A bioactive peptide with antioxidant function TDEFQLHTNVNDGTEFGGSIYQK

Abstract

The present invention discloses a bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK with antioxidant function, and its amino acid sequence is: Thr-Asp-Glu-Phe-Gln-Leu-His-Thr-Asn-Val-Asn-Asp-Gly-Thr-Glu-Phe-Gly-Gly-Ser-Ile-Tyr-Gln-Lys. The bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK of the present invention can withstand digestion by gastrointestinal digestive enzymes, and can be completely absorbed by intestinal epithelial cells, and will not be degraded by enzymes of intestinal epithelial cells. And through cell experiments, it is verified that TDEFQLHTNVNDGTEFGGSIYQK has good antioxidant function. The bioactive peptide is of great significance for the development of drugs with antioxidant function.

Description

Technical Field

[0001] The invention relates to the technical field of functional foods, and in particular to a bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK with antioxidant function. Background Art

[0002] Antioxidant peptides refer to a class of active substances that can scavenge free radicals, inhibit lipid peroxidation, chelate transition metal ions, reduce the rate of cell autooxidation, and effectively capture and neutralize free radicals. Studies have shown that meat and meat products are a good source of antioxidant peptides. Among them, fermented meat products, such as fermented sausages and ham, undergo a long-term fermentation and maturation process, and the protein is strongly degraded by various endogenous enzymes and microorganisms, generating rich polypeptides and small peptides. Therefore, traditional fermented meat products are a good source of antioxidant peptides.

[0003] Before the antioxidant peptides can play their antioxidant function in the body after oral administration, they must overcome the effects of gastric acid, the alkaline environment of the small intestine, and a series of enzymes such as pepsin, pancreatic enzymes, and peptidase, and they must also overcome the absorption barrier of the small intestine to enter the body, which is an important prerequisite for their physiological function. However, there are no reports of natural, digestible, and highly bioavailable antioxidant peptides derived from meat products at home and abroad. Summary of the invention

[0004] The invention uses Xuanwei ham from Yunnan as a raw material, and screens antioxidant peptides that have antioxidant properties, are resistant to digestion, and can completely pass through the small intestinal mucosal epithelium through an in vitro digestion model and a small intestinal epithelial cell absorption model.

[0005] The technical solution adopted by the present invention is a bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK with antioxidant function, and its amino acid sequence is: Thr-Asp-Glu-Phe-Gln-Leu-His-Thr-Asn-Val-Asn-Asp-Gly-Thr-Glu-Phe-Gly-Gly-Ser-Ile-Tyr-Gln-Lys.

[0006] A method for preparing a bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK with antioxidant function is prepared by a solid phase synthesis method.

[0007] Application of a bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK with antioxidant function, and application of the bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK with antioxidant function in the preparation of a drug with antioxidant function.

[0008] An antioxidant functional product comprises a bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK having an antioxidant function, and the antioxidant functional product comprises an antioxidant drug.

[0009] The beneficial effects of the present invention are as follows: (1) Using Xuanwei ham as raw material, a bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK that is resistant to digestion and can pass through the small intestinal mucosal epithelium completely is obtained through simulated in vitro digestion and Caco-2 cell model screening. (2) The bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK has a good protective effect on HepG2 cells damaged by oxidation, and the effect is better than glutathione (GSH). BRIEF DESCRIPTION OF THE DRAWINGS

[0010] Figure 1 : Total ion current of F4 component peptide solution.

[0011] Figure 2 : Total ion current of peptide solution in the F4 fraction of crude peptide that can pass through the small intestinal mucosal epithelium.

[0012] Figure 3 : HPLC retention time of synthetic peptide TK-23.

[0013] Figure 4 : MS / MS spectrum of synthetic peptide TK-23.

[0014] Figure 5 :The effect of peptide TK-23 on CAT activity of HepG2 cells.

[0015] Figure 6 :The effect of peptide TK-23 on SOD activity of HepG2 cells.

[0016] Figure 7 :The effect of peptide TK-23 on the activity of GSH-Px in HepG2 cells. DETAILED DESCRIPTION

[0017] In order to make the purpose, technical solutions and advantages of the embodiments of the present invention clearer, the technical solutions in the embodiments of the present invention will be clearly and completely described below in conjunction with the drawings in the embodiments of the present invention. Obviously, the described embodiments are part of the embodiments of the present invention, not all of the embodiments. Generally, the components of the embodiments of the present invention described and shown in the drawings here can be arranged and designed in various different configurations.

[0018] The purpose of the present invention is to provide an antioxidant peptide that is resistant to digestion and can pass through the small intestinal mucosal epithelium intact, so as to solve the problem of bioavailability of bioactive peptide products. The peptide is obtained by subjecting Xuanwei ham to in vitro simulated digestion to obtain a crude peptide solution, screening peptide segments that are both resistant to digestion and can be absorbed and utilized by small intestinal cells through a Caco-2 cell model, and then obtaining it through multiple gel filtration chromatography and liquid chromatography, or by a solid phase synthesis method, preferably a solid phase synthesis method.

[0019] (1) Preparation, separation, purification and identification of active peptides

[0020] Take 5-15 g of Xuanwei ham biceps brachii in a 100-500 mL centrifuge tube, add 15-30 mL of simulated salivary electrolytes, 10-30 mL of simulated gastric fluid electrolytes, and 15-30 mL of simulated intestinal fluid electrolytes, respectively, and shake at a constant speed of 100-200 rpm in a constant temperature shaker for 2-4 hours to simulate human small intestinal digestion. After obtaining the simulated digestive fluid, heat the sample in a 90-100℃ water bath for 10-20 min. Centrifuge and vacuum freeze-dry to obtain the crude peptide powder of in vitro simulated digestive fluid.

[0021] The simulated in vitro digestion products of Xuanwei ham were ultrafiltered through a 3-5 kDa ultrafiltration membrane, and then gel filtration chromatography was used to obtain four components, F1, F2, F3 and F4. The F4 component with the smallest molecular weight was selected for Caco-2 cell transport experiment. 1.5-3 mL of balanced salt buffer containing crude peptide samples was added to the upper and lower sides of the Caco-2 cell model, respectively. The culture plate was placed in a carbon dioxide cell culture incubator for absorption and transport for 2-3 h, and then the solutions on both sides were collected for LC-MS / MS analysis. It was determined that the peptide segments in the F4 component that were completely absorbed by Caco-2 cells included: Thr-Asp-Glu-Phe-Gln-Leu-His-Thr-Asn-Val-Asn-Asp-Gly-Thr-Glu-Phe-Gly-Gly-Ser-Ile-Tyr-Gln-Lys (TDEFQLHTNVNDGTEFGGSIYQK).

[0022] (2) Active peptides have antioxidant effects

[0023] The peptide TDEFQLHTNVNDGTEFGGSIYQK, which can pass through Caco-2 cells completely, was synthesized by solid phase synthesis. The synthesized peptide showed good antioxidant activity in vitro. 2+ The chelating ability is significantly higher than that of GSH. At the same time, the results of HepG2 oxidative damage cell experiments showed that the peptide TDEFQLHTNVNDGTEFGGSIYQK can regulate the activity of antioxidant enzymes and has a protective effect on the oxidative stress of HepG2 cells.

[0024] Example 1: Preparation, separation, purification and identification of active peptides.

[0025] (1) Take 5 g of Xuanwei ham biceps brachii in a 100 mL centrifuge tube, add 15 mL of simulated salivary electrolyte and 75 μL of calcium chloride dihydrate solution, respectively, and place the centrifuge tube in an ice bath in a beaker. Use a homogenizer to homogenize to simulate human oral chewing.

[0026] (2) Add 10 mL of simulated gastric fluid electrolyte to the homogenized minced meat sample, adjust the pH value of the sample to 2.5, add an appropriate amount of simulated gastric fluid electrolyte to 30 mL, add 0.24 g of pepsin powder according to the enzyme: sample = 1:20 (w / w), set the parameters of the constant temperature shaker incubator to 37 °C, 100 rpm, reaction time for 2 h, and oscillate at a constant speed to simulate human gastric digestion.

[0027] (3) Take the above gastric chyme sample, add 24 mL of simulated intestinal fluid electrolytes, adjust the pH value of the sample to 7.0, add an appropriate amount of simulated intestinal fluid electrolytes to 60 mL, add 0.25 g of ox bile salt and 0.1 g of trypsin powder according to the ratio of enzyme: sample = 1:50 (w / w), place it in a constant temperature shaker at 37 °C and shake at a constant speed of 100 rpm for 2 hours to simulate human small intestinal digestion, and obtain simulated digestive fluid.

[0028] (4) Heat the digestive fluid sample after in vitro simulated digestion in a 95°C water bath for 10 min. Centrifuge at 4°C and 12,000 × g for 20 min. Collect the supernatant in the centrifuge tube, filter it, and then freeze-dry it in a vacuum to obtain crude peptide powder of in vitro simulated digestive fluid.

[0029] (5) Ultrafiltration was performed on the crude peptide powder using an ultrafiltration centrifuge tube (ultrafiltration membrane pore size was 3 kDa), and the peptide powder less than 3 kDa after freeze-drying was re-dissolved, and the peptide powder was separated and purified using a chromatography column (stationary phase: dextran gel G-15, mobile phase: deionized water, flow rate: 1 mL / min); the detection wavelength of the detector was 280 nm. After the sample peak appeared, a protein collector was used to collect 5 mL of eluate per tube, and the eluates belonging to the same peak segment were mixed into the same sample. Four polypeptide components F1, F2, F3 and F4 with different antioxidant abilities were obtained according to the molecular weight, among which the F4 component had the smallest molecular weight and the strongest antioxidant ability.

[0030] (6) First, culture Caco-2 cells in 25 cm 2The culture medium in the cell culture flask was high-glucose medium (DMEM) containing 16% fetal bovine serum (FBS, v / v), 1% non-essential amino acids (NEAA, v / v), 100 U / mL penicillin and 0.1 mg / mL streptomycin. The culture conditions were 37°C, 5% CO2, and 90% relative humidity. The cells were cultured for 21 days.

[0031] (7) Cell transport experiment. Gently wash Caco-2 cells with PBS three times, add 1.5 mL and 3 mL of 37°C preheated balanced salt buffer to the upper side (AP) and lower side (BL) of the Caco-2 cell model, respectively, and equilibrate at 37°C for 30 min. Then remove the balanced salt buffer on the AP side, add the balanced salt buffer solution containing peptide sample F4, place the Transwell culture plate in a carbon dioxide cell culture incubator for 2 h of absorption and transport, and then collect the solutions on both sides for liquid chromatography-mass spectrometry (LC-MS / MS) analysis.

[0032] (8) The conditions for determining the polypeptide sequence of F4 by LC-MS were as follows. Liquid phase conditions: Mobile phase A: 0.1% formic acid in water; Mobile phase B: 0.1% formic acid dissolved in 80% acetonitrile. Elution program: 0 ~ 95 min, mobile phase B 3%; 95 ~ 105 min, mobile phase B 32%; 105 ~ 120 min, mobile phase B 100%. Flow rate: 200 nL / min; Injection volume: 3 μL. Mass spectrometry conditions: MS scanning range (m / z): 355-1700, resolution: 70000, maximum ion injection time: 100 ms; MS / MS scanning range (m / z): 200-2000, ion injection time: 75 ms, resolution: 35000; fragmentation mode: high energy collision; fragmentation energy: 27. The results are shown in Appendix 1.

[0033] (9) There were three peptides in the F4 fraction that were completely absorbed by Caco-2 cells, with lengths of 19, 20, and 23 amino acids, respectively. Among them, the peptide TDEFQLHTNVNDGTEFGGSIYQK consisting of 23 amino acids had the best in vitro antioxidant effect.

[0034] Example 2: Bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK (TK-23) has good antioxidant effect

[0035] (1) The active peptide TDEFQLHTNVNDGTEFGGSIYQK was synthesized by solid phase synthesis with a purity of 99%.

[0036] (2) HepG2 cell culture. First, the HepG2 cell culture medium was changed to a high-glucose medium (DMEM) containing 10% fetal bovine serum (FBS, v / v), 100U / mL penicillin and 0.1 mg / mL streptomycin. The culture conditions were 37°C, 5% CO2, and 90% relative humidity. The culture medium was replaced every 2 days. When the HepG2 cells covered about 80% of the culture area of ​​the culture flask, the cells were digested with trypsin containing 0.25% EDTA and subcultured.

[0037] (3) Experimental design and modeling method. The laboratory was divided into a blank group, a model group (oxidative damage model), a GSH group, and an active peptide group (with 4 gradients of 0.50, 0.75, 1.00, and 1.25 mg / mL). The H2O2 concentrations for the modeling of HepG2 oxidative damage cells were 100, 200, 300, 400, 500, 600, 700, 800, and 1000 μmol / L, respectively. After culturing for 2 h, 4 h, and 6 h, the cell viability was detected by the MTT method, and the survival rate of HepG2 cells was calculated. 100 μL of culture medium was added to the blank group. The H2O2 concentration with a survival rate of about 50% was used as the modeling concentration of the cells.

[0038] (4) Take 1×10 5 HepG2 cells at 100 μmol / mL were inoculated in six-well plates, with 2.5 mL of cells in each well. After the cells were cultured to 80% confluent, the cells were incubated with different concentrations of active peptides and GSH for 24 h, and then the culture medium was discarded. 800 μmol / L hydrogen peroxide (H2O2) was added to each well and incubated for 2 h. HepG2 cells were lysed with cell lysis buffer, and the supernatant was taken after centrifugation. The protein concentration was determined using a bovine serum albumin (BCA) kit, and the antioxidant enzyme activity in the cells was determined using cell superoxide dismutase (SOD), glutathione peroxidase (GSH-PX) and catalase (CAT) kits.

[0039] (5) Result analysis. Effect of peptide TK-23 on the antioxidant enzyme activity of HepG2 cells Figures 5 - 7 As shown. After adding TK-23, the CAT, SOD and GSH-Px activities of the cells were significantly enhanced. From the activity of CAT, it can be seen that under the incubation condition of 0.50 mg / mL GSH, the CAT activity was not significantly different from that of the blank cell group ( P >0.05). The CAT activity of HepG2 cells incubated with 0.50 and 0.75 mg / mL TK-23 was significantly higher than that of the oxidative damage model group and the GSH group ( * P <0.05, **P <0.01). It can be seen from the SOD activity that under the incubation condition of 0.50 mg / mL GSH, the SOD activity was significantly higher than that of the blank cells and oxidative damage model group ( ## P <0.01), indicating that GSH can reduce the oxidative stress level of HepG2 cells. The SOD activity of HepG2 cells incubated with 0.50, 0.75, 1.00, and 1.25 mg / mL T-23 was significantly higher than that of the GSH group ( ** P <0.01). This indicates that T-23 has a better regulatory effect on antioxidant enzymes in HepG2 cells than GSH. From the activity of GSH-Px, it can be seen that under the incubation condition of 0.50 mg / mL GSH, the SOD activity was not significantly different from that of the blank cell group ( P >0.05). The GSH-Px activity of HepG2 cells incubated with 0.75 mg / mL TK-23 was significantly higher than that of the oxidative damage group and the GSH group ( ** P <0.01). Based on the above results, it can be seen that after entering the cells, TK-23 can regulate the activity of antioxidant enzymes in HepG2 cells, thereby regulating the oxidative stress level of the cells, thereby preventing the cells from oxidative damage.

[0040] Table 1. Peptide sequences of crude peptide F4 fraction and peptides of F4 fraction that can pass through Caco-2 cells.

[0041] Before transfer After transfer [K].LGGSAVISLEGKPL.[-] [K].ITVVGVGAVGMACAISILMK.[E] [K].MSINAEEVVVGDLVEVK.[G] [K].AGFAGDDAPR.[A] [K].TITLEVEPSDTIENVK.[AG] [R].KVESLQEEIAFLKK.[L] [R].EVAAFAQFGSDLDAATQQLLSR.[G] [K].TDEFQLHTNVNDGTEFGGSIYQK.[V] [K].LSENNIQTIFAVTEEFQPVYK.[E] [K].TDLEKDIISDTSGDFRK.[L] [R].LLVFSTDAGFHFAGDGK.[L] [K].ILLAELEQLKGQGK.[S] [K].DLYANTVLSGGTTMYPGIADR.[M] [K].HNDDEQYAWESSAGGSFTVR.[T] [K].GHYTEGAELVDSVLDVVRK.[E] [K].AYHEQLSVAEITNACFEPANQMVK.[C] [Y].TEGAELVDSVLDVVR.[K] [R].VDDKVNFHFILFNNVDGHLYELDGR.[M] [K].HNDDEQYAWESSAGGSFTVR.[T] K].FGANAILGVSLAVCK.[A] [K].TVEEVLGHFGVNESTGLSLEQVK.[K] [K].LGEYGFQNALIVR.[Y] [R].GLYQGFNVSVQGIIIYR.[A] [R].EMEENFAVEAANYQDTIGR.[L] [R].VAPEEHPVLLTEAPLNPK.[A] [R].AFVHWYVGEGMEEGEFSEAR.[E] [-].MVNPTVFFDIAVDGEPLGR.[V] [K].ITVVGVGQVGMACAISILGK.[S] [M].VNPTVFFDIAVDGEPLGR.[V] [K].FWEVISDEHGIDPTGTYHGDSDLQLDR.[I] [K].TIGGGDDSFNTFFSETGAGK.[H] [R].FRCPEALFQPSFLGMESCGIHETTFNSIMK.[C] [K].TDEFQLHTNVNDGTEFGGSIYQK.[V] [R].SGPFGQIFRPDNFVFGQSGAGNNWAK.[G] [K].CIIVEEGKEILVGDVGVTITDPFK.[H] <h2 style=";text-align:left;direction:ltr">[R].ISEQFTAMFR.[R] <h2 style=";text-align:left;direction:ltr"> [K].AFMEALQAGADISMIGQFGVGFYSAYLVAEK.[V] <h2 style=";text-align:left;direction:ltr"> [K].MAVTFIGNSTAIQELFKR.[I] <h2 style=";text-align:left;direction:ltr"> [K].LADQCTGLQGFLVFHSFGGGTGSGFTSLLMER.[L] <h2 style=";text-align:left;direction:ltr"> [R].TNQELQEINR.[V] <h2 style=";text-align:left;direction:ltr"> [R].AVFVDLEPTVIDEVR.[T] <h2 style=";text-align:left;direction:ltr"> [R].RAEDGSVIDYELIDQDAR.[D] <h2 style=";text-align:left;direction:ltr"> [K].NNFSDTGNFGFGIQEHIDLGIK.[Y] <h2 style=";text-align:left;direction:ltr"> [R].ILGADTSVDLEETGR.[V] <h2 style=";text-align:left;direction:ltr"> [R].FDGALNVDLTEFQTNLVPYPR.[AI] <h2 style=";text-align:left;direction:ltr"> [K].ADLINNLGTIAK.[S] <h2 style=";text-align:left;direction:ltr"> [R].LISQIVSSITASLR.[F] <h2 style=";text-align:left;direction:ltr"> [R].AVFPSIVGR.[P] <h2 style=";text-align:left;direction:ltr"> [K].DGVFLYFEDNAGVIVNNK.[G] <h2 style=";text-align:left;direction:ltr"> [R].KNNFSDTGNFGFGIQEHIDLGIK.[Y] <h2 style=";text-align:left;direction:ltr"> [R].GTTITLVLKEEASDYLELDTIK.[N] <h2 style=";text-align:left;direction:ltr"> [K].GHYTEGAELVDSVLDVVRK.[E] <h2 style=";text-align:left;direction:ltr"> [R].SGETEDTFIADLVVGLCTGQIK.[T] <h2 style=";text-align:left;direction:ltr"> [R].GYSFTTTAER.[E] <h2 style=";text-align:left;direction:ltr"> [K].NIILEEGKEILVGDVGQTVDDPYATFVK.[M] <h2 style=";text-align:left;direction:ltr"> [R].QVQSLTCEVDALKGTNESLER.[Q] <h2 style=";text-align:left;direction:ltr"> [K].LCYVALDFEQEMATAASSSSLEK.[S] <h2 style=";text-align:left;direction:ltr"> [K].EIIDLVLDR.[I] <h2 style=";text-align:left;direction:ltr"> [K].GHYTEGAELVDSVLDVVR.[K] <h2 style=";text-align:left;direction:ltr"> [K].EAFQLFDR.[T] <h2 style=";text-align:left;direction:ltr"> [R].LGEHNIDVLEGNEQFINAAK.[I] <h2 style=";text-align:left;direction:ltr"> [R].IEDGNNFGVSIQEETVAELR.[T] <h2 style=";text-align:left;direction:ltr"> [K].DLVILLYETALLSSGFSLEDPQTHANR.[I] <h2 style=";text-align:left;direction:ltr"> [R].KDLYANTVLSGGTTMYPGIADR.[M] <h2 style=";text-align:left;direction:ltr"> [K].EDQVFPMNPPK.[F] <h2 style=";text-align:left;direction:ltr"> [Y].LQLVEISR.[A] <h2 style=";text-align:left;direction:ltr"> [L].TEQLGSSGK.[T] <h2 style=";text-align:left;direction:ltr"> [K].TKGVDEVTIVNILTNR.[S] <h2 style=";text-align:left;direction:ltr"> [K].SKFGANAILGVSLAVCK.[A] <h2 style=";text-align:left;direction:ltr"> [R].EGSRTDDEVVQREEEAIQLDGLNASQIR.[E] <h2 style=";text-align:left;direction:ltr"> [K].ESDDPMAYIHFTAEGEVTFK.[S] <h2 style=";text-align:left;direction:ltr"> [K].QTALVELLK.[H] <h2 style=";text-align:left;direction:ltr"> [R].ALTVPELTQQVFDAK.[N] <h2 style=";text-align:left;direction:ltr"> [G].FAGDDAPR.[A] <h2 style=";text-align:left;direction:ltr">[Y].GFQNALIVR.[Y] <h2 style=";text-align:left;direction:ltr"> [R].LHFFMPGFAPLTSR.[G] <h2 style=";text-align:left;direction:ltr"> [K].EKLCYVALDFEQEMATAASSSSLEK.[S] <h2 style=";text-align:left;direction:ltr"> [R].VIEVSHWGNIAVEENVDLK.[H] <h2 style=";text-align:left;direction:ltr"> [K].AELNEFLTR.[E] <h2 style=";text-align:left;direction:ltr"> [L].LTEAPLNPK.[A] <h2 style=";text-align:left;direction:ltr"> [R].HVFGESDELIGQK.[V] <h2 style=";text-align:left;direction:ltr"> [K].LLAVAATAPPDAPNREEVFDER.[A] <h2 style=";text-align:left;direction:ltr"> [K].HLAILGAGLMGAGIAQVSVDK.[H] <h2 style=";text-align:left;direction:ltr"> [R].ELISNASDALDKIR.[L] <h2 style=";text-align:left;direction:ltr"> [R].EIADGLCLEVEGK.[M] <h2 style=";text-align:left;direction:ltr"> [K].LLCGLLAER.[L] <h2 style=";text-align:left;direction:ltr"> [K].QVEYLLIHGTADDNVHFQQSAQLSK.[A] <h2 style=";text-align:left;direction:ltr"> [K].LVAIVDVIDQNR.[A] <h2 style=";text-align:left;direction:ltr"> [K].DHASIQMNVAEVDKVTGR.[F] <h2 style=";text-align:left;direction:ltr"> [R].ISVYYNEATGGK.[Y] <h2 style=";text-align:left;direction:ltr"> [R].FSLENNFLLQHNIR.[K] <h2 style=";text-align:left;direction:ltr"> [K].LTLSALIDGK.[N] <h2 style=";text-align:left;direction:ltr"> [R].IEGDMIVCAAYAHELPK.[Y] <h2 style=";text-align:left;direction:ltr"> [K].IFGVTTLDIVR.[A] <h2 style=";text-align:left;direction:ltr"> [A].GFAGDDAPR.[A] <h2 style=";text-align:left;direction:ltr"> [R].YLTVAAVFR.[G] <h2 style=";text-align:left;direction:ltr"> [K].RAFVHWYVGEGMEEGEFSEAR.[E] <h2 style=";text-align:left;direction:ltr"> [K].VIPELNGK.[L] <h2 style=";text-align:left;direction:ltr"> [K].VILHLKEDQTEYLEER.[R] <h2 style=";text-align:left;direction:ltr"> [R].YYTSASGDEMVSLKDYCTR.[M] <h2 style=";text-align:left;direction:ltr"> [K].HNNDTQHIWESDSNEFSVIADPR.[G] <h2 style=";text-align:left;direction:ltr"> [K].MALDIEIATYR.[K]

[0042] The above shows and describes the basic principles and main features of the present invention and the advantages of the present invention. It should be understood by those skilled in the art that the present invention is not limited to the above embodiments. The above embodiments and descriptions are only for explaining the principles of the present invention. Without departing from the spirit and scope of the present invention, the present invention may have various changes and improvements, which fall within the scope of the present invention to be protected. The scope of protection of the present invention is defined by the attached claims and their equivalents. Sequence Listing <110> Dongguan University of Technology <120> A bioactive peptide with antioxidant function TDEFQLHTNVNDGTEFGGSIYQK <130> 1835 <141> 2022-06-14 <160> 1 <170> SIPOSequenceListing 1.0 <210> 1 <211> 23 <212> PRT <213> Artificial Sequence <400> 1 Thr Asp Glu Phe Gln Leu His Thr Asn Val Asn Asp Gly Thr Glu Phe 1 5 10 15 Gly Gly Ser Ile Tyr Gln Lys 20

Claims

1. An antioxidant functional product, characterized in that: The invention comprises a bioactive peptide TDEFQLHTNVNDGTEFGGSIYQK with antioxidant function, whose amino acid sequence is: Thr-Asp-Glu-Phe-Gln-Leu-His-Thr-Asn-Val-Asn-Asp-Gly-Thr-Glu-Phe-Gly-Gly-Ser-Ile-Tyr-Gln-Lys, which is prepared by solid phase synthesis method. The antioxidant function product comprises antioxidant drugs.

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