Corn active peptide with alcoholism, uric acid and antioxidant efficacy, preparation and application thereof

Abstract

The application discloses corn active peptides with effects of dispelling alcohol, reducing uric acid and resisting oxidation, a preparation and application thereof, and belongs to the technical field of bioactive peptides.The amino acid sequence of the corn active peptides is at least one of LMFP, FEGLFR, FLR and QLPSYR.The corn active peptides with effects of dispelling alcohol, reducing uric acid and resisting oxidation are separated from corn germ meal through enzymolysis, ultrafiltration and other technologies, the amino acid sequences of the separated peptide segments are determined, and bioinformatics technology is combined for screening, and finally four peptide segments are obtained.The identified peptide segment sequences are chemically synthesized, and the effects of dispelling alcohol, reducing uric acid and resisting oxidation of the synthesized single peptide segments and compound peptide segments are determined.The corn active peptides all have good XOD inhibition rate, DPPH clearance rate and ADH activation rate, and have important application prospects in the development of products with effects of dispelling alcohol, reducing uric acid and resisting oxidation.

Description

TECHNICAL FIELD

[0001] The application belongs to the technical field of bioactive peptides, and particularly relates to corn active peptides with the effects of alcoholism relief, uric acid reduction and oxidation resistance, a preparation and application thereof. BACKGROUND

[0002] Hyperuricemia and alcoholic liver disease have become a worldwide public health problem threatening human health. Allopurinol and benzbromarone are drugs for treating hyperuricemia and gout in clinical practice. These drugs can rapidly reduce serum uric acid levels, but can cause some adverse reactions in patients. The pathogenesis of alcoholic liver disease is complex, and there is no clear targeted therapeutic drug. The most common steroid therapy, corticosteroids, is not satisfactory.

[0003] In recent years, a large number of studies have shown that food protein-derived bioactive peptides are potential efficacy factors for regulating body metabolism and promoting human health. Bioactive peptides are usually composed of 2-20 amino acids. These sequences often do not exhibit biological activity because they are embedded in the parent protein sequence. After hydrolysis by fermentation, enzymatic digestion and gastrointestinal digestion, they usually exhibit stronger physiological activity. Compared with proteins, peptides have low molecular weight, are easily absorbed, and have high stability.

[0004] Therefore, it is of great significance to separate corn germ meal multifunctional active peptides with uric acid reduction and alcoholism relief effects from corn germ meal proteins to enrich uric acid reduction and alcoholism relief drugs and protect human health. SUMMARY

[0005] In view of the problems in the prior art, the purpose of the present application is to provide corn active peptides with the effects of alcoholism relief, uric acid reduction and oxidation resistance, a preparation and application thereof.

[0006] In order to achieve the above-mentioned purpose, the technical scheme adopted by the present application is as follows:

[0007] The corn active peptides with the effects of alcoholism relief, uric acid reduction and oxidation resistance have at least one of the amino acid sequences LMFP, FEGLFR, FLR and QLPSYR.

[0008] The application of the corn active peptides with the effects of uric acid reduction and oxidation resistance is for preparing a drug with the effects of uric acid reduction and oxidation resistance or a food with the effect of oxidation resistance.

[0009] On the basis of the above-mentioned scheme, the drug further comprises a pharmaceutically acceptable excipient, and the food further comprises a food acceptable excipient.

[0010] A preparation with the effects of alcoholism relieving, uric acid reducing and antioxidation, the effective component being at least one of LMFP, FEGLFR, FLR and QLPSYR.

[0011] On the basis of the above scheme, the concentration of the effective component is 1 mg / mL.

[0012] On the basis of the above scheme, the alcoholism relieving effect is achieved by improving the ADH activation rate.

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

[0014] On the basis of the above scheme, the antioxidation is the DPPH free radical scavenging effect.

[0015] The advantages of the technical scheme of the present application are as follows:

[0016] The present application separates corn active peptides with the effects of alcoholism relieving, uric acid reducing and antioxidation from corn germ meal by enzymolysis, ultrafiltration and other technologies, determines the amino acid sequences of the separated peptide segments and screens them by bioinformatics technology, and finally obtains four peptide segments. The alcoholism relieving, uric acid reducing and antioxidation effects of the synthesized single peptide segments and complex peptide segments are determined according to the identified peptide segment sequences, and these corn active peptides all have good XOD inhibition rate, DPPH scavenging rate and ADH activation rate, and can be used as natural antioxidants in food, medicine and / or cosmetics, and can also be used as natural uric acid reducing supplements and alcoholism relieving agents in medicine, and have important application prospects in the development of products with the effects of alcoholism relieving, uric acid reducing and antioxidation. BRIEF DESCRIPTION OF DRAWINGS

[0017] Figure 1 DPPH scavenging rate (A), ADH activation rate (B) and XOD inhibition rate (C) of different molecular weight polypeptide components;

[0018] Figure 2 It is a Sephadex G-15 gel chromatography separation diagram;

[0019] Figure 3 It is the DPPH scavenging rate (A), ADH activation rate (B) and XOD inhibition rate (C) of C1, C2, C3 and C4 four components;

[0020] Figure 4 Total ion chromatogram;

[0021] Figure 5 Mass spectrum of LMFP;

[0022] Figure 6 Mass spectrum of FEGLFR;

[0023] Figure 7 Mass spectrum of FLR;

[0024] Figure 8 Mass spectrum of QLPSYR;

[0025] 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;

[0026] Figure 10 Effects of different enzymolysis time on DH (A), DPPH radical scavenging rate (B), ADH activation rate (C) and XOD inhibition rate (D) of corn hydrolysate;

[0027] Figure 11 Effects of different enzyme addition amount on DH (A), DPPH radical scavenging rate (B), ADH activation rate (C) and XOD inhibition rate (D) of corn hydrolysate;

[0028] Figure 12 Effects of different solid-liquid ratio on DH (A), DPPH radical scavenging rate (B), ADH activation rate (C) and XOD inhibition rate (D) of corn hydrolysate;

[0029] Figure 13 Response surface plots of each experimental factor on DH (A), DPPH radical scavenging rate (B), ADH activation rate (C) and XOD inhibition rate (D);

[0030] Figure 14 DPPH scavenging rate (A), ADH activation rate (B) and XOD inhibition rate (C) of single corn active peptide;

[0031] Figure 15 DPPH scavenging rate (A), ADH activation rate (B) and XOD inhibition rate (C) of corn active peptide after compounding.

[0032] In the above specification, different lowercase letters a-e in the figures represent significant differences (p<0.05). DETAILED DESCRIPTION

[0033] The terms used in the present application have the meanings generally understood by those of ordinary skill in the art, unless otherwise specified. The present application is described in further detail below in conjunction with specific examples and with reference to the data. The following examples are merely intended to illustrate the present application and in no way limit the scope of the present application.

[0034] The experimental methods in the following examples are all conventional methods, and are carried out according to the techniques or conditions described in the literature in the art or according to the product instructions, unless otherwise specified. The experimental materials, reagents, and medicines used in the following examples can be purchased through general channels, unless otherwise specified.

[0035] In the following examples,

[0036] 1. The determination method of the degree of hydrolysis DH is as follows:

[0037] The determination of corn protein hydrolysis uses the pH-Stat method. The pH value of the solution will drop sharply when the protein releases protons during the hydrolysis process. At this time, 0.1 M NaOH solution is added to maintain the pH. The degree of hydrolysis (DH) can be calculated by the volume of the added alkali solution. The calculation formula is as follows:

[0038]

[0039] In the formula, C is the concentration of the NaOH solution, moL / L;

[0040] V is the volume of the consumed NaOH solution, mL;

[0041] a is the dissociation degree of a-amino group; wherein pH is the pH value of the hydrolysis system, and pKa is the pKa of the amino group, wherein T is the temperature in Kelvin;

[0042] m is the mass of corn protein in the solution, g;

[0043] htot is the total number of peptide bonds in the substrate protein, mmol / g, and for corn protein, hot = 7.35.

[0044] 2. Determination of DPPH free radical scavenging capacity:

[0045] The protein peptide solution is mixed with an equal volume of 0.1 mmol / L DPPH ethanol solution, and the mixture is reacted at room temperature for 30 min in the dark. The absorbance value is measured at a wavelength of 517 nm and is recorded as A 样品 An equal amount of ethanol is used to replace the DPPH ethanol solution to determine the corresponding absorbance value, which is recorded as A 空白 An equal amount of distilled water is used to replace the protein peptide solution to determine the corresponding absorbance value, which is recorded as A 对照 The DPPH free radical scavenging rate is calculated, and the formula is as follows:

[0046]

[0047] 3. Determination of ADH activation rate:

[0048] The 50 μL sample solution was mixed with 150 μL detection reagent (containing 22.4 mM sodium pyrophosphate buffer, 3.3% ethanol and 7.8 mM NAD+), after equilibration at 37 °C for 5 min, 50 μL ADH (0.2 U / mL) was added to initiate the reaction. The absorbance value at 340 nm was detected using a microplate reader Varioskan Flash full-wavelength scanning multifunctional reader, recorded once every 10 s, for 10 min. Distilled water instead of sample was used as negative control. The first derivative of the kinetic curve at 0 min was obtained by fitting the reaction kinetic curve, 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 could be obtained according to the following equation:

[0049]

[0050] 4. Determination of XOD inhibition rate

[0051] Xanthine solution preparation (0.48 mM): 7.30 mg of xanthine powder was weighed, first dissolved in 400 μL of 1 mol / L NaOH, and then diluted with PBS buffer to 100 mL to obtain the required xanthine solution.

[0052] 50 μL peptide solution, 50 μL 0.02 U / mL xanthine oxidase solution, mixed and incubated at 25 °C for 5 min. Then 150 μL of 0.48 mmol / L xanthine solution was added, mixed and incubated at 25 °C for 25 min. After the reaction was stopped by adding 80 μL of 1M HCl, the absorbance value of the supernatant of each component was measured at 290 nm. The absorbance value of the sample group was recorded as A, the absorbance value of the group without enzyme was recorded as B, the absorbance value of the group without sample was recorded as C, and the absorbance value of the group without enzyme and sample was recorded as D. The xanthine oxidase inhibition was calculated using the following formula:

[0053]

[0054] The corn germ meal protein in the following examples was purchased from Weifang Shengtai Pharmaceutical Co., Ltd.

[0055] Example 1

[0056] A corn active peptide having the effects of alcoholism relief, uric acid reduction and antioxidant, the corn active peptide being a peptide of an amino acid sequence represented by at least one of SEQ ID NO: 1, SEQ ID NO: 2, SEQ ID NO: 3, and SEQ ID NO: 4:

[0057] SEQ ID NO: 1: LMFP;

[0058] SEQ ID NO: 2: FEGLFR;

[0059] SEQ ID NO: 3: FLR;

[0060] SEQ ID NO: 4: QLPSYR.

[0061] Example 2

[0062] The method for isolating corn active peptides with alcoholism, uric acid and antioxidant effects from corn germ meal is as follows:

[0063] (1) Corn germ meal protein pretreatment: according to the solid-liquid ratio of 27.44%, corn germ meal protein was weighed and dissolved in 50 mL water at 90°C for 10 min to make the protein pre-denatured;

[0064] (2) Enzymolysis: 1.35% (1.35% of the mass of corn germ meal protein) of alkaline protease was added to the corn germ meal protein solution for hydrolysis, and the enzyme was hydrolyzed at 55°C and pH 10 for 2.3 h. The protein solution was continuously stirred and the pH of the system was controlled with 0.1M NaOH to maintain the optimum pH of the protease. After the enzyme hydrolysis was completed, the enzyme was denatured and inactivated at 90°C for 15 min to terminate the reaction. Then the enzyme hydrolysate was centrifuged at 4000 r / min for 20 min in a refrigerated centrifuge at 4°C, and the supernatant was reserved.

[0065] (3) Ultrafiltration separation: the supernatant of the corn germ meal protein enzyme hydrolysate obtained in step (2) was first filtered with a 0.22 μm filter membrane, and then separated into three components with different molecular weights: >10 KDa, 3-10 KDa and <3 KDa using 10 kDa and 3 kDa ultrafiltration centrifuge tubes. The XOD inhibition rate, DPPH clearance rate and ADH activation rate of the components with different molecular weights were determined, and the results are shown in Table 1. Figure 1

[0066] (4) Protein purification instrument (ÄKTA pure) separation: the gel chromatography column used was Sephadex G-25, and the corn germ meal protein enzyme hydrolysate with a molecular weight of <3 KDa was separated by the protein purification instrument, with a loading concentration of 15 mg / mL, a loading amount of 5 mL, an eluent of ultrapure water, a flow rate of 2 mL / min, and a detection wavelength of 280 nm. Four groups of polypeptide mixtures with different molecular weights were obtained. Figure 2 ​); the XOD inhibition rate, DPPH scavenging rate and ADH activation rate of each molecular weight component were determined. The results showed that the XOD inhibition rate, DPPH scavenging rate and ADH activation rate of component C2 all showed good effects Figure 3 ).

[0067] (5) LC-MSMS mass spectrometry sequencing: the above component C2 was subjected to mass spectrometry sequencing, and through database sequence alignment, a total of 841 corn polypeptides were obtained Figure 4 ).

[0068] (6) Screening of corn germ meal multifunctional active peptides by bioinformatics technology: the screening criteria were as follows: ① the molecular weight of polypeptide was generally selected to be no more than 1 KDa short peptide; ② the higher the ALC value, the higher the reliability, and polypeptides 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 area>105 were selected; ④ PeptideRanker program was used to predict the potential biological activity of polypeptide, and the higher the score, the stronger the potential biological activity, and peptides with score>0.5 were selected; ⑤ ToxinPred3.0 program was used to predict biological toxicity, and nontoxic peptides were selected; ⑥ Peptideproperty calculator program could be used to predict the water solubility of polypeptide, and peptides with good water solubility were selected.

[0069] After the above screening elements and criteria, a total of 4 corn active polypeptides were selected, which were LMFP, FEGLFR, FLR and QLPSYR (Table 1), and the above polypeptide sequences were not retrieved in the BIOPEP database, which were new peptides not reported.

[0070] Table 1 Characteristics of the screened corn polypeptides

[0071]

[0072] (7) Chemical synthesis of corn germ meal multifunctional active peptides LMFP, FEGLFR, FLR and QLPSYR, and the mass spectra of the four peptides are shown in Figures 5-8 .

[0073] Example 3

[0074] Effect of the type of protease on the degree of hydrolysis, XOD inhibition rate, DPPH scavenging rate and ADH activation rate of corn germ meal protein peptides

[0075] (1) Corn germ meal protein pretreatment: 5 g of corn germ meal protein was weighed and dissolved in 50 mL of water (solid-liquid ratio 10%), and heated at 90°C for 10 min to make the protein pre-denatured;

[0076] (2) Enzymatic hydrolysis: Four portions of the protein solution prepared in step (1) were hydrolyzed with 1% (1% of the protein mass of corn germ meal) of different proteases (neutral protease, alkaline protease, papain, and trypsin). The hydrolysis was carried out at the optimal temperature and optimal pH (Table 2) for 2 h for each protease. During this process, the protein solution was continuously stirred and the pH of the system was kept constant with 0.1M NaOH, and always maintained at the optimal pH of each protease. After the hydrolysis was completed, the hydrolysate was heated at 90℃ for 15 min to denature and inactivate the enzyme to terminate the reaction. Then the hydrolysate was centrifuged at 4000 r / min for 20 min in a refrigerated centrifuge at 4℃, and the supernatant was retained. The concentration of the supernatant was diluted to 5 mg / mL, and the effects of the type of protease on the degree of hydrolysis, XOD inhibition rate, DPPH scavenging rate, and ADH activation rate of corn germ meal protein peptides were determined.

[0077] Table 2. Optimal temperature and pH for different proteases

[0078]

[0079] The results are as follows Figure 9 As shown, the DH of alkaline protease was 19.31%, significantly higher than that of the other proteases. The DPPH free radical scavenging rate of alkaline protease was 59.31%, also significantly higher than that of the other proteases. Regarding ADH activation rate, neutral protease had the highest rate (31.43%), followed by papain (28.82%), and then alkaline protease (19.67%). In terms of XOD inhibition rate, alkaline protease (20.26%), papain (19.70%), and neutral protease (18.60%) showed a decreasing trend, with little overall difference. Based on these four indicators, alkaline protein was selected as the optimal hydrolyzed protein from corn germ meal.

[0080] Example 4

[0081] Effects of enzymatic hydrolysis parameters on the degree of hydrolysis, XOD inhibition rate, DPPH scavenging rate, and ADH activation rate of corn germ meal protein peptides

[0082] 1. Effects of enzymatic hydrolysis time on the degree of hydrolysis, XOD inhibition rate, DPPH scavenging rate, and ADH activation rate of corn germ meal protein peptides

[0083] (1) Pretreatment of corn germ meal protein: Weigh 15 g of corn germ meal protein and dissolve it in 50 mL of water (material-to-liquid ratio 30%), heat at 90℃ for 10 min to pre-denature the protein;

[0084] (2) Enzymatic hydrolysis: 1% (1% of the protein mass of corn germ meal) of alkaline protease was added to the corn germ meal protein solution for hydrolysis. Hydrolysis was performed at 55℃ and pH 10 for 1 h, 2 h, 3 h, 4 h, and 5 h, respectively. The protein solution was continuously stirred during this process, and the pH of the system was kept constant using 0.1 M NaOH, maintaining it at the optimal pH for the protease. After hydrolysis, the hydrolysate was heated at 90℃ for 15 min to denature and inactivate the enzyme, thus terminating the reaction. The hydrolysate was then centrifuged at 4000 r / min for 20 min in a refrigerated centrifuge at 4℃, and the supernatant was retained. The effects of hydrolysis time on the degree of hydrolysis, XOD inhibition rate, DPPH scavenging rate, and ADH activation rate of corn germ meal protein peptides were determined.

[0085] The results are as follows Figure 10 As shown, when the enzymatic hydrolysis time is 1-5 h, the four indicators—DH and DPPH free radical scavenging rates, ADH activation rate, and XOD inhibition rate—all show a trend of first increasing and then decreasing with increasing hydrolysis time, reaching their highest values ​​at 2 h. Therefore, 1.5-3 h is the optimal enzymatic hydrolysis time range for alkaline protease.

[0086] 2. Effects of enzyme dosage on the degree of hydrolysis, XOD inhibition rate, DPPH scavenging rate, and ADH activation rate of corn germ meal protein peptides

[0087] (1) Pretreatment of corn germ meal protein: Weigh 15 g of corn germ meal protein and dissolve it in 50 mL of water (material-to-liquid ratio 30%), heat at 90℃ for 10 min to pre-denature the protein;

[0088] (2) Enzymatic hydrolysis: 0.5%, 1%, 1.5%, 2%, and 2.5% (0.5%, 1%, 1.5%, 2%, and 2.5% of the protein content of corn germ meal) of alkaline protease were added to the corn germ meal protein solution for hydrolysis. Hydrolysis was carried out at 55℃ and pH=10 for 2 hours. During this process, the protein solution was continuously stirred, and the pH of the system was controlled constant using 0.1 M NaOH, maintaining it at the optimal pH for the protease. After hydrolysis, the hydrolysate was heated at 90℃ for 15 minutes to denature and inactivate the enzyme, thus terminating the reaction. The hydrolysate was then centrifuged at 4000 r / min for 20 minutes in a refrigerated centrifuge at 4℃, and the supernatant was retained. The effects of enzyme dosage on the degree of hydrolysis, XOD inhibition rate, DPPH scavenging rate, and ADH activation rate of corn germ meal protein peptides were determined.

[0089] The results are as follows Figure 11As shown in the table, when the enzyme dosage is 0.5%-2.5%, DH increases with the increase of enzyme dosage, but slowly increases and almost tends to be stable when the enzyme dosage exceeds 1.5%. The DPPH free radical scavenging rate, ADH activation rate and XOD inhibition rate all show a trend of first increasing and then decreasing with the increase of enzyme dosage. The optimal enzyme dosage interval is selected as 1%-1.5%.

[0090] 3. Effect of material-liquid ratio on DH, XOD inhibition rate, DPPH scavenging rate and ADH activation rate of corn germ meal protein peptide

[0091] (1) Corn germ meal protein pretreatment: 5 g, 10 g, 15 g, 20 g and 25 g of corn germ meal protein were respectively weighed and dissolved in 50 mL of water (material-liquid ratio was 10%, 20%, 30%, 40% and 50% respectively), and heated at 90°C for 10 min to make the protein pre-denatured;

[0092] (2) Enzymolysis: 1% (1% of the mass of corn germ meal protein) of alkaline protease was added to the corn germ meal protein solution for hydrolysis, and the enzyme was hydrolyzed at 55°C and pH 10 for 2 h. The protein solution was continuously stirred and the pH of the system was controlled by 0.1 M NaOH to maintain the optimal pH of the protease. After the enzyme hydrolysis was completed, the enzyme was denatured and inactivated at 90°C for 15 min to terminate the reaction. Then the enzyme hydrolysate was centrifuged at 4000 r / min for 20 min in a refrigerated centrifuge at 4°C, and the supernatant was reserved. The effect of material-liquid ratio on DH, XOD inhibition rate, DPPH scavenging rate and ADH activation rate of corn germ meal protein peptide was determined.

[0093] The results are shown in Figure 12 As shown in the table, when the material-liquid ratio is 10%-50%, DH, DPPH free radical scavenging rate, ADH activation rate and XOD inhibition rate all show a trend of first increasing and then decreasing with the increase of material-liquid ratio, and the optimal material-liquid ratio interval is selected as 20%-35%.

[0094] Example 5

[0095] Optimization of enzyme hydrolysis conditions by response surface test

[0096] The DH, XOD inhibition rate, DPPH scavenging rate and ADH activation rate of corn germ meal protein peptide were used as indexes to design a response surface test for enzyme dosage (%), enzyme hydrolysis time (h) and material-liquid ratio (%) parameters (Table 3). After the enzyme hydrolysis was completed, the enzyme hydrolysate was then centrifuged at 4000 r / min for 20 min in a refrigerated centrifuge at 4°C, and the supernatant was reserved. The effect of different conditions on the DH, XOD inhibition rate, DPPH scavenging rate and ADH activation rate of the enzyme hydrolysate was determined.

[0097] Table 3 Results of response surface test

[0098]

[0099] The data in Table 3 were processed by Design Expert software to obtain a response surface graph (Fig. 1). Figure 13 The response values DH and ADH activation rate were greatly affected by the factors B enzymolysis time and C feed liquid ratio: the slope of the response surface was relatively steep, and the contour shape was oval, indicating that the interaction between the factors B and C was strong.

[0100] The data in Table 3 were optimized by Design Expert software, and the optimal process was as follows: enzyme addition amount 1.35%, enzymolysis time 2.30 h, and feed liquid ratio 27.44%. Under the process, the biological activity of the corn enzymolysis liquid prepared was as follows: DPPH clearance rate 55.79%, ADH activation rate 12.92%, and XOD inhibition rate 46.61%.

[0101] Example 6

[0102] A corn active peptide preparation having the effects of alcoholism relief, uric acid reduction, and antioxidant, wherein the effective component is at least one of corn active peptides LMFP, FEGLFR, FLR, and QLPSYR.

[0103] The four peptide segments LMFP, FEGLFR, FLR, and QLPSYR were respectively denoted as 1, 2, 3, and 4. An ultrapure water was used to prepare a solution with a concentration of 1 mg / mL, and the XOD inhibition rate, DPPH clearance rate, and ADH activation rate of the single peptide segment were determined, and the results are shown in Table 2 and Fig. 2. Figure 14 Among them, the activity of FLR was the strongest: the DPPH free radical clearance rate was 59.68%, the ADH activation rate was 13.91%, and the XOD inhibition rate was 43.51%.

[0104] The four peptide segments were respectively compounded according to Table 4, wherein 1, 2, 3, and 4 respectively represented the peptide segments LMFP, FEGLFR, FLR, and QLPSYR; and the final concentration of each peptide segment was 1 mg / mL. The XOD inhibition rate, DPPH clearance rate, and ADH activation rate of the different compounded polypeptide solutions were determined, and the results are shown in Table 4 and Fig. 3. Figure 15As shown, the DPPH scavenging rate of the four different combinations of corn polypeptides varies the most (34.91% - 82.06%), and the relative average is the ADH activation rate (26.39% - 32.09%) and the XOD inhibition rate (43.67% - 51.00%). Among them, the biological activity of the 1&3 and 3&4 combinations of the corn polypeptide double combination is relatively high, the DPPH scavenging rate is more than 70%, the ADH activation rate is more than 27%, and the XOD inhibition rate is more than 45%. The activity of the 2&3&4 combination of the corn polypeptide triple combination is the best, which is DPPH scavenging rate 80.15%, ADH activation rate 28.58%, and XOD inhibition rate 43.67%. The activity of the four combinations is the best, which is 82.06%, 31.55%, and 45.55%, respectively.

[0105] The activity of the corn polypeptide combination is better than that of the single peptide segment, and there is a certain synergistic relationship between the combinations. The most significant synergistic relationship is the effect on the ADH activation rate, which is up to 31.55%, which is 2.27 times that of the single peptide segment (FLR), and the second is the effect on the DPPH scavenging rate, which is 1.38 times that of the single peptide segment (FLR). The effect on XOD is not obvious, and it is basically flat.

[0106] Table 4 XOD inhibition rate, DPPH scavenging rate and ADH activation rate of the compound peptide segment solution

[0107]

[0108] The above is only a preferred embodiment of the present application, and is not intended to limit the other forms of the present application. Any skilled person in the art can use the disclosed technical content to make changes or modifications to equivalent embodiments. However, any simple modification, equivalent change and modification of the above embodiments without departing from the technical solution of the present application, according to the technical essence of the present application, still belongs to the protection scope of the technical solution of the present application.

Claims

1. A corn active peptide having uric acid-lowering and antioxidant effects, characterized in that, The amino acid sequence of the corn active peptide is one of LMFP, FEGLFR and QLPSYR. 2.The application of the corn active peptide with the function of reducing uric acid and antioxidation according to claim 1, characterized in that, The application relates to a medicine with the functions of reducing uric acid and resisting oxidation or a food with the function of resisting oxidation. 3.The application of corn active peptide with uric acid-lowering and antioxidant efficacy according to claim 2, characterized in that, The medicine further comprises pharmaceutically acceptable excipients, and the food further comprises food acceptable excipients.

4. A preparation having uric acid-lowering and antioxidant efficacy, characterized by, The effective component is one of LMFP, FEGLFR and QLPSYR.

5. A preparation having alcoholism-relieving, uric acid-lowering and antioxidant effects, characterized by, The effective component is at least two of LMFP, FEGLFR, FLR and QLPSYR. 6.The preparation with uric acid-lowering and antioxidant efficacy according to claim 4 or the preparation with alcohol-dissipating, uric acid-lowering and antioxidant efficacy according to claim 5, characterized in that, The concentration of the effective component is 1 mg / mL. 7.The preparation having the effects of alcoholism relief, uric acid reduction and antioxidation according to claim 5, characterized in that, The alcoholism relieving effect is achieved by improving the activation rate of ADH. 8.The preparation with uric acid-lowering and antioxidant efficacy according to claim 4 or the preparation with alcohol-dissipating, uric acid-lowering and antioxidant efficacy according to claim 5, characterized in that, The uric acid reducing effect is achieved by improving the inhibition rate of XOD. 9.The preparation with uric acid-lowering and antioxidant efficacy according to claim 4 or the preparation with alcohol-dissipating, uric acid-lowering and antioxidant efficacy according to claim 5, characterized in that, The oxidation resistance is the DPPH free radical scavenging effect.

10. The application of the preparation with the functions of relieving alcoholism, reducing uric acid and resisting oxidation in the preparation of a medicine with the functions of relieving alcoholism, reducing uric acid and resisting oxidation or the preparation of a food with the function of resisting oxidation.

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