JPH0826960A - Cosmetic - Google Patents

Abstract

PURPOSE:To obtain a cosmetic containing the solvent extract of Cassia auriculata, high in a beautifully whitening effect, inhibiting the activity of hyaluronidase, strong in a collagenase activity-inhibiting action, and effective for skin roughness, etc. CONSTITUTION:The small leaves and barks of a plant of the genus Kawara ketsumei, Cassia auriculata, is extracted with water or a hydrophilic organic solvent (e.g. ethanol). The extract is suitably compounded with other cosmetic raw materials, prepared in the forms of lotions, creams, emulsions or packs, and subsequently used. The Cassia auriculata has a skin-beautifully whitening action, a hyaluronidase activity-inhibiting action, an active oxygen-inhibiting action, an antioxidizing action, an antiplasmin action, a collagenase activity- inhibiting action, etc. The cosmetic is stronger in the above-mentioned actions than those of cosmetics containing other plants of the genus Kawara ketsumei, and is effective for the beautiful whitening of skins, skin roughness, skin luster and skin tension.

Description

Detailed Description of the Invention

[0001]

BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a cosmetic composition which has a high whitening effect, inhibits the activity of hyaluronidase, has a strong inhibitory effect on collagenase activity, and is effective for rough skin.

[0002]

[Prior Art] Cassia Auriculator (scientific name: Ca
ssia auriculata) is a plant belonging to the genus Kawaraketsumei (Kawahara Kyomei), distributed in the arid regions of Sri Lanka, India, and its leaves are used as laxatives. In Africa, bark is used to treat rheumatism, eye diseases, gonorrhea, purulent conjunctivitis, and gout.

Regarding the plant of the genus Kawaratsukitsume, the inventors of the present invention have disclosed a whitening effect in JP-A-6-87731.
It was reported that it has a strong anti-oxidant effect and has an effect of preventing rough skin, and is optimal as a raw material for cosmetics.

On the other hand, collagen is also called collagen and is a protein that constitutes connective tissue of animal cells and is widely distributed in the living body. It is considered to exist in multicellular animals, and at least 11 kinds of molecules have been discovered to date, and these genes have different genes from each other.

Collagen, which is the main component of the skeletal structure, has a platelet aggregation action and is also involved in thrombus formation. It has also been suggested that collagen is involved in liver cirrhosis and arteriosclerosis.

Collagenase is an enzyme produced by animal tissue cells, inflammatory cells, tumor cells, etc., which decomposes type I, type II and type III collagen. Elucidation of proteins that inhibit collagen degradation
h) is a metalloprotease inhibitor protein (TIMP)
The gene was isolated from human tissue and successfully cloned. Metalloprotease is an enzyme that decomposes collagen (a kind of collagenase), and TIMP inhibits the activity of this enzyme. This TIMP is expected to be an effective therapeutic drug for arthritis, cancer, and skin lesions.

The collagenase inhibitor refers to a substance that inhibits the activity of collagenase as described above. In the process of tissue destruction and repair during pathology, abnormalities in collagenase activity are observed. These conditions include rheumatoid arthritis,
There are periodontitis, corneal ulcer, congenital epidermolysis bullosa, etc. Therefore, it is considered that the collagenase inhibitor prevents or cures the deterioration of these pathological conditions by inhibiting the collagenase activity.

As a conventional technique relating to a collagenase inhibitor, JP-A-1-222782 discloses a collagenase inhibitor characterized in that a solution of a collagenase inhibitor is brought into contact with a red dye-binding carrier or a blue dye-binding carrier to elute the collagenase inhibitor solution. A law has been proposed. This is just a method for purifying collagenase inhibitors.

Further, in Japanese Patent Laid-Open No. 3-44331,
A collagenase inhibitor comprising an extract extracted from cacao husk, which is a soybean hull of cocoa beans, is disclosed. In terms of a collagenase inhibitor consisting of an extract extracted from a natural product, there is a part common to the present invention,
Clearly, the natural product itself is quite different.

Further, Japanese Patent Publication No. 2-502537 discloses a synthetic inhibitor of mammalian collagenase. This is to prevent the synthesis of collagenase in the mammalian body and is a thiol-containing peptide, which is different from the present invention in that it is a synthetic product.

On the other hand, various substances are known as substances having a whitening effect which can be used as a raw material for cosmetics, but synthetic products have no guarantee of safety when applied to human skin for a long period of time. , Its use is being limited. In addition, many natural products have a weak whitening effect. However, from the viewpoint of safety for human skin, it is a natural product, and people eat it for many years,
Guaranteed in terms of safety and strong whitening effect,
Furthermore, a substance that also has other effects on the skin has been desired.

[0012]

DISCLOSURE OF THE INVENTION The object of the present invention is that it is safe to be applied to the skin, has a large whitening effect and inhibits the activity of hyaluronidase, has a strong inhibitory effect on collagenase activity, and is effective for rough skin and the like. To provide cosmetics containing ingredients.

[0013]

[Means for Solving the Problems] In order to solve the above-mentioned problems, the present inventors have screened and investigated plants that have been used for food for many years and have been confirmed to be safe for the human body. I examined what is useful as. As a result, they have found that Cassia auriculata (scientific name: Cassia auriculata) is effective as a raw material for cosmetics or as a quasi drug, and thus completed the present invention. That is, the cosmetic of the present invention is a cassia auriculator (scientific name: Cassia aur
iculata) solvent extract.

In the present invention, the above-mentioned Cassia auriculator is disclosed in Japanese Patent Application Laid-Open No. 6-87 filed by the present inventors.
Although it is a plant included in the genus Kawarakeimei described in Japanese Patent No. 731, the cosmetic of the present invention is a cosmetic using a plant of the genus Kawarakeimei such as Yamabiso, Nanbansai Kachi described in the above-mentioned prior application. In comparison, it has a very strong whitening effect, and a remarkable effect such as an active oxygen suppressive effect, a hyaluronidase activity inhibitory effect, an antiplasmin effect and the like, and a novel collagenase activity inhibitory effect, and this The Cassia auriculator is not described or illustrated in the above-mentioned prior application.

[0015]

[Action] The confirmed action of the solvent extract of Cassia auriculata (scientific name: Cassia auriculata) used as the cosmetics of the present invention is to whiten skin, suppress hyaluronidase activity, suppress active oxygen, and antioxidative effect. , Antiplasmin action and collagenase activity inhibition action. The activity suppressing effect of the hyaluronidase will be described in more detail. Hyaluronidase is widely distributed in the living body,
It is an enzyme that is also present in the skin, and as its name implies, it decomposes hyaluronic acid. Hyaluronic acid is a linear polymer polysaccharide in which β-D-N-acetylglucosamine and β-D-glucuronic acid are alternately bound, and is a glycosaminoglucan that widely exists in connective tissues of mammals along with chondroitin sulfate and the like. Is a kind of. The action of hyaluronic acid in connective tissue is to retain water in the intercellular spaces, form a jelly-like matrix in the tissue to retain cells,
It is thought to maintain the lubricity and flexibility of the skin and prevent external forces (mechanical damage) and bacterial infections. In addition, it is said that hyaluronic acid in the skin decreases with age, resulting in aging such as wrinkles and bulkiness. Therefore, suppressing the activity of hyaluronidase that decomposes this hyaluronic acid, the stability of hyaluronic acid used in the formulation, the hyaluronic acid of the formulation after application to the skin and the hyaluronic acid present in the skin It is thought to contribute to stability.

Further, the action of suppressing the active oxygen will be described in more detail. Generally, no organisms (except anaerobic ones) can exist without oxygen in the air. However, oxygen becomes active oxygen under the influence of ultraviolet rays and enzymes. This active oxygen oxidizes a fatty acid and produces a peroxide. It also oxidizes and damages the phospholipids of biological membranes in the body. Furthermore, it is said that the generated peroxide and active oxygen damage DNA and accelerate aging. This active oxygen is
It also affects the mechanism of melanin production from tyrosine and is involved in skin darkening. Suppressing this active oxygen is an important factor for the skin, in other words, an important factor required for cosmetics.

The antiplasmin action will be described in more detail. Normally, erythema and edema are formed by irradiating the skin with ultraviolet rays (UVB) in an amount twice the minimum amount of erythema.
It has been reported that histamine, serotonin, prostaglandin E ₂ , F _2α quinine and the like are involved as chemical mediators in this UV inflammatory reaction. In addition, after UV irradiation, the plasmin activity in rabbit skin tissues was enhanced, the plasmin activity varied well in parallel with the degree of swelling of the skin, and the administration of the antiplasmin agent tranexamic acid caused swelling of the skin. Is known to be severely suppressed. Therefore, the antiplasmin agent is also one of the important chemical mediators in the UV inflammatory reaction, and suppressing this plasmin is an important factor for the skin, in other words, an important factor required for cosmetics.

Furthermore, the collagenase activity inhibitory action will be explained. As described above, tissue destruction during pathological conditions,
Since abnormalities in collagenase activity are observed in the repair process, inhibition of this collagenase activity is important for the skin, in other words, an important factor required for cosmetics.

The details of the present invention will be described below.
In the present invention, Cassia auriculator (scientific name:
Cassia auriculata) can be used by extraction with water or a hydrophilic organic solvent such as ethanol, methanol or acetone. However, it is natural that extraction with water, ethanol, or a mixed solvent thereof is preferable because it is extraction of cosmetic raw materials. In some cases, a polyhydric alcohol such as glycerin, 1,3-butylene glycol, propylene glycol or a mixed liquid of polyhydric alcohol and water can be used for extraction. Furthermore, freeze-drying and using it as a powder is also effective depending on the method of use.

In the cosmetic of the present invention, this solvent extract is used as another cosmetic raw material, for example, liquid oil such as squalane and jojoba oil, solid oil such as beeswax and cetyl alcohol, various activators, glycerin, 1,3. -Cosmetics of various dosage forms can be prepared by adding moisturizing agents such as butylene glycol and various agents. For example, a lotion, a cream, a milky lotion, a pack or the like can be prepared into cosmetics of various usage forms according to the purpose.

[0021]

[Examples] Hereinafter, production examples of an extract of Cassia auriculata (scientific name: Cassia auriculata) used in the present invention and examples of actual utilization are described, but the present invention describes these production examples and It is not limited in any way by the embodiment.

[Production Example 1] 300 g of ethanol was added to 10 g of small leaves (dried product) of Cassia auriculator, and the mixture was left for 5 days with occasional stirring. This was filtered and freeze-dried.

[Production Example 2] 10 g of leaflets (dried product) of Cassia auriculator were added to 30 g of 50% ethanol aqueous solution.
0 ml was added and left for 5 days with occasional stirring. This was filtered and freeze-dried.

[Production Example 3] Purified water (300 ml) was added to 10 g of leaflets (dried product) of Cassia auriculator and heated for 3 hours. This was allowed to cool, then filtered and freeze-dried.

[Production Example 4] 300 g of ethanol was added to 10 g of bark (dry product) of Cassia auriculator, and the mixture was left for 5 days with occasional stirring. This was filtered and freeze-dried.

[Production Example 5] Cask auriculator bark (dry product) 10 g, 50% ethanol aqueous solution 30
0 ml was added and left for 5 days with occasional stirring. This was filtered and freeze-dried.

[Production Example 6] To 10 g of bark (dried product) of Cassia auricator, 300 ml of purified water was added and heated for 3 hours. This was allowed to cool, then filtered and freeze-dried.

[Example 1 (Preparation of lotion)] The following ingredients were mixed to prepare a lotion by a conventional method. (% By weight) Olive oil 0.5 Ethanol extract of Cassia auriculator from Production Example 0.3 Polyoxyethylene (20 E.O.) sorbitan monostearate 2.0 Polyoxyethylene (60 E.O.) hydrogenated castor Oil 2.0 Ethanol 10.0 1.0% sodium hyaluronate aqueous solution 5.0 Purified water 80.2

[Example 2 (Preparation of cream)] A and B each consisting of the following components were heated to 70 ° C, and then A was slowly added to B with stirring and then slowly stirred. While cooling to 30 ° C, a cream was prepared. (Wt%) A squalane 20.0 Olive oil 2.0 Mink oil 1.0 Jojoba oil 5.0 Beeswax 5.0 Cetostearyl alcohol 2.0 Glycerin monostearate 1.0 Sorbitan monostearate 2.0 Production example 2 Cassia auriculator 50% ethanol extract 0.5 B Purified water 48.4 Polyoxyethylene (20 E.O.) sorbitan monostearate 2.0 Polyoxyethylene (60 E.O.) hydrogenated castor oil 1. 0 Glycerin 5.0 1.0% aqueous sodium hyaluronate solution 5.0 Methyl paraoxybenzoate 0.1

[Example 3 (Preparation of lotion)] The extract of Production Example 1 in Example 1 was replaced with the extract of Production Example 3 to prepare.

Example 4 (Preparation of Cream) Example 2
Was prepared by replacing the extract of Production Example 1 with the extract of Production Example 4.

[Example 5 (Preparation of lotion)] The extract of Production Example 1 in Example 1 was replaced with the extract of Production Example 5 to prepare.

Example 6 (Preparation of Cream) Example 2
Was prepared by replacing the extract of Production Example 1 with the extract of Production Example 6.

[Inhibition of Tyrosinase Activity] (Test Method) Mcllvaln Buffer Solution 0.9 m
l, 1.66 mM Tyrosine solution 1.0 ml, 0.01 wt / v% aqueous solution of each of the above production examples (freeze-dried product) (if it is difficult to dissolve, add ethanol to dissolve it, then add purified water and evaporate After removing the ethanol,
1.0 ml (prepared to be 0.01 wt / v%) was placed in a screw vial and heated in a 37 ° C. constant temperature water bath for 5 minutes or more. 0.1 ml of a tyrosinase solution (Sigma, mushroom-derived, 914 units / ml) was added, and the mixture was kept warm in a constant temperature water bath at 37 ° C., and after 10 minutes, the absorbance was measured at 475 nm. As a control, pure water was added instead of the sample solution, and the measurement was performed in the same manner. In this test, the final concentration of the sample is 0.0033.
%. (Calculation formula) Tyrosinase activity inhibition rate (%) = {B- (AP)} /
B × 100 However, A: Absorbance of sample specimen B: Absorbance of control P: Absorbance due to coloring of sample specimen (3-fold dilution)

As a production comparative example, Japanese Patent Laid-Open No. 6-87.
No. 731 publication, Nanbansai Kachi of the genus Kawarakeimei, Yamaboshi (Kawara Ketsumei, Scientific name: Cassia nomam
The following is the one from the whole plant of e). [Production Comparative Example 1] 300 g of 50% aqueous methanol solution was added to 10 g of Nanbansai Kachi (dry product) and left for 5 days with occasional stirring. This was filtered and freeze-dried.

[Production Comparative Example 2] Yamaboso (dry product) 10 g
Add 300 ml of ethanol aqueous solution to 5 while stirring occasionally.
Left for days. This was filtered, evaporated and freeze-dried.

[Manufacturing Comparative Example 3] Yamabiso (dry product) 10 g
To the solution was added 300 ml of 50% aqueous ethanol solution and the mixture was left for 5 days with occasional stirring. This is filtered and then evaporated,
Lyophilized. The above Production Comparative Examples 1 to 3 were tested by the above-described test method for inhibiting tyrosinase activity. Production Example 1 above
~ 6, the results of tyrosinase activity inhibition of Production Comparative Examples 1 to 3 are shown in Table 1 below.

[0038]

[Table 1]

As is clear from the results shown in Table 1 above, Production Examples 1 to 6, which are extracts of the Cassia auriculator used in the present invention, are the mosquitoes of the genus Kawara Keimei described in JP-A-6-87731. It was revealed that the tyrosinase activity inhibitory action was remarkably higher than that of Production Comparative Examples 1 to 3 which were extracts of Yamaboso, and the difference between the two was remarkable.

[Hyaluronidase activity inhibition test] (Test method) 0.4% sodium hyaluronate 0.1M
(PH 6.0) 6 g of phosphate buffer solution was weighed and allowed to stand in a 37 ° C. constant temperature water bath for 5 minutes, and then 0.1 wt / v% aqueous solution of the above production example (lyophilized product) In addition, after dissolving, purified water was added to the solution to evaporate it, and ethanol was removed. Then, the solution was adjusted to 0.1 wt / v%. 1.0 ml was added and stirred, and 0.01% hyaluronidase (manufactured by Sigma) Made of testicles, type I-S)
1 ml of 0.1 M (pH 6.0) phosphate buffer was added and immediately stirred, and 6 ml was placed in an Ostwald viscometer placed in a 37 ° C. constant temperature water bath. The viscosity was measured after 1 minute, 5 minutes, 10 minutes, 20 minutes, and 40 minutes. Further, as a control, pure water was added instead of the sample solution, and the same measurement was performed. In this test, the final concentration of each sample is 0.0125% of the concentration of the analyte. The viscosity after 1 minute is 100
The respective results are shown in Tables 2 and 3 below.

[0041]

[Table 2]

[0042]

[Table 3]

[Active Oxygen Suppression Test] There are various methods for measuring the effect of suppressing active oxygen, but the following method was used this time. pH 7.8 50 mM potassium phosphate buffer (containing 1.3 mM DETAPAC) 133 ml 40 unit / ml potassium phosphate buffer above 5 ml of catalase 5 ml 2 mM potassium phosphate buffer above nitroblue tetrazolium 5 ml 1.8 mM xanthine above phosphate Potassium buffer 17 ml 160 ml

2.4 ml of the above mixture of reagents and 0.3 ml of the sample
In addition, a solution of xanthine oxynase (prepared with water as a sample in advance and adjusted with the above-mentioned potassium phosphate buffer solution so that the absorbance increases by about 0.02 per minute) is used.
Add 1 ml and measure the absorbance (560 nm) immediately (measurement is 2
Quantile and confirm linearity). (Calculation formula) Inhibition rate = {(A−B) / A} × 100 where A: change in absorbance per minute when the sample is water B: change in absorbance per minute of sample Several steps were carried out to find the 50% active oxygen production inhibitory concentration. The preparation method of the sample is the above manufacturing example (freeze-dried product)
An aqueous solution having an appropriate concentration was prepared (if it is difficult to dissolve, ethanol was added to dissolve it, and purified water was added to the solution to evaporate it to remove ethanol, and then an appropriate concentration was prepared). The results are shown in Table 4 below.

[0045]

[Table 4]

[Antioxidant Test] The following 50 ml test tube with a screw cap was prepared. Specimen 5 mg 2% linoleic acid ethanol solution 10 ml 0.1 M, pH 7.0 phosphate buffer 10 ml Purified water 5 ml This 50 ml test tube with a screw cap was left in a thermostat bath at 50 ° C in the dark. Before putting this in a constant temperature bath, 3 days later, 6
The following measurements were made after 10 days. Test solution 0.125
ml, 75% ethanol 12.125 ml, 30% ammonium thiocyanate 0.125 ml, and the mixture is stirred.
After standing for 3 minutes, 0.125 ml of 0.02N ferrous chloride 3.5% HCL aqueous solution is added and stirred, and after standing for 3 minutes, 500
Absorbance was measured in nm. The cell length was 10 mm, and the control cell had the test solution replaced with water. The results are shown in Table 5 below.

[0047]

[Table 5]

As is clear from the results shown in Table 5, it was found that the antioxidant activity is higher than that of vitamin E currently used as an antioxidant.

[Antiplasmin test] (Test method) 4 ml of a plasminogen-removing fibrinogen type 2-0.6% aqueous solution was placed in a 9 cm Petri dish, and 4 ml of 0.1 M phosphate buffer of pH 7.4 was added and stirred. 0.1 ml of thrombin (10 units / ml) was added dropwise, mixed gently and left for 30 minutes. Fibrinogen was converted to fibrin by the addition of thrombin and formed a gel. 30 μl of a mixture of 0.1 ml sample and 0.1 ml plasmin solution (10 units / ml)
Was placed on the gel of a petri dish and left at 37 ° C. for 2 hours. Then, the dissolved area of fibrinogen was measured. In addition, the same experiment was performed using water instead of the sample, and the inhibition rate of the brasmin activity was calculated by the following formula.

[0050]

[Equation 1]

When tranexamic acid and ε-aminocaproic acid were tested as positive controls, 50% inhibitory concentration was 30 mg / ml of tranexamic acid and 40 ε-aminocaproic acid.
It was mg / ml. Table 6 shows the results.

[0052]

[Table 6]

[Collagenase Inhibition Test] (Test Method) Type I Collagenase Activity Measurement Kid YU-1
Experiments were performed using 6001 Cosmo Bio. That is, fluorescence labeled type I collagen (50 μm
g / 50 μl / tube) and reagents, samples, etc. were added as shown in Table 7 below. Here, the neutralization solution, enzyme reaction terminator, collagenase solution, and TOTAL blank in Table 7 below
It is as follows. The neutralizing solution is a 0.1 M tris (oxymethyl) aminomethane (abbreviation Tris) -hydrochloric acid buffer solution having a pH of 7.5, 0.4 M NaCl, 0.01
It contains M CaCl ₂ and NaN ₃ (sodium azide).
The enzyme reaction terminator is an O-phenanthrone (containing ethanol) solution. The collagenase solution is a 1 unit / ml, 2-fold diluted neutralizing solution of collagenase (1000 unit / mg manufactured by Amano). The TOTAL blank is used to check the correctness of the test method when the concentration of the collagenase solution is too high.

[0054]

[Table 7]

Then, the collagenase activity inhibition rate was determined by the following formula. The results are shown in Table 8 below.

[0056]

[Equation 2]

[0057]

[Table 8]

(Use test) The face of 9 females was divided into right and left, the lotion and cream of the example were set on one side, and the lotion and cream of the comparative example were set on the other side and used once or more daily. After three months,
The whitening, the prevention of rough skin, the gloss of the skin and the suppleness of the skin were evaluated. In the comparative example, the extract of various Cassia auriculators in the production examples from the examples was replaced with water (Comparative Examples 1 and 2). In addition, 27 people were divided into 3 groups and tested using the samples shown in Table 9 below.

[0059]

[Table 9]

The evaluation was made according to the following evaluation criteria, and the results are summarized in Table 10 below. (Evaluation Criteria) The Example is Better 3 The Example is Better 2 The Example is Better 1 No Difference 0 The Comparative Example Better -1 The Comparative Example Better- 2 The comparative example is much better -3

[0061]

[Table 10]

Results of tyrosinase activity inhibition test (Table 1), hyaluronidase activity inhibition test results (Tables 2 and 3), active oxygen inhibition test results (Table 4), antioxidant test results (Table 5), antiplasmin test As is clear from the results (Table 6), the collagenase inhibition test results (Table 8), and the use test (Table 10), the cosmetics containing the solvent extract of Cassia auriculator of the present invention were found to have tyrosinase activity and hyaluronidase. It was found that it inhibits the activity and the active oxygen of Escherichia coli and the inhibition of antiplasmin and collagenase is remarkably high, and is effective for whitening, prevention of rough skin, skin radiance and skin firmness.

[0063]

INDUSTRIAL APPLICABILITY According to the present invention, compared to other cosmetics made from the genus Kawaretsutsumei, it has not only a strong whitening effect, but also an active oxygen suppressing effect, an antioxidant effect, a hyaluronidase activity inhibiting effect, and an antiplasmin effect A cosmetic having a strong collagenase activity-inhibiting effect and effective against rough skin is provided.

 ─────────────────────────────────────────────────── ─── Continuation of the front page (72) Kenji Shimomura 3-16-32 Funae, Ise City, Mie Prefecture (72) Koichi Iida 56-1 Kurose-cho, Ise City, Mie Prefecture

Claims (1)

[Claims] 1. A Cassia auriculator (Cassia a
cosmetics containing a solvent extract of uriculata).