Preparation method and application of oat active peptide for promoting secretion of glp-1

Abstract

The application provides a preparation method and application of oat active peptides for promoting GLP-1 secretion, wherein the oat active peptides contain any one or more of peptide segments NDQRGEII, KQGDVIALPA, PFVQQQQ and PSEQYQPYPEQQEPFVQ. The preparation method of the oat active peptides comprises enzymolysis, chemical synthesis or genetic engineering. The oat active peptides can significantly promote the secretion of GLP-1 by intestinal endocrine cells, and have the advantages of safe and non-toxic side effects, tolerance to gastrointestinal digestive enzyme hydrolysis and easy absorption. The application has simple operation, low requirement for equipment, is suitable for industrial large-scale production, and can be used for the development of new drugs for controlling blood sugar or food for assisting in controlling blood sugar, drugs for controlling body weight or food for assisting in controlling body weight and the like.

Description

TECHNICAL FIELD

[0001] The application belongs to the field of biological small molecule peptides, and particularly relates to a preparation method and application of an oat active peptide for promoting GLP-1 secretion. BACKGROUND

[0002] Diabetes, especially type II diabetes, is closely related to insulin resistance and impaired beta cell function. Glucagon-like peptide-1 (GLP-1) is an intestinal insulinotropic hormone secreted by L cells in the intestinal tract, which plays a key role in the regulation of blood glucose homeostasis. GLP-1 can promote insulin secretion, inhibit glucagon release, delay gastric emptying, and increase satiety in a glucose concentration-dependent manner, thereby efficiently and safely lowering blood glucose. Therefore, the GLP-1 signaling pathway has become an important target for the treatment of type II diabetes. At present, the clinical treatment strategies based on GLP-1 mainly include two categories: one is to use GLP-1 receptor agonists (such as liraglutide, semaglutide, etc.), and the other is to use dipeptidyl peptidase-4 (DPP-4) inhibitors (such as sitagliptin) to delay the degradation of endogenous GLP-1. However, these drugs are mostly chemically synthesized or biologically engineered, which has some limitations:

[0003] (1) High cost: high research and production costs, leading to high treatment costs, which brings heavy economic burden to patients and society;

[0004] (2) Inconvenient administration: most GLP-1 receptor agonists need to be injected subcutaneously, and the patient compliance is poor;

[0005] (3) Potential side effects: may cause gastrointestinal discomfort (such as nausea, vomiting, diarrhea) and other adverse reactions;

[0006] (4) Non-natural source: some patients have psychological resistance or safety concerns about synthetic drugs.

[0007] Therefore, it is of great significance to develop a natural source, high safety, orally available and effective active substance for promoting the secretion of endogenous GLP-1 for the prevention and adjuvant treatment of diabetes and related metabolic diseases. Calcium-sensing receptor (CaSR) as a widely expressed G protein-coupled receptor is an important target for the development of functional active ingredients for GLP-1 secretion. It not only senses extracellular calcium ion concentration, but also can be specifically activated by various amino acids and peptides. Studies have shown that active peptides derived from food proteins can act as allosteric agonists to bind to CaSR, induce changes in receptor conformation, and then activate the downstream signaling pathway. It is particularly worth noting that the activation of CaSR on the surface of intestinal L cells can effectively stimulate the secretion of GLP-1.

[0008] Food-derived bioactive peptides have attracted much attention due to their natural, safe, easily absorbed and various bioactivities. Oat, as a kind of nutritionally complete whole grain resource, is rich in high-quality protein and is an ideal raw material for preparing bioactive peptides. At present, it has been reported that the peptides with antioxidant, antihypertensive (ACE inhibition) or immunomodulatory activities can be obtained by enzymatic hydrolysis of oat protein. However, so far, there is no report or disclosure that specific enzymatic hydrolysis of oat protein can obtain active peptides with the function of significantly promoting GLP-1 secretion, and there is no clear amino acid sequence, preparation method and application in the prevention or adjuvant treatment of diabetes. The unique composition of oat protein contains a large number of potential bioactive sequences that can be released by enzymatic hydrolysis, indicating its great potential as a CaSR agonist peptide. Therefore, using enzymatic hydrolysis technology to prepare active peptides from oat protein that can efficiently activate CaSR and indirectly promote the secretion of endogenous GLP-1 has become an attractive and urgently needed innovative strategy in the field of nutritional intervention for metabolic diseases such as diabetes and obesity. In view of the above background, the present application aims to provide a novel preparation method and application of oat active peptide for this purpose.

[0009] The existing technology on the enzymatic hydrolysis process of oat protein is mainly focused on improving the solubility of protein or obtaining general antioxidant peptides, and the enzymatic hydrolysis process lacks specificity, the bioactivity of the obtained peptide product is single and unstable, especially for the specific function of promoting GLP-1 secretion, there are problems such as weak purpose, low activity and unclear mechanism.

[0010] In summary, there is an urgent need in the art to efficiently and directionally prepare specific peptide sequences with strong GLP-1 secretion promoting activity from natural oat protein, and to clarify the preparation method and application in improving blood glucose, in order to fill the gap in the prior art. Therefore, developing active peptides with the function of promoting GLP-1 secretion from oat hydrolyzed protein has great economic and social benefits, which can not only be used as functional ingredients of health foods, but also be applied to produce a new generation of anti-diabetic drugs, and has a very broad prospect. SUMMARY

[0011] In view of the above technical problems, the first object of the present application is to provide an oat active peptide for promoting GLP-1 secretion.

[0012] The second object of the present application is to provide a preparation method of the oat active peptide.

[0013] The third object of the present application is to provide a preparation method of an enzymatic hydrolysate containing the oat active peptide.

[0014] The fourth object of the present application is to provide an application of the oat active peptide in preparing a medicine for controlling blood glucose or a food for adjuvantly controlling blood glucose.

[0015] A fifth object of the present application is to provide the use of the oat active peptide in the preparation of a medicine for controlling body weight or a food for assisting in controlling body weight.

[0016] Technical solution: An oat active peptide for promoting GLP-1 secretion, containing any one or more of peptide segments NDQRGEII, KQGDVIALPA, PFVQQQQ, and SEQYQPYPEQQEPFVQ; the amino acid sequence of the peptide segment NDQRGEII is shown in SEQ ID NO. 1, and the amino acid sequence is Asn-Asp-Gln-Arg-Gly-Glu-Ile-Ile; the amino acid sequence of the peptide segment KQGDVIALPA is shown in SEQ ID NO. 2, and the amino acid sequence is Lys-Gln-Gly-Asp-Val-Ile-Ala-Leu-Pro-Ala; the amino acid sequence of the peptide segment PFVQQQQ is shown in SEQ ID NO. 3, and the amino acid sequence is Pro-Phe-Val-Gln-Gln-Gln-Gln; the amino acid sequence of the peptide segment PSEQYQPYPEQQEPFVQ is shown in SEQ ID NO. 4, and the amino acid sequence is Pro-Ser-Glu-Gln-Tyr-Gln-Pro-Tyr-Pro-Glu-Gln-Gln-Glu-Pro-Phe-Val-Gln.

[0017] The preparation method of the above-mentioned oat active peptide includes enzymatic hydrolysis, chemical synthesis, or genetic engineering.

[0018] The above-mentioned enzymatic hydrolysis is to obtain the oat active peptide by enzymatic hydrolysis of oat protein, and the specific method includes the following steps:

[0019] S1. Crush oat bran and mix with water, adjust the pH value of the material liquid, add alkaline protease for enzymatic hydrolysis, and obtain a crude protein liquid;

[0020] S2. Add neutral protease and flavor protease to the crude protein liquid for second enzymatic hydrolysis, and prepare a second enzymatic hydrolysis liquid;

[0021] S3. Add acid protease to the second enzymatic hydrolysis liquid for third enzymatic hydrolysis, inactivate the third enzymatic hydrolysis liquid, first perform solid-liquid separation and decolorization, then perform microfiltration and ultrafiltration, finally concentrate, sterilize, and prepare an oat hydrolyzed protein liquid;

[0022] S4. Dry, screen, and magnetically select the oat hydrolyzed protein liquid to prepare an oat hydrolyzed protein, and the oat hydrolyzed protein contains the oat active peptide.

[0023] As a preferred, the mass-volume ratio of oat bran to water in step S1 is 1:8-12.

[0024] Preferably, the pH of the liquid in step S1 is 7.5-8.5.

[0025] Preferably, the amount of alkaline protease added in step S1 is 2-10 wt%.

[0026] Preferably, the temperature of enzymolysis in step S1 is 50-65℃, and the time of enzymolysis is 1-3 h.

[0027] Preferably, the amount of neutral protease added in step S2 is 0.1-5 wt%.

[0028] Preferably, the amount of flavor protease added in step S2 is 0.1-1 wt%.

[0029] Preferably, the pH of enzymolysis in step S2 is 6.5-7.5, the temperature of enzymolysis is 50-65℃, and the time of enzymolysis is 0.5-1.5 h.

[0030] Preferably, the amount of acid protease added in step S3 is 0.5-5 wt%.

[0031] Preferably, the pH of enzymolysis in step S3 is 6.0-7.0, the temperature of enzymolysis is 50-65℃, and the time of enzymolysis is 0.5-1.5 h.

[0032] Preferably, the temperature of enzyme inactivation in step S3 is 90-95℃, and the time of enzyme inactivation is 10-30 min.

[0033] Preferably, the pore size of microfiltration in step S3 is 0.22-1.0 μm.

[0034] Preferably, the pore size of ultrafiltration in step S3 is 5-10 kDa.

[0035] The above chemical synthesis method is to synthesize the oat active peptide by using the traditional solid-phase synthesis method.

[0036] The above genetic engineering method is based on DNA recombination technology, and the sequence synthesis of polypeptide is controlled by a suitable DNA template.

[0037] The above oat active peptide is used in the preparation of a medicine for controlling blood sugar or a food for assisting in controlling blood sugar.

[0038] The above oat active peptide is used in the preparation of a medicine for controlling weight or a food for assisting in controlling weight.

[0039] Beneficial effects:

[0040] 1. The present application provides an oat active peptide which can promote GLP-1 secretion, containing any one or more of the peptide segments NDQRGEII, KQGDVIALPA, PFVQQQQ and PSEQYQPYPEQQEPFVQ, and the oat active peptide can be obtained by artificial synthesis or enzymatic hydrolysis of oat protein. In animal experiments, oat hydrolyzed protein containing oat active peptide at a dose of 125 mg / kg can significantly increase the GLP-1 level in mouse serum, about 5 times higher than the control group during 2-3 h after intervention, fully verifying its significant GLP-1 promoting effect in vivo. In cell level experiments, four oat active peptide segments synthesized by chemical solid phase method can significantly stimulate STC-1 cells to secrete GLP-1 at a concentration of 5 mmol / L, and the GLP-1 secretion amount is increased to 1.4-1.8 times compared with the blank group, showing excellent GLP-1 secretion promoting ability.

[0041] 2. The present application provides a preparation method of oat active peptide obtained by enzymatic hydrolysis of oat protein, which is prepared by using oat protein as raw material, homogenizing treatment, and then using triple-step enzymatic hydrolysis technology for controllable enzymatic hydrolysis, and then filtering, concentrating, drying, screening and magnetic separation to obtain oat hydrolyzed protein containing oat active peptide. The process is simple in operation, low in equipment requirement, safe in preparation of oat active peptide without toxic side effects, excellent in flavor, no obvious bitter or astringent taste, suitable in taste, easy to apply in functional products, and has good industrialization amplification potential. BRIEF DESCRIPTION OF DRAWINGS

[0042] Figure 1 Effect of oat hydrolyzed protein on GLP-1 secretion of mouse STC-1 cells;

[0043] Figure 2 Oat hydrolyzed protein mass spectrum;

[0044] Figure 3 Distribution of oat active peptides NDQRGEII and KQGDVIALPA in oat 12S seed storage globulin 1;

[0045] Figure 4 Distribution of oat active peptides PFVQQQQ and PSEQYQPYPEQQEPFVQ in oat alcohol-soluble protein;

[0046] Figure 5 Effect of oat active peptides of examples 4-7 on STC-1 cell viability;

[0047] Figure 6 Effect of oat active peptides of examples 4-7 on GLP-1 secretion of STC-1 cells. DETAILED DESCRIPTION

[0048] The application will be further described in connection with the following examples, which are intended to be illustrative only and not limiting of the application.

[0049] The enzyme activity of the alkaline protease involved in the following examples and comparative examples was 200,000 U / g, purchased from Ningxia Xiasen Industrial Group Co., Ltd.; the enzyme activity of the neutral protease was 50,000 U / g, purchased from Henan Xinyangshao Biological Technology Co., Ltd.; the enzyme activity of the flavor protease was 50,000 U / g, purchased from Yantai Mai Tel Biological Technology Co., Ltd.; and the enzyme activity of the acid protease was 100,000 U / g, purchased from Nanning Pangbo Biological Engineering Co., Ltd.

[0050] Example 1

[0051] This example is a preparation method of oat hydrolyzed protein, comprising the following steps:

[0052] S1. 100 g of oat bran was crushed and added to 800 mL of water, and stirred uniformly at 60°C, the pH value of the material liquid was adjusted to 7.5, 2 wt% of alkaline protease was added, and enzymolysis was performed at 60°C for 3.0 h to prepare a crude protein liquid;

[0053] S2. The pH value of the crude protein liquid was adjusted to 7.0, 0.5 wt% of neutral protease and 0.1 wt% of flavor protease were added, and enzymolysis was performed at 65°C for 1.0 h to prepare a second enzymolysis liquid;

[0054] S3. The pH value of the second enzymolysis liquid was adjusted to 7.0, 0.5 wt% of acid protease was added, and enzymolysis was performed at 55°C for 0.5 h to prepare a third enzymolysis liquid;

[0055] S4. The temperature of the third enzymolysis liquid was increased to 95°C for enzyme inactivation, after solid-liquid separation and decolorization, the third enzymolysis liquid was first filtered through a microfiltration membrane with a pore size of 0.45 μm, and then filtered through an ultrafiltration membrane with a pore size of 10 kDa, after sterilization, drying, screening and magnetic separation, oat hydrolyzed protein was prepared.

[0056] Example 2

[0057] This example is the effect of oat hydrolyzed protein on the secretion of GLP-1 by intestinal endocrine cells in mice, comprising the following steps:

[0058] S1. After the ICR mice were adaptively fed for 1 week, they were randomly divided into 8 groups (6 in each group);

[0059] S2. The control group was given physiological saline by gavage, and the experimental group was given oat hydrolyzed protein prepared in Example 1 (125 mg / kg body weight) by gavage. At 0 min, 15 min, 30 min, 60 min, 90 min, 120 min, 180 min, 240 min and 360 min after gavage, the eyeballs were removed to take blood, which was placed in a centrifuge tube containing EDTA (final concentration 1 mg / mL) and aprotinin (final concentration 0.6 TIU / mL). The supernatant was obtained by centrifugation, and the GLP-1 hormone content in the serum was detected by using a commercial GLP-1 kit from Nanjing Jiancheng Biological Engineering Institute by ELISA method.

[0060] As shown in Figure 1 The GLP-1 in the serum of the control group (physiological saline) maintained at about 57 pg / mL during this period, and the oat hydrolyzed protein (Example 1) could quickly increase the serum GLP-1 level to about 80 pg / mL after 15 min of intervention, and could increase the serum GLP-1 level by about 5 times after 120 min of intervention, indicating that the oat hydrolyzed protein can increase the GLP-1 level in the mouse body, and at the same time, it shows that the oat hydrolyzed protein has the advantages of resisting gastrointestinal digestive enzyme digestion and easy absorption.

[0061] Example 3

[0062] This example is to analyze the mass spectrum and separate the protein of the oat hydrolyzed protein prepared in Example 1, which includes the following steps:

[0063] S1. The oat hydrolyzed protein was dissolved and ultrafiltered through a 10 KDa ultrafiltration tube, desalted by using a Waters SEP-PAK C18 solid phase extraction column, freeze-dried, redissolved with 1% formic acid aqueous solution, centrifuged, and the supernatant was subjected to chromatography-mass spectrometry detection;

[0064] S2. The A liquid used in liquid phase is 0.1% formic acid aqueous solution, and the B liquid is 0.1% formic acid acetonitrile aqueous solution (acetonitrile is 80%). The liquid chromatography column (50 μm*150 mm, Acclaim PepMapTM RSLC, Thermo Scientific Technology Inc) is equilibrated with 92% A liquid, the injection amount is 1 μL, and the related liquid phase gradient is set as follows: 0~98 min, B liquid linear gradient is 8~28%; 9~113 min, B liquid linear gradient is 28~37%; 113~117 min, B liquid linear gradient is 37~100%; 117~120 min, B liquid maintains at 100%;

[0065] S3. The raw mass spectrometry test files were retrieved using Proteome Discoverer 2.5 software to search relevant databases, yielding 190 peptides. Twenty-two peptides with a relative content >1.0% were retained. The calcium-sensitive receptor (CaSR) structure and its ligand peptide sequence and 3D structure data were collected from the public database UniProt (https: / / www.uniprot.org / ) to construct a training dataset. Subsequently, the multiple sequence alignment tool Clustal Omega was used to identify key conserved residues in the CaSR binding domain, and a 3D model of the receptor-peptide complex was generated based on AlphaFold2 (https: / / alphafold2.biodesign.ac.cn / ). Then, the molecular docking software AutoDock Vina (Scripps, USA) was used to simulate the binding modes of the 22 peptides with a relative content >1.0% to CaSR, calculating parameters such as binding free energy, hydrogen bond interaction, and spatial complementarity. Finally, a peptide binding affinity prediction score was output. The four oat bioactive peptides with the highest predicted scores are NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ.

[0066] like Figure 2 The image shown is a mass spectrum of hydrolyzed oat protein.

[0067] Oat proteins are mainly globulins, with the amino acid sequence of oat 12S seed storage globulin 1 shown in SEQ ID NO. 5 and the amino acid sequence of oat gliadin shown in SEQ ID NO. 6.

[0068] like Figure 3 As shown, oat bioactive peptides NDQRGEII and KQGDVIALPA exist in oat protein, therefore, oat bioactive peptides NDQRGEII and KQGDVIALPA can be prepared from oat protein.

[0069] like Figure 4 As shown, oat bioactive peptides PFVQQQQ and PSEQYQPYPEQQEPFVQ exist in oat protein, therefore, oat bioactive peptides PFVQQQQ and PSEQYQPYPEQQEPFVQ can be prepared from oat protein.

[0070] Example 4

[0071] This example illustrates the effects of the oat bioactive peptide NDQRGEII (Asn-Asp-Gln-Arg-Gly-Glu-Ile-Ile) on the viability and GLP-1 secretion of STC-1 cells, including the following steps:

[0072] S1. The oat active peptide NDQRGEII was synthesized by Nanjing Jinsswai Biological Technology Co., Ltd. using solid-phase synthesis method, and the purity of the synthesized peptide was verified to be greater than 95% by high-performance liquid chromatography and mass spectrometry;

[0073] S2. STC-1 cells were cultured in DMEM medium containing 10% fetal bovine serum (FBS), 1% non-essential amino acids (NEAA), 100 U / mL penicillin and 0.1 mg / mL streptomycin, and the cells were incubated at 37°C in a cell incubator containing 5% CO2, and when the density reached 80~90%, the cells were subcultured by trypsin digestion;

[0074] S3. STC-1 cell activity determination: the effect of oat active peptide on STC-1 cell activity was tested and evaluated by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) cell proliferation and cytotoxicity test: MTT was added to the STC-1 cells after treatment in a 96-well plate, and metabolically active cells would cleave the yellow tetrazolium salt MTT into purple formazan crystals, and the formed formazan was dissolved, and the absorbance was measured at a detection wavelength of 570 nm by an enzyme-labeled instrument, and the results were expressed as a percentage of the control group;

[0075] S4. Determination of the amount of hormone GLP-1 secreted by STC-1 cells: the oat active peptide was dissolved in Hank's buffer to prepare a 5 mmol / L peptide solution, and STC-1 cells were inoculated in a 24-well culture plate at a density of 1.25×10 5 cells; when the cells reached 80~90% density, the cells were washed twice with Hank's buffer to remove the culture medium; the peptide solution was added to the STC-1 cells, and the cells were incubated in an incubator at 37°C for 2 h, centrifuged at 1000×g for 20 min, and the supernatant was taken to determine the GLP-1 content using a commercial GLP-1 kit from Nanjing Jiancheng Biological Engineering Institute.

[0076] Example 5

[0077] This example is the effect of oat active peptide KQGDVIALPA (Lys-Gln-Gly-Asp-Val-Ile-Ala-Leu-Pro-Ala) on the activity of STC-1 cells and the secretion of GLP-1, and the specific steps are the same as in Example 4.

[0078] Example 6

[0079] This example is the effect of oat active peptide PFVQQQQ (Pro-Phe-Val-Gln-Gln-Gln-Gln) on the activity of STC-1 cells and the secretion of GLP-1, and the specific steps are the same as in Example 4.

[0080] Example 7

[0081] This example is the effect of oat active peptide PSEQYQPYPEQQEPFVQ (Pro-Ser-Glu-Gln-Tyr-Gln-Pro-Tyr-Pro-Glu-Gln-Gln-Glu-Pro-Phe-Val-Gln) on the viability of STC-1 cells and the secretion of GLP-1, and the specific steps are the same as in Example 4.

[0082] As shown in Table 1, oat active peptides NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ had no significant change in the viability of STC-1 cells at the test concentration (0, 5, 10 mmol / L) compared with the control group, indicating that oat active peptides NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ were not toxic to cells. Figure 5 As shown in Table 2, oat active peptides NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ could all significantly promote the secretion of GLP-1 by intestinal endocrine cells STC-1. At present, a large number of studies have confirmed that GLP-1 has physiological functions such as promoting the secretion of insulin, promoting the proliferation and inhibiting the apoptosis of pancreatic beta cells, inhibiting the secretion of glucagon after meals, reducing the synthesis of liver glycogen, improving the sensitivity of insulin, and controlling appetite, so increasing the secretion of GLP-1 is of great significance for the prevention and treatment of type II diabetes.

[0083] Figure 6 Example 8

[0084] This example is the sensory evaluation of the oat hydrolyzed protein prepared in Example 1, including the following steps:

[0085] This example is the sensory evaluation of the oat hydrolyzed protein prepared in Example 1, including the following steps:

[0086] S1. Recruit and train 20 sensory evaluators (half male and half female, aged 25-45 years old), all evaluators have no smoking history, normal sensory function, and have undergone basic taste recognition training;

[0087] S2. Accurately weigh 1.0 g of oat active peptide product and control sample (commercial soy peptide powder and commercial wheat peptide powder) respectively, dissolve in 100 mL of normal temperature pure water to prepare a 1% (w / v) solution as the test solution, all samples are numbered with random three-digit numbers, and the evaluation is carried out in the same light and odor-free environment;

[0088] ​S3. Using quantitative descriptive analysis method, the evaluator tastes each test liquid (about 5-10 mL each time, rinses the mouth after tasting, and interval 2 min to eliminate sensory fatigue), and scores according to the following indexes according to 0-5 points (0 points represent no feeling, and 5 points represent extremely strong intensity):

[0089] Bitterness: characteristic bitterness intensity;

[0090] Astringency: intensity of the feeling of contraction and dryness in the mouth;

[0091] Unpleasant aftertaste: intensity of the unpleasant taste remaining after swallowing;

[0092] Overall acceptability: the degree of acceptance of the overall flavor of the sample (1 point: completely unacceptable; 5 points: very delicious).

[0093] Table 1 Sensory score table

[0094]

[0095] As shown in Table 1, the 1% aqueous solution of the oat hydrolyzed protein powder prepared by the method of the present application has significantly lower scores for bitterness, astringency and unpleasant aftertaste than the commercially available ordinary plant peptide product (* p<0.01), and the overall acceptability score is much higher than that of the control sample (* p<0.01). Specifically, it has a soft taste, only a very weak and easily acceptable basic taste, no obvious bitter and astringent taste characteristic of peptides, and no unpleasant residual feeling in the mouth after swallowing.

[0096] The above only describes the preferred embodiments of the present application and does not limit the present application in any form. Any person skilled in the art can make many possible changes and modifications to the technical solutions of the present application, or modify equivalent embodiments, without departing from the spirit and technical solutions of the present application, using the disclosed methods and technical contents. Therefore, any simple modification, equivalent replacement, equivalent change and modification of the above embodiments according to the technical essence of the present application, which does not deviate from the technical solutions of the present application, still belongs to the protection scope of the technical solutions of the present application.

Claims

1. Use of an oat active peptide in the manufacture of a medicament for the control of blood glucose or a foodstuff for the adjunctive control of blood glucose, characterised in that: The oat active peptide is any one or more of peptide segments NDQRGEII, KQGDVIALPA, PFVQQQQ, and SEQYQPYPEQQEPFVQ.

2. Use according to claim 1, characterized in that: The preparation method of the oat active peptide includes enzymatic hydrolysis, chemical synthesis, or genetic engineering.

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