID NO.1 to SEQ ID NO.
25.
4. A food, characterized in that The food contains additives, which are salty peptides or salty peptide compositions or salt-substitute seasonings.
5. Use of the salty peptide according to claim 1, the salty peptide composition according to claim 2, or the salt substitute seasoning according to claim 3 in food preparation.
6. The use according to claim 5, characterized in that: The food is a low-salt food.
7. The use according to claim 5, characterized in that: The food is a seasoning.
8. The use according to claim 7, characterized in that: The seasoning is a low-sodium food additive for compound seasoning powder, seasoning sauce and liquid seasoning.
9. The use according to claim 5, characterized in that: The low-salt food is food for infants and the elderly, nutritional dietary food for cardiovascular patients or pet food.