Pinctada fucata body surface mucus antioxidant active peptide as well as preparation and application thereof

Abstract

The invention discloses a pinctada fucata martensii body surface mucus antioxidant active peptide as well as preparation and application thereof. The amino acid sequence of the pinctada fucata martensii body surface mucus antioxidant active peptide is Arg-Trp-Ala-Ser-Trp. The preparation method of the active peptide comprises the following steps: collecting pearl shells, collecting mucus, collecting supernate, identifying the supernate and screening and determining the active peptide. The antioxidant active peptide obtained from the pinctada fucata martensii body surface mucus has high activity, free radicals can be well removed, and damage of H2O2 to skin fibroblasts is relieved; the skin wound healing can be promoted. The antioxidant active peptide has a good prospect when being applied to drugs or instruments for relieving cell oxidative stress.

Description

Technical Field

[0001] The invention belongs to the technical field of biological polypeptides, and particularly relates to an antioxidant active peptide from the body surface mucus of the pearl oyster, and a preparation method and application thereof. Background Art

[0002] Antioxidant peptides have the advantages of wide sources, high biological activity, and few side effects. They can be extracted from a variety of organisms, including plants, animals, and microorganisms. Moreover, their digestion and absorption process in the body is relatively simple, and they are easily used by the human body in the form of food or medicine. In particular, antioxidant peptides extracted from marine organisms are polypeptides, which often show excellent antioxidant capacity due to their unique amino acid sequence and structure. The development of new polypeptide antioxidants from marine organisms can not only broaden the source of antioxidants, but also help to improve the efficacy and application range of antioxidants.

[0003] Chinese patent CN114031669A (publication date: February 11, 2022) discloses a thick-shelled mussel antioxidant active peptide and its preparation and application, which relates to the field of polypeptide technology. A thick-shelled mussel antioxidant peptide Gln-Glu-Thr-Tyr and Tyr-Glu-Leu-His-Asp can reduce the production of intracellular reactive oxygen species ROS and form a protective effect. It activates the Keap1 / Nrf2 signaling pathway, exerts an antioxidant effect and protects vascular endothelial cells, and can provide candidate drugs for the prevention and treatment of cardiovascular and cerebrovascular diseases such as hypertension, coronary heart disease, cerebral thrombosis, myocardial infarction, atherosclerosis, heart failure, etc.

[0004] Chinese patent CN114317654A (publication date: April 12, 2022) discloses a method for preparing marine antioxidant active peptides, which relates to the technical field of antioxidant active peptides. The method comprises: S1) extracting collagen from crushed squid tissue; S2) mixing the extracted collagen, trypsin, papain and flavor protease in water for enzymolysis to obtain an enzymolysis solution; S3) subjecting the enzymolysis solution to salting out precipitation and dialysis treatment to obtain marine antioxidant active peptides. Compared with the prior art, the extraction of antioxidant active peptides using squid as raw material and the adoption of different enzymolysis methods can effectively and thoroughly catalyze the protein, thereby obtaining active polypeptides with good quality, reasonable amino acid composition, stable efficacy and reliable quality.

[0005] Chinese patent CN116904542A (publication date: October 20, 2023) discloses an antioxidant active peptide based on oyster shell and a preparation method thereof, which relates to the technical field of comprehensive utilization of oyster shells. This patent is used to solve the problem that the lack of research on antioxidant active peptides based on oyster shells has resulted in the comprehensive utilization of oyster shells being still not ideal, limiting the development and utilization of oyster shell resources; the preparation method first fully refines the oyster shells, making it easy to extract the protein on the oyster shells, and then dissolves the protein to achieve excellent protein extraction effects, and then uses a variety of proteases for testing to screen out proteases suitable for proteins on oyster shells, so that the proteins can be fully enzymolyzed to form active peptides, and then the oyster shell enzymatic hydrolysate is subjected to step-by-step ultrafiltration, so that the components with antioxidant capacity are concentrated, the antioxidant properties of the antioxidant active peptides are improved, and the oyster shell resources are fully utilized, which is of great significance to the development and utilization of oyster shell resources.

[0006] After searching, it was found that although there are some patents on the preparation of antioxidant peptides using shellfish as raw materials, their research direction is mainly on how to use shellfish shells to prepare antioxidant peptides, and the preparation process is complicated.

[0007] The Pearl Oyster (Pinctada pukinensis) is a common shellfish used in pearl production. Its body mucus is an underutilized biological resource. Currently, there is little research on the antioxidant active peptides derived from the Pearl Oyster's body mucus, the amino acid sequence of the polypeptide is unclear, and the preparation method and application need to be further developed. Summary of the invention

[0008] In order to solve the above technical problems, the present invention provides an antioxidant active peptide from the body surface mucus of Pinctada fucata and its preparation and application.

[0009] Disclosed is an antioxidant active peptide from the body surface mucus of Pinctada fucata, wherein the amino acid sequence of the antioxidant active peptide is Arg-Trp-Ala-Ser-Trp.

[0010] The antioxidant active peptide can bind to the antioxidant protease;

[0011] The antioxidant protease is any one of SOD, CAT and keap1.

[0012] A method for preparing anti-oxidative active peptides from the mucus on the surface of the pearl oyster, comprising the following steps:

[0013] S1: Collect pearl oysters and remove impurities from the shells;

[0014] S2: opening the shellfish and collecting the mucus. After opening the shellfish, the shellfish meat and the mucus are placed in a plastic basket with apertures for separation, the shellfish meat and the mucus are separated, and the filtered mucus is collected;

[0015] S3: initial separation of mucus, the mucus is centrifuged and the supernatant is collected;

[0016] S4: Screening peptides, using molecular docking prediction and screening antioxidant active peptides from the supernatant;

[0017] S5: Synthesize peptides using solid phase synthesis and verify antioxidant properties.

[0018] Furthermore, the centrifugal treatment in step S3 has a centrifugal speed of 10000-12000 rpm and a centrifugal time of 10-15 min.

[0019] Furthermore, in step S6, the antioxidant activity is verified by using free radical scavenging rate as an evaluation index; the free radicals include DPPH, ABTS and hydroxyl.

[0020] Furthermore, in step S6, AutoDock Vina is used to simulate the binding ability of active peptides with antioxidant enzymes SOD, CAT and Keap1, and the free radical scavenging ability of the peptides is detected.

[0021] Application of an antioxidant active peptide from the body surface mucus of Pinctada fucata in the preparation of a drug or device for alleviating cellular oxidative stress.

[0022] Compared with the prior art, the advantages and effects of the present invention are as follows:

[0023] 1. The present invention provides an antioxidant active peptide Arg-Trp-Ala-Ser-Trp from the surface mucus of the pearl oyster, which can promote the proliferation of human fibroblasts, can be used to promote skin wound healing, and can be used to promote and discover new drugs that promote wound healing.

[0024] 2. The present invention provides a method for preparing antioxidant active peptides from the surface mucus of pearl oysters. The preliminary separation of the surface mucus of pearl oysters is helpful for rapid protein and peptide identification. Antioxidant peptides are screened by molecular docking and then solid-phase synthesized, which helps to improve the efficiency of developing marine-derived active peptides.

[0025] 3. The present invention provides an application of an antioxidant active peptide from the surface mucus of the pearl oyster. The antioxidant active peptide has good free radical scavenging ability and reduces the damage of H2O2 to cells. The application of the antioxidant active peptide in drugs or devices for reducing cellular oxidative stress has good prospects.

[0026] The above description is only an overview of the technical solution of the present application. In order to more clearly understand the technical means of the present application so that it can be implemented in accordance with the contents of the specification, and to make the above and other purposes, features and advantages of the present application more obvious and easy to understand, the following is a detailed description of the preferred embodiments of the present application in conjunction with the accompanying drawings as follows.

[0027] Based on the detailed description of the specific embodiments of the present application in combination with the accompanying drawings below, those skilled in the art will become more aware of the above and other objects, advantages and features of the present application. BRIEF DESCRIPTION OF THE DRAWINGS

[0028] In order to more clearly illustrate the technical solutions in the embodiments of the present application or the prior art, the drawings required for use in the embodiments or the prior art descriptions are briefly introduced below. Obviously, the drawings described below are some embodiments of the present application. For ordinary technicians in this field, other drawings can also be obtained based on these drawings without creative work. In all drawings, similar elements or parts are generally identified by similar reference numerals. In the drawings, each element or part is not necessarily drawn according to the actual scale.

[0029] in:

[0030] Figure 1 LC-MS spectrum of the polypeptide prepared by the present invention

[0031] Figure 2 Schematic diagram of the 2D simulated structure of the polypeptide prepared by the present invention

[0032] Figure 3 Schematic diagram of the simulated combination of the polypeptide prepared by the present invention and the antioxidant enzyme

[0033] Figure 3 (a) is a schematic diagram of the simulated binding of the polypeptide prepared by the present invention with the antioxidant enzyme SOD

[0034] Figure 3 (b) is a schematic diagram of the simulated binding of the polypeptide prepared by the present invention with the antioxidant enzyme CAT

[0035] Figure 3 (c) is a schematic diagram of the simulated binding of the polypeptide prepared by the present invention with the antioxidant enzyme Keap1

[0036] Figure 4 Comparison of free radical scavenging results of the polypeptide prepared by the present invention

[0037] Figure 4 (a) is a statistical diagram of the results of the polypeptide prepared by the present invention scavenging DPPH free radicals

[0038] Figure 4 (b) is a statistical graph showing the results of the polypeptide prepared by the present invention scavenging ABTS free radicals

[0039] Figure 4 (c) is a statistical graph showing the results of the polypeptide prepared by the present invention scavenging hydroxyl radicals

[0040] Figure 5Comparison of the results of the polypeptide prepared by the present invention promoting fibroblast migration

[0041] Figure 5 (a) The results of the control group fibroblasts before migration

[0042] Figure 5 (b) is the result of fibroblast migration before the peptide composition

[0043] Figure 5 (c) Results of fibroblast migration in the control group

[0044] Figure 5 (d) The result of fibroblast migration after peptide composition

[0045] Figure 6 Comparison of detection of the polypeptide prepared by the present invention protecting cells from H2O2 damage

[0046] Figure 6 (a) The control group protected cells from H2O2 damage.

[0047] Figure 6 (b) The results of the control group protecting cells from H2O2 damage

[0048] Figure 6 (c) Detection results of peptide group protecting cells from H2O2 damage

[0049] Figure 7 Comparison of the results of the polypeptide prepared by the present invention promoting wound healing in diabetic rats

[0050] Figure 7 (a) The wound healing results of diabetic rats in the control group

[0051] Figure 7 (b) The wound healing results of diabetic rats in the peptide group DETAILED DESCRIPTION

[0052] To make the purpose, technical scheme and advantages of the embodiment of the present application clearer, the technical scheme in the embodiment of the present application will be clearly and completely described below in conjunction with the accompanying drawings in the embodiment of the present application. Obviously, the described embodiment is a part of the embodiment of the present application, rather than all of the embodiments. In the following description, specific details such as specific configuration and components are provided only to help fully understand the embodiments of the present application. Therefore, it should be clear to those skilled in the art that various changes and modifications can be made to the embodiments described herein without departing from the scope and spirit of the present application. In addition, for clarity and brevity, the description of known functions and structures is omitted in the embodiment.

[0053] It should be understood that the references to "one embodiment" or "this embodiment" throughout the specification mean that the specific features, structures, or characteristics associated with the embodiment are included in at least one embodiment of the present application. Therefore, the references to "one embodiment" or "this embodiment" appearing throughout the specification do not necessarily refer to the same embodiment. In addition, these specific features, structures, or characteristics may be combined in any suitable manner in one or more embodiments.

[0054] In addition, the present application may repeat reference numerals and / or letters in different examples. This repetition is for the purpose of simplicity and clarity, and does not in itself indicate the relationship between the various embodiments and / or settings discussed.

[0055] The term "and / or" in this article is only a description of the association relationship of associated objects, indicating that there can be three relationships. For example, A and / or B can mean: A exists alone, B exists alone, and A and B exist at the same time. The term " / and" in this article describes another type of association object relationship, indicating that there can be two relationships. For example, A / and B can mean: A exists alone, and A and B exist alone. In addition, the character " / " in this article generally indicates that the previous and next associated objects are in an "or" relationship.

[0056] The term "at least one" in this article is merely a description of the association relationship of associated objects, indicating that there may be three relationships. For example, at least one of A and B can mean: A exists alone, A and B exist at the same time, and B exists alone.

[0057] It should also be noted that, in this article, relational terms such as first and second, etc. are only used to distinguish one entity or operation from another entity or operation, and do not necessarily require or imply any such actual relationship or order between these entities or operations. Moreover, the terms "include", "comprises" or any other variations thereof are intended to cover non-exclusive inclusions.

[0058] Example 1

[0059] This embodiment is a method for preparing antioxidant active peptides from the mucus on the surface of the pearl oyster.

[0060] Combined with the specific experimental description, the method for preparing the antioxidant polypeptide includes the following steps:

[0061] S1: Collect pearl oysters and remove the shells, sand and seaweed;

[0062] S2: Open the shellfish and place the shellfish meat and mucus on a mesh with a pore size of 0.5-1 cm, let it stand for 60 minutes, separate the shellfish meat and mucus, and collect the filtered mucus;

[0063] S3: The mucus was centrifuged at 10,000 rpm and the supernatant was collected;

[0064] S4: Sequence identification of the initially isolated mucus peptides was performed, and peptides were screened using molecular docking simulation methods;

[0065] S5: Peptide synthesis using solid phase synthesis.

[0066] The amino acid sequence of the polypeptide is Arg-Trp-Ala-Ser-Trp.

[0067] Technical effect of this embodiment: Preparing antioxidant peptides by a simple method helps to improve the efficiency of developing marine-derived active peptides.

[0068] Example 2

[0069] Based on Example 1, this example is a method for identifying synthetic polypeptides.

[0070] like Figure 1 As shown, Figure 1 The LC-MS spectrum of the polypeptide prepared by the present invention shows that the synthesized polypeptide has obvious characteristic peaks, indicating that the synthesized polypeptide has a high purity.

[0071] The technical effect of this embodiment: the antioxidant active peptides prepared by the present invention from the surface mucus of the pearl oyster have a higher purity.

[0072] Example 3

[0073] Based on Example 2, this example is to establish a molecular model of the polypeptide Arg-Trp-Ala-Ser-Trp.

[0074] The peptide molecules predicted to be highly active were modeled using Discovery Studio software. Figure 2 , Figure 2 The 2D simulated structure diagram of the polypeptide prepared by the present invention shows that the predicted structure of the polypeptide Arg-Trp-Ala-Ser-Trp presents a compact ring conformation, in which the hydrophobic residues W and A are located on one side of the ring to form a hydrophobic pocket. This structure is conducive to interaction with the hydrophobic region of the target protein.

[0075] Technical effect of this embodiment: The present invention models the polypeptide molecules predicted to be highly active using Discovery Studio software, and can determine whether such a structure is conducive to interaction with the hydrophobic region of the target protein.

[0076] Example 4

[0077] Based on Examples 1-3, this example is a verification of the oxidation activity of the polypeptide Arg-Trp-Ala-Ser-Trp.

[0078] The open source molecular docking tool AutoDockVina software was used to perform molecular docking simulation on the interaction between the peptide Arg-Trp-Ala-Ser-Trp and the antioxidant proteins SOD, CAT and Keap1.

[0079] Before docking simulation, the peptide and target protein structures are preprocessed, including adding hydrogen atoms, calculating charges and assigning flexibility. Then, a docking algorithm is selected for docking simulation to reveal the potential biological activity and mechanism of action of the docked peptide by evaluating binding energy and analyzing interaction patterns.

[0080] like Figure 3 As shown, Figure 3 The schematic diagram of the simulated binding of the polypeptide prepared by the present invention and the antioxidant enzyme is shown in FIG. Figure 3 (a) is a schematic diagram of the simulated binding of the polypeptide prepared by the present invention and the antioxidant enzyme SOD. The results show that the hydrophobic residues W and A of the polypeptide Arg-Trp-Ala-Ser-Trp may interact with the hydrophobic pocket of SOD, thereby stabilizing the structure of the enzyme and possibly enhancing its catalytic activity; this binding may help improve the scavenging efficiency of SOD for superoxide free radicals, thereby enhancing the antioxidant defense of cells.

[0081] Figure 3 (b) is a schematic diagram of the simulated binding of the polypeptide prepared by the present invention with the antioxidant enzyme CAT. The results show that the compact ring conformation and hydrophobic residues of the polypeptide may bind to the corresponding region of CAT through hydrophobic interaction, thereby enhancing the structural stability and catalytic ability of the enzyme. Figure 3 (c) is a schematic diagram of the simulated binding of the polypeptide prepared by the present invention with the antioxidant enzyme Keap1. The results show that the compact ring conformation and hydrophobic residues may enable it to form a tight interaction with the binding pocket of Keap1, thereby disrupting the normal binding of Nrf2 and activating the Nrf2-mediated antioxidant response.

[0082] Technical effect of this embodiment: Through molecular docking simulation and analysis of the simulation results, it can be found that the polypeptide has potential antioxidant activity.

[0083] Example 5

[0084] Based on Example 4, this example is a test of the ability of the polypeptide Arg-Trp-Ala-Ser-Trp to scavenge DPPH, ABTS and hydroxyl free radicals.

[0085] like Figure 4 As shown, Figure 4 This is a comparison chart of the free radical scavenging results of the polypeptides prepared by the present invention (P<0.01). Figure 4(a) is a statistical graph of the results of scavenging DPPH free radicals by the polypeptide prepared in the present invention. The results show that the DPPH free radical scavenging rate increases with the increase in the concentration of the polypeptide solution. When the concentration of Arg-Trp-Ala-Ser-Trp is 0.5 mg / mL, the DPPH free radical scavenging rate is 29.8%; when the concentration of Arg-Trp-Ala-Ser-Trp is 1.5 mg / mL, the DPPH free radical scavenging rate is 52.5%.

[0086] Figure 4 (b) is a statistical graph of the results of scavenging ABTS free radicals by the polypeptide prepared in the present invention. The results show that the ABTS free radical scavenging rate increases with the increase of the concentration of the polypeptide solution. When the concentration of Arg-Trp-Ala-Ser-Trp is 0.5 mg / mL, the ABTS free radical scavenging rate is 27.1%; when the concentration of Arg-Trp-Ala-Ser-Trp is 1.5 mg / mL, the ABTS free radical scavenging rate is 41.3%.

[0087] Figure 4 (c) is a statistical graph of the results of scavenging hydroxyl radicals by the polypeptide prepared by the present invention. The results show that when the concentration of Arg-Trp-Ala-Ser-Trp is 0.8 mg / mL, the scavenging rate of hydroxyl radicals is 8.9%; when the concentration of Arg-Trp-Ala-Ser-Trp is 1.0 mg / mL, the scavenging rate of hydroxyl radicals is 8.9%; when the concentration of Arg-Trp-Ala-Ser-Trp is 1.8 mg / mL, the scavenging rate of hydroxyl radicals is 26.5%.

[0088] Technical effect of this embodiment: By comparing the DPPH, ABTS and hydroxyl radical scavenging rates of the polypeptide Arg-Trp-Ala-Ser-Trp at different concentrations, it can be found that the polypeptide has a significant ability to scavenge DPPH, ABTS and hydroxyl free radicals (P<0.01), and the antioxidant capacity of the polypeptide solution is positively correlated with its concentration.

[0089] Example 6

[0090] Based on Example 5, this example verifies the promoting effect of the polypeptide Arg-Trp-Ala-Ser-Trp on fibroblast migration.

[0091] like Figure 5 As shown, Figure 5 This is a comparison chart of the results of the polypeptide prepared by the present invention promoting fibroblast migration. Figure 5 (a) is the result of the control group (no polypeptide added) before fibroblast migration. Figure 5 (b) is the result of the fibroblasts in the polypeptide group before migration. It can be seen from the figure that the distance between the fibroblasts in the control group and the polypeptide group before migration is 250 μm. Figure 5 (c) is the result of the migration of fibroblasts in the control group. It can be seen from the figure that after 12 hours, the distance between fibroblasts in the control group is about 200 μm, indicating that the migration of fibroblasts is not obvious; Figure 5 (d) is the result of the polypeptide-containing fibroblast migration. It can be seen from the figure that after 12 hours, the distance between the polypeptide-containing fibroblasts is about 50 μm, indicating that the polypeptide Arg-Trp-Ala-Ser-Trp significantly promotes the migration of fibroblasts.

[0092] The technical effect of this example is to verify that the polypeptide Arg-Trp-Ala-Ser-Trp promotes fibroblast migration.

[0093] Example 7

[0094] Based on Example 6, this example verifies the effect of the polypeptide Arg-Trp-Ala-Ser-Trp in protecting cells from damage by H2O2.

[0095] like Figure 6 As shown, Figure 6 This is a comparison chart of the detection of the polypeptide prepared by the present invention protecting cells from H2O2 damage. Figure 6 (a) is a test result of the control group (no polypeptide added) protecting cells from H2O2 damage. The results show that in the absence of H2O2, the cells exhibit lower fluorescence intensity and lower ROS production.

[0096] Figure 6 (b) is the detection result of the control group's protected cells damaged by H2O2. The results show that after H2O2 treatment, the fluorescence intensity is increased and the cellular ROS production increases;

[0097] Figure 6 (c) is a test result of the peptide group protecting cells from H2O2 damage. The results show that after incubation with the peptide, the fluorescence intensity of the cells decreased, indicating that the peptide can reduce the production of ROS in cells.

[0098] The technical effect of this embodiment is as follows: it is verified that the polypeptide Arg-Trp-Ala-Ser-Trp can protect cells from damage by H2O2.

[0099] Example 8

[0100] Based on Example 7, this example verifies the effect of the polypeptide Arg-Trp-Ala-Ser-Trp in promoting wound healing in diabetic rats.

[0101] like Figure 7 As shown, Figure 7 This is a comparison chart of the results of the polypeptide prepared by the present invention promoting wound healing in diabetic rats; wherein, Figure 7(a) is the wound healing results of diabetic rats in the control group (no peptide added). Figure 7 (b) is the wound healing result of diabetic rats in the peptide group;

[0102] The results showed that after 18 days, the wounds of the diabetic rats in the control group still had obvious wounds. After the diabetic rats in the peptide group were treated with peptides, the wounds of the rats' skin were basically healed, and obvious new skin could be observed.

[0103] The technical effect of this embodiment is to verify that the polypeptide Arg-Trp-Ala-Ser-Trp can effectively promote the healing of diabetic wounds.

[0104] In summary, the present invention provides an antioxidant active peptide from the body surface mucus of the pearl oyster, and its preparation and application. The amino acid sequence of the antioxidant active peptide from the body surface mucus of the pearl oyster is Arg-Trp-Ala-Ser-Trp, which has high activity, can better scavenge free radicals, and protect H2O2 from damaging cell activity; it can promote skin wound healing; the application of the antioxidant active peptide in drugs or devices for reducing cell oxidative stress has good prospects, and the invention is innovative.

[0105] The specific implementation methods described above further illustrate the objectives, technical solutions and beneficial effects of the present invention in detail. It should be understood that the above description is only a specific implementation method of the present invention and is not intended to limit the present invention. Any modifications, equivalent substitutions, improvements, etc. made within the spirit and principles of the present invention should be included in the scope of protection of the present invention.

Claims

1. An antioxidant active peptide from the mucus of the pearl oyster, characterized in that: The amino acid sequence of the antioxidant active peptide is Arg-Trp-Ala-Ser-Trp.

2. The anti-oxidative active peptide from the body surface mucus of the pearl oyster according to claim 1, characterized in that: The antioxidant active peptide can bind to the antioxidant protease.

3. The anti-oxidative active peptide from the body surface mucus of the pearl oyster according to claim 2, characterized in that: The antioxidant protease is any one of SOD, CAT and keap1.

4. A method for preparing an antioxidant active peptide from the body surface mucus of Pinctada fucata according to any one of claims 1 to 3, characterized in that: The following steps are involved: S1: Collect pearl oysters and remove impurities from the shells; S2: opening the shellfish and collecting the mucus. After opening the shellfish, the shellfish meat and the mucus are placed in a plastic basket with apertures for separation, the shellfish meat and the mucus are separated, and the filtered mucus is collected; S3: initial separation of mucus, the mucus is centrifuged and the supernatant is collected; S4: Screening peptides, using molecular docking prediction and screening antioxidant active peptides from the supernatant; S5: Synthesize peptides using solid phase synthesis and verify antioxidant properties.

5. The method for preparing the anti-oxidative active peptides from the body surface mucus of Pinctada fucata according to claim 4, characterized in that: The centrifugal treatment in step S3 has a centrifugal speed of 10000-12000 rpm and a centrifugal time of 10-15 min.

6. The method for preparing the anti-oxidative active peptide from the body surface mucus of the pearl oyster according to claim 4 or 5, characterized in that: In the step S6, the antioxidant activity is verified by using the free radical scavenging rate as an evaluation index; the free radicals include DPPH, ABTS and hydroxyl.

7. Use of an antioxidant active peptide from the body surface mucus of the pearl oyster according to any one of claims 1 to 3 in the preparation of drugs or devices for reducing cellular oxidative stress.

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