CN114276408A - Extraction method and application of acanthopanax senticosus glycoprotein - Google Patents

Abstract

The invention provides an extraction method and application of acanthopanax senticosus glycoprotein, wherein the extraction method comprises the step of heating and extracting acanthopanax senticosus coarse powder, wherein the extraction solution is PBS (phosphate buffer solution) with the pH value of 5-9, the extraction temperature is 30-40 ℃, and a table concentrator is also adopted for assisting in the heating and extraction process. The invention adopts PBS buffer solution with pH value of 5-9 as leaching solution, and the extraction is carried out at specific leaching temperature with the aid of a table concentrator, so that the extraction rate of glycoprotein can be improved, the obtained acanthopanax glycoprotein has stable structure, and the activity of glycoprotein is ensured.

Description

A kind of extraction method and application of Acanthopanax senticosus glycoprotein

technical field

The invention relates to the technical field of biochemistry, in particular to an extraction method and application of Acanthopanax senticosus glycoprotein.

Background technique

Glycoproteins are substances in which oligosaccharide chains and polypeptides are covalently linked in various forms and have biological activity. Glycoproteins are one of the important biological macromolecules in living organisms and widely exist in animals, plants and microorganisms, even in single-celled organisms and viruses. It is also found in various forms and types that are distributed in the intracellular and extracellular fluids and tissues of the organism, and constitute a variety of active substances in the organism. Natural glycoproteins have physiological activities such as antioxidant, anti-tumor, and immunity enhancement. Glycoproteins play an important role in various life activities such as growth and development, information transmission, immune system, nervous system, etc., and are also related to the occurrence of various diseases (such as cardiovascular disease, liver and kidney disease, diabetes, tumor and cancer, etc.).

Acanthopanax senticosus, also known as Acanthopanax quinquefolius, Acanthopanax quinquefolius, Acanthopanax senticosus, Acanthopanax senticosus, etc., is a plant of the genus Araliaceae, distributed in Heilongjiang, Jilin, Liaoning, Hebei and Shanxi, China. It is a rhizome medicinal material with rich nutrition, various physiological functions and development potential. Acanthopanax senticosus has a wide range of uses, with the effects of invigorating the spleen, invigorating the spleen, nourishing the kidney and soothing the nerves. Insomnia and other symptoms.

But so far, no method for extracting glycoproteins from Acanthopanax senticosus has been found. The extracts of Acanthopanax senticosus mentioned in the prior art are crude extracts with complex components and lack of in-depth research significance. Further high-end applications.

SUMMARY OF THE INVENTION

Aiming at the problems existing in the prior art, the present invention provides an extraction method and application of Acanthopanax senticosus glycoprotein.

In the first aspect, the present invention provides a method for extracting glycoprotein from Acanthopanax senticosus, including the step of heating and leaching the coarse powder of Acanthopanax senticosus, wherein the leaching solution is a PBS buffer solution with a pH of 5-9, and the leaching temperature is The temperature is 30-40°C, and a shaker is also used to assist in the process of the heating and leaching.

In the prior art, the method of water extraction and alcohol precipitation is generally used to extract active ingredients from the medicinal materials of Acanthopanax senticosus, and then a series of purification steps are performed to obtain the extract of Acanthopanax senticosus with acceptable purity, that is, the existing method is complicated and the quality of the obtained product is generally. According to the research of the present invention, the use of PBS buffer solution with pH of 5-9 as the leaching solution, at a specific leaching temperature and supplemented by a shaking table, can improve the extraction rate of glycoprotein, the obtained Acanthopanax senticosus glycoprotein has a stable structure, and at the same time The activity of the glycoprotein is also ensured, and the extraction method of the present invention has simple operation, mild conditions, good repeatability, and is easy to popularize and apply.

Further, during the heating and leaching process, the shaking rate of the shaker is 40-300 r/min.

Further, in the heating leaching process, the ratio of material to liquid is 1:10-1:20g/mL, the leaching time is 6-48h, and the number of times of leaching is 2-4 times.

In a preferred embodiment of the present invention, during the heating leaching process, the leaching solution is a PBS buffer solution with a pH of 8, the leaching temperature is 30° C., the shaking rate of the shaker is 160 r/min, and the ratio of material to liquid is 160 r/min. It is 1:15g/mL, the extraction time is 12h, and the extraction times are 3 times.

Further, after the heating extraction is performed to obtain the crude extract of Acanthopanax senticosus glycoprotein, the steps of removing free protein and dialysis and freeze-drying are also included.

In the specific embodiment provided by the present invention, the extraction method comprises the following steps:

(1) Pre-treatment: pulverize the medicinal materials of Acanthopanax senticosus into coarse powder of Acanthopanax senticosus;

(2) Shaker-assisted + heating extraction: Mix the Acanthopanax senticosus powder obtained in step (1) with pH=5-9 PBS buffer solution at a material-to-liquid ratio of 1:10-1:20 g/mL, and shake the The shaking rate is 40-300r/min, heating and leaching at 30-40°C for 6-48h, and the extraction times are 1-4 times, then filter, and combine the filtrates to obtain the crude extract of Acanthopanax senticosus glycoprotein;

(3) removal of free protein: the crude extract of Acanthopanax senticosus glycoprotein obtained in step (2) adopts the Sevage method to remove free protein to obtain a solution of Acanthopanax senticosus glycoprotein;

(4) dialysis freeze-drying: put the Acanthopanax senticosus glycoprotein solution obtained in step (3) into a dialysis bag, place in distilled water, dialyze for 48 hours, and freeze-dry the dialysis retentate to obtain the Acanthopanax senticosus glycoprotein powder.

In the present invention, the PBS solution is used for extraction with the aid of a shaker to obtain a crude glycoprotein extract with a protein content of about 15%, and then the free protein is removed to obtain the remaining protein linked with sugar, which is glycoprotein, and then further Purification to obtain the glycoprotein fraction of Acanthopanax senticosus with higher purity. The method for extracting glycoprotein from Acanthopanax senticosus has the advantages of reasonable design, simple process, convenient operation, high product extraction rate, high purity, stable properties, no need to use a large amount of organic reagents, low preparation cost, easy popularization and application, and the like.

It should be noted that the coarse powder mentioned in the present invention means that all the powders pass through the No. 1 sieve, but mixed with the powder that can pass through the No. 3 sieve no more than 20%.

Further, using the Sevage method to remove free protein specifically includes: adding Sevage reagent to the crude extract of Acanthopanax senticosus glycoprotein, shaking at 4°C for 1 hour, then centrifuging at 9000r/min for 15-20min, collecting For the supernatant, repeat this step until no protein layer is precipitated.

Further preferably, the dosage of the Sevage reagent is 1/4 of the volume of the crude extract of Acanthopanax senticosus, and the Sevage reagent is prepared by mixing n-butanol and chloroform in a ratio of 1:4.

Further, the dialysis operation was performed at 4° C., the molecular weight cut-off of the dialysis bag used was 0.1 kDa, and the dialysate was replaced every 6-7 hours during the dialysis process.

In a second aspect, the present invention provides a glycoprotein from Acanthopanax senticosus, which is extracted by the above-mentioned method for extracting glycoprotein from Acanthopanax senticosus.

Further, the sum of sugar content and protein content in the Acanthopanax senticosus glycoprotein is 50-80%, that is, the purity of the Acanthopanax senticosus glycoprotein is 50-80%.

In a third aspect, the present invention provides the application of the above-mentioned Acanthopanax senticosus glycoprotein in the preparation of a functional product with anti-skin oxidation and/or anti-aging.

The present invention proves that the acanthopanax senticosus glycoprotein has a significant effect on anti-oxidation and skin photodamage through in vivo and in vitro experiments, and provides a reference for the research and development of the acanthopanax senticosus glycoprotein applied to skin care products.

The invention provides a method and application for extracting glycoprotein from Acanthopanax senticosus. By using a PBS buffer solution with a pH of 5-9 as a leaching solution, and extracting at a specific leaching temperature and supplemented by a shaking table, the glycoprotein can be improved. The extraction rate is high, the obtained Acanthopanax senticosus glycoprotein is stable in structure, and the activity of the glycoprotein is also ensured, and the extraction method of the invention has simple operation, mild conditions, good repeatability, and is easy to popularize and apply.

Description of drawings

Fig. 1 is the effect of Acanthopanax senticosus glycoprotein of Example 1 of the present invention on SOD activity in mouse skin tissue;

Fig. 2 is the effect of Acanthopanax senticosus glycoprotein of Example 1 of the present invention on MDA activity in mouse skin tissue;

Fig. 3 is the effect of Acanthopanax senticosus glycoprotein of Example 1 of the present invention on GSH-Px activity in mouse skin tissue;

Fig. 4 is the effect of Acanthopanax senticosus glycoprotein of Example 1 of the present invention on HYP activity in mouse skin tissue.

Detailed ways

In order to make the purposes, technical solutions and advantages of the embodiments of the present invention clearer, the technical solutions in the embodiments of the present invention are described clearly and completely below. Obviously, the described embodiments are part of the embodiments of the present invention, but not all of them. Example. Based on the embodiments of the present invention, all other embodiments obtained by those of ordinary skill in the art without creative efforts shall fall within the protection scope of the present invention.

Unless otherwise specified, the experimental reagents and materials used in the examples of the present invention are all commercially available.

Unless otherwise specified, the technical means used in the embodiments of the present invention are conventional means well known to those skilled in the art.

Among them, the determination of purity is as follows:

Glycoprotein is a macromolecular compound, and its purity standard cannot be measured by the usual purity standard of small molecular compound, because even the pure product of glycoprotein is not uniform at the microscopic level. Therefore, the method for characterizing the purity of the glycoprotein prepared by the present invention is It is: Acanthopanax senticosus glycoprotein purity = sugar content + protein content.

①Determination of sugar content

Determination method: use the phenol-sulfuric acid method to measure the absorbance of different concentrations of glucose to formulate a concentration-absorbance standard curve, and then prepare the Acanthopanax senticosus glycoprotein sample into a solution of a certain concentration and measure its absorbance according to the standard curve, and substitute it into the concentration-absorbance standard The curve equation was calculated to obtain the sugar content in the resulting glycoprotein.

Preparation of standard curve: Accurately weigh 2 mg of anhydrous glucose standard, add appropriate amount of distilled water to dissolve, use a 50 mL volumetric flask to make up to the mark, shake well, and prepare a standard solution of 40 μg/mL.

Draw 0.1, 0.2, 0.3, 0.4, 0.5, 0.6, 0.7, 0.8, 0.9 and 1.0 mL of glucose standard solution, respectively, and make up to 1.0 mL with deionized water. Then add, add 0.5 mL of 6% phenol and 2.5 mL of concentrated sulfuric acid, shake well, and place it at room temperature for 30 minutes to measure the absorbance at 490 nm, add 0.5 mL of phenol and 2.5 mL of concentrated sulfuric acid to 1.0 mL of distilled water as a blank, and take the polysaccharide concentration as the horizontal Coordinates, absorbance is the ordinate to draw a standard curve. A linear regression equation was made from the measurement results: y=0.0077X+0.223, R ² was 0.9994, where y was the absorbance value, and x was the polysaccharide concentration in mg/mL.

Accurately weigh 2 mg of Acanthopanax senticosus glycoprotein, add distilled water to dissolve, dilute to 10 mL, and the final concentration of the sample is 0.2 mg/mL; accurately draw 1 mL of each sample solution, and then measure its absorbance value according to the standard curve preparation method.

②Determination of protein content

The protein content of Acanthopanax senticosus glycoprotein was determined by BCA method. The protein standard preparation solution was prepared into 0.5mg/mL protein standard solution, and 0, 1, 2, 4, 8, 12, 16, 20 μL were added to the standard wells of the 96-well plate, and the standard diluent was added. After making up to 20 μL, add 200 μL of BCA working solution to each well, place at 37° C. for 20-30 min, and measure the absorbance at a wavelength of 562 nm. Taking the absorbance as the ordinate and the concentration of the protein standard solution as the abscissa, draw the standard curve and fit the regression equation.

The results showed that the regression equation of the protein standard curve was: y=0.8369X+0.1588 (r=0.9964), where x was the protein concentration (unit: mg.mL ^-1 ), and y was the absorbance value.

Acanthopanax senticosus glycoproteins were assayed using BCA kits on a microplate reader or UV-Vis spectrophotometer, all of which were strictly operated in accordance with the kit instructions.

To sum up, the Acanthopanax senticosus glycoprotein purity prepared by the present invention=sugar content+protein content.

Example 1

The present embodiment provides a method for extracting glycoprotein from Acanthopanax senticosus, and the specific steps are as follows:

(1) Pre-treatment: pulverize the medicinal materials of Acanthopanax senticosus into coarse powder of Acanthopanax senticosus;

(2) Shaker-assisted + heating extraction: 3 g of Acanthopanax senticosus powder obtained in step (1) and PBS buffer solution with pH=8 were uniformly mixed at a material-to-liquid ratio of 1:15 g/mL, and the shaking rate of the shaking table was 160r/min, heating and leaching at 30°C for 12h, the extraction times were 3 times, then filtered, and the filtrates were combined to obtain the crude extract of Acanthopanax senticosus glycoprotein;

(3) removal of free protein: the crude extract of Acanthopanax senticosus glycoprotein obtained in step (2) adopts the Sevage method to remove free protein to obtain a solution of Acanthopanax senticosus glycoprotein;

(4) lyophilization by dialysis: the glycoprotein solution of Acanthopanax senticosus obtained in step (3) was put into a dialysis bag with a molecular weight cut-off of 0.1 kDa, placed in distilled water, dialyzed for 48h, and the dialysis retentate was freeze-dried to obtain Acanthopanax senticosus protein powder.

After testing, in this example, the yield of Acanthopanax senticosus glycoprotein (yield refers to the amount of the obtained glycoprotein freeze-dried powder/3g of Acanthopanax senticosus coarse powder) was 8.61%, and the purity was 73.16%.

Example 2

The present embodiment provides a method for extracting glycoprotein from Acanthopanax senticosus, and the specific steps are as follows:

(1) Pre-treatment: pulverize the medicinal materials of Acanthopanax senticosus into coarse powder of Acanthopanax senticosus;

(2) Shaker-assisted + heating extraction: 3 g of Acanthopanax senticosus powder obtained in step (1) and PBS buffer solution with pH=8 were uniformly mixed at a material-to-liquid ratio of 1:15 g/mL, and the shaking rate of the shaking table was 160r/min, heating and leaching at 60°C for 12h, the extraction times were 3 times, then filtered, and the filtrates were combined to obtain the crude extract of Acanthopanax senticosus glycoprotein;

(3) removal of free protein: the crude extract of Acanthopanax senticosus glycoprotein obtained in step (2) adopts the Sevage method to remove free protein to obtain a solution of Acanthopanax senticosus glycoprotein;

(4) lyophilization by dialysis: the glycoprotein solution of Acanthopanax senticosus obtained in step (3) was put into a dialysis bag with a molecular weight cut-off of 0.1 kDa, placed in distilled water, dialyzed for 48h, and the dialysis retentate was freeze-dried to obtain Acanthopanax senticosus protein powder.

After testing, in this example, the yield of Acanthopanax senticosus glycoprotein was 7.86%, and the purity was 57.35%.

Example 3

The present embodiment provides a method for extracting glycoprotein from Acanthopanax senticosus, and the specific steps are as follows:

(1) Pre-treatment: pulverize the medicinal materials of Acanthopanax senticosus into coarse powder of Acanthopanax senticosus;

(2) Shaker-assisted + heating extraction: 3 g of Acanthopanax senticosus powder obtained in step (1) and PBS buffer solution with pH=8 were uniformly mixed at a material-to-liquid ratio of 1:15 g/mL, and the shaking rate of the shaking table was 400r/min, heating and leaching at 30°C for 12h, the extraction times were 3 times, then filtered, and the filtrates were combined to obtain the crude extract of Acanthopanax senticosus glycoprotein;

(3) removal of free protein: the crude extract of Acanthopanax senticosus glycoprotein obtained in step (2) adopts the Sevage method to remove free protein to obtain a solution of Acanthopanax senticosus glycoprotein;

(4) lyophilization by dialysis: the glycoprotein solution of Acanthopanax senticosus obtained in step (3) was put into a dialysis bag with a molecular weight cut-off of 0.1 kDa, placed in distilled water, dialyzed for 48h, and the dialysis retentate was freeze-dried to obtain Acanthopanax senticosus protein powder.

After testing, in this example, the yield of Acanthopanax senticosus glycoprotein was 9.12%, and the purity was 68.56%.

Example 4

The present embodiment provides a method for extracting glycoprotein from Acanthopanax senticosus, and the specific steps are as follows:

(1) Pre-treatment: pulverize the medicinal materials of Acanthopanax senticosus into coarse powder of Acanthopanax senticosus;

(2) Shaker-assisted + heating extraction: 3 g of Acanthopanax senticosus powder obtained in step (1) and PBS buffer solution with pH=7 were uniformly mixed at a material-to-liquid ratio of 1:20 g/mL, and the shaking rate of the shaking table was 200r/min, heating and leaching at 40°C for 24h, the extraction times were 4 times, then filtered, and the filtrates were combined to obtain the crude extract of Acanthopanax senticosus glycoprotein;

(3) removal of free protein: the crude extract of Acanthopanax senticosus glycoprotein obtained in step (2) adopts the Sevage method to remove free protein to obtain a solution of Acanthopanax senticosus glycoprotein;

(4) lyophilization by dialysis: the glycoprotein solution of Acanthopanax senticosus obtained in step (3) was put into a dialysis bag with a molecular weight cut-off of 0.1 kDa, placed in distilled water, dialyzed for 48h, and the dialysis retentate was freeze-dried to obtain Acanthopanax senticosus protein powder.

After testing, in this example, the yield of Acanthopanax senticosus glycoprotein was 8.21%, and the purity was 62.36%.

Application Example Skin Antioxidant Experiment of Acanthopanax senticosus glycoprotein

The antioxidant effect of the Acanthopanax senticosus glycoprotein prepared in Example 1 of the present invention was verified by experiments, and the experimental methods and results were as follows:

1. Subject: SD rats.

2. Indicator measurement and analysis methods

The determination of SOD, MDA, GSH-Px, and HYP in skin tissue was carried out on a microplate reader or a UV-Vis spectrophotometer, which was strictly operated in accordance with the kit instructions.

Superoxide Dismutase (SOD) Kit (Item No. A001-1, Production Lot: 20210423), Malondialdehyde (MDA) Assay Kit (Item No. A003-1-2, Production Lot: 20201203), Glutathione Peroxidase (GSH-Px) Test Kit (Item No.: A005-1-1, Production Lot: 20201222), Hydroxyproline (Alkaline Hydrolysis) Kit (Item No. A030-2-1, Production Lot: 20201223) ) were provided by Nanjing Jiancheng Bioengineering Institute.

3. Animal grouping, modeling, administration

Thirty SD female rats were selected and randomly divided into blank group, model group, positive control group, and Acanthopanax senticosus glycoprotein high, medium and low dose groups, with 5 rats in each group. The dorsal hair in the area of about 3cm × 4cm on the back of the mice in all groups was removed by electric shaving. It is not suitable to give ultraviolet irradiation on the day of hair removal. After the start of the experiment, the same method was used to remove the hair of all groups of mice every 3 days. Next, ultraviolet irradiation was performed, and the radiation intensity of UVA and UVB lamps was measured before irradiation, and the minimum erythema quantity was determined to be 37.34 J/cm ² by an ultraviolet radiation meter. The irradiation time was set according to the minimum amount of erythema. The shaved rats were placed in a self-made ultraviolet light box, and the irradiation distance was fixed at 10 cm, and ultraviolet (UVA+UVB) irradiation was performed. 0.5h/day in the first week, 1h/day in the second week, 2h/day in the third week, and then maintained for 2h/day until the skin on the back of the rat was dry, peeled, or even partially ulcerated. The method of administration after modeling was adopted. Except for the blank group, the positive control group was smeared with vitamin E solution 10mg/mL 0.5mL on the back, and the high, medium and low dose groups of Acanthopanax senticosus were smeared with the total glycoprotein of Acanthopanax senticosus 25mg/mL. , 10mg/mL, 1mg/mL 0.5mL, each group had free access to food and water for 4 consecutive weeks.

4. Skin Treatment

After the last administration, the patients were sacrificed by cervical dislocation, the skin tissue was cut, the surrounding connective tissue was stripped, freshly weighed, and the data were recorded.

5. Preparation of Tissue Homogenates

The accurately weighed skin tissue was added to 9 times the volume of normal saline, processed in a homogenizer to prepare a homogenate, and then the homogenate was centrifuged at 4000 r/min for 20 min, and the supernatant was taken to obtain a 10% skin tissue homogenate, which was frozen for later use.

6. Data processing

SPSS16.0 software was used for statistical analysis of experimental data, expressed as mean and standard deviation (x±S), and t-test was used for comparison between groups, with P<0.05 or P<0.01 as the difference, indicating that the difference between groups was statistically significant study meaning.

7. Experimental results

7.1 Effects of Acanthopanax senticosus glycoprotein on SOD activity in mouse skin tissue

The results are shown in Figure 1. It can be seen from the figure that compared with the blank group, the SOD activity in the skin of the rats in the model group was significantly decreased. Compared with the model group, the SOD activity of the Acanthopanax senticosus glycoprotein administration group was significantly increased, and it was positively correlated with the dose. The SOD activity of Acanthopanax senticosus glycoprotein group was higher than that of the positive group, indicating that Acanthopanax senticosus glycoprotein and vitamin E have similar antioxidant effects, and its effect may be better than that of vitamin E.

7.2 Effect of Acanthopanax senticosus glycoprotein on MDA activity in mouse skin tissue

The results are shown in Figure 2. It can be seen from the figure that compared with the blank group, the MDA content in the skin of the rats in the model group was significantly increased. Compared with the model group, the MDA content in the Acanthopanax senticosus glycoprotein administration group was significantly decreased, and the MDA content gradually decreased with the increase of the Acanthopanax senticosus glycoprotein dose. The content of MDA in the Acanthopanax senticosus glycoprotein group was lower than that in the positive group, indicating that the effect of Acanthopanax senticosus glycoprotein in inhibiting oxidative stress and MDA production was better than that of VE.

7.3 Effects of Acanthopanax senticosus glycoprotein on GSH-Px activity in mouse skin tissue

The results are shown in Figure 3. It can be seen from the figure that compared with the blank group, the GSH-Px activity in the skin of the rats in the model group was significantly decreased. Compared with the model group, the GSH-Px activity of the Acanthopanax senticosus glycoprotein administration group was significantly increased, and it was positively correlated with the dose. The GSH-Px activity of the Acanthopanax senticosus glycoprotein group was higher than that of the positive group, indicating that the Acanthopanax senticosus glycoprotein can promote the production of glutathione peroxidase in the body, which has the effect of scavenging free radicals and derivatives, and also reduces lipid peroxidation It enhances the body's ability to resist oxidative damage.

7.4 Effects of Acanthopanax senticosus glycoprotein on HYP activity in mouse skin tissue

The results are shown in Figure 4. It can be seen from the figure that compared with the blank group, the HYP content in the skin of the rats in the model group was significantly decreased. Compared with the model group, the content of HYP in the Acanthopanax senticosus glycoprotein administration group was significantly increased, and it was positively correlated with the dose. Hydroxyproline is a major amino acid contained in collagen. Collagen is the main component of collagen fibers in the interstitial cells of skin connective tissue, indicating that Acanthopanax senticosus can promote damaged skin to generate collagen and repair damage.

To sum up, the glycoprotein of Acanthopanax senticosus has significant anti-oxidation and has a good repairing effect on skin photoaging, which maximizes the development and utilization of Acanthopanax senticosus in the research and development of antioxidant drugs, health food and skin care products of Acanthopanax senticosus References are provided.

Finally, it should be noted that the above embodiments are only used to illustrate the technical solutions of the present invention, but not to limit them; although the present invention has been described in detail with reference to the foregoing embodiments, those of ordinary skill in the art should understand that it can still be Modifications are made to the technical solutions described in the foregoing embodiments, or some technical features thereof are equivalently replaced; and these modifications or replacements do not make the essence of the corresponding technical solutions depart from the spirit and scope of the technical solutions of the embodiments of the present invention.

Claims (10)

1. a method for extracting glycoprotein of Acanthopanax senticosus, it is characterized in that, comprise the step that acanthopanax senticosus coarse powder is carried out heating leaching, wherein, the leaching solution is that pH is the PBS buffer solution of 5-9, and the leaching temperature is 30-40°C, shaker is also used to assist in the process of heating and leaching. 2. the extraction method of a kind of Acanthopanax senticosus glycoprotein according to claim 1, is characterized in that, in described heating leaching process, the shaking rate of shaker is 40-300r/min. 3. the extraction method of a kind of Acanthopanax senticosus glycoprotein according to claim 1 and 2, is characterized in that, in the described heating leaching process, the solid-liquid ratio is 1:10-1:20g/mL, and the leaching time It is 6-48h, and the extraction times are 2-4 times. 4. the extraction method of a kind of Acanthopanax senticosus glycoprotein according to claim 3, is characterized in that, in described heating leaching process, leaching solution is the PBS buffer solution that pH is 8, and leaching temperature is 30 ℃, The shaking rate of the shaker was 160 r/min, the material-liquid ratio was 1:15 g/mL, the leaching time was 12 h, and the number of leaching was 3 times. 5. the extraction method of a kind of Acanthopanax senticosus glycoprotein according to claim 1, is characterized in that, after carrying out described heating leaching to obtain Acanthopanax senticosus glycoprotein crude extract, also comprises removing free protein and dialysis freeze-dried step. 6. the extraction method of a kind of Acanthopanax senticosus glycoprotein according to claim 5, is characterized in that, adopts Sevage method to remove free protein. 7. the extraction method of a kind of Acanthopanax senticosus glycoprotein according to claim 5, is characterized in that, dialysis operation is carried out at 4 ℃, and the molecular weight cut-off of used dialysis bag is 0.1kDa, in dialysis process, replace every 6-7 hours One dialysate. 8. An acanthopanax glycoprotein, characterized in that, it is obtained by the extraction method of the acanthopanax glycoprotein according to any one of claims 1-7. 9 . The glycoprotein of Acanthopanax senticosus according to claim 8 , wherein the sum of sugar content and protein content is 50-80%. 10 . 10. The application of the Acanthopanax senticosus glycoprotein according to claim 9 in the preparation of a functional product with anti-skin oxidation and/or anti-aging.

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