Corn active peptide with effects of dispelling effects of alcohol, reducing uric acid and resisting oxidation, preparation and application of corn active peptide

Abstract

The invention discloses a corn active peptide with effects of dispelling effects of alcohol, reducing uric acid and resisting oxidation, a preparation and application of the corn active peptide, and belongs to the technical field of biological active peptides. The amino acid sequence of the corn active peptide is at least one of LMFP, FEGLFR, FLR and QLPSYR. The corn active peptide with the effects of dispelling the effects of alcohol, reducing uric acid and resisting oxidation is separated from corn germ meal through enzymolysis, ultrafiltration and other technologies, amino acid sequence determination is conducted on the separated peptide fragments, screening is conducted in combination with the bioinformatics technology, and finally four peptide fragments are obtained. According to the present invention, the corn active peptides are identified, chemical synthesis is performed according to the identified peptide fragment sequence, the effects of alcohol effect dispelling, uric acid reducing and oxidation resistance of the synthesized single peptide fragment and the compounded peptide fragment are determined, and the corn active peptides have good XOD inhibition rate, good DPPH clearance rate and good ADH activation rate, and have important application prospects in the development of the products with effects of alcohol effect dispelling, uric acid reducing and oxidation resistance.

Description

Technical Field

[0001] The present invention belongs to the technical field of bioactive peptides, and in particular relates to corn active peptides with alcohol-relieving, uric acid-lowering and anti-oxidation effects, preparations and applications thereof. Background Art

[0002] Hyperuricemia and alcoholic liver disease (ALD) have become global public health issues threatening human health. Allopurinol and benzbromarone are clinically used to treat conditions such as hyperuricemia and gout. While these drugs can rapidly lower serum uric acid levels, they can also cause adverse reactions in patients. The pathogenesis of ALD is complex, and there are no clearly targeted therapeutic agents. The most common steroid treatment, corticosteroids, has been unsatisfactory.

[0003] In recent years, numerous studies have demonstrated that bioactive peptides derived from food proteins are potential factors in regulating metabolism and promoting human health. Bioactive peptides typically consist of 2-20 amino acids. These sequences often lack biological activity due to being embedded within the parent protein. However, they typically exhibit enhanced physiological activity after hydrolysis and release through fermentation, enzymatic hydrolysis, and gastrointestinal digestion. Compared to proteins, peptides possess the advantages of low molecular weight, ease of absorption, and high stability.

[0004] Therefore, isolating multifunctional active peptides from corn germ meal that have the effects of lowering uric acid and relieving alcohol from corn germ meal protein is of great significance for enriching medicines, foods or health products with the effects of lowering uric acid and relieving alcohol, and protecting human health. Summary of the Invention

[0005] In view of the problems existing in the prior art, the purpose of the present invention is to provide corn active peptides, preparations and applications thereof with alcohol-relieving, uric acid-lowering and antioxidant effects.

[0006] In order to achieve the above object, the present invention adopts the following technical solutions: A corn active peptide with alcohol sobering, uric acid lowering and antioxidant effects, wherein the amino acid sequence of the corn active peptide is at least one of LMFP, FEGLFR, FLR and QLPSYR.

[0007] The application of the corn active peptide with the effects of sobering up, lowering uric acid and anti-oxidation is used to prepare products with the effects of sobering up, lowering uric acid and anti-oxidation.

[0008] Based on the above solution, the product is food, medicine or health product.

[0009] Based on the above solution, the product further comprises excipients acceptable to food, medicine or health products.

[0010] A preparation with alcohol sobering, uric acid lowering and antioxidant effects, wherein the active ingredient is at least one of LMFP, FEGLFR, FLR and QLPSYR.

[0011] Based on the above protocol, the concentration of the active ingredient was 1 mg / mL.

[0012] On the basis of the above scheme, the hangover-relieving effect is achieved by increasing the ADH activation rate.

[0013] On the basis of the above scheme, the uric acid lowering effect is achieved by increasing the XOD inhibition rate.

[0014] On the basis of the above scheme, the antioxidant has a DPPH free radical scavenging effect.

[0015] Advantages of the technical solution of the present invention: The present invention isolates corn active peptides with alcohol-relieving, uric acid-lowering, and antioxidant effects from corn germ meal through enzymatic hydrolysis, ultrafiltration, and other techniques. The isolated peptides are subjected to amino acid sequence determination and bioinformatics screening, ultimately obtaining four peptides. Chemical synthesis is performed based on the identified peptide sequences, and the alcohol-relieving, uric acid-lowering, and antioxidant effects of the synthesized single and composite peptides are determined. These corn active peptides all have good XOD inhibition rates, DPPH clearance rates, and ADH activation rates. They can be used not only as natural antioxidants in foods, medicines, and / or cosmetics, but also as natural uric acid-lowering supplements and alcohol-relieving agents in medicines, foods, and / or health products. These peptides have important application prospects in the development of products with alcohol-relieving, uric acid-lowering, and antioxidant effects. BRIEF DESCRIPTION OF THE DRAWINGS

[0016] Figure 1 DPPH scavenging rate (A), ADH activation rate (B), and XOD inhibition rate (C) of polypeptide fractions with different molecular weights; Figure 2 This is a Sephadex G-15 gel chromatography separation diagram; Figure 3 The DPPH scavenging rate (A), ADH activation rate (B) and XOD inhibition rate (C) of the four components C1, C2, C3 and C4; Figure 4 is the total ion chromatogram; Figure 5 is the mass spectrum of LMFP; Figure 6 is the mass spectrum of FEGLFR; Figure 7 is the mass spectrum of FLR; Figure 8 is the mass spectrum of QLPSYR; Figure 9 Effects of four different proteases on DH (A), DPPH radical scavenging rate (B), ADH activation rate (C), and XOD inhibition rate (D) of corn hydrolysate; Figure 10 Effects of different enzymatic hydrolysis times on DH (A), DPPH radical scavenging rate (B), ADH activation rate (C), and XOD inhibition rate (D) of corn hydrolysates; Figure 11 Effects of different enzyme addition amounts on DH (A), DPPH free radical scavenging rate (B), ADH activation rate (C) and XOD inhibition rate (D) of corn hydrolysate; Figure 12 Effects of different material-liquid ratios on DH (A), DPPH radical scavenging rate (B), ADH activation rate (C), and XOD inhibition rate (D) of corn hydrolyzate; Figure 13 Response surface plots of each experimental factor DH (A), DPPH free radical scavenging rate (B), ADH activation rate (C) and XOD inhibition rate (D); Figure 14 DPPH scavenging rate (A), ADH activation rate (B), and XOD inhibition rate (C) of a single corn active peptide; Figure 15 DPPH scavenging rate (A), ADH activation rate (B), and XOD inhibition rate (C) of compound corn active peptides.

[0017] In the figures of the above description, different lowercase letters ae indicate significant differences (p<0.05). DETAILED DESCRIPTION

[0018] The terms used in the present invention, unless otherwise specified, generally have the meanings commonly understood by those of ordinary skill in the art. Below, in conjunction with specific examples, the present invention will be further described in detail with reference to data. The following examples are merely for illustration of the present invention and are not intended to limit the scope of the present invention in any way.

[0019] The experimental methods in the following examples, unless otherwise specified, are all conventional methods and are performed according to the techniques or conditions described in the literature in this field or according to the product instructions. The experimental materials, reagents, and drugs used in the following examples, unless otherwise specified, can all be purchased through general channels.

[0020] In the following examples, 1. The method for determining the degree of hydrolysis DH is as follows: The pH-Stat method is used to determine the hydrolysis of corn protein. During the hydrolysis process, as protons are released, the pH value of the solution drops sharply. At this time, 0.1 M NaOH solution is added to maintain the pH. The degree of hydrolysis (DH) can be calculated based on the volume of alkali solution added. The calculation formula is as follows: Where: C, concentration of NaOH solution, moL / L; V, volume of NaOH solution consumed, mL; a, degree of dissociation of α-amino group; , where pH is the pH value of the hydrolysis system, pKa is the pKa of the amino group, , where T is the temperature in Kelvin; m, mass of zein in solution, g; htot, the total number of peptide bonds in the substrate protein, mmol / g, for zein hot = 7.35.

[0021] 2. Determination of DPPH free radical scavenging ability: The protein peptide solution was mixed with an equal volume of 0.1 mmol / L DPPH ethanol solution and reacted at room temperature in the dark for 30 min. The absorbance was measured at a wavelength of 517 nm and recorded as A. 样品 , use an equal amount of ethanol to replace the DPPH ethanol solution to determine the corresponding absorbance value, recorded as A 空白 , an equal amount of distilled water was used to replace the protein peptide solution to determine the corresponding absorbance value, which was recorded as A 对照 , calculate the DPPH free radical scavenging rate, the formula is as follows: 3. Determination of ADH activation rate: 50 μL of sample solution was mixed with 150 μL of detection reagent (containing 22.4 mM sodium pyrophosphate buffer, 3.3% ethanol and 7.8 mM NAD+), and after equilibration at 37 °C for 5 min, 50 μL of ADH (0.2 U / mL) was added to initiate the reaction. The absorbance at 340 nm was detected using a Varioskan Flash full-wavelength scanning multifunctional reader, and recorded every 10 s for 10 min. Distilled water was used instead of the sample as a negative control. The reaction kinetic curve was fitted, and the first derivative of the curve at 0 min was obtained, which was the initial reaction rate. The initial reaction rate of the sample was recorded as Vs, while that of the negative control was recorded as V0. The ADH activation rate of the sample can be calculated according to the following equation: 4. Determination of XOD inhibition rate Preparation of xanthine solution (0.48 mM): Weigh 7.30 mg of xanthine powder and dissolve it in 400 μL of 1 mol / L NaOH. Then, dilute to 100 mL with PBS buffer to obtain the desired xanthine solution.

[0022] 50 μL of peptide solution, 50 μL of 0.02 U / mL xanthine oxidase solution, mix well and incubate at 25 degrees for 5 min. Then add 150 μL of 0.48 mmol / L xanthine solution, mix well and incubate at 25°C for 25 min. After the reaction, add 80 μL of 1M HCl to terminate the reaction. Then measure the absorbance of the supernatant of each component at a wavelength of 290 nm. The absorbance value of the sample group is recorded as A, the absorbance value of the group without enzyme is recorded as B, the absorbance value of the group without sample is recorded as C, and the absorbance value of the group without enzyme and sample is recorded as D. The xanthine oxidase inhibition effect is calculated using the following formula: The corn germ meal protein in the following examples was purchased from Weifang Shengtai Pharmaceutical Co., Ltd.

[0023] Example 1 A corn active peptide with alcohol sobering, uric acid lowering and antioxidant effects, wherein the corn active peptide is a peptide having an amino acid sequence shown by at least one of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, and SEQ ID NO: 4: SEQ ID NO: 1: LMFP; SEQ ID NO: 2: FEGLFR; SEQ ID NO: 3: FLR; SEQ ID NO:4: QLPSYR.

[0024] Example 2 A method for isolating corn active peptides having alcohol-relieving, uric acid-lowering and antioxidant effects from corn germ meal, comprising the following steps: (1) Pretreatment of corn germ meal protein: corn germ meal protein was dissolved in 50 mL of water at a solid-liquid ratio of 27.44%, and heated at 90 °C for 10 min to pre-denature the protein; (2) Enzymatic hydrolysis: 1.35% (1.35% of the corn germ meal protein mass) of alkaline protease was added to the corn germ meal protein solution for hydrolysis. The enzymatic hydrolysis was carried out at 55°C and pH 10 for 2.3 h. During this process, the protein solution was continuously stirred and the pH of the system was controlled with 0.1 M NaOH to maintain the pH at the optimal pH of the protease. After the enzymatic hydrolysis was completed, the enzymatic hydrolyzate was heated at 90°C for 15 min to denature and inactivate the enzyme to terminate the reaction. The enzymatic hydrolyzate was then centrifuged at 4000 r / min in a refrigerated centrifuge at 4°C for 20 min, and the supernatant was retained.

[0025] (3) Ultrafiltration separation: The supernatant of the corn germ meal protein hydrolysate obtained in step (2) was first filtered with a 0.22 μm filter membrane, and then separated into three different molecular weight fractions using 10 kDa and 3 kDa ultrafiltration centrifuge tubes: >10 KDa, 3-10 KDa, and <3 KDa. The XOD inhibition rate, DPPH clearance rate, and ADH activation rate of the fractions with different molecular weights were measured. The results are as follows: Figure 1 As shown in the figure, the XOD inhibition rate, DPPH clearance rate and ADH activation rate of the molecules with molecular weight <3 KDa showed good effects.

[0026] (4) Protein purification instrument (ÄKTA pure) separation: The gel chromatography column used was Sephadex G-25. The corn germ meal protein hydrolysate with a molecular weight of <3 KDa was separated by a protein purification instrument. The sample concentration was 15 mg / mL, the sample volume was 5 mL, the eluent was ultrapure water, the flow rate was 2 mL / min, and the detection wavelength was 280 nm. A total of 4 groups of polypeptide mixtures with different molecular weight components were obtained ( Figure 2 ); Determine the XOD inhibition rate, DPPH clearance rate and ADH activation rate of each molecular weight component. The results show that component C2 has a good effect in XOD inhibition rate, DPPH clearance rate and ADH activation rate ( Figure 3 ).

[0027] (5) LC-MSMS sequencing: The above-mentioned component C2 was subjected to mass spectrometry sequencing, and a total of 841 corn peptides were obtained after database sequence comparison ( Figure 4 ).

[0028] (6) Bioinformatics technology was used to screen multifunctional active peptides from corn germ meal: Screening criteria: ① The molecular weight of the peptide was generally selected as short peptides not exceeding 1KDa; ② The higher the ALC value, the higher the credibility, and peptides with ALC>80% were selected; ③ The larger the relative peak area, the higher the relative content of the substance, and peptides with relative peak area>105 were selected; ④ The PeptideRanker program was used to predict the potential biological activity of the peptide online, and the higher the score, the stronger the potential biological activity, and peptides with a score>0.5 were selected; ⑤ The ToxinPred3.0 program was used to predict biological toxicity, and non-toxic peptides were selected; ⑥ The Peptideproperty calculator program could predict the water solubility of the peptide, and peptides with good water solubility were selected.

[0029] Based on the above screening factors and standards, a total of four active maize peptides were selected, namely LMFP, FEGLFR, FLR and QLPSYR (Table 1). The above peptide sequences were not retrieved in the BIOPEP database and are new peptides that have not been reported.

[0030] Table 1 Characteristics of the screened corn peptides (7) Chemical synthesis of corn germ meal multifunctional active peptides LMFP, FEGLFR, FLR and QLPSYR. The mass spectra of the four peptides are shown in the following figure: Figure 5-Figure 8 As shown, you get it.

[0031] Example 3 Effects of protease types on hydrolysis degree, XOD inhibition rate, DPPH clearance rate and ADH activation rate of corn germ meal protein peptides (1) Pretreatment of corn germ meal protein: 5 g corn germ meal protein was dissolved in 50 mL water (solid-liquid ratio 10%) and heated at 90 °C for 10 min to pre-denature the protein. (2) Enzymatic hydrolysis: 4 portions of the protein solution prepared by the method of step (1) were taken and hydrolyzed by adding 1% (1% of the corn germ meal protein mass) of different proteases (neutral protease, alkaline protease, papain and trypsin) respectively. The enzymatic hydrolysis was carried out for 2 h at the optimum temperature and optimum pH (Table 2) of each protease. During this process, the protein solution was continuously stirred and the pH of the system was controlled with 0.1 M NaOH to maintain the pH constant at the optimum pH of each protease. After the enzymatic hydrolysis was completed, the enzymatic hydrolysis product was heated at 90 ° C for 15 min to denature and inactivate the enzyme to terminate the reaction. The enzymatic hydrolysis solution was then centrifuged at 4000 r / min in a refrigerated centrifuge at 4 ° C for 20 min, and the supernatant was retained. The supernatant was diluted to a concentration of 5 mg / mL, and the effect of the type of protease on the hydrolysis degree, XOD inhibition rate, DPPH clearance rate and ADH activation rate of corn germ meal protein peptides was determined.

[0032] Table 2 Optimum temperature and optimum pH of different proteases The results are as follows Figure 9 As shown, among the four proteases, alkaline protease had a DH of 19.31%, significantly higher than the other proteases. Its DPPH free radical scavenging rate was 59.31%, also significantly higher than the other proteases. Regarding ADH activation rate, neutral protease had the highest (31.43%), followed by papain (28.82%), and alkaline protease ranked third (19.67%). Comparing XOD inhibition rates, alkaline protease (20.26%), papain (19.70%), and neutral protease (18.60%) decreased in descending order, with little overall difference. Based on these four indicators, alkaline protein was selected as the optimal corn germ meal hydrolyzed protein.

[0033] Example 4 Effects of enzymatic hydrolysis parameters on hydrolysis degree, XOD inhibition rate, DPPH clearance rate and ADH activation rate of corn germ meal protein peptides 1. Effect of enzymatic hydrolysis time on hydrolysis degree, XOD inhibition rate, DPPH clearance rate and ADH activation rate of corn germ meal protein peptides (1) Pretreatment of corn germ meal protein: 15 g corn germ meal protein was dissolved in 50 mL water (solid-liquid ratio 30%) and heated at 90 °C for 10 min to pre-denature the protein. (2) Enzymatic hydrolysis: 1% (1% of the corn germ meal protein mass) alkaline protease was added to the corn germ meal protein solution for hydrolysis. The enzymatic hydrolysis was carried out at 55°C and pH 10 for 1 h, 2 h, 3 h, 4 h, and 5 h, respectively. During this process, the protein solution was stirred continuously and the pH of the system was controlled with 0.1 M NaOH to maintain it at the optimal pH of the protease. After the enzymatic hydrolysis was completed, the enzymatic hydrolyzate was heated at 90°C for 15 min to denature and inactivate the enzyme to terminate the reaction. The enzymatic hydrolyzate was then centrifuged at 4000 r / min in a refrigerated centrifuge at 4°C for 20 min, and the supernatant was retained. The effects of enzymatic hydrolysis time on the hydrolysis degree, XOD inhibition rate, DPPH clearance rate, and ADH activation rate of corn germ meal protein peptides were determined.

[0034] The results are as follows Figure 10 As shown in the figure, when the enzymatic hydrolysis time was 1-5 hours, the four indicators of DH, DPPH free radical scavenging rate, ADH activation rate, and XOD inhibition rate all showed a trend of first increasing and then decreasing with the increase of enzymatic hydrolysis time. At 2 hours, the DH, DPPH free radical scavenging rate, ADH activation rate, and XOD inhibition rate reached their highest values. Therefore, the optimal enzymatic hydrolysis time range for alkaline protease was 1.5-3 hours.

[0035] 2. Effect of enzyme addition amount on hydrolysis degree, XOD inhibition rate, DPPH clearance rate and ADH activation rate of corn germ meal protein peptide (1) Pretreatment of corn germ meal protein: 15 g corn germ meal protein was dissolved in 50 mL water (solid-liquid ratio 30%) and heated at 90 °C for 10 min to pre-denature the protein. (2) Enzymatic hydrolysis: 0.5%, 1%, 1.5%, 2%, and 2.5% (0.5%, 1%, 1.5%, 2%, and 2.5% of the corn germ meal protein mass) of alkaline protease were added to the corn germ meal protein solution for hydrolysis at 55°C and pH = 10 for 2 h. During this process, the protein solution was continuously stirred and the pH of the system was controlled with 0.1 M NaOH to maintain it at the optimal pH of the protease. After the enzymatic hydrolysis was completed, the enzymatic hydrolyzate was heated at 90°C for 15 min to denature and inactivate the enzyme to terminate the reaction. The enzymatic hydrolyzate was then centrifuged at 4000 r / min in a refrigerated centrifuge at 4°C for 20 min, and the supernatant was retained. The effect of the amount of enzyme added on the hydrolysis degree, XOD inhibition rate, DPPH clearance rate, and ADH activation rate of corn germ meal protein peptides was determined.

[0036] The results are as follows Figure 11As shown, DH increased with increasing enzyme dosage at 0.5%-2.5%, but slowly increased after exceeding 1.5%, reaching a near plateau. DPPH radical scavenging rate, ADH activation rate, and XOD inhibition rate all showed an initial upward and then downward trend with increasing enzyme dosage. The optimal enzyme dosage range was 1%-1.5%.

[0037] 3. Effect of material-liquid ratio on hydrolysis degree, XOD inhibition rate, DPPH clearance rate and ADH activation rate of corn germ meal protein peptide (1) Pretreatment of corn germ meal protein: 5 g, 10 g, 15 g, 20 g, and 25 g of corn germ meal protein were dissolved in 50 mL of water (the material-liquid ratio was 10%, 20%, 30%, 40%, and 50%, respectively), and heated at 90 °C for 10 min to pre-denature the protein; (2) Enzymatic hydrolysis: 1% (1% of the corn germ meal protein mass) of alkaline protease was added to the corn germ meal protein solution for hydrolysis at 55°C and pH 10 for 2 h. During this process, the protein solution was continuously stirred and the pH of the system was controlled with 0.1 M NaOH to maintain the pH at the optimal pH of the protease. After the enzymatic hydrolysis was completed, the enzymatic hydrolyzate was heated at 90°C for 15 min to denature the enzyme and terminate the reaction. The enzymatic hydrolyzate was then centrifuged at 4000 r / min in a refrigerated centrifuge at 4°C for 20 min, and the supernatant was retained. The effects of the material-liquid ratio on the hydrolysis degree, XOD inhibition rate, DPPH scavenging rate, and ADH activation rate of corn germ meal protein peptides were determined.

[0038] The results are as follows Figure 12 As shown in the figure, when the material-liquid ratio is 10%-50%, the DH and DPPH free radical scavenging rates, ADH activation rates and XOD inhibition rates all show a trend of first increasing and then decreasing with the increase of the material-liquid ratio. 20%-35% is selected as the optimal material-liquid ratio range.

[0039] Example 5 Optimization of enzymatic hydrolysis conditions using response surface methodology A response surface experiment was designed using the degree of hydrolysis, XOD inhibition, DPPH scavenging rate, and ADH activation rate of corn germ meal protein peptides as indicators (Table 3). The enzyme dosage (%), hydrolysis time (h), and solid-liquid ratio (%) were adjusted. After enzymatic hydrolysis, the hydrolyzate was centrifuged at 4000 r / min for 20 min at 4°C, and the supernatant was retained. The hydrolysis degree, XOD inhibition, DPPH scavenging rate, and ADH activation rate of the hydrolyzate were determined under different conditions.

[0040] Table 3 Results of response surface experiments The data in Table 3 were processed by Design Expert software to obtain the response surface diagram ( Figure 13 ), the response values ​​DH and ADH activation rates are greatly affected by the enzymatic hydrolysis time of factor B and the material-liquid ratio of factor C: the slope of the response surface is steep and the contour line shape is elliptical, indicating that the interaction between factors BC is strong.

[0041] The data in Table 3 were optimized using Design Expert software. The optimal process was as follows: enzyme dosage of 1.35%, enzymatic hydrolysis time of 2.30 h, and solid-liquid ratio of 27.44%. The biological activities of the corn enzymatic hydrolysate prepared under this process were: DPPH clearance rate of 55.79%, ADH activation rate of 12.92%, and XOD inhibition rate of 46.61%.

[0042] Example 6 A corn active peptide preparation with alcohol-relieving, uric acid-lowering and anti-oxidation effects, wherein the active ingredient is at least one of the corn active peptides LMFP, FEGLFR, FLR and QLPSYR.

[0043] The four peptides LMFP, FEGLFR, FLR and QLPSYR were marked as 1, 2, 3 and 4 respectively. Ultrapure water was used to prepare a solution with a concentration of 1 mg / mL. The XOD inhibition rate, DPPH clearance rate and ADH activation rate of the single peptide were measured. The results are shown in Figure 2. Figure 14 Among them, FLR had the strongest activity: DPPH free radical scavenging rate was 59.68%, ADH activation rate was 13.91%, and XOD inhibition rate was 43.51%.

[0044] The four peptides were compounded according to Table 4, where 1, 2, 3, and 4 represent peptides LMFP, FEGLFR, FLR, and QLPSYR, respectively; the final concentration of each peptide was 1 mg / mL. The XOD inhibition rate, DPPH clearance rate, and ADH activation rate of the different compound peptide solutions were measured, and the results are shown in Table 4 and Figure 15 As shown, among the four corn peptide combinations, DPPH scavenging rates varied the most (34.91% to 82.06%), while ADH activation rates (26.39% to 32.09%) and XOD inhibition rates (43.67% to 51.00%) were relatively average. Among the two corn peptide combinations, combinations 1&3 and 3&4 showed the highest overall bioactivity, with DPPH scavenging rates exceeding 70%, ADH activation rates exceeding 27%, and XOD inhibition rates exceeding 45%. Among the three corn peptide combinations, combinations 2&3&4 showed the highest activity, with DPPH scavenging rates of 80.15%, ADH activation rates of 28.58%, and XOD inhibition rates of 43.67%, respectively. The four combinations showed the highest activity, at 82.06%, 31.55%, and 45.55%, respectively.

[0045] The overall activity of the corn peptide combination was superior to that of a single peptide, demonstrating a synergistic relationship between the combinations. The most significant synergistic effect was on ADH activation, reaching a maximum of 31.55%, 2.27 times that of a single peptide (FLR). This was followed by DPPH clearance, which was 1.38 times that of a single peptide (FLR). The effect on XOD was less pronounced, remaining roughly the same.

[0046] Table 4 XOD inhibition rate, DPPH clearance rate and ADH activation rate of the composite peptide solution The above description is merely a preferred embodiment of the present invention and is not intended to limit the present invention in any other manner. Any person skilled in the art may utilize the above-disclosed technical content to modify or modify the present invention into equivalent embodiments. However, any simple modifications, equivalent variations, and modifications to the above embodiments that do not depart from the technical content of the present invention and are based on the technical essence of the present invention remain within the scope of protection of the present invention.

Claims

1. A corn active peptide with alcohol-relieving, uric acid-lowering and antioxidant effects, characterized in that: The amino acid sequence of the corn active peptide is at least one of LMFP, FEGLFR, FLR and QLPSYR.

2. The use of the corn active peptide having alcohol-relieving, uric acid-lowering and antioxidant effects according to claim 1, characterized in that: Used to prepare products with alcohol-relieving, uric acid-lowering and antioxidant effects.

3. The use of the corn active peptide having the effects of sobering up, lowering uric acid and anti-oxidation according to claim 2, characterized in that: The product is food, medicine or health product.

4. The use of the corn active peptide having the effects of sobering up, lowering uric acid and resisting oxidation according to claim 3, characterized in that: The product further comprises excipients acceptable to food, medicine or health care products.

5. A preparation having the effects of sobering up, lowering uric acid and anti-oxidation, characterized in that: The active ingredient is at least one of LMFP, FEGLFR, FLR and QLPSYR.

6. The preparation having the effects of sobering up, lowering uric acid and resisting oxidation according to claim 5, characterized in that: The concentration of active ingredient is 1 mg / mL.

7. The preparation having the effects of sobering up, lowering uric acid and resisting oxidation according to claim 5 or 6, characterized in that: It has the effect of sobering up by increasing the activation rate of ADH.

8. The preparation having the effects of sobering up, lowering uric acid and resisting oxidation according to claim 5 or 6, characterized in that: It exerts the effect of lowering uric acid by increasing the XOD inhibition rate.

9. The preparation having the effects of sobering up, lowering uric acid and resisting oxidation according to claim 5 or 6, characterized in that: The antioxidant has a DPPH free radical scavenging effect.

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