Umami peptide derived from soybean residue, preparation method and application thereof

Abstract

The present invention belongs to the field of soybean residue resource utilization and food flavor chemistry, and specifically relates to an umami peptide derived from soybean residue, and a preparation method and application thereof. In order to promote the comprehensive utilization of soybean residue, an oligopeptide with umami taste was developed therefrom. The present invention uses soybean residue as raw material, separates and purifies to obtain a FAPEFLEH umami peptide with a molecular weight of 989.4729Da. The umami peptide derived from soybean residue prepared by the present invention has the advantages of high purity, good activity, artificial synthesis, safety and non-toxicity. Sensory evaluation and threshold determination found that the umami peptide has good umami and flavor enhancement properties, the umami threshold is 0.18mmoL / L, and the synergistic flavor enhancement threshold with MSG is 0.07mmoL / L. It can be used to prepare functional flavor bases, which is beneficial to the high-value utilization of soybean by-product soybean residue.

Description

Technical Field

[0001] The invention belongs to the field of soybean residue resource utilization and food flavor chemistry, and particularly relates to an umami peptide derived from soybean residue, a preparation method and an application thereof. Background Art

[0002] Okara is a byproduct of soy milk and tofu production. my country produces approximately 6 million tons of soybeans annually for traditional tofu and soy products, resulting in a significant amount of okara produced annually. Due to its perishable nature, poor flavor, and rough texture, okara is often used to make fertilizer, feed, or even discarded. This not only creates increasingly serious environmental problems but also deprives okara of valuable new uses. Although a bulky material, okara is rich in nutrients, including protein, dietary fiber, and oligosaccharides. Therefore, the processing and utilization of okara is of great significance.

[0003] Patent document CN108929892A discloses a method for extracting soluble okara protein and polypeptides from bean dregs. This method uses okara, a byproduct of soy product processing, as the raw material. The okara is mixed with water, heated, and stirred to dissolve the protein in the okara. After the system cools, enzyme complex I is added for a primary extraction, followed by centrifugation, and the supernatant is collected. The solid phase obtained from the primary extraction is crushed and dissolved, and enzyme complex II is added again for a secondary extraction, followed by centrifugation, and the supernatant is collected. The two supernatants are combined, the enzymes are inactivated, the pH is adjusted to precipitate the soluble proteins and polypeptides, and the solid phase is collected and dried to obtain the finished soluble okara protein and polypeptide product. This method utilizes a multi-enzyme extraction process, leveraging the synergistic effects of alkaline protease, papain, and cellulase to simultaneously extract soluble proteins and polypeptides from the okara. This improves the utilization rate and economic added value of the okara and reduces its environmental pollution.

[0004] Patent document CN115868603A discloses an enzymatically hydrolyzed soybean dregs powder and a preparation method thereof. The preparation method comprises the following steps: (S1) taking soybean dregs, adding cellulase and protease for enzymatic hydrolysis to obtain an enzymatic hydrolysis product; (S2) adding 2-5% amino acids by weight of the soybean dregs, 2-5% reducing sugars by weight of the soybean dregs, and 1-2% garlic extract by weight of the soybean dregs to the enzymatic hydrolysis product, mixing them uniformly, and then subjecting the mixture to a browning reaction to obtain a reactant; (S3) removing water from the reactant by pressure filtration, and then drying the reactant by microwave drying until the water content is less than 8% by weight to obtain a dried product; (S4) pulverizing the dried product and sieving it using a graded sieve to obtain enzymatically hydrolyzed soybean dregs powder of different particle sizes. The enzymatically hydrolyzed soybean dregs powder obtained effectively removes the beany odor, has a better taste, and exhibits excellent antioxidant and antibacterial properties, while also providing certain flavor substances.

[0005] Currently, research on okara generally focuses on optimizing the enzymatic hydrolysis of okara proteins and peptides, with less research on umami peptides. Umami is one of the five human tastes. Umami substances primarily include free amino acids, nucleotides, organic acids, organic bases, and peptides, which can enhance the flavor of food, making it softer, more harmonious, and mellower. Umami peptides are compounds composed of amino acids linked by peptide chains. They possess outstanding umami properties and are one of the most important sources of umami in food, alongside volatile and non-volatile flavor compounds. Compared to some traditional umami ingredients, umami peptides not only possess umami properties but also synergize with other substances to enhance freshness, reduce bitterness, and reduce some adverse reactions. Therefore, fully utilizing high-quality plant protein resources such as okara to conduct research on umami peptides holds significant market value. Summary of the Invention

[0006] To expand the comprehensive utilization value of soybean residue, the present invention provides umami peptides derived from soybean residue. Specifically, fresh soybean residue is used as a substrate, inoculated with the fungus Neurospora crassa, and fermented to produce red fungus tofu. Umami peptides are then isolated and purified from the red fungus tofu. The red fungus tofu fermented from soybean residue is rich in protein, with a high proportion of umami amino acids in the protein. Umami peptides of high purity and activity can be isolated and purified from this protein.

[0007] To achieve the above object, the technical solution adopted by the present invention is:

[0008] The invention provides an umami peptide derived from soybean residues. The amino acid sequence of the umami peptide is: Phe-Ala-Pro-Glu-Phe-Leu-Glu-His (FAPEFLEH).

[0009] The soybean residue-derived umami peptide provided by the present invention is prepared by inoculating Neurospora crassa with fresh soybean residue as raw material and fermenting it to produce red mushroom tofu. The red mushroom tofu is then crushed, extracted, ultrafiltered, and separated by dextran gel permeation chromatography. With sensory umami as the guide, the main umami parts of the red mushroom tofu are obtained. Nano-liquid chromatography-tandem mass spectrometry (NanoLC-MS / MS) is used to analyze the polypeptide structure. Computer simulation and molecular docking technology are used to screen potential umami peptides. Umami peptide monomers are chemically synthesized in vitro for sensory verification to obtain an oligopeptide with strong umami taste. The amino acid sequence of the oligopeptide is Phe-Ala-Pro-Glu-Phe-Leu-Glu-His (FAPEFLEH), and the molecular weight is 989.4729 Da.

[0010] Sensory evaluation and threshold determination revealed that the FAPEFLEH umami peptide exhibited excellent umami and flavor-enhancing properties, with an umami threshold of 0.18 mmoL / L and a synergistic flavor-enhancing threshold of 0.07 mmoL / L with monosodium glutamate. Furthermore, prediction of the functional activities of the FAPEFLEH umami peptide using the BIOPEP-UWM database revealed that the FAPEFLEH umami peptide exhibited ACE inhibitory activity, DPP-IV inhibitory activity, α-glucosidase inhibitory activity, and renin inhibitory activity, demonstrating that the soybean residue-derived umami peptide provided by the present invention has the efficacy of lowering blood pressure and blood sugar.

[0011] Furthermore, the specific preparation method of the soybean residue-derived umami peptide comprises the following steps:

[0012] Step S1, preparation of red mushroom tofu:

[0013] Fresh soybean residue is crushed, sieved, sterilized, cooled, and inoculated with Neurospora crassa for fermentation to obtain red fungus tofu;

[0014] Step S2, polypeptide extraction:

[0015] The red fungus tofu prepared in step S1 is crushed and sieved to obtain red fungus tofu powder, and the red fungus tofu powder is dissolved in deionized water to obtain a suspension. The suspension is then placed in a 100°C water bath for 100-120 minutes, filtered, and the filtrate is collected. The filtrate is cooled to room temperature and centrifuged to obtain the supernatant to obtain a crude polypeptide extract;

[0016] Step S3, polypeptide separation, purification and identification:

[0017] The crude polypeptide extract obtained in step S2 is subjected to ultrafiltration separation, the separated components are evaluated for umami taste, the component with the strongest umami taste is selected for gel chromatography separation and purification, the component with the strongest umami taste is selected through sensory evaluation, and then separated and identified by liquid chromatography-mass spectrometry to obtain.

[0018] Furthermore, in step S1, the inoculation amount of Neurospora crassa is 0.1-0.2% (w / w), and the fermentation conditions are: fermentation at a temperature of 28-32° C. and a humidity of 70-80% for 24-48 hours.

[0019] Furthermore, the centrifugation conditions in step S2 are: centrifugation at a temperature of 4° C. and a rotation speed of 7000 to 10000 r / min for 10 to 15 minutes.

[0020] Furthermore, the ultrafiltration separation conditions in step S3 are as follows: filtering the crude polypeptide extract with a 0.45 μm aqueous filter membrane, taking the filtrate, and then passing the filtrate through 10 kDa, 5 kDa, 3 kDa, and 1 kDa ultrafiltration membranes in sequence at 4°C.

[0021] Furthermore, the conditions for gel chromatography separation and purification in step S3 are: the specification of the dextran gel is G-15, the injection concentration is 20 mg / mL, ultrapure water is used as the eluent, the flow rate is 1.0 mL / min, and the wavelength is 220 nm.

[0022] Furthermore, in step S3, the liquid chromatography-mass spectrometry instrument uses a C18 reverse phase analytical chromatographic column for liquid phase separation.

[0023] Furthermore, in the C18 reverse-phase analytical chromatographic column: mobile phase A is 0.1% formic acid solution, mobile phase B is a mixed solution of 80% acetonitrile and 0.1% formic acid, the flow rate is 600 nL / min, and the time is 66 min; the liquid chromatography elution gradient is: 0-2 min, 4%-8% mobile phase B; 2-45 min, 8%-28% mobile phase B; 45-55 min, 28%-40% mobile phase B; 55-56 min, 40%-95% mobile phase B; 56-66 min, 95% mobile phase B.

[0024] In addition, the present invention also provides the use of the soybean residue-derived umami peptide in the preparation of food additives.

[0025] At the same time, the present invention also provides an umami peptide preparation, including the above-mentioned umami peptide. Of course, in order to improve the scope of application of the preparation, it can also include other auxiliary materials that can be used in the field of food additives. The preparation can be prepared in the form of granules, pastes and powders.

[0026] In summary, compared with the existing technology, the umami peptide derived from soybean residue provided by the present invention has high purity, good activity, can be artificially synthesized, and is safe and non-toxic. Sensory evaluation and threshold measurement found that the umami peptide has a strong umami taste, can be used in the field of food additives to enhance flavor, and is conducive to the resource utilization of soybean waste. BRIEF DESCRIPTION OF THE DRAWINGS

[0027] Figure 1 This is a graph showing the umami evaluation of the four fractions (H1-H4) separated from the crude polypeptide extract by ultrafiltration.

[0028] Figure 2 A diagram of the fraction collection (F1-F4) of the H4 component with the strongest umami taste separated and purified by gel chromatography.

[0029] Figure 3 The umami evaluation graph of the subfractions (F1-F4) separated by gel chromatography.

[0030] Figure 4 This is the total ion current chromatogram of the F2 component polypeptide.

[0031] Figure 5 This is the result of qualitative identification of polypeptides in the F2 component.

[0032] Figure 6 This is the umami evaluation chart of FAPEFLEH, the peptide with the strongest umami taste synthesized in vitro. DETAILED DESCRIPTION

[0033] The present invention is further described below by describing specific embodiments, but this is not intended to limit the present invention. Those skilled in the art may make various modifications or improvements based on the basic concept of the present invention, but as long as they do not deviate from the basic concept of the present invention, they are all within the scope of the present invention. The experimental methods used in the following examples are all conventional methods unless otherwise specified; the materials, reagents, etc. used are reagents and materials that can be obtained from commercial channels unless otherwise specified.

[0034] Example 1. Preparation of umami peptides from soybean residue

[0035] Step S1, preparation of red mushroom tofu:

[0036] (1) Material preparation: Fresh soybean residue from Panlong Market in Guangdong Province; Neurospora crassa was obtained from the Provincial Key Laboratory of Lingnan Specialty Food Science and Technology in Guangdong Province.

[0037] (2) Fermentation of soybean residue: fresh soybean residue was crushed, passed through a 60-mesh sieve, and sterilized in an autoclave (121°C, 30 min). After sterilization, the residue was spread out and cooled to room temperature. After cooling, 0.1% (w / w) Neurospora crassa was inoculated and mixed evenly to obtain a mixture. The mixture was placed in a tofu frame for shaping, and fermented in an artificial climate incubator at a temperature of 30°C and a humidity of 75% for 36 h to obtain red fungus tofu. The tofu was then frozen in a -20°C refrigerator for later use.

[0038] Step S2, polypeptide extraction:

[0039] The red mushroom tofu prepared in step S1 was crushed and passed through a 40-mesh sieve to obtain red mushroom tofu powder. The red mushroom tofu powder was dissolved in deionized water at a material-liquid ratio of 1 g:20 mL to obtain a suspension. The suspension was then placed in a 100° C. pot water bath for 120 min, filtered through gauze, and the filtrate was taken. After the filtrate was cooled to room temperature, the filtrate was centrifuged at a temperature of 4° C. and a speed of 8000 r / min for 15 min, and the supernatant was taken to obtain a crude polypeptide extract.

[0040] Step S3, polypeptide separation, purification and identification:

[0041] (1) Sensory evaluation method:

[0042] The researchers recruited 10 healthy panelists (5 women and 5 men, aged 23-28 years) with experience in sensory evaluation. Panelists were screened and trained to conduct sensory evaluations for 2 weeks and were asked to write sensory descriptions of sweetness (sucrose), sourness (citric acid), saltiness (sodium chloride), bitterness (L-isoleucine), and umami (MSG). All samples were dissolved in deionized water and sensory tests were performed at room temperature. Panelists were asked to rest for 5 minutes between two different samples to avoid aftertaste and sensory fatigue effects during the experiment. Taste characteristics used a 10-point intensity scale (0 means no taste; 10 means the strongest taste).

[0043] (2) Ultrafiltration separation of polypeptide crude extract:

[0044] (1) Ultrafiltration separation:

[0045] The crude polypeptide extract obtained in step S2 was subjected to ultrafiltration separation. The crude polypeptide extract was filtered through a 0.45 μm aqueous filter membrane. The filtrate was taken and passed through a 10 kDa ultrafiltration membrane at 4°C, and then through 5 kDa, 3 kDa, and 1 kDa ultrafiltration membranes in sequence. After classification, four components were obtained, namely H1 (5 kDa < molecular mass < 10 kDa), H2 (3 kDa < molecular mass < 5 kDa), H3 (1 kDa < molecular mass < 3 kDa), and H4 (molecular mass < 1 kDa). After rotary evaporation, they were freeze-dried into polypeptide powder and stored at -20°C for future use.

[0046] (2) Sensory evaluation:

[0047] The sensory evaluation of the four components (H1-H4) separated by ultrafiltration of the polypeptide crude extract was carried out using the sensory evaluation method (I). The umami evaluation results of the four components (H1-H4) separated by ultrafiltration of the polypeptide crude extract are as follows: Figure 1 In order to screen out the main umami substances in red mushroom tofu, the red mushroom tofu water extract - polypeptide crude extract was separated by ultrafiltration technology to obtain four components named H1, H2, H3, and H4. The four components were then subjected to sensory evaluation. Figure 1 It can be seen that all separated components can perceive umami, sweetness and sourness, with basically no bitterness or saltiness. Among them, H4 has the highest umami and sweetness values ​​and a lower sourness value, which is higher than the umami value of the unseparated component (HJDF component) of red mushroom tofu. This indicates that H4 has a more significant umami taste among the four separated components and may contain a large amount of umami peptides.

[0048] (III) Gel chromatography separation of H4 component:

[0049] (1) Gel chromatography separation:

[0050] The H4 component, which possesses the strongest umami flavor, was isolated and purified using Sephadex G-15. Based on the gel properties of the specified gel and the required dosage for the experiment, an appropriate amount of Sephadex G-15 powder was soaked in superheated ultrapure water for 24 hours to swell. The fully swollen filler was then poured into a chromatography column (1.6 cm diameter, 80 cm length) using ultrapure water as the mobile phase. To ensure uniform and firm filling of the column with the dextran gel, the column was allowed to settle naturally for 2 hours. The column was then flushed with ultrapure water at a flow rate of 2 mL / min for 4 hours. The H4 component, which exhibited the strongest umami flavor after ultrafiltration, was diluted to a concentration of 20 mg / mL in ultrapure water. The solution was then passed through a 0.22 μm aqueous filter membrane before being added to the sample. Ultrapure water was used as the eluent at a flow rate of 1.0 mL / min, with the eluate collected every 3 minutes. After detection by ultraviolet absorption spectrum at 220 nm, all components corresponding to one peak were mixed, freeze-dried and used for the next sensory evaluation.

[0051] (2) Gel chromatography separation and sensory evaluation:

[0052] (a) The H4 component with the strongest umami taste was separated and purified by gel chromatography and the fractions (F1-F4) were collected. The results are as follows Figure 2 As shown. Gel chromatography separation and purification relies on the molecular size difference of sample molecules in the gel filler to achieve separation, which can remove both large and small molecular impurities. The ultrafiltration fraction H4 (<1kDa) is separated by gel chromatography on a Sephadex G-15 column. According to the separation characteristics of the column, the molecular weight decreases as the component flows out. Figure 2 As shown, four separated components were obtained within the elution time of 30 to 150 minutes, namely F1, F2, F3 and F4.

[0053] (b) The umami taste of the sub-fractions (F1-F4) separated by gel chromatography was evaluated by sensory evaluation method (I). Figure 3 As shown. Figure 3As can be seen, the F2 fraction had the strongest umami flavor, with sweetness and a slight bitterness. Umami dominated the flavor, far outweighing the sour and salty flavors in this fraction, which were essentially neutral. Compared to the other three fractions, the F2 fraction had a richer flavor profile, combining umami, sweetness, and a slight bitterness. Although the F3 fraction had the highest peptide content, its umami intensity was moderate, suggesting that the umami peptide content in the F3 fraction was lower than that in the F2 fraction. The F4 fraction had the lowest peptide content and the lowest umami value, suggesting that it contained virtually no umami peptides. None of the fractions had a distinct salty or sour flavor, demonstrating that gel chromatography effectively separated and purified umami components and performed a desalting function. Based on these results, we speculate that the majority of the umami compounds in red mushroom tofu are concentrated in the peptides of the F2 fraction.

[0054] (IV) Peptide identification of F2 component:

[0055] (1) LC-MS / MS identification of peptides:

[0056] (a) Sample Pretreatment: Take an appropriate amount of the F2 fraction sample and add dithiothreitol (DTT) solution to a final concentration of 10 mmol / L. Reduce the sample in a 56°C water bath for 1 h. Add iodoacetamide (IAM) solution to a final concentration of 55 mmol / L and incubate in the dark for 40 min. Desalt the sample using a self-packed desalting column and evaporate the solvent in a vacuum centrifuge at 45°C.

[0057] (b) Injection: 5 μL of sample was injected into a C18 reverse phase analytical column (150 μm id × 150 mm, packed with Acclaim PepMap RPLC C18, 1.9 μm, ), mobile phase A was 0.1% formic acid solution, mobile phase B was a mixed solution of 80% acetonitrile and 0.1% formic acid, the flow rate was 600 nL / min; the time was 66 min; the liquid chromatography elution gradient was: 0-2 min, 4%-8% mobile phase B; 2-45 min, 8%-28% mobile phase B; 45-55 min, 28%-40% mobile phase B; 55-56 min, 40%-95% mobile phase B; 56-66 min, 95% mobile phase B.

[0058] (c) Primary mass spectrometry parameters: resolution 70,000; automatic gain control (AGC) target 3e6; maximum fill time 100 ms; mass scan range 100–1500 m / z. Secondary mass spectrometry parameters: resolution 17,500; AGC target 1e5; maximum fill time 50 ms; TopN 20; normalized collision energy (NCE) 28. Peptide sequence analysis was performed using a Byonic search of the target protein database. Parameters were set as follows: protein modifications were carbamidomethylation (C) (fixed), oxidation (M) (variable), and acetyl (protein N-terminus) (variable); enzyme specificity was set to nonspecific; maximum missed excision was set to 3; precursor ion mass tolerance was set to 20 ppm, and MS / MS tolerance was set to 0.02 Da.

[0059] (2) Peptide identification results:

[0060] (a) To clarify the composition of umami substances in red mushroom tofu, LC-MS / MS was used to identify the amino acid sequence of the umami peptide F2, the most potent umami component. The total ion current chromatogram contains the sum of the intensities of all ions in the mass spectrum at each time point and their retention times in the chromatogram. The total ion current chromatogram of the F2 component peptide is shown in Figure 1. Figure 4 shown.

[0061] (b) Qualitative identification results of polypeptides in F2 fraction Figure 5 In this study, a total of 1540 valid peptides were identified from the F2 fraction, most of which were peptides with a molecular mass of less than 1 kDa. Due to the large number of peptides identified by mass spectrometry, it was necessary to quickly screen the target umami peptides through preliminary umami peptide screening and machine learning. The peptide chain length of umami peptides is usually a peptide segment with a molecular mass of less than 1kDa, so peptides less than 1kDa were selected for the next step of machine learning screening of potential umami peptides. Among them, there are 9 tripeptides less than 1kDa, accounting for 0.58% of the total, 67 tetrapeptides, accounting for 4.35% of the total, 208 pentapeptides, accounting for 13.51% of the total, 115 hexapeptides, accounting for 7.47% of the total, 96 heptapeptides, accounting for 6.23% of the total, 111 octapeptides, accounting for 7.21% of the total, 133 nonapeptides, accounting for 8.64% of the total, and 159 decapeptides, accounting for 10.32% of the total. The number of peptides below decapeptides accounts for 58.31% of the total, and the number of peptides above undine peptides accounts for 41.69%.

[0062] (V) Prediction of umami peptide activity:

[0063] The iUmami-SCM database was used to predict the flavor activity of umami peptides, and the peptide sequences with the strongest umami flavor were predicted through computer-simulated molecular docking. The identified amino acid sequences were input into the "Sensory Peptides and Amino Acids" module to predict the frequency of occurrence of umami fragments. Nine peptides with the highest frequency of umami-active fragments were screened, and FAPEFLEH was found to be the peptide with the strongest umami flavor. The results are shown in Table 1.

[0064] Table 1 Five peptide sequences with the strongest umami taste predicted by computer simulation molecular docking

[0065]

[0066] Example 2: Artificial Synthesis Verification and Sensory Evaluation of FAPEFLEH Umami Peptide

[0067] In order to verify the FAPEFLEH umami peptide, the umami peptide was synthesized by chemical synthesis and sensory evaluation was performed.

[0068] (1) Synthesis of umami peptides by solid phase synthesis:

[0069] Based on the molecular docking results, the peptide with the lowest binding energy was selected for solid-phase synthesis. Based on the known amino acid sequence Phe-Ala-Pro-Glu-Phe-Leu-Glu-His (FAPEFLEH), peptide chains were linked via amino acid condensation reactions, using Fmoc as the α-amino protecting group and benzyl alcohols for side chain protection. During synthesis, an Fmoc-amino acid derivative was covalently cross-linked to the resin, Fmoc was removed with alkali, and the free amino terminus was neutralized with triethylamine. The peptide was then activated via DCC and coupled to the next amino acid. Beijing Bio-Tech Biotechnology Co., Ltd. was commissioned to perform solid-phase peptide synthesis. The molecular weight of the synthesized peptide was determined by mass spectrometry, and the purity of the peptide was determined by high-performance liquid chromatography.

[0070] (2) Determination of the umami threshold of FAPEFLEH synthetic peptide:

[0071] The umami threshold of the synthetic peptide was determined using a taste dilution assay. Using deionized water as the experimental solvent at room temperature, the synthetic peptide was serially diluted 1:1 (v / v) with deionized water. Samples at each dilution level were tested using the trigonometric method. When the panelists could only distinguish between the previous sample and two blank controls (ultrapure water) but not between the next concentration and the blank controls, the average of the last two concentrations of the synthetic peptide was used as the umami threshold. The results are shown in Table 2.

[0072] Table 2 Taste description, umami threshold, umami enhancement threshold and umami enhancement value of FAPEFLEH with NaCl

[0073]

[0074] The results in Table 2 indicate that the FAPEFLEH umami peptide isolated and synthesized by the present invention has a strong umami flavor. This umami peptide is expected to be applied in the field of food flavor chemistry, laying the foundation for the future application of food-derived umami peptides.

[0075] (3) Umami evaluation of FAPEFLEH synthetic peptide:

[0076] The sensory evaluation results of FAPEFLEH synthetic peptide were as follows: Figure 6 As shown. Figure 6 It can be seen that FAPEFLEH synthetic peptide exhibits a strong umami taste accompanied by sweetness, while other flavors are weaker. Compared with the traditional umami substance MSG (monosodium glutamate), FAPEFLEH synthetic peptide has a stronger umami taste.

[0077] Example 3: Prediction of the functional activity of FAPEFLEH umami peptide

[0078] The functional activity of FAPEFLEH was predicted using the BIOPEP-UWM database. The amino acid sequences were aligned with the database and the frequencies of active fragments were calculated to predict the functional activity of peptides with potential umami flavor. The results of computer simulation prediction of the health-promoting activity of the FAPEFLEH umami peptide are shown in Table 3.

[0079] Table 3 Computer simulation prediction results of FAPEFLEH umami peptide health activity

[0080]

[0081] As shown in Table 3, FAPEFLEH umami peptide has ACE inhibitory activity, DPP-IV inhibitory activity, α-glucosidase inhibitory activity, and renin inhibitory activity. Based on the characteristics of the oligopeptide amino structure, FAPEFLEH umami peptide has the effect of lowering blood pressure and blood sugar.

Claims

1. An umami peptide derived from soybean residue, characterized in that: The amino acid sequence of the umami peptide is: Phe-Ala-Pro-Glu-Phe-Leu-Glu-His.

2. Use of the soybean residue-derived umami peptide according to claim 1 in the preparation of food additives.

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