CN115812889B - Application of acanthopanax extract in preparation of tyrosinase inhibitor product - Google Patents
Application of acanthopanax extract in preparation of tyrosinase inhibitor product Download PDFInfo
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- CN115812889B CN115812889B CN202211417072.7A CN202211417072A CN115812889B CN 115812889 B CN115812889 B CN 115812889B CN 202211417072 A CN202211417072 A CN 202211417072A CN 115812889 B CN115812889 B CN 115812889B
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- 239000000284 extract Substances 0.000 title claims abstract description 28
- 101710147108 Tyrosinase inhibitor Proteins 0.000 title claims abstract description 14
- 238000002360 preparation method Methods 0.000 title description 9
- 102000003425 Tyrosinase Human genes 0.000 claims abstract description 56
- 108060008724 Tyrosinase Proteins 0.000 claims abstract description 56
- 239000000469 ethanolic extract Substances 0.000 claims abstract description 47
- 230000005764 inhibitory process Effects 0.000 claims abstract description 42
- 230000000694 effects Effects 0.000 claims abstract description 36
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims abstract description 30
- WTDRDQBEARUVNC-LURJTMIESA-N L-DOPA Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C(O)=C1 WTDRDQBEARUVNC-LURJTMIESA-N 0.000 claims abstract description 26
- QJVXKWHHAMZTBY-GCPOEHJPSA-N syringin Chemical compound COC1=CC(\C=C\CO)=CC(OC)=C1O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 QJVXKWHHAMZTBY-GCPOEHJPSA-N 0.000 claims abstract description 24
- QJVXKWHHAMZTBY-KSXIZUIISA-N syringin Natural products COc1cc(C=CCO)cc(OC)c1O[C@H]2O[C@@H](CO)[C@H](O)[C@@H](O)[C@@H]2O QJVXKWHHAMZTBY-KSXIZUIISA-N 0.000 claims abstract description 24
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- FFDULTAFAQRACT-JSGUJALWSA-N Eleutheroside E Chemical compound COC1=CC([C@@H]2[C@@H]3[C@H]([C@@H](OC3)C=3C=C(OC)C(O[C@H]4[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O4)O)=C(OC)C=3)CO2)=CC(OC)=C1O[C@@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1O FFDULTAFAQRACT-JSGUJALWSA-N 0.000 description 14
- XUMBMVFBXHLACL-UHFFFAOYSA-N Melanin Chemical compound O=C1C(=O)C(C2=CNC3=C(C(C(=O)C4=C32)=O)C)=C2C4=CNC2=C1C XUMBMVFBXHLACL-UHFFFAOYSA-N 0.000 description 8
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- BJRNKVDFDLYUGJ-RMPHRYRLSA-N hydroquinone O-beta-D-glucopyranoside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=CC=C(O)C=C1 BJRNKVDFDLYUGJ-RMPHRYRLSA-N 0.000 description 2
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- BEJNERDRQOWKJM-UHFFFAOYSA-N kojic acid Chemical compound OCC1=CC(=O)C(O)=CO1 BEJNERDRQOWKJM-UHFFFAOYSA-N 0.000 description 1
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- WZNJWVWKTVETCG-UHFFFAOYSA-N kojic acid Natural products OC(=O)C(N)CN1C=CC(=O)C(O)=C1 WZNJWVWKTVETCG-UHFFFAOYSA-N 0.000 description 1
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Classifications
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02A—TECHNOLOGIES FOR ADAPTATION TO CLIMATE CHANGE
- Y02A40/00—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production
- Y02A40/90—Adaptation technologies in agriculture, forestry, livestock or agroalimentary production in food processing or handling, e.g. food conservation
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- Cosmetics (AREA)
Abstract
The invention relates to an application of acanthopanax extract in preparing tyrosinase inhibitor products, belonging to the fields of cosmetics and foods. The application of the acanthopanax extract in preparing a tyrosinase inhibitor product is characterized in that the acanthopanax extract is obtained by the following method: mixing radix Acanthopanacis Senticosi fruit powder with ethanol water solution with certain concentration, and performing ultrasonic treatment for a certain time to obtain extractive solution; filtering, distilling and drying the obtained extract to obtain the acanthopanax ethanol extract. The in vitro enzyme activity test results prove that: the acanthopanax ethanol extract has certain inhibition activity on tyrosinase under different concentrations when L-dopa and L-tyrosine are taken as substrates, the inhibition effect of main active components of acanthopanaxoside E and syringin on tyrosine is also very obvious, and the main active components of the acanthopanax ethanol extract and the syringin have obvious reversible competitive inhibition effect on tyrosinase. Therefore, the acanthopanax ethanol extract is an excellent tyrosinase natural inhibitor and has the potential of further developing into beauty cosmetics or food antistaling agents.
Description
Technical Field
The invention relates to an application of acanthopanax extract in preparing tyrosinase inhibitor products, belonging to the fields of cosmetics and foods.
Background
Tyrosinase is the main rate limiting enzyme in the process of melanin production, which is formed by tyrosine through a series of chemical reactions. In melanocytes, tyrosine is hydroxylated to produce dopa and dopaquinone by tyrosinase, which is converted to indoloquinone by oxidation, decarboxylation, etc., and finally the indoloquinone is polymerized to melanin. Inhibition of tyrosinase has been established as one of the main strategies for regulating melanin production, and is used to treat hyperpigmentation and other adverse effects from melanin production. There are various drugs for inhibiting melanin generation, which can treat excessive melanin generation or pigmentation of human skin, such as arbutin, ascorbic acid, etc. of natural plant origin.
Many tyrosinase inhibitors are limited in application due to their safety, so searching for natural effective tyrosinase inhibitors has become a research development trend in the food and cosmetic industries. At present, research and development on an inhibitor for inhibiting tyrosinase activity by acanthopanax extract are not available. The invention provides a preparation method of an acanthopanax ethanol extract and a new application of the acanthopanax ethanol extract serving as a tyrosinase inhibitor. The in vitro tyrosinase inhibition activity research shows that the acanthopanax ethanol extract has obvious tyrosinase inhibition activity, the main active components of the acanthopanaxoside E and the syringin have obvious inhibition effect on tyrosine, and the acanthopanaxoside E and the syringin have obvious reversible competitive inhibition effect on tyrosinase, so that the acanthopanax ethanol extract can be used as a natural tyrosinase inhibitor. Can be developed into functional foods and cosmetics with whitening function and food preservative for preventing food browning, and provides reliable basis for developing acanthopanax health care products, foods and cosmetics in future.
Disclosure of Invention
The invention aims to provide a new application of an acanthopanax ethanol extract as a tyrosinase inhibitor. The tyrosinase activity inhibition experiment using L-dopa and L-tyrosine as substrates is established, the acanthopanax ethanol extract is used as a natural inhibitor, and the tyrosinase inhibition mechanism of two main active components is discussed.
The application of the acanthopanax extract in preparing a tyrosinase inhibitor product is characterized in that the acanthopanax extract is obtained by the following method: mixing radix Acanthopanacis Senticosi fruit powder with ethanol water solution with certain concentration, and performing ultrasonic treatment for a certain time to obtain extractive solution; filtering, distilling and drying the obtained extract to obtain the acanthopanax ethanol extract.
Preferably, the volume fraction of ethanol in the ethanol water solution is 30-80%; the mass-volume ratio of the acanthopanax fruit powder to the ethanol water solution is 1g:10 mL-1 g:50mL.
Preferably, the ultrasonic treatment time is 180 min-250 min.
Preferably, the distillation step is: and (3) rotationally evaporating the filtered extracting solution at 40-55 ℃ to remove ethanol in the extracting solution, thus obtaining the acanthopanax ethanol crude extract.
Preferably, the drying step is: and (3) performing vacuum drying or low-temperature freeze drying on the obtained acanthopanax coarse extract to obtain an acanthopanax ethanol extract.
In the application of the invention, when L-dopa and L-tyrosine are used as substrates, the tyrosinase activity is obviously inhibited by the acanthopanax ethanol extract in a concentration-dependent manner, and when the tyrosinase activity is reduced by half, the concentration (IC 50) of the acanthopanax ethanol extract is respectively 1.77+/-0.96 mg/ml and 1.86+/-0.75 mg/ml; the inhibition rates of the acanthopanax ethanol extract on tyrosinase at different concentrations (1 mg/ml, 2.5mg/ml, 5mg/ml and 7.5 mg/ml) are 34.51+/-2.05% and 40.86 +/-0.03%, 55.31 +/-0.6% and 40.38+/-2.84%, 84.33+/-2.71% and 88.03 +/-0.78%, 90.47+/-0.87% and 94.87+/-0.30% respectively when the L-dopa and the L-tyrosine are used as substrates.
In the application of the invention, the inhibition rate IC 50 values of the main active components of the acanthopanax senticosus extract, namely acanthopanaxoside E and syringin, on tyrosinase are respectively 11.13+/-0.50 mu M and 15.41+/-0.22 mu M, and the inhibition rates are respectively 51.53 +/-0.01% and 55.03+/-3.38% when the concentration is 20 mu M; and the results of tyrosinase kinetics experiments show that the acanthopanax glycoside E and the syringin have reversible competitive inhibition reaction on tyrosinase.
In particular, the invention provides an application of acanthopanax extract in preparing food preservative products.
Specifically, the invention provides application of acanthopanax extract in preparing whitening and brightening daily chemical washing and caring products, wherein the daily chemical washing and caring products are facial cleanser, facial cream, hand cream, emulsion and facial mask.
Specifically, the invention provides application of acanthopanax extract in preparing whitening and brightening functional food, wherein the functional food is in the form of solid powder, oral drink, tabletting candy, food preservative film additive and the like.
The beneficial effects of the invention are as follows: the invention provides a preparation method of an acanthopanax ethanol extract and a new application of the acanthopanax ethanol extract serving as a tyrosinase inhibitor. The in vitro tyrosinase activity inhibition research shows that the acanthopanax ethanol extract has remarkable tyrosinase inhibition activity, can effectively inhibit melanin generation, and is used as a natural tyrosinase inhibitor. Can be developed into functional foods and cosmetics with whitening function and food preservative for preventing food browning, and provides reliable basis for developing acanthopanax health care products, foods and cosmetics in future. The acanthopanax ethanol extract provided by the invention can be used as a natural plant tyrosinase inhibitor, and has the advantages of simple extraction process, low production cost and easiness in industrial production.
Drawings
FIG. 1 shows the effect of different concentrations of an ethanol extract of acanthopanax on tyrosinase activity when L-dopa is used as a substrate;
FIG. 2 shows the effect of different concentrations of an extract of acanthopanax senticosus ethanol on tyrosinase activity using L-tyrosine as a substrate;
FIG. 3 inhibition of tyrosinase by eleutheroside E at various concentrations using L-dopa as substrate (A); a graph (B) of the reaction rate of eleutheroside E and tyrosinase activity; a linewiriver-Burk double reciprocal curve (C) of eleutheroside E at different substrate L-dopa concentrations;
FIG. 4 inhibition of tyrosinase by syringin at various concentrations using L-dopa as substrate (A); a graph (B) of the reaction rate of syringin versus tyrosinase activity; lineweaver-Burk double reciprocal curves (C) for syringin at different substrate L-dopa concentrations;
Note that: the letters in the figures represent significant differences between the comparison groups within the 95% confidence interval, P <0.05, P <0.01, P <0.001, P <0.0001, and statistical calculations were performed using ANOVA.
Detailed Description
The following non-limiting examples will enable those of ordinary skill in the art to more fully understand the invention and are not intended to limit the invention in any way.
The test methods described in the following examples, unless otherwise specified, are all conventional; the reagents and materials, unless otherwise specified, are commercially available.
One of the specific embodiments is as follows:
the invention provides an acanthopanax ethanol extract, which is prepared by the following steps:
Step 1: collecting Acanthopanax senticosus (Acanthopanax senticosus) fruit powder, mixing with ethanol water solution of certain concentration, and standing for ultrasonic treatment for a certain time to obtain extractive solution.
Step 2: filtering the extractive solution, and distilling the solvent under reduced pressure to obtain crude ethanol extract of radix Acanthopanacis Senticosi.
Step 3: and (3) taking the acanthopanax ethanol crude extract, and drying to obtain the acanthopanax ethanol extract.
Preferably, in the preparation method of the acanthopanax ethanol extract, the volume fraction of ethanol in the ethanol aqueous solution is 30-80%; the mass-volume ratio of the acanthopanax fruit powder to the ethanol water solution is 1: 10-1:50, wherein the ultrasonic time is 180-250 min.
Preferably, the volume fraction of ethanol in the ethanol aqueous solution is 70%, and the mass-volume ratio of the acanthopanax fruit powder to the ethanol aqueous solution is 1:25, wherein the ultrasonic time is 180min.
Preferably, in the preparation method of the acanthopanax ethanol extract provided by the invention, the step 2 specifically comprises the steps of filtering the obtained extract, performing rotary evaporation at 40-55 ℃, and removing ethanol in the extract obtained in the step 1 to obtain the acanthopanax ethanol crude extract.
Preferably, in the preparation method of the acanthopanax ethanol extract provided by the invention, the drying step of the step 3 is specifically that the obtained acanthopanax crude extract is subjected to vacuum drying or low-temperature freeze drying to obtain the acanthopanax ethanol extract.
Preferably, the drying method of the acanthopanax ethanol extract is vacuum drying.
Another object of the present invention is to provide an acanthopanax extract prepared by the above method and use of the acanthopanax extract in preparing tyrosinase inhibitor products.
Example 1
A preparation method of radix Acanthopanacis Senticosi ethanol extract comprises adding radix Acanthopanacis Senticosi fruit powder into ethanol water solution, ultrasonic mixing, filtering, steaming, and lyophilizing to obtain radix Acanthopanacis Senticosi ethanol extract, and comprises the following steps:
weighing 20g of acanthopanax fruit powder, adding 500ml of 70% ethanol solution, and performing ultrasonic treatment at 45 ℃ for 180min to obtain an acanthopanax ethanol crude extract. The crude extract obtained was filtered and, after filtration, spin-distilled at 40 ℃ until the ethanol solution was completely removed. And (3) performing vacuum drying and freeze-drying on the extract obtained after rotary steaming to obtain an acanthopanax ethanol extract, collecting and storing at the temperature of minus 80 ℃.
1. Tyrosinase inhibition activity assay:
Tyrosinase is the main rate limiting enzyme in the process of melanin production, and during the process of melanin production by tyrosinase reaction, the catalytic action of tyrosinase mainly occurs in two reactions of converting tyrosine into dopa and converting dopa into dopaquinone, wherein dopaquinone is a colored substance and has a maximum absorption peak at 475nm wavelength. The inhibition effect of the sample on tyrosinase was calculated by measuring the amount of dopaquinone using L-dopa or L-tyrosine as substrate.
Mu.L of 2.5mM L-dopa or L-tyrosine solution is mixed with 200 mu.L of 0.1M phosphate buffer, incubated at 25 ℃, then 11 mu.L of acanthopanax extract solution (concentration of 1mg/mL, 2.5mg/mL, 5mg/mL, 7.5mg/mL respectively) and 11 mu L of tyrosinase aqueous solution (1000 unit/mL) are added, the total reaction system is mixed evenly 333 mu L, and absorbance at 475nm is detected for incubation 540 s. Kojic acid served as a positive control for this experiment.
Tyrosinase activity= (a sample/a control) ×100% (absorbance is average value)
The experimental data provided by the invention are shown in figures 1 and 2, wherein the experimental data respectively show the inhibition rate of the acanthopanax ethanol extract on tyrosinase when the acanthopanax ethanol extract takes L-dopa and L-tyrosine as substrates, and the acanthopanax ethanol extract has good tyrosinase inhibition effect when the acanthopanax ethanol extract takes L-dopa and L-tyrosine, and shows good correlation with the concentration of the acanthopanax ethanol extract, namely, the inhibition rate also shows corresponding increasing trend along with the increase of the concentration of the acanthopanax ethanol extract.
As a result, as shown in FIG. 1, the inhibition ratio of the ethanol extract of acanthopanax was 34.51.+ -. 2.05% at a concentration of 1mg/ml, the highest inhibition ratio was 90.47.+ -. 0.87% at 7.5mg/ml, and the IC 50 value was 1.77.+ -. 0.96mg/ml when the substrate of L-dopa was used. As a result, as shown in FIG. 2, when L-tyrosine was used as a substrate, the inhibition rate of the ethanol extract of acanthopanax was 40.86.+ -. 0.03% at the minimum value of the inhibition rate measured at a concentration of 1mg/ml, 94.87.+ -. 0.30% at the maximum inhibition rate at 7.5mg/ml, and the IC 50 value was 1.86.+ -. 0.75mg/ml.
Therefore, the acanthopanax extract is an excellent tyrosinase natural inhibitor, and can be developed into functional foods with whitening function, beauty cosmetics or food preservative for preventing food browning.
2. Tyrosinase kinetics assay:
In order to judge whether the reaction of the eleutheroside E and the syringin on the tyrosinase is reversible or not, the eleutheroside E and the syringin (20 mu M, 10 mu M, 5 mu M, 2.5 mu M and 1.25 mu M) with different concentrations are added into a reaction system, when the concentration of the substrate L-dopa is unchanged (2.5 mM), the adding amount of the tyrosinase (1000U, 500U, 250U and 125U) is changed, and the relation of the activity of the oxidation of the tyrosine catalytic substrate along with the enzyme amount is measured. In the figure, v represents the change in absorbance per minute at 475nm wavelength, and E represents the activity of the enzyme.
The Lineweaver-Burk double reciprocal graph method can obtain a series of intersecting straight lines, and the dynamic parameters such as the Michaelis constant K m, the maximum speed V max, the inhibition constant K i and the like of the tyrosinase oxidation L-DOPA can be obtained by combining a secondary graph method, so that the inhibition type of the inhibitor on the tyrosinase activity can be judged, and the possible inhibition mechanism of the inhibitor can be analyzed according to the inhibition type.
Specifically, 111. Mu.L of L-DOPA (0.125 mM, 0.25mM, 0.5mM, 1mM, 2 mM) solution with 0.1M phosphate buffer (211. Mu.L) were mixed uniformly and incubated at 25 ℃, then 11. Mu.L of tyrosinase aqueous solution (1000 unit/mL) was added, 333. Mu.L of the total reaction system was mixed uniformly, absorbance values of samples were measured at 475nm after incubation for 540s, and the effect of inhibitors at different concentrations on the enzymatic reaction rates of L-DOPA at different concentrations was determined. And calculating enzyme inhibition kinetic parameters according to a Lineweaver-Burk double reciprocal mapping method, and obtaining the inhibition type and inhibition mechanism of the inhibitor on tyrosinase activity.
To assess the type of tyrosinase inhibition by eleutheroside E and syringin, a Lineweaver-Burk double reciprocal mapping method was used. The linehaver-Burk equation for competitive inhibition kinetics analysis is as follows:
wherein V is the reaction rate, K m is the Michaelis constant of tyrosinase, V max is the maximum reaction rate, K i is the inhibition constant of inhibitor, [ S ] is the substrate L-dopa concentration, and [ I ] is the inhibitor concentration.
FIGS. 3A and 4A show the inhibition of tyrosinase by eleutheroside E and syringin (1.25. Mu.M, 2.5. Mu.M, 5. Mu.M, 10. Mu.M, 20. Mu.M) at different concentrations, both of which were found to exhibit a degree of dose dependence with IC 50 values of 11.13.+ -. 0.50 and 15.41.+ -. 0.22. Mu.M, respectively, when L-dopa was used as substrate. Wherein the inhibition rate of eleutheroside E is 34.12+ -0.23% at 1.25 μm and 51.53 + -0.08% at 20 μm. The syringin concentration is increased from 1.25 to 20 mu M, the inhibition rate is increased from 10.36+/-2.15% to 55.03+/-4.83%, and the concentration dependence is shown.
As can be seen from fig. 3B and 4B, the straight lines each pass through the far point of the coordinate axis. And the slope of the straight line is reduced along with the increasing concentration of the added eleutheroside E and the syringin along with the increasing of the enzyme activity, so that the inhibition effect of the eleutheroside E and the syringin on tyrosinase is proved to be a reversible process.
As shown in FIGS. 3C and 4C, the concentration of the immobilized enzyme in the living system was changed to change the concentration of the substrate L-dopa, and the effect of different concentrations of eleutheroside E and syringin (20. Mu.M, 10. Mu.M, 5. Mu.M, 2.5. Mu.M, 1.25. Mu.M) on the enzyme activity was measured. The intersection of the lines can be seen in the graph at the y-axis, with no change in V max values for both K m values, indicating that both eleutheroside E and syringin are typical competitive inhibitors. The K i values are 0.364 and 0.591 respectively, which shows that the binding affinity of the acanthopanaxoside E is better than that of the syringin.
It can also be derived that syringin reacts faster than eleutheroside E to tyrosinase inhibition but that eleutheroside E is slightly better than syringin in terms of binding affinity to enzymes. This conclusion can be made available for later investigation.
Application example 1
A preparation method of strippable paste mask gel containing acanthopanax ethanol extract specifically comprises the following steps:
sterile deoxidized water 56.6% and polyvinyl alcohol 15% are heated to 90 ℃ together, and are stirred slowly (60 rpm) during the period, glycerol 5% is added after the polyvinyl alcohol is completely swelled, and the mixture is fully and uniformly stirred and cooled to 50 ℃; mixing radix Acanthopanacis Senticosi ethanol extract 3%, tween-80.4%, and sterile deoxygenated water 20%, slowly adding cooled polyvinyl alcohol-glycerol water solution, and stirring; then degassing, and filtering by using a 220-mesh pipeline filter after degassing; sterilizing by gamma-ray irradiation, and then aseptic canning to obtain the finished product.
Claims (3)
1. The application of the acanthopanax extract in preparing tyrosinase inhibitor products is characterized in that: the acanthopanax root extract is obtained by the following method: mixing acanthopanax fruit powder with ethanol water solution with a certain concentration, and performing ultrasonic treatment for 180-250 min to obtain an extracting solution; filtering the obtained extracting solution, performing rotary evaporation at 40-55 ℃ to remove ethanol in the extracting solution to obtain a crude acanthopanax ethanol extract, and drying to obtain the acanthopanax ethanol extract, wherein the volume fraction of ethanol in the ethanol aqueous solution is 30-80%; the mass-volume ratio of the acanthopanax fruit powder to the ethanol water solution is 1 g:10 mL~1 g:50 mL;
The inhibition rate IC 50 values of the main active components of the acanthopanax extract, namely the acanthopanaxoside E and the syringin, on tyrosinase are respectively 11.13+/-0.50 mu M and 15.41+/-0.22 mu M, the concentration of the acanthopanaxoside E and the syringin are respectively 20 mu M, and the inhibition rates are respectively 51.53 +/-0.01% and 55.03+/-3.38%; and the results of tyrosinase kinetics experiments show that the acanthopanax glycoside E and the syringin have reversible competitive inhibition reaction on tyrosinase.
2. The use according to claim 1, characterized in that: the drying step is as follows: and (3) performing vacuum drying or low-temperature freeze drying on the obtained acanthopanax coarse extract to obtain an acanthopanax ethanol extract.
3. The use according to claim 1, characterized in that: when L-dopa and L-tyrosine are used as substrates, tyrosinase activity is obviously inhibited by the acanthopanax ethanol extract in a concentration-dependent manner, and when the tyrosinase activity is reduced by half, the concentration IC 50 of the acanthopanax ethanol extract is respectively 1.77+/-0.96 mg/ml and 1.86+/-0.75 mg/ml; the inhibition rates of the acanthopanax ethanol extract on tyrosinase at different concentrations of 1 mg/ml, 2.5 mg/ml, 5 mg/ml and 7.5 mg/ml are 34.51+/-2.05% and 40.86 +/-0.03%, 55.31 +/-0.6% and 40.38+/-2.84%, 84.33+/-2.71% and 88.03 +/-0.78%, 90.47+/-0.87% and 94.87+/-0.30% respectively when the L-dopa and the L-tyrosine are used as substrates.
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| CN103948529A (en) * | 2014-01-26 | 2014-07-30 | 广州丹奇日用化工厂有限公司 | Cosmetic combination containing tomato pulp extract |
| KR20220031274A (en) * | 2020-09-04 | 2022-03-11 | 주식회사 코씨드바이오팜 | Cosmetic Composition for Skin Whitening Containing Eleutheroside E As Active Ingredient |
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| CN102600221A (en) * | 2012-04-20 | 2012-07-25 | 苏州大学 | Preparation method of acanthopanax root extract |
| CN111789785A (en) * | 2020-08-11 | 2020-10-20 | 陈阳东 | Plant extract for inhibiting tyrosinase activity, preparation method and application thereof in cosmetics |
| CN112998106A (en) * | 2021-03-15 | 2021-06-22 | 国健药业(深圳)集团有限公司 | Compound health tea and preparation method thereof |
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| CN103948529A (en) * | 2014-01-26 | 2014-07-30 | 广州丹奇日用化工厂有限公司 | Cosmetic combination containing tomato pulp extract |
| KR20220031274A (en) * | 2020-09-04 | 2022-03-11 | 주식회사 코씨드바이오팜 | Cosmetic Composition for Skin Whitening Containing Eleutheroside E As Active Ingredient |
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