Method for producing an active peptide derived from oats that promotes GLP-1 secretion, and its use.

Abstract

This invention provides a method for producing an active peptide derived from oats that promotes GLP-1 secretion, and its use. [Solution] The oat-derived active peptide contains one or more of the peptide fragments NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ. Methods for producing the oat-derived active peptide include enzymatic hydrolysis, chemical synthesis, or genetic engineering. The oat-derived active peptide has the advantages of significantly promoting GLP-1 secretion from enteroendocrine cells, being safe, free from toxic side effects, resistant to enzymatic hydrolysis by gastrointestinal digestive enzymes, and easily absorbed.

Description

Technical Field

[0001] The present invention belongs to the field of biological small molecular peptides, and specifically relates to a method for producing an oat-derived active peptide that promotes GLP-1 secretion and use thereof. Background Art

[0002] Diabetes, particularly type II diabetes, has a pathogenesis closely related to insulin resistance and pancreatic β-cell dysfunction. Glucagon-like peptide-1 (abbreviated as GLP-1) is an incretin hormone secreted by intestinal L cells and plays an important role in the regulation of blood glucose homeostasis. GLP-1 can reduce blood glucose efficiently and safely by promoting insulin secretion in a glucose concentration-dependent manner, inhibiting glucagon release, delaying gastric emptying, and enhancing satiety. Therefore, the GLP-1 signaling pathway has already become an important target for the treatment of type II diabetes. Currently, GLP-1-based clinical treatment strategies are mainly classified into two types. One is the use of GLP-1 receptor agonists (e.g., liraglutide, semaglutide, etc.), and the other is a method of delaying the degradation of endogenous GLP-1 using a dipeptidyl peptidase-4 (DPP-4) inhibitor (e.g., sitagliptin). However, most of these drugs are produced by chemical synthesis or bioengineering, and have the following limitations: (1) High cost: high research and development and production costs lead to very high treatment expenses, which impose a great economic burden on patients and society. (2) Inconvenience of administration: most GLP-1 receptor agonists require subcutaneous injection, resulting in low patient compliance. (3) Potential side effects: the drugs may cause side effects such as gastrointestinal discomfort (e.g., nausea, vomiting, diarrhea). (4) Non-natural origin: some patients have psychological resistance or safety concerns about synthetic drugs.

[0003] Therefore, the development of naturally derived, highly safe, orally administered active substances that can effectively promote the secretion of endogenous GLP-1 is of paramount importance for the prevention and adjunctive therapy of diabetes and related metabolic diseases. Calcium-sensitive receptors (CaSRs), as widely expressed G protein-coupled receptors, are an important target in the development of functional active ingredients that promote GLP-1 secretion. CaSRs can not only sense extracellular calcium ion concentrations but can also be specifically activated by various amino acids and peptides. Studies have shown that active peptides derived from food proteins can bind to CaSR as allosteric agonists, inducing conformational changes in the receptor and activating downstream signaling pathways. Of particular note is the demonstration that activation of CaSRs on the surface of intestinal L cells can effectively stimulate GLP-1 secretion.

[0004] Food-derived active peptides are attracting significant attention due to their natural, safe, and easily absorbed nature, as well as their diverse biological activities. Oats, as a whole-grain resource with excellent nutritional balance and rich in high-quality protein, are an ideal raw material for producing biologically active peptides. Currently, research has already reported that enzymatic hydrolysis of oat-derived proteins yields active peptides with effects such as antioxidant, blood pressure lowering (ACE inhibition), or immunomodulation. However, to date, no studies have been published or reported demonstrating that the specific enzymatic hydrolysis of oat-derived proteins can yield active peptides that significantly promote GLP-1 secretion function. Furthermore, there are no reports regarding their clear amino acid sequence, manufacturing method, or use in the prevention or adjunctive therapy of diabetes. Oat-derived proteins have a unique composition and contain numerous potentially biologically active sequences that can be released by enzymatic hydrolysis, suggesting great potential as an ideal source of CaSR agonist peptides. Therefore, indirectly promoting endogenous GLP-1 secretion by selectively producing active peptides capable of efficiently activating CaSR from oat-derived proteins using enzymatic hydrolysis technology is already a highly attractive and innovative strategy in the field of nutritional intervention for metabolic diseases such as diabetes and obesity, and requires urgent development. Against this backdrop, the present invention aims to provide a novel method for producing and using oat-derived active peptides specifically for this purpose.

[0005] Many conventional enzymatic degradation processes for oat-derived proteins focus on improving protein solubility or obtaining general-purpose antioxidant peptides. However, these processes lack targeting, and the resulting peptide products have a single, unstable biological activity. In particular, those with the specific function of promoting GLP-1 secretion suffer from low purposefulness, weak activity, and an unclear mechanism of action.

[0006] Therefore, in this field, in order to fill the gaps in conventional technology, there is a strong need for a technology that can efficiently and precisely produce specific peptide sequences with potent GLP-1 secretion-promoting activity from proteins derived from natural oats, and to clarify the manufacturing method and its use in blood glucose improvement. Accordingly, developing active peptides with GLP-1 secretion-promoting function using hydrolyzed proteins derived from oats has significant economic and social benefits, and can be used not only as functional ingredients in health foods but also in the production of new generation antidiabetic drugs, thus having very broad future potential. [Overview of the project] [Problems that the invention aims to solve]

[0007] To address the above technical problems, the first object of the present invention is to provide an active peptide derived from oats that promotes GLP-1 secretion.

[0008] A second object of the present invention is to provide a method for producing the oat-derived active peptide.

[0009] A third object of the present invention is to provide a method for producing an enzymatically degraded product containing the active peptide derived from oats.

[0010] A fourth object of the present invention is to provide the use of the oat-derived active peptide in the manufacture of drugs that control blood glucose or foods that assist in blood glucose control.

[0011] A fifth object of the present invention is to provide the use of the oat-derived active peptide in the manufacture of a drug that controls weight or a food that assists in weight control. [Means for solving the problem]

[0012] An active peptide derived from oats that promotes GLP-1 secretion, comprising peptide fragments NDQRGEII, KQGDVIALPA, PFVQQQQ, andPSEQYQPYPEQQEPFVQ It contains one or more of the following, and the amino acid sequence of the peptide fragment NDQRGEII is as shown in SEQ ID NO: 1, and the shown amino acid sequence is Asn-Asp-Gln-Arg-Gly-Glu-Ile-Ile, the amino acid sequence of the peptide fragment KQGDVIALPA is as shown in SEQ ID NO: 2, and the shown amino acid sequence is Lys-Gln-Gly-Asp-Val-Ile-Ala-Leu-Pro-Ala, the amino acid sequence of the peptide fragment PFVQQQQ is as shown in SEQ ID NO: 3, and the shown amino acid sequence is Pro-Phe-Val-Gln-Gln-Gln-Gln, the amino acid sequence of the peptide fragment PSEQYQPYPEQQEPFVQ is as shown in SEQ ID NO: 4, and the shown amino acid sequence is Pro-Ser-Glu-Gln-Tyr-Gln-Pro-Tyr-Pro-Glu-Gln-Gln-Glu-Pro-Phe-Val-Gln.

[0013] The above methods for producing the oat-derived active peptide include enzymatic hydrolysis, chemical synthesis, or genetic engineering.

[0014] The above enzymatic hydrolysis method involves enzymatically hydrolyzing oat-derived proteins to obtain the oat-derived active peptide, and the specific method is as follows: Step S1 involves crushing oat bran, mixing it with water, adjusting the pH of the raw material solution, and adding alkaline protease to perform enzymatic hydrolysis to obtain a crude protein solution. Step S2 involves adding neutral protease and flavor protease to the crude protein solution and performing a second enzymatic digestion to obtain the second enzymatic digestion solution. Step S3 involves adding acidic protease to the second enzyme hydrolysis solution, performing a third enzyme hydrolysis, inactivating the enzyme in the third enzyme hydrolysis solution, first performing solid-liquid separation and decolorization, then microfiltration and ultrafiltration, and finally concentration and sterilization to obtain a hydrolyzed protein solution derived from oats. comprising step S4: subjecting the oat-derived hydrolyzed protein solution to drying, sieving and magnetic separation to obtain an oat-derived hydrolyzed protein containing said oat-derived active peptide.

[0015] Preferably, in said step S1, the mass-volume ratio of oat bran to water is 1:8-12.

[0016] Preferably, in said step S1, the pH value of the raw material liquid is 7.5-8.5.

[0017] Preferably, in said step S1, the addition amount of alkaline protease is 2-10 wt%.

[0018] Preferably, in said step S1, the enzymatic hydrolysis temperature is 50-65°C, and the enzymatic hydrolysis time is 1-3 h.

[0019] Preferably, in said step S2, the addition amount of neutral protease is 0.1-5 wt%.

[0020] Preferably, in said step S2, the addition amount of flavor protease is 0.1-1 wt%.

[0021] Preferably, in said step S2, the pH value of enzymatic hydrolysis is 6.5-7.5, the enzymatic hydrolysis temperature is 50-65°C, and the enzymatic hydrolysis time is 0.5-1.5 h.

[0022] Preferably, in said step S3, the addition amount of acid protease is 0.5-5 wt%.

[0023] Preferably, in said step S3, the pH value of enzymatic hydrolysis is 6.0-7.0, the enzymatic hydrolysis temperature is 50-65°C, and the enzymatic hydrolysis time is 0.5-1.5 h.

[0024] Preferably, in said step S3, the enzyme deactivation temperature is 90-95°C, and the enzyme deactivation time is 10-30 min.

[0025] Preferably, the pore size of the microfiltration in said step S3 is 0.22~1.0 μm.

[0026] Preferably, the pore size of the ultrafiltration in said step S3 is 5~10 kDa.

[0027] The above chemical synthesis method uses a conventional solid-phase synthesis method to synthesize the oat-derived active peptide.

[0028] The above genetic engineering method controls sequence synthesis of the polypeptide by using an appropriate DNA template based on DNA recombination technology.

[0029] Use of the above oat-derived active peptide in the manufacture of a medicament for controlling blood glucose or a food for assisting blood glucose control.

[0030] Use of the above oat-derived active peptide in the manufacture of a medicament for controlling body weight or a food for assisting body weight control.

Effects of the Invention

[0031] 1. The present invention provides an oat-derived active peptide capable of promoting GLP-1 secretion, which contains one or more of the peptide fragments NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ, and the oat-derived active peptide can be obtained by artificial synthesis or enzymatic hydrolysis of oat-derived protein. In animal experiments, when oat-derived hydrolyzed protein containing the oat-derived active peptide was administered at a dose of 125 mg / kg, the GLP-1 levels in the serum of mice increased significantly, rising approximately five times compared to the control group within 2-3 hours after intervention, thoroughly verifying that it has a significant GLP-1 secretion-promoting effect in vivo. In cell-level experiments, four oat-derived active peptide fragments synthesized by chemical solid-phase methods significantly promoted GLP-1 secretion in STC-1 cells at a concentration of 5 mmol / L. Compared to the blank group, GLP-1 secretion increased 1.4 to 1.8 times, demonstrating excellent GLP-1 secretion-promoting ability.

[0032] 2. The present invention provides a method for obtaining oat-derived active peptides by enzymatic hydrolysis of oat-derived proteins. This method uses oat-derived proteins as raw materials, undergoes homogenization, then performs controllable enzymatic hydrolysis using a three-step stepwise enzymatic hydrolysis technique, followed by filtration, concentration, drying, sieving, and magnetic separation to obtain oat-derived hydrolyzed protein containing oat-derived active peptides. This process is simple to operate, requires little equipment, and the produced oat-derived active peptides are safe, free from toxic side effects, have good flavor, no noticeable bitterness or astringency, and have a pleasant mouthfeel, making them easy to use in functional products and offering good industrial scale-up potential. [Brief explanation of the drawing]

[0033] [Figure 1] This figure shows the effect of hydrolyzed oat protein on GLP-1 secretion in mouse STC-1 cells. [Figure 2] This is a mass spectrum of hydrolyzed protein derived from oats. [Figure 3] This shows the distribution of oat-derived active peptides NDQRGEII and KQGDVIALPA in oat-derived 12S seed storage globulin 1. [Figure 4] This shows the distribution of oat-derived active peptides PFVQQQQ and PSEQYQPYPEQQEPFVQ in oat-derived alcohol-soluble proteins. [Figure 5] This figure shows the effect of oat-derived active peptides from Examples 4-7 on STC-1 cell viability. [Figure 6] This figure shows the effects of oat-derived active peptides from Examples 4-7 on GLP-1 secretion in STC-1 cells. [Modes for carrying out the invention]

[0034] The present invention will be further described below with reference to examples, and the following examples are intended to interpret the present invention and not to limit it.

[0035] The alkaline protease used in the following examples and comparative examples had an enzyme activity of 200,000 U / g and was purchased from Ningxia Xia Sheng Industrial Group Co., Ltd. in China. The neutral protease had an enzyme activity of 50,000 U / g and was purchased from Henan Xinyangshao Biotechnology Co., Ltd. in China. The flavor protease had an enzyme activity of 50,000 U / g and was purchased from Yantai MATBIO Technology Co., Ltd. in China. The acidic protease had an enzyme activity of 100,000 U / g and was purchased from Nanning Pangbo Biological Engineering Co., Ltd. in China.

[0036] (Example 1) This embodiment describes a method for producing hydrolyzed protein derived from oats, and includes S1 to S4.

[0037] In S1, 100g of oat bran was crushed and added to 800mL of water, and the mixture was uniformly stirred at 60°C to adjust the pH of the raw material solution to 7.5. 2 wt% alkaline protease was added, and the mixture was enzymatically hydrolyzed at 60°C for 3.0 hours to obtain a crude protein solution.

[0038] In S2, the pH of the crude protein solution was adjusted to 7.0, 0.5 wt% neutral protease and 0.1 wt% flavor protease were added, and enzymatic hydrolysis was carried out at 65°C for 1.0 hour to obtain the second enzymatic hydrolysis solution.

[0039] In S3, the pH of the second enzyme-digested solution was adjusted to 7.0, 0.5 wt% acidic protease was added, and the solution was enzymatically digested at 55°C for 0.5 hours to obtain the third enzyme-digested solution.

[0040] In S4, the temperature of the third enzymatic hydrolysis solution was raised to 95°C to inactivate the enzyme, followed by solid-liquid separation and decolorization. The solution was then filtered first through a microfiltration membrane with a pore size of 0.45 μm, followed by ultrafiltration through an ultrafiltration membrane with a pore size of 10 kDa. After sterilization, the solution was dried, sieved, and magnetically separated to obtain hydrolyzed protein derived from oats.

[0041] (Example 2) This example relates to the effect of hydrolyzed oat protein on GLP-1 secretion by mouse enteroendocrine cells, and includes S1 and S2.

[0042] In S1, ICR mice were acclimatized for one week and then randomly divided into eight groups (6 mice per group).

[0043] In S2, the control group received intragastric infusion of physiological saline, while the experimental group received intragastric infusion of hydrolyzed oat protein (125 mg / kg body weight) prepared in Example 1. At 0 min, 15 min, 30 min, 60 min, 90 min, 120 min, 180 min, 240 min, and 360 min after intragastric infusion, the eyeballs were removed and blood was collected. The blood was placed in a centrifuge tube containing EDTA (final concentration 1 mg / mL) and aprotinin (final concentration 0.6 TIU / mL), and the supernatant was collected by centrifugation. The GLP-1 hormone content in the serum was detected by ELISA using a commercial GLP-1 kit manufactured by the Nanjing Jiancheng Institute of Bioengineering in China.

[0044] As shown in Figure 1, the serum GLP-1 level in the control group (physiological saline) was maintained at approximately 57 pg / mL during this period. The oat-derived hydrolyzed protein (Example 1) was able to rapidly increase the serum GLP-1 level to approximately 80 pg / mL 15 minutes after intervention, and to increase the serum GLP-1 level by approximately 5 times 120 minutes after intervention. This demonstrates that the oat-derived hydrolyzed protein can increase the GLP-1 level in mice, and also explains that the oat-derived hydrolyzed protein has the advantage of being resistant to enzymatic degradation by gastrointestinal digestive enzymes and is easily absorbed.

[0045] (Example 3) This example involves mass spectrometry and protein separation of hydrolyzed proteins derived from oats produced in Example 1, and includes S1 to S3.

[0046] In S1, hydrolyzed proteins derived from oats were dissolved, ultrafiltration was performed using a 10 kDa ultrafiltration tube, desalting was carried out using a WatersSEP-PAKC18 solid-phase extraction column, and after freeze-drying, the proteins were redissolved in a 1% formic acid aqueous solution, centrifuged, and the supernatant was collected for detection by chromatography-mass spectrometry.

[0047] In S2, solution A used for liquid chromatography was a 0.1% formic acid aqueous solution, and solution B was a 0.1% formic acid-acetonitrile aqueous solution (80% acetonitrile). The liquid chromatography column (50 μm * 150 mm, Acclaim PepMap™ RSLC, Thermo Scientific Technology Inc) was equilibrated with 92% solution A, and the sample injection volume was 1 μL. Chromatographic column separation was performed, and the associated liquid gradient was set so that the linear gradient of solution B was 8-28% from 0 to 98 min, 28-37% from 9 to 113 min, 37-100% from 113 to 117 min, and maintained at 100% from 117 to 120 min.

[0048] In S3, raw files from mass spectrometry tests were retrieved from corresponding databases using the software Proteome Discoverer 2.5 to obtain a total of 190 peptide fragments. 22 peptide fragments with relative content >1.0% were retained. The structure of the calcium-sensitive receptor (CaSR) and the sequence and three-dimensional structural data of its ligand peptide fragments were collected from the shared database UniProt (https: / / www.uniprot.org / ) to construct a training dataset. Next, important conserved residues in the CaSR-binding domain were identified using the multi-sequence alignment tool Clustal Omega, and a three-dimensional model of the receptor-peptide fragment complex was generated based on AlphaFold2 (https: / / alphafold2.biodesign.ac.cn / ). Furthermore, the binding modes of the 22 peptide fragments, each with relative content >1.0%, to CaSR were simulated using the molecular docking software AutoDock Vina (Scripps, USA), and parameters such as binding free energy, hydrogen bond interactions, and spatial complementarity were calculated. Finally, peptide fragment binding affinity prediction scores were output. The four oat-derived active peptide fragments with the highest prediction scores were NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ.

[0049] As shown in Figure 2, this is the mass spectrum of hydrolyzed protein derived from oats.

[0050] The proteins derived from oats are mainly globulins. Of these, the amino acid sequence of oat-derived 12S seed storage globulin 1 is shown in SEQ ID NO: 5, and the amino acid sequence of oat-derived alcohol-soluble protein is shown in SEQ ID NO: 6.

[0051] As shown in Figure 3, the oat-derived active peptides NDQRGEII and KQGDVIALPA are present in oat-derived proteins, and therefore, the oat-derived active peptides NDQRGEII and KQGDVIALPA can be produced from oat-derived proteins.

[0052] As shown in Figure 4, the oat-derived active peptides PFVQQQQ and PSEQYQPYPEQQEPFVQ are present in oat-derived proteins, and therefore, the oat-derived active peptides PFVQQQQ and PSEQYQPYPEQQEPFVQ can be produced from oat-derived proteins.

[0053] (Example 4) This example concerns the effects of the oat-derived active peptide NDQRGEII (Asn-Asp-Gln-Arg-Gly-Glu-Ile-Ile) on STC-1 cell viability and GLP-1 secretion, and includes S1-S4.

[0054] In S1, the oat-derived active peptide NDQRGEII was synthesized by Nanjing Genscript Biotech Co., Ltd. in China using a solid-phase synthesis method, and the purity of the synthesized peptide was confirmed to be greater than 95% using high-performance liquid chromatography and mass spectrometry.

[0055] In 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. The cells were then cultured at 37°C in a cell incubator containing 5% CO2, and when the density reached 80-90%, they were subcultured by trypsin digestion.

[0056] In S3, an STC-1 cell viability assay was performed using 3-(4,5-dimethylthiazole-2-yl)-2,5-diphenyltetrazolium bromide (MTT) to evaluate the effect of oat-derived active peptides on STC-1 cell viability. MTT was added to STC-1 cells treated in a 96-well plate. Cells with high metabolic activity decomposed the yellow tetrazolium salt MTT into purple formazan crystals. The formed formazan was dissolved, and the absorbance at a detection wavelength of 570 nm was measured using a microplate reader. The results were expressed as a percentage relative to the control group.

[0057] In S4, measurement of hormone GLP-1 secretion by STC-1 cells: Oat-derived active peptides were prepared as 5 mmol / L peptide solutions in Hank's buffer, and STC-1 cells were cultured in 24-well plates at a concentration of 1.25 × 10⁶. 5 Cells were inoculated at a density of 1, and once the cells reached 80-90% density, they were washed twice with Hank's buffer to remove the culture medium. Peptide solutions were added to each of the STC-1 cells, and the cells were cultured in an incubator at 37°C for 2 hours. The cells were then centrifuged at 1000×g for 20 minutes, the supernatant was collected, and the GLP-1 content was measured using a commercial GLP-1 kit from the Nanjing Institute of Bioengineering, China.

[0058] (Example 5) This example concerns the effects of the oat-derived active peptide KQGDVIALPA (Lys-Gln-Gly-Asp-Val-Ile-Ala-Leu-Pro-Ala) on STC-1 cell viability and GLP-1 secretion, and the specific steps were the same as in Example 4.

[0059] (Example 6) This example concerns the effects of the oat-derived active peptide PFVQQQQ (Pro-Phe-Val-Gln-Gln-Gln-Gln) on STC-1 cell viability and GLP-1 secretion, and the specific steps were the same as in Example 4.

[0060] (Example 7) This example concerns the effects of the oat-derived active peptide PSEQYQPYPEQQEPFVQ (Pro-Ser-Glu-Gln-Tyr-Gln-Pro-Tyr-Pro-Glu-Gln-Gln-Glu-Pro-Phe-Val-Gln) on STC-1 cell viability and GLP-1 secretion, and the specific steps were the same as in Example 4.

[0061] As shown in Figure 5, the oat-derived active peptides NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ did not show any significant change in STC-1 cell viability compared to the control group at test concentrations (0, 5, and 10 mmol / L). This explains that the oat-derived active peptides NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ are non-toxic to cells.

[0062] As shown in Figure 6, the oat-derived active peptides NDQRGEII, KQGDVIALPA, PFVQQQQ, and PSEQYQPYPEQQEPFVQ can all significantly promote GLP-1 secretion from enteroendocrine cells STC-1. Numerous studies have demonstrated that GLP-1 has physiological functions such as promoting insulin secretion, promoting pancreatic β-cell proliferation and suppressing its apoptosis, suppressing postprandial glucagon secretion, reducing hepatic glycogen synthesis, improving insulin sensitivity, and controlling appetite. Therefore, increasing GLP-1 secretion has significant importance in the prevention and treatment of type II diabetes.

[0063] (Example 8) This example is a sensory evaluation of hydrolyzed oat protein produced in Example 1, and includes S1 to S3.

[0064] In S1, 20 sensory evaluators (10 men and 10 women, aged 25-45) were recruited and trained. All evaluators had no history of smoking, possessed normal sensory functions, and received basic taste discrimination training.

[0065] In S2, 1.0 g each of the oat-derived active peptide product and control samples (commercially available soy peptide powder and commercially available wheat peptide powder) were accurately weighed, dissolved in 100 mL of purified water at room temperature to prepare a 1% (w / v) solution, and used as the test solution. A three-digit number was randomly assigned to all samples, and they were evaluated under the same lighting and odorless environment.

[0066] In S3, quantitative descriptive analysis was used, with evaluators sequentially tasting each test solution (approximately 5-10 mL at a time, rinsing their mouths afterward, and allowing a 2-minute interval to allow for sensory fatigue), and scoring the following indicators on a scale of 0 to 5 (a score of 0 indicates no sensation, and a score of 5 indicates extremely high intensity). Bitterness: The intensity of a characteristic bitterness. Astringency: The intensity of astringency or dryness in the mouth. Unpleasant aftertaste: The intensity of an unpleasant taste that remains after swallowing. Overall Acceptability: Acceptance of the overall flavor of the sample (1 point: completely unacceptable. 5 points: very tasty).

[0067] [Table 1]

[0068] As shown in Table 1, the hydrolyzed oat protein powder produced by the present invention had significantly lower bitterness, astringency, and unpleasant aftertaste intensity scores in a 1% aqueous solution compared to commercially available general plant peptide products (*p<0.01), and its overall acceptability score was far higher than that of the control sample (*p<0.01). Specifically, it had a soft mouthfeel, only an extremely weak and easily acceptable base flavor, lacked the obvious bitterness and astringency characteristic of peptides, and left no unpleasant residue in the mouth after swallowing.

[0069] The above description is merely one example of a preferred embodiment of the present invention and does not limit the invention. Those skilled in the art can make many possible changes and modifications to the technical solution of the present invention, or modify it into equivalent embodiments with equivalent changes, using the methods and technical content described above, without departing from the spirit and essence of the invention and the technical solution. Therefore, any simple modifications, equivalent substitutions, equivalent changes, and modifications made to the above embodiments based on the technical essence of the invention, as long as they do not depart from the content of the technical solution of the present invention, are all within the scope of protection of the technical solution of the present invention.

Claims

1. A drug for blood glucose control by promoting GLP-1 secretion, characterized by containing one or more of the peptide fragments KQGDVIALPA, PFVQQQQ, and PSECQYQPYPEQQEPFVQ as active ingredients.

2. A food product for supporting blood glucose control by promoting GLP-1 secretion, characterized by containing one or more peptide fragments from KQGDVIALPA, PFVQQQQ, and PSECQYQPYPEQQEPFVQ.

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