Antioxidant active douchi umami peptide, preparation method and application thereof

Abstract

This invention discloses umami peptides from fermented black soybeans with antioxidant activity, their preparation methods, and applications, relating to food processing technology and seasoning bases. Five umami peptides from fermented black soybeans (TYDGDTEP, VGSEL, FGDEL, IGISIDDH, and RDLL) were screened and obtained. Verification showed that these five umami peptides have significant umami-enhancing effects, providing novel umami peptide resources for seasoning preparation. Further enhancement through antioxidant and Fe... 3+ Tests on reducing power and tyrosinase inhibition revealed that these five umami peptides also possess certain antioxidant capabilities and Fe... 3+ Its reducing power and tyrosinase inhibition capabilities provide technical support for the development of antioxidant products, products that improve iron deficiency anemia (helping to improve iron absorption), and skin whitening products.

Description

Technical Field

[0001] This invention relates to the fields of food processing technology and seasoning bases, and in particular to umami peptides of fermented black soybean with antioxidant activity, their preparation methods and applications. Background Technology

[0002] Fermented black beans (douchi), a traditional fermented food, have a long history and rich cultural connotations in my country. In recent years, research has found that douchi is rich in antioxidant umami peptides, which are low-cost and natural, bringing significant benefits to the food industry and human health.

[0003] Fermented black soybeans (douchi) are a popular food ingredient, abundant in raw materials, widely available, and affordable. Extracting antioxidant umami peptides using biotechnology can not only reduce production costs but also increase the added value of the product, bringing significant economic benefits to food companies. Secondly, douchi antioxidant umami peptides possess natural properties. The extraction process adheres to green and environmentally friendly principles, employing physical methods to ensure the product's natural attributes. This makes douchi antioxidant umami peptides safer and more reliable for application in food, health products, and other fields, meeting consumer demand for green and natural products. Furthermore, douchi antioxidant umami peptides possess various physiological activities, which give them broad application prospects in health foods, cosmetics, and other fields. Simultaneously, they can also serve as a novel food additive, improving the taste and quality of food and enhancing the consumer's eating experience. Based on this, this invention aims to develop new douchi antioxidant umami peptides for use in the food and health product industries. Summary of the Invention

[0004] The purpose of this invention is to provide umami peptides from fermented black soybeans with antioxidant activity, their preparation method, and applications, thereby solving the problems existing in the prior art. The umami peptides from fermented black soybeans developed in this invention have a significant flavor-enhancing effect and also possess certain antioxidant capacity and Fe content. 3+ Its reducing power and tyrosinase inhibition capabilities provide technical support for the development of flavorings, antioxidant products, products that help improve iron absorption, and skin whitening products.

[0005] To achieve the above objectives, the present invention provides the following solution:

[0006] This invention provides a fermented black bean umami peptide with antioxidant activity, wherein the amino acid sequence of the fermented black bean umami peptide is shown in any one of SEQ ID NO.1-5.

[0007] The present invention also provides a method for preparing the above-mentioned fermented black bean umami peptide, including the step of preparing the fermented black bean umami peptide by solid-phase synthesis.

[0008] The present invention also provides the application of the above-mentioned fermented black bean flavor peptide in the preparation of seasonings or in enhancing the umami flavor of food.

[0009] The present invention also provides the application of the above-mentioned fermented soybean umami peptide in the preparation of products that help with antioxidation, wherein the products are pharmaceuticals or health products.

[0010] The present invention also provides the application of the above-mentioned fermented soybean flavor peptide in the preparation of products that improve iron deficiency anemia, wherein the products are pharmaceuticals or health products.

[0011] The present invention also provides the application of the above-mentioned fermented soybean umami peptide in the preparation of tyrosinase inhibitors or whitening products.

[0012] The present invention also provides a condiment comprising the above-mentioned fermented black bean umami peptide.

[0013] The present invention also provides a product that helps with anti-oxidation, the active ingredient of which includes the above-mentioned fermented black bean umami peptide;

[0014] The product in question is a pharmaceutical or health supplement.

[0015] The present invention also provides a product for improving iron deficiency anemia, the active ingredient of which includes the above-mentioned fermented soybean umami peptide;

[0016] The product in question is a pharmaceutical or health supplement.

[0017] The present invention also provides a tyrosinase inhibitor, the active ingredient of which includes the above-mentioned fermented black bean umami peptide.

[0018] The present invention discloses the following technical effects:

[0019] This invention employs ultrafiltration extraction combined with ion exchange resin purification and separation. After debittering treatment of fermented soybean peptides, five fermented soybean umami peptides (TYDGDTEP, VGSEL, FGDEL, IGISIDDH, and RDLL) were screened and obtained. Verification showed that these five fermented soybean umami peptides have significant umami-enhancing effects, with a relative umami intensity of 82.70%-92.34% compared to monosodium glutamate, and a relatively weak bitterness. This invention provides a novel umami peptide resource for the preparation of condiments.

[0020] Further through antioxidant, Fe 3+ Tests on reducing power and tyrosinase inhibition revealed that these five fermented soybean umami peptides also possess certain antioxidant capabilities and Fe... 3+ Its reducing power and tyrosinase inhibition capabilities provide technical support for the development of antioxidant products, products that improve iron deficiency anemia (helping to improve iron absorption), and skin whitening products. Attached Figure Description

[0021] To more clearly illustrate the technical solutions in the embodiments of the present invention or the prior art, the drawings used in the embodiments will be briefly introduced below. Obviously, the drawings described below are only some embodiments of the present invention. For those skilled in the art, other drawings can be obtained based on these drawings without creative effort.

[0022] Figure 1 This is a schematic diagram of the process for separating, purifying, and extracting the finished product, fermented black soybeans.

[0023] Figure 2 Sensory radar chart of umami peptides;

[0024] Figure 3 The results of constructing the concentration-relative umami intensity curve of umami peptide TYDGDTEP are shown; where A is the fitting curve between different concentrations of umami peptide TYDGDTEP and the corresponding MSG concentration; B is the relationship curve between each concentration of umami peptide TYDGDTEP and the relative umami intensity.

[0025] Figure 4 The results of constructing the umami peptide VGSEL concentration-relative umami intensity curve are shown; where A is the fitting curve between different concentrations of umami peptide VGSEL and the corresponding MSG concentration; B is the relationship curve between each concentration of umami peptide VGSEL and the relative umami intensity.

[0026] Figure 5 The results of constructing the umami peptide FGDEL concentration-relative umami intensity curve are shown; where A is the fitting curve between different concentrations of umami peptide FGDEL and the corresponding MSG concentration; B is the relationship curve between each concentration of umami peptide FGDEL and the relative umami intensity.

[0027] Figure 6 The results of constructing the umami peptide IGISIDDH concentration-relative umami intensity curve are shown; where A is the fitting curve between different concentrations of umami peptide IGISIDDH and the corresponding MSG concentration; B is the relationship curve between each concentration of umami peptide IGISIDDH and the relative umami intensity.

[0028] Figure 7 The results of constructing the umami peptide RDLL concentration-relative umami intensity curve are shown; where A is the fitting curve between different concentrations of umami peptide RDLL and the corresponding MSG concentration; B is the relationship curve between each concentration of umami peptide RDLL and the relative umami intensity.

[0029] Figure 8 This is a taste intensity diagram showing the synergistic effect of umami peptides.

[0030] Figure 9 The results of the detection of the ability of umami peptides to scavenge DPPH free radicals are shown in the figure.

[0031] Figure 10 For umami peptides to Fe 3+ Image showing the test results of reducing power;

[0032] Figure 11 The graph shows the results of the detection of the inhibitory effect of umami peptides on tyrosinase. Detailed Implementation

[0033] Various exemplary embodiments of the present invention will now be described in detail. This detailed description should not be considered as a limitation of the present invention, but rather as a more detailed description of certain aspects, features, and embodiments of the present invention.

[0034] It should be understood that the terminology used in this invention is merely for describing particular embodiments and is not intended to limit the invention. Furthermore, with respect to numerical ranges in this invention, it should be understood that each intermediate value between the upper and lower limits of the range is also specifically disclosed. Any stated value or intermediate value within a stated range, as well as each smaller range between any other stated value or intermediate value within said range, is also included within the scope of this invention. The upper and lower limits of these smaller ranges may be independently included or excluded from the range.

[0035] Unless otherwise stated, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art. While only preferred methods and materials have been described herein, any methods and materials similar or equivalent to those described herein may be used in the implementation or testing of this invention. All references to this specification are incorporated by way of citation to disclose and describe methods and / or materials associated with those references. In the event of any conflict with any incorporated reference, the content of this specification shall prevail.

[0036] Various modifications and variations can be made to the specific embodiments described in this specification without departing from the scope or spirit of the invention, as will be apparent to those skilled in the art. Other embodiments derived from this specification will also be apparent to those skilled in the art. This specification and embodiments are merely exemplary.

[0037] The terms “include,” “including,” “have,” “contain,” etc., used in this article are all open-ended terms, meaning that they include but are not limited to.

[0038] Example 1

[0039] like Figure 1 As shown, the finished fermented black soybeans were separated, purified, and extracted:

[0040] (1) Take 200g of finished fermented black beans and soak them in ice water for 15 minutes. Drain the water, add 600mL of purified water and mix. Place the mixture in a mixer and stir for 2 minutes. Then place it in a water bath at 45℃ for 1 hour. Centrifuge (3000×g, 40min, 20℃). Pass the supernatant through 100-mesh nylon gauze.

[0041] (2) The above filtrate is filtered through an ultrafiltration membrane with a molecular weight cutoff of 3kDa. Peptides with a molecular weight less than 3kDa are collected. The filtrate is then subjected to rotary evaporation. The temperature of the rotary evaporator during concentration is 45℃.

[0042] (3) The above concentrate was debittered using an XAD-7 ion exchange resin chromatography column. Based on the separation principle of XAD-7HP ion exchange resin, it was eluted with ultrapure water, 20% edible ethanol, and 40% edible ethanol respectively at a flow rate of 5.0 mL / min. The eluents of each component were collected and concentrated by rotary evaporation and freeze-dried to obtain three components A3-I, A3-II, and A3-III with yields of 60.12%, 8.63%, and 0.82%, respectively.

[0043] Example 2

[0044] Umami peptides were screened from the A3-I component obtained in Example 1:

[0045] (1) The amino acid sequences of the crude umami peptide extract were identified by UPLC-MS / MS, revealing 205 peptide segments, ranging from tetrapeptides to dodecapeptides, with relative molecular masses distributed between 300 and 1300. Among them, peptides with a molecular weight <1 kDa were the most numerous, totaling 163 segments, accounting for 79.5%; the remainder were polypeptides with a molecular weight >1500 Da. In terms of the number of amino acids, peptides containing 4 to 10 amino acids were the most numerous, totaling 184 segments, accounting for 89.8%; the remainder were polypeptides containing more than 10 amino acids.

[0046] (2) Using toxicity, relative molecular mass of peptides and amino acid backbone structure of umami peptides (number of carbon atoms n = 3 to 9) as the initial screening criteria, a total of 76 peptides were screened. Molecular docking was used to virtually screen 19 umami peptides that could bind to the umami receptors T1R1 / T1R3. Based on the binding energy, 5 umami peptides with the lowest binding energy to the umami receptors were screened out, namely: TYDGDTEP (SEQ ID NO.1), VGSEL (SEQ ID NO.2), FGDEL (SEQ ID NO.3), IGISIDDH (SEQ ID NO.4) and RDLL (SEQ ID NO.5).

[0047] Example 3

[0048] Synthesis of umami peptides:

[0049] The five umami peptides screened in Example 2 were synthesized using a solid-phase synthesis method, as follows:

[0050] The C-terminal protected amino acid (using Fmoc as a protecting group) is chemically bonded to the resin; the N-terminal protecting group of the amino acid is removed using DMF; the next amino acid with both an N-terminal protecting group and a side-chain protecting group is added, and a condensing agent is used to promote the formation of an amide bond between the two amino acids; after the reaction is complete, the unreacted amino group is blocked to ensure that each step is a quantitative reaction; the above steps are repeated to sequentially link the amino acids to the growing peptide chain in a predetermined order until the synthesis of the entire sequence is completed; after synthesis, the complete polypeptide chain is cleaved from the resin using a strong acid (trifluoroacetic acid), while all side-chain protecting groups are removed simultaneously.

[0051] Example 4

[0052] The five umami peptides synthesized in Example 3 were tested as follows:

[0053] 1. Sensory evaluation and flavor threshold test

[0054] Sensory evaluation: The peptide concentration in the sensory evaluation was 1%. A scoring method was used to evaluate the samples, ranging from 0 to 10 points. 0 points indicated that the tested sample had no taste, while 10 points indicated that the sample had a significant taste. 0.7% edible salt solution, 0.35% MSG solution, 1% sucrose solution, 0.08% citric acid solution, and 0.5% L-leucine solution were selected as standards for saltiness, umami, sweetness, sourness, and bitterness, respectively, and scored out of 5 points.

[0055] Taste threshold determination: The stimulation threshold of synthetic peptide samples was determined by the taste dilution method. A 1% synthetic peptide solution was prepared and gradually diluted at a 1:1 ratio according to the triangulation test principle. Each dilution level was evaluated by 3 measurements until it was just distinguishable from the other two blank controls (pure water). The sample concentration at this point is the taste threshold of the sample. The stimulation threshold of each evaluation group was the average of the results of each taster.

[0056] like Figure 2The sensory evaluation results showed that TYDGDTEP, VGSEL, and FGDEL had high umami scores of 8.5 and 7.8, respectively, with slightly sour, bitter, and astringent tastes, and good flavor performance. IGISIDDH and RDLL had prominent sweetness but weaker flavor performance. Peptides containing glutamic acid or aspartic acid had higher umami scores and lower flavor thresholds. For example, the flavor thresholds for peptides TYDGDTEP, FGDEL, and IGISIDDH were 1.0 mg / mL, and for VGSEL, 0.5 mg / mL, as shown in Table 1. RDLL had a relatively high flavor threshold of 2.0 mg / mL, possibly due to the hydrophobic amino acids at the peptide chain ends affecting the solubility equilibrium of the peptide in low-concentration solutions. RDLL also had a prominent bitterness, which is related to its hydrophobic amino acids. Hydrophobic amino acids can cause a certain degree of bitterness, and the number of hydrophobic amino acids in the peptide chain may be positively correlated with the bitterness of the peptide.

[0057] Table 1 Flavor characteristics and flavor thresholds of peptides

[0058]

[0059] 2. Test of relative umami intensity of umami peptides

[0060] The umami intensity of five umami peptides was compared using the 2-AFC sensory evaluation method. All members of the 2-AFC sensory evaluation team received relevant training. In each test, team members received three sets of samples. Each set consisted of a 5 mL umami peptide solution and a monosodium glutamate (MSG) solution, and the testing order was randomized. Furthermore, different concentrations of umami peptides were compared with three concentrations of MSG solutions; the specific umami peptides and their corresponding MSG concentrations are shown in Table 2. During the sensory evaluation, team members were required to focus on the umami intensity of the umami peptides in each sample solution, rotating the solution in their mouths for 10 seconds. To avoid solution residue in the mouth, team members were required to rinse their mouths with mineral water at least three times, rest for 5 minutes, and then proceed to the next set of solution samples for sensory evaluation. The proportion of team members who considered the MSG sample to have a higher umami intensity was called the selection rate. A linear regression curve was then plotted based on the relationship between the selection rate and the MSG concentration. When the selection rate is 50%, the corresponding MSG concentration is the equivalent umami intensity of the peptide. Then, a curve of umami peptide concentration versus relative umami intensity is plotted.

[0061] Table 2. Correspondence between the concentrations of umami peptides and monosodium glutamate.

[0062]

[0063] Figures 3-7Table 3 shows the fitting curves between different concentrations of umami peptides and their corresponding MSG concentrations, while Table 3 provides the fitting equations for different concentrations of umami peptides. When the y-value is 50%, the equation y = 113.33x - 15.667 yields x = 0.58, meaning that 0.58 mg / mL MSG is equivalent to 0.5 mg / mL TYDGDTEP in umami intensity. Therefore, the MSG concentration corresponding to the 50% screening is calculated as the equivalent umami intensity of the umami peptide, thus obtaining the relationship curves between each concentration of umami peptide and its relative umami intensity, as detailed in Table 4. The calculation method for the umami intensity of other umami peptides is consistent with that for TYDGDTEP. The results show that within the detected concentration range, there is a logarithmic relationship between the relative MSG umami intensity and the umami peptide concentration. Using a 5 mg / mL umami peptide concentration as a baseline, the relative umami intensity (based on MSG concentration) is calculated and compared using concentration-taste curves, and the results are shown in Table 4. Among the five umami peptides, TYDGDTEP (4.617 mg / mL) and VGSEL (4.546 mg / mL) had higher relative umami intensity than the others, while RDLL (4.172 mg / mL) had the lowest relative umami intensity. This indicates that all five umami peptides possess good umami flavor and richness, and have significant application value in the food industry.

[0064] Table 3. Fitting curves between different concentrations of umami peptides and corresponding MSG concentrations.

[0065]

[0066]

[0067] Table 4. Relationship curves between umami peptides at different concentrations and relative umami intensity.

[0068]

[0069] 3. Descriptive evaluation of umami peptides

[0070] Using the umami flavor of a 0.35% MSG solution as a sensory standard, with a score of 5, synthetic peptides were added to the MSG solution, resulting in a peptide concentration of 2 mg / mL in the 0.35% MSG solution. The umami flavor was then evaluated to assess its umami-enhancing effect. Similarly, using the saltiness flavor of a 0.35% salt solution as a sensory standard, with a score of 5, synthetic peptides were added to the salt solution, resulting in a peptide concentration of 2 mg / mL in the 0.35% salt solution. The saltiness flavor was then evaluated, with the standard salt solution scoring 5 points, to assess the synergistic effect of the synthetic peptides and salt. Finally, using a mixed solution of 0.35% NaCl and MSG as a sensory standard, with a score of 5, synthetic peptides were added to the NaCl and MSG mixed solution to achieve a synthetic umami peptide concentration of 2 mg / mL. The sensory characteristics of the synthetic peptide + MSG + NaCl sample group were then evaluated.

[0071] The synergistic flavor-enhancing effect score of umami peptides is as follows: Figure 8 As shown, in MSG solution, peptides TYDGDTEP, VGSEL, and IGISIDDH exhibit strong umami-enhancing effects. Peptide VGSEL shows a significant umami enhancement and a relatively thick flavor-enhancing effect, while peptide IGISIDDH has a slightly salty taste. Peptides FGDEL and RDLL have mild umami-enhancing effects, while peptide RDLL has a slightly astringent taste. All five synthetic peptides mentioned above enhance umami in MSG solution and can combine with other umami substances to further enhance umami flavor.

[0072] In a descriptive evaluation experiment using synthetic peptides at a concentration of 2.0 mg / mL added to a salt solution, it was found that peptides TYDGDTEP and IGISIDDH slightly enhanced the saltiness and made the original salt solution taste richer and more harmonious. Among them, peptide TYDGDTEP scored the highest. Peptides VGSEL, FGDEL, and RDLL, when synergistically reacted with the salt solution, could enhance the saltiness of the solution and add a slightly astringent taste.

[0073] In a simulated umami solution, the five synthetic peptides significantly enhanced both umami and saltiness. Compared to a single umami solution (MSG+NaCl), TYDGDTEP and VGSEL showed particularly significant umami enhancement, exhibiting distinct umami characteristics. FGDEL, IGISIDDH, and RDLL showed similar effects in enhancing umami. Compared to saltiness, these five synthetic peptides performed more prominently in enhancing umami, indicating that they possess strong umami properties and can synergistically enhance umami with other umami components.

[0074] Example 5

[0075] Antioxidant activity tests were performed on the five umami peptides synthesized in Example 3:

[0076] Measurement of DPPH free radical scavenging ability: Sample concentrations of 0.4, 0.8, 1.2, 1.6, and 2.0 mg / mL were prepared. 2.0 mL of sample solution was mixed with an equal volume of 0.1 mmol / L DPPH solution using a vortex mixer. After reacting for 30 min, the absorbance was measured at 517 nm and recorded as A1. Absorbance was measured under the same conditions using an equal volume of anhydrous ethanol solution instead of the DPPH solution and the sample solution, and recorded as A2 and A0, respectively. Anhydrous ethanol was used for zeroing. Vitamin C (Vc) was used as a positive control for comparative analysis. The DPPH free radical scavenging rate was calculated using the following formula:

[0077] DPPH free radical scavenging rate % = (1 - (A1 - A2) / A0) × 100%.

[0078] like Figure 9 As shown, the free radical scavenging abilities of umami peptides TYDGDTEP, VGSEL, FGDEL, IGISIDDH, and RDLL increased with increasing sample concentration, with peptide RDLL exhibiting the strongest DPPH free radical scavenging ability. At a concentration of 2 mg / mL, RDLL's free radical scavenging ability reached 53.04%, which is 56.76% of the DPPH free radical scavenging rate of vitamin C. Following closely were peptides TYDGDTEP, IGISIDDH, FGDEL, and VGSEL, with DPPH free radical scavenging abilities of 43.52%, 39.14%, 36.98%, and 31.6%, respectively, indicating that the umami peptides synthesized in this invention possess strong antioxidant capabilities.

[0079] Example 6

[0080] The five umami peptides synthesized in Example 3 were subjected to Fe... 3+ Restoration ability test:

[0081] The samples were diluted to concentrations of 0.4, 0.8, 1.2, 1.6, and 2.0 mg / mL. 0.1 mL of sample was mixed with 0.1 mL of PBS (0.2 mol / L, pH 6.6) and 0.1 mL of 1% potassium ferricyanide, and incubated in a 50°C water bath for 20 min. Then, 0.1 mL of 10% trichloroacetic acid (TCA), 2 mL of distilled water, and 0.08 mL of 0.2% ferric chloride were added, and the OD was measured. 700nm The value was determined using vitamin C as a positive control.

[0082] like Figure 10 As shown, the Fe content of umami peptides TYDGDTEP, VGSEL, FGDEL, IGISIDDH, and RDLL is... 3+ The reducing power increased with increasing sample concentration, with peptide FGDEL exhibiting the strongest reducing power. At a concentration of 2 mg / mL, the absorbance of RDLL was 0.055, which is equivalent to that of vitamin C. 3+ The reducing power was 2.91%. This was followed by peptides FGDEL, TYDGDTEP, VGSEL, and IGISIDDH. 3+ The reducing abilities were 2.64%, 2.59%, 2.59%, and 2.32% of vitamin C, respectively, indicating that the umami peptides synthesized in this invention possess certain Fe content. 3+ Its reducing power can help improve the absorption of iron.

[0083] Example 7

[0084] The tyrosinase inhibitory activity of the five umami peptides synthesized in Example 3 was tested:

[0085] Weigh different peptides and prepare sample solutions at concentrations of 0.4, 0.8, 1.2, 1.6, and 2.0 mg / mL. Add reagents sequentially to 96-well plates according to the dosages in Table 5, followed by the tyrosinase solution. Shake well and incubate at 25°C for 20 min. Measure the absorbance at 475 nm using a microplate reader, with ascorbic acid as a positive control. Perform three replicates per group. Calculate the tyrosinase inhibition rate using the following formula: Inhibition rate / % = (1 - OD0)2 样品 / OD 空白 )×100%.

[0086] Table 5. Reagents and dosages added to 96-well plates

[0087]

[0088] like Figure 11 As shown, the tyrosinase inhibition rates of umami peptides TYDGDTEP, VGSEL, FGDEL, IGISIDDH, and RDLL increased with increasing sample concentration, with TYDGDTEP exhibiting the strongest overall tyrosinase inhibition rate. At a concentration of 2 mg / mL, the tyrosinase inhibition rates of TYDGDTEP, IGISIDDH, and RDLL were similar, at 67.64%, 67.69%, and 67.64%, respectively, with IGISIDDH showing an inhibition rate of 74.29% of that of vitamin C. Following closely were FGDEL and VGSEL, with inhibition rates of 62.71% and 57.25%, respectively, indicating that the umami peptides synthesized by fermented black soybeans possess a strong tyrosinase inhibitory ability.

[0089] The embodiments described above are merely preferred embodiments of the present invention and are not intended to limit the scope of the present invention. Various modifications and improvements made by those skilled in the art to the technical solutions of the present invention without departing from the spirit of the present invention should fall within the protection scope defined by the claims of the present invention.

Claims

1. Use of a fermented soybean flavor peptide in the preparation of a product that helps against oxidation, characterized in that, The product is a health product; The amino acid sequence of the fresh-taste peptide of black bean is shown as SEQ ID NO.

1.

2. Use of the soybean flavor peptide in the preparation of a product for improving iron deficiency anemia, characterized in that, The product is a health product or a medicine; The amino acid sequence of the fresh-taste peptide of black bean is shown as SEQ ID NO.

1.

3. Use of a fermented soybean flavor peptide in the preparation of a whitening product, characterized in that, The amino acid sequence of the fresh-taste peptide of black bean is shown as SEQ ID NO. 1.

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