A whitening and spot-lightening recombinant collagen cosmetic composition and preparation method thereof

Abstract

The present invention relates to the technical field of cosmetics, and provides a whitening and freckle-removing recombinant collagen cosmetic composition and a preparation method. The components of the cosmetic composition include modified recombinant collagen, glutathione, glycerol, water, vegetable oil, emulsifier, thickener, and preservative. The present invention prepares modified recombinant collagen by introducing butylthionone structure and benzimidazole structure into the peptide chain of recombinant collagen. After adding cosmetics, it can not only accurately promote the transdermal penetration of collagen, but also improve the binding ability of collagen with the copper ion active center of tyrosinase, thereby significantly improving the inhibitory effect of collagen on tyrosinase activity, significantly reducing melanin production, and giving the cosmetic composition better whitening and freckle-removing effect.

Description

Technical Field

[0001] The invention relates to the technical field of cosmetics, and provides a recombinant collagen cosmetic composition for whitening and lightening spots and a preparation method thereof. Background Art

[0002] Skin whitening and spot removal can be achieved through the following approaches: (1) inhibiting tyrosinase activity, thereby inhibiting the formation of melanin; (2) inhibiting the proliferation of melanocytes and reducing the production of melanin; (3) anti-oxidation, removing oxygen free radicals, and maintaining normal skin metabolism; (4) improving skin blood circulation, removing harmful substances in a timely manner, and dissipating pigments. Among them, inhibiting tyrosinase activity is the most direct, simple, and commonly used method.

[0003] Tyrosinase is a key enzyme in the synthesis of melanin. It is a copper-containing oxidoreductase that can catalyze the conversion of L-tyrosine to L-DOPA and L-DOPA to dopaquinone, so it has dual activity of monophenolase and diphenolase. There are several mechanisms of action of tyrosinase inhibitors: the inhibitor binds to the binuclear copper ion active site of the enzyme, thereby inhibiting the binding of the substrate to the active site; the inhibitor acts on the amino acid residues outside the active center of the enzyme, changing the conformation of the enzyme, thereby reducing the enzyme activity; the inhibitor complexes with the enzyme-substrate and undergoes a slow reversible isomerization process.

[0004] Glutathione is a tripeptide containing γ-amide bonds and sulfhydryl groups, composed of glutamic acid, cysteine ​​and glycine. It can bind to the copper ion in the active center of tyrosinase through carboxyl groups, sulfhydryl groups, etc., thereby inhibiting the binding of substrates to the active sites. Therefore, glutathione can be added to cosmetics as a tyrosinase inhibitor, giving cosmetics the effect of whitening and lightening spots. However, glutathione may cause allergies to sensitive skin, and it has some odor itself, so the amount added is usually low, and it needs to be used in combination with other tyrosinase inhibitors to achieve the ideal whitening and lightening effect.

[0005] Recombinant collagen has good biocompatibility and safety. It can use the groups on the amino acids to bind to the copper ions in the active center of tyrosinase, thereby inhibiting the activity of tyrosinase. However, collagen's ability to bind to copper ions is worse than glutathione. In addition, collagen has a larger molecular weight than glutathione, and its transdermal penetration process is slower. It cannot contact the tyrosinase located in the basal layer of the skin in time. Therefore, the whitening and freckle-removing effect of collagen on the skin is not obvious enough. Summary of the invention

[0006] In view of the above situation, the present invention proposes a recombinant collagen cosmetic composition for whitening and lightening spots and a preparation method, which combines recombinant collagen with glutathione, and introduces a butylthione structure and a benzimidazole structure into the peptide chain of the recombinant collagen, which can enhance the inhibitory effect on the activity of tyrosinase and enhance the whitening and lightening effect of the cosmetic.

[0007] The specific technical solutions involved in the present invention are as follows:

[0008] Firstly, the present invention provides a recombinant collagen cosmetic composition for whitening and lightening spots, wherein the components of the cosmetic composition include modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative.

[0009] in:

[0010] The vegetable oil is preferably at least one of shea butter, almond oil and avocado oil.

[0011] The emulsifier is preferably at least one of polysorbate, glyceryl stearate and ricinoleamide.

[0012] The thickener is preferably at least one of xanthan gum and carbomer.

[0013] The preservative is preferably at least one of methylparaben, ethylparaben and propylparaben.

[0014] Regarding the distribution ratio of each component, preferably, the mass ratio of modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative is 2-6: 0.5-1: 4-8: 80-90: 6-8: 2-3: 0.1-0.2: 0.05-0.2.

[0015] Furthermore, the preparation process of the modified recombinant collagen is as follows:

[0016] (1) Add 4-(4-bromobutyloxy)benzaldehyde and octanoic acid to ethanol, heat to 45-55°C, then add recombinant collagen, stir and reflux for 1-2 hours, filter, wash repeatedly with ethanol, and vacuum dry to obtain recombinant collagen A;

[0017] (2) Mix o-phenylenediamine and phosphoric acid, heat to 100-105°C, add recombinant collagen A, stir and reflux for 1.5-2.5 hours, adjust the pH value to 8, filter, wash repeatedly with ethanol, and vacuum dry to obtain recombinant collagen B;

[0018] (3) Sodium sulphonylbenzoylmide and polyethylene glycol are added to acetonitrile, heated to 80-90°C, and then recombinant collagen B is added. The mixture is stirred and refluxed for 18-22 hours, filtered, repeatedly washed with ethanol, and vacuum dried to obtain modified recombinant collagen.

[0019] Preferably, the recombinant collagen in step (1) is recombinant type III humanized collagen with a molecular weight of 1000-3000 Daltons.

[0020] Preferably, the number average molecular weight of the polyethylene glycol in step (3) is 400-600.

[0021] Preferably, in step (1), the mass ratio of recombinant collagen, 4-(4-bromobutyloxy)benzaldehyde, caprylic acid and ethanol is 100:18-22:0.8-1.2:400-600.

[0022] Preferably, in step (2), the mass ratio of recombinant collagen A, o-phenylenediamine, and phosphoric acid is 100:8-10:120-150.

[0023] Preferably, in step (3), the mass ratio of recombinant collagen B, sodium o-sulfonylbenzoylmide, polyethylene glycol, and acetonitrile is 100:16-18:1.5-2:400-600.

[0024] It is well known that the peptide chain of collagen contains amino and carboxyl groups, which give it reactive activity and can be used as reaction sites for modification. In view of this, the present invention creatively modifies the recombinant collagen as follows: in the above step (1), octanoic acid is used as a catalyst to react the aldehyde group of 4-(4-bromobutyloxy)benzaldehyde with the amino group of the recombinant collagen to generate a Schiff base structure and convert -CH 2 CH 2 CH 2 CH 2 Br is introduced into the polypeptide chain of collagen. In the above step (2), phosphoric acid is used as a catalyst to react o-phenylenediamine with the carboxyl group of recombinant collagen to generate a benzimidazole structure. In the above step (3), polyethylene glycol is used as a catalyst to react sodium o-sulfonylbenzoimide (i.e. sodium saccharin) with -CH 2 CH 2 CH 2 CH 2 Br reaction is performed to generate an N-substituted benzisothiazolone structure (i.e., thiazone structure). That is, through the reaction of step (1) and step (3), a butylthiazone structure is introduced into the amino position of the recombinant collagen peptide chain; through the reaction of step (2), a benzimidazole structure is formed at the carboxyl position of the recombinant collagen peptide chain. The structure of the modified recombinant collagen prepared by the method of the present invention is as shown in the attached figure. Figure 1 shown.

[0025] The present invention also provides a method for preparing the above-mentioned recombinant collagen cosmetic composition for whitening and lightening spots, and the specific preparation process is as follows:

[0026] S1. Mix the vegetable oil and the emulsifier, and stir evenly at 70-80°C to obtain a mixture a;

[0027] S2. Add the thickener to the glycerol and stir to disperse, then add the modified recombinant collagen, glutathione and water, and stir evenly at 70-80° C. to obtain a mixture b;

[0028] S3. Add mixture a to mixture b, stir at high speed for 10-20 min at 70-80°C, cool to 40-50°C, add preservatives, stir at low speed for 2-5 min, and cool to room temperature.

[0029] In S3, the rotation speed of the high-speed stirring is preferably 2500-3500 rpm, and the rotation speed of the low-speed stirring is preferably 800-1200 rpm.

[0030] The modified recombinant collagen described above is used as a component of a cosmetic composition, which has the following advantages: first, a thiazolidine structure with a butyl chain connected to the N position is introduced into the peptide chain of the recombinant collagen through modification, and the structure can interact with the lipids between keratinocytes, destroy the tight structure of the bimolecular lipid layer of the stratum corneum, and reduce the orderliness of the lipid arrangement, thereby increasing the looseness of the structure and the fluidity of the lipids, making the stratum corneum barrier more permeable, which is conducive to promoting the recombinant collagen to penetrate into the basal layer of the skin, so as to contact with tyrosinase in time and play a role in inhibiting its activity in time; second, a benzimidazole structure is formed on the peptide chain of the recombinant collagen through modification. Since benzimidazole is easy to form coordination with metal ions, it can improve the binding ability of collagen with the copper ion in the active center of tyrosinase, thereby improving the inhibitory effect on tyrosinase activity and reducing the formation of melanin. It can be seen that through modification, on the one hand, the transdermal penetration ability of collagen is improved, and on the other hand, the binding ability of collagen with the copper ion active center is improved. Under the joint action of these two aspects, the inhibitory effect of collagen on the activity of tyrosinase can be significantly improved, thereby achieving better whitening and freckle-removing effects.

[0031] Further, compared with directly adding a penetration enhancer, the present invention introduces the structure that can play a penetration-promoting effect into the collagen peptide chain. Because the addition amount of the penetration enhancer is too high, it can damage the skin and reduce the immune barrier function of the skin, thus, a lower penetration enhancer addition amount should be used in cosmetics. When the penetration enhancer is directly added, a relatively small amount of penetration enhancer can only act at the position in contact with the skin, and the collagen component is not completely at these positions, so it has certain limitations in promoting the penetration of collagen. The thiol ketone structure is introduced into the collagen peptide chain, so that the penetration-promoting structure is connected with the collagen structure, and the penetration-promoting structure acts at which position of the skin, which can directly promote collagen to penetrate at this position, that is, the penetration-promoting structure can more accurately promote the transdermal penetration of collagen, so as to more timely and efficiently play the role of inhibiting tyrosinase activity, and realize further improving the whitening and spot-removing effect of cosmetics.

[0032] In summary, the present invention provides a recombinant collagen cosmetic composition for whitening and lightening spots and a preparation method thereof. Compared with the prior art, the present invention has the following beneficial effects: the present invention uses modified recombinant collagen in combination with glutathione as a tyrosinase inhibitor for cosmetics, and introduces a butylthionone structure and a benzimidazole structure into the peptide chain of the recombinant collagen, which can not only accurately promote the transdermal penetration of collagen, but also improve the binding ability of collagen to the copper ion active center of tyrosinase, thereby significantly improving the inhibitory effect of collagen on the activity of tyrosinase, reducing the production of melanin, and making the cosmetic composition have better whitening and lightening effects. BRIEF DESCRIPTION OF THE DRAWINGS

[0033] Figure 1 It is a schematic diagram of the structure of the modified recombinant collagen of the present invention. DETAILED DESCRIPTION

[0034] The present invention is further described in detail below through specific embodiments, but this should not be construed as limiting the scope of the present invention to the following examples. Without departing from the above-mentioned method concept of the present invention, various substitutions or changes made according to common technical knowledge and conventional means in the art should be included in the scope of the present invention.

[0035] Example 1

[0036] Preparation of modified recombinant collagen:

[0037] (1) Add 4-(4-bromobutyloxy)benzaldehyde and octanoic acid to ethanol, heat to 50°C, then add recombinant collagen, stir and reflux for 1.5 hours, filter, wash repeatedly with ethanol, and vacuum dry to obtain recombinant collagen A;

[0038] (2) Mix o-phenylenediamine and phosphoric acid, heat to 105°C, add recombinant collagen A, stir and reflux for 2 hours, adjust the pH value to 8, filter, wash repeatedly with ethanol, and vacuum dry to obtain recombinant collagen B;

[0039] (3) Sodium sulphonylbenzoylmide and polyethylene glycol (PEG400) are added to acetonitrile, heated to 85°C, and then recombinant collagen B is added. The mixture is stirred and refluxed for 20 hours, filtered, repeatedly washed with ethanol, and vacuum dried to obtain modified recombinant collagen.

[0040] Among them, the recombinant collagen is recombinant type III humanized collagen, purchased from Jibaikang Biotechnology Co., Ltd., and its molecular weight is 2250 Daltons after testing; 4-(4-bromobutoxy)benzaldehyde was purchased from Shanghai Haohong Biotechnology Co., Ltd.; other raw materials are all common commercially available products.

[0041] In step (1), the mass ratio of recombinant collagen, 4-(4-bromobutyloxy)benzaldehyde, caprylic acid and ethanol is 100:20:1:500;

[0042] In step (2), the mass ratio of recombinant collagen A, o-phenylenediamine, and phosphoric acid is 100:9:130;

[0043] In step (3), the mass ratio of recombinant collagen B, sodium phthalimide, polyethylene glycol, and acetonitrile is 100:17:1.7:500.

[0044] Preparation of cosmetic composition:

[0045] S1. Mix the vegetable oil and the emulsifier, and stir evenly at 78° C. to obtain a mixture a;

[0046] S2. Add the thickener to the glycerol and stir to disperse, then add the modified recombinant collagen, glutathione and water, and stir evenly at 78° C. to obtain a mixture b;

[0047] S3. Add mixture a to mixture b, stir at 2500 rpm for 20 min at 78°C, cool to 48°C, add preservatives, stir at 800 rpm for 5 min, and cool to room temperature.

[0048] Among them: the vegetable oil is shea butter; the emulsifier is ricinoleamide; the thickener is xanthan gum; and the preservative is methylparaben.

[0049] Raw material ratio: the mass ratio of modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative is 6:0.75:6:85:7:2.5:0.15:0.1.

[0050] Example 2

[0051] Preparation of modified recombinant collagen: same as Example 1.

[0052] Preparation of cosmetic composition:

[0053] S1. Mix the vegetable oil and the emulsifier, and stir evenly at 70° C. to obtain a mixture a;

[0054] S2. Add the thickener to the glycerol and stir to disperse, then add the modified recombinant collagen, glutathione and water, and stir evenly at 70° C. to obtain a mixture b;

[0055] S3. Add mixture a to mixture b, stir at 3500 rpm for 10 min at 70°C, cool to 40°C, add preservatives, stir at 1200 rpm for 2 min, and cool to room temperature.

[0056] Among them: the vegetable oil is almond oil; the emulsifier is polysorbate; the thickener is carbomer 940; and the preservative is ethylparaben.

[0057] Raw material ratio: The mass ratio of modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative is 5:0.75:6:85:7:2.5:0.15:0.1.

[0058] Example 3

[0059] Preparation of modified recombinant collagen: same as Example 1.

[0060] Preparation of cosmetic composition:

[0061] S1. Mix the vegetable oil and the emulsifier, and stir evenly at 80° C. to obtain a mixture a;

[0062] S2. Add the thickener to the glycerol and stir to disperse, then add the modified recombinant collagen, glutathione and water, and stir evenly at 80° C. to obtain a mixture b;

[0063] S3. Add mixture a to mixture b, stir at high speed at 3100 rpm for 13 min at 80°C, cool to 50°C, add preservatives, stir at low speed at 1100 rpm for 3 min, and cool to room temperature.

[0064] Among them: the vegetable oil is shea butter; the emulsifier is ricinoleamide; the thickener is xanthan gum; and the preservative is propylparaben.

[0065] Raw material ratio: The mass ratio of modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative is 4:0.75:6:85:7:2.5:0.15:0.1.

[0066] Example 4

[0067] Preparation of modified recombinant collagen: same as Example 1.

[0068] Preparation of cosmetic composition:

[0069] S1. Mix the vegetable oil and the emulsifier, and stir evenly at 72° C. to obtain a mixture a;

[0070] S2. Add the thickener to the glycerol and stir to disperse, then add the modified recombinant collagen, glutathione and water, and stir evenly at 72° C. to obtain a mixture b;

[0071] S3. Add mixture a to mixture b, stir at 2600 rpm for 20 min at 72°C, cool to 42°C, add preservatives, stir at 900 rpm for 5 min, and cool to room temperature.

[0072] Among them: the vegetable oil is almond oil; the emulsifier is glyceryl stearate; the thickener is carbomer 940; and the preservative is methylparaben.

[0073] Raw material ratio: The mass ratio of modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative is 3:0.75:6:85:7:2.5:0.15:0.1.

[0074] Example 5

[0075] Preparation of modified recombinant collagen: same as Example 1.

[0076] Preparation of cosmetic composition:

[0077] S1. Mix the vegetable oil and the emulsifier, and stir evenly at 75° C. to obtain a mixture a;

[0078] S2. Add the thickener to the glycerol and stir to disperse, then add the modified recombinant collagen, glutathione and water, and stir evenly at 75° C. to obtain a mixture b;

[0079] S3. Add mixture a to mixture b, stir at 2800 rpm for 15 min at 75°C, cool to 45°C, add preservatives, stir at 1000 rpm for 4 min, and cool to room temperature.

[0080] Among them: the vegetable oil is avocado oil; the emulsifier is polysorbate; the thickener is xanthan gum; and the preservative is ethylparaben.

[0081] Raw material ratio: The mass ratio of modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative is 2:0.75:6:85:7:2.5:0.15:0.1.

[0082] Comparative Example 1

[0083] Preparation of modified recombinant collagen: Compared with the preparation method of Example 1, in Comparative Example 1, only the thiazone structure is introduced into the recombinant collagen peptide chain, and no benzimidazole structure is introduced. Other raw materials and processes are the same as those of Example 1.

[0084] Preparation of cosmetic composition: same as Example 1.

[0085] Comparative Example 2

[0086] Preparation of modified recombinant collagen: Compared with the preparation method of Example 1, Comparative Example 2 only introduces a benzimidazole structure into the recombinant collagen peptide chain, and does not introduce a thiazone structure. Other raw materials and processes are the same as those of Example 1.

[0087] Preparation of cosmetic composition: same as Example 1.

[0088] Comparative Example 3

[0089] Preparation of modified recombinant collagen:

[0090] (1) Sodium o-sulfonylbenzoylmide and polyethylene glycol (PEG400) are added to acetonitrile, heated to 85°C, and then 4-(4-bromobutyloxy)benzaldehyde is added, stirred and refluxed for 20 hours, filtered, repeatedly washed with ethanol, and vacuum dried to obtain a thiazide penetration enhancer;

[0091] (2) Mix o-phenylenediamine and phosphoric acid, heat to 105°C, add recombinant collagen, stir and reflux for 2 hours, adjust the pH value to 8, filter, wash repeatedly with ethanol, and vacuum dry to obtain recombinant collagen C;

[0092] (3) Evenly mix the thiophene permeation enhancer and recombinant collagen C to obtain modified recombinant collagen.

[0093] It can be seen that compared with the preparation method of Example 1, Comparative Example 3 introduces a benzimidazole structure into the recombinant collagen peptide chain, but does not introduce a thiazone structure into the peptide chain, but directly adds (i.e., blends) the thiazone penetration enhancer after preparation. Other raw materials and processes are the same as those of Example 1.

[0094] Preparation of cosmetic composition: same as Example 1.

[0095] Performance Testing:

[0096] (1) The cosmetic compositions prepared in Examples 1-5 and Comparative Examples 1-3 were used as test samples. With reference to T / ZHCA 001-2018 "Test Method for Whitening and Anti-freckle Effect of Cosmetics", volunteers were selected according to the requirements of the standard. Each test sample was a group, and 30 people were selected in each group. The three primary color stimulation values ​​were tested before and after 4 weeks of use (once in the morning and once in the evening each day), and the ITA° value was calculated according to the method of the standard. The difference △ITA° between the ITA° value before and after use was used to characterize the whitening and freckle-removing effect of the cosmetic composition. The larger the △ITA°, the better the whitening and freckle-removing effect. The test site was the inner side of the bent arm, and the test area was 2 cm×2 cm. Each volunteer selected 5 different positions for testing, and the average value was taken, and the average value of each group of volunteers was calculated. The test environment conditions were: temperature 22±1°C, humidity 50±5%, and sitting for 20 minutes before testing. The test results are shown in Table 1.

[0097] It can be seen from Table 1 that the cosmetic composition prepared by the method of the present invention has better whitening and freckle-removing effects, and the greater the amount of modified recombinant collagen added, the better the whitening and freckle-removing effects; since Comparative Example 1 does not introduce a benzimidazole structure, its binding ability with the copper ion in the active center of tyrosinase is not as good as that in Example 1, and thus the whitening and freckle-removing effects are worse than those in Example 1; since Comparative Example 2 does not introduce a thiazone structure, the transdermal penetration ability of collagen is not as good as that in Example 1, and thus the whitening and freckle-removing effects are significantly worse than those in Example 1; although Comparative Example 3 adds a thiazone penetration enhancer, it is not introduced into the peptide chain but directly added, and its penetration-promoting effect on collagen is not as precise as that in Example 1, and thus the whitening and freckle-removing effects are slightly worse than those in Example 1.

[0098] Table 1:

[0099]

[0100] (2) Using 20 wt% DMSO (dimethyl sulfoxide) solution as solvent, add the modified recombinant collagen prepared in Example 1 and Comparative Example 1 respectively to prepare a collagen solution with a concentration of 30 mg / mL; L-DOPA solution (4.5mmol / L), 0.5mL collagen solution, 1.5mL phosphate buffer (0.067mol / L) were mixed, kept in a 37℃ water bath for 10min, and then 0.5mL tyrosinase solution (200U / mL) was added, mixed, kept in a 37℃ water bath for 15min, and the absorbance A1 was measured at 475nm; the tyrosinase solution was replaced by phosphate buffer, and the absorbance was tested again in the above manner as A2; the collagen solution in A1 was replaced by 20wt% DMSO solution, and the absorbance was tested again in the above manner as B1; the collagen solution in A2 was replaced by 20wt% DMSO solution, and the absorbance was tested again in the above manner as B2; the inhibition rate of the modified recombinant collagen solution sample on DOPA oxidase was calculated as follows: Inhibition rate = [1-(A1-A2) / (B1-B2)]×100%. The test results are shown in Table 2.

[0101] By replacing the L-dopa solution (4.5 mmol / L) in the above test with an L-tyrosine solution (10 mmol / L), the inhibition rate of the modified recombinant collagen solution sample on tyrosine hydroxylase can be obtained. The test results are shown in Table 2.

[0102] It can be seen from Table 2 that compared with Comparative Example 1, the modified recombinant collagen of Example 1 has a stronger binding ability with the copper ion in the active center of tyrosinase due to the introduction of the benzimidazole structure, so its solution has a higher tyrosinase inhibition rate.

[0103] Table 2:

[0104]

[0105] (3) Using TP-6 ​​transdermal diffusion instrument, Strat-M TM The skin-specific membrane (purchased from Merck Millipore, USA) was fixed between the sample pool and the receiving pool; the modified recombinant collagen (first tested as M1) prepared in Example 1 and Comparative Examples 2-3 were respectively used to prepare a 10wt% collagen aqueous solution, added to the sample pool, and the receiving pool was filled with water, the water bath temperature was 37°C, and the stirring speed was 200rpm; after 2h of penetration, the solution in the sample pool was poured out, the water was evaporated and removed, and the mass of the remaining collagen was tested as M2, and the permeability of the modified recombinant collagen solution sample for 2h was calculated as follows: Permeability = (1-M2 / M1) × 100%. The test results are shown in Table 3.

[0106] By changing the penetration time in the above test to 6 hours, the 6-hour permeability of the sample can be obtained. The test results are shown in Table 3.

[0107] It can be seen from Table 3 that: compared with Comparative Example 2, the modified recombinant collagen of Example 1 exhibits significantly stronger transdermal permeability due to the introduction of the thiazone structure; compared with Comparative Example 3, the thiazone permeation-enhancing structure of Example 1 is located on the collagen peptide chain, which can more accurately promote the transdermal permeation of collagen, and thus the transdermal permeability of the collagen of Example 1 is better than that of Comparative Example 3.

[0108] Table 3:

[0109]

Claims

1. A recombinant collagen cosmetic composition for whitening and lightening spots, the components of the cosmetic composition comprising modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative, It is characterized in that The preparation process of the modified recombinant collagen is as follows: (1) Add 4-(4-bromobutyloxy)benzaldehyde and octanoic acid to ethanol, heat to 45-55°C, then add recombinant collagen, stir and reflux for 1-2 hours, filter, wash repeatedly with ethanol, and vacuum dry to obtain recombinant collagen A; (2) Mix o-phenylenediamine and phosphoric acid, heat to 100-105°C, add recombinant collagen A, stir and reflux for 1.5-2.5 hours, adjust the pH value to 8, filter, wash repeatedly with ethanol, and vacuum dry to obtain recombinant collagen B; (3) Add sodium succinylbenzoylmide and polyethylene glycol to acetonitrile, heat to 80-90°C, then add recombinant collagen B, stir and reflux for 18-22 hours, filter, wash repeatedly with ethanol, and vacuum dry to obtain modified recombinant collagen; The number average molecular weight of the polyethylene glycol in step (3) is 400-600.

2. The cosmetic composition according to claim 1, Features: The recombinant collagen in step (1) is recombinant type III humanized collagen with a molecular weight of 1000-3000 Daltons.

3. The cosmetic composition according to claim 1, Features: In step (1), the mass ratio of recombinant collagen, 4-(4-bromobutyloxy)benzaldehyde, caprylic acid and ethanol is 100:18-22:0.8-1.2:400-600.

4. The cosmetic composition according to claim 1, Features: In step (2), the mass ratio of recombinant collagen A, o-phenylenediamine, and phosphoric acid is 100:8-10:120-150.

5. The cosmetic composition according to claim 1, Features: In step (3), the mass ratio of recombinant collagen B, sodium o-sulfonylbenzoylmide, polyethylene glycol, and acetonitrile is 100:16-18:1.5-2:400-600.

6. The cosmetic composition according to claim 1, Features: The vegetable oil is at least one of shea butter, almond oil, and avocado oil; the emulsifier is at least one of polysorbate, glyceryl stearate, and ricinoleamide; the thickener is at least one of xanthan gum and carbomer; and the preservative is at least one of methylparaben, ethylparaben, and propylparaben.

7. The cosmetic composition according to claim 1, Features: The mass ratio of modified recombinant collagen, glutathione, glycerin, water, vegetable oil, emulsifier, thickener and preservative is 2-6: 0.5-1: 4-8: 80-90: 6-8: 2-3: 0.1-0.2: 0.05-0.

2.

8. A method for preparing the cosmetic composition according to any one of claims 1 to 7, It is characterized in that The preparation process of the cosmetic composition is as follows: S1. Mix the vegetable oil and the emulsifier, and stir evenly at 70-80° C. to obtain a mixture a; S2. Add the thickener to the glycerol and stir to disperse, then add the modified recombinant collagen, glutathione and water, and stir evenly at 70-80° C. to obtain a mixture b; S3. Add mixture a to mixture b, stir at high speed for 10-20 min at 70-80°C, cool to 40-50°C, add preservatives, stir at low speed for 2-5 min, and cool to room temperature.

9. A method for preparing the cosmetic composition according to claim 8, Features: In S3, the rotation speed of high-speed stirring is 2500-3500 rpm, and the rotation speed of low-speed stirring is 800-1200 rpm.

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