Preparation method and application of fish type I collagen sodium alginate supramolecular assembly

Abstract

The invention discloses a preparation method and application of a fish I-type collagen sodium alginate supramolecular assembly, fish processing byproducts are used as raw materials, and the fish I-type collagen is prepared by an acetic acid extraction and salting-out column chromatography purification integrated technology. The preparation method comprises the following steps: by taking fish type I collagen as a raw material, adding sodium alginate, and carrying out composite reaction, so as to obtain a mixed solution of the fish type I collagen, the sodium alginate and the fish type I collagen sodium alginate supramolecular assembly; and purifying the product by using a salting-out membrane separation integration technology to obtain the fish type I collagen sodium alginate supramolecular assembly. The fish type I collagen sodium alginate supramolecular assembly prepared by the invention keeps a triple helix structure of the type I collagen, shows good biocompatibility, and solves the application bottleneck problems of poor solubility and stability of the fish type I collagen and the like; the composition has the advantages of excellent solubility, high thermal stability, remarkable anti-wrinkle and moisturizing effects and good safety, so that the composition is very suitable for being applied to the field of anti-aging cosmetics.

Description

Technical Field

[0001] The invention belongs to the technical field of common cosmetic raw materials, and specifically relates to a preparation method and application of a fish type I collagen sodium alginate supramolecular assembly. Background Art

[0002] Type I collagen is a natural biomacromolecule with biological activity, which is widely found in animal tissues such as teeth, skin and tendons. It has a triple helix structure, which is composed of three left-handed helical α peptide chains bonded by hydrogen bonds to form a stable right-handed superhelical structure. The unique triple helix structure of type I collagen gives it low antigenicity, good biocompatibility and biodegradability, making it widely used in the fields of cosmetics and biomedicine. In the cosmetics industry, type I collagen has been included in the US CTFA Cosmetic Ingredients Handbook and is listed as a natural substance and functional cosmetic raw material.

[0003] Traditionally, type I collagen comes from terrestrial animals such as pigs and cattle, but in recent years, fish type I collagen has become a potential substitute for terrestrial type I collagen. In recent years, research on the preparation of type I collagen from fish resources to replace terrestrial type I collagen has received widespread attention. For example, the El-Rashidy AA R&D team in Egypt used tilapia scales as raw materials, and prepared tilapia type I collagen through pepsin extraction, sodium chloride salting out, acetic acid and pure water dialysis purification. The Thuy LTM R&D team in Japan used multi-toothed snake mullet, blackfish and yellowback sea bream scales as raw materials, and used acetic acid extraction, tris(hydroxymethylaminomethane) / sodium chloride salting out, acetic acid and pure water dialysis purification to prepare type I collagen.

[0004] In 2018, the market size of fish type I collagen was US$594.76 million, and is expected to reach US$1,055.27 million by 2026, with an annual growth rate of 7.39% between 2019 and 2026. However, fish type I collagen has technical bottlenecks such as poor solubility and poor thermal stability, which limit its large-scale production and promotion and application. Therefore, it is urgent to develop a fish type I collagen sodium alginate supramolecular assembly with good solubility and high thermal stability that can be industrialized and its preparation method to promote the further application and development of fish type I collagen. Summary of the invention

[0005] The present invention aims to overcome the defects of the prior art and provide a method for preparing a fish type I collagen sodium alginate supramolecular assembly.

[0006] Another object of the present invention is to provide an application of the fish type I collagen sodium alginate supramolecular assembly prepared by the above preparation method.

[0007] It should be noted that ordinary cosmetics are also called non-special-purpose cosmetics, which mainly play the role of cleaning, care and beautification, and do not claim to have therapeutic functions.

[0008] The technical solution of the present invention is as follows:

[0009] The preparation method of fish type I collagen sodium alginate supramolecular assembly comprises the following steps:

[0010] (1) mixing the fish processing byproducts after pretreatment and impurity removal with an acetic acid solution with a concentration of 0.5-1 M, stirring and extracting at a temperature below 10° C. for 10-20 hours, and then performing solid-liquid separation to obtain a crude type I collagen extract solution;

[0011] (2) adding sodium chloride having a final concentration of 3-5% by weight volume to the crude type I collagen extract solution obtained in step (1) for salting out, and then centrifuging to obtain a precipitate;

[0012] (3) adding 0.1-0.5 M acetic acid to the precipitate obtained in step (2), stirring and dissolving the mixture, and removing inorganic salts using an ion exchange resin to obtain a type I collagen solution;

[0013] (4) freeze-drying the type I collagen solution obtained in step (3) to obtain fish type I collagen;

[0014] (5) adding the sodium alginate solution to a reaction kettle, and then adding the fish type I collagen obtained in step (4), and performing a composite reaction at a temperature below 10° C., wherein the mass ratio of fish type I collagen to sodium alginate is 1-10:1, the pH value of the reaction system is 3-6, and the reaction time is 2-8 h. After the reaction, the solution is centrifuged to remove impurities, thereby obtaining a mixed solution containing fish type I collagen, sodium alginate, and fish type I collagen sodium alginate supramolecular assembly;

[0015] (6) Adding sodium chloride with a final concentration of 3-5% by mass volume to the mixed solution obtained in step (5) for salting out, centrifuging to remove the fish type I collagen precipitate, removing sodium alginate from the obtained clear solution using an ultrafiltration membrane, and then freeze-drying to obtain a fish type I collagen sodium alginate supramolecular assembly.

[0016] In a preferred embodiment of the present invention, the fish processing by-products include at least one of fish scales, fish skin and fish bladder.

[0017] In a preferred embodiment of the present invention, the flow rate of the ion exchange resin is 10-30m 3 / h.

[0018] In a preferred embodiment of the present invention, the cut-off relative molecular mass of the ultrafiltration membrane is 200-350 kD.

[0019] In a preferred embodiment of the present invention, in step (1), the mass ratio of the pretreated fish processing by-products to the acetic acid solution is 1:3-10.

[0020] Application of the fish type I collagen sodium alginate supramolecular assembly prepared by the preparation method in the preparation of an anti-aging cosmetic composition.

[0021] In a preferred embodiment of the present invention, the anti-aging cosmetic composition is in the form of a serum.

[0022] An anti-aging cosmetic composition, the effective ingredients of which include the fish type I collagen sodium alginate supramolecular assembly prepared by the above preparation method.

[0023] In a preferred embodiment of the present invention, the effective ingredient is the fish type I collagen sodium alginate supramolecular assembly obtained by the preparation method.

[0024] More preferably, the composition is in the form of serum.

[0025] The beneficial effects of the present invention are:

[0026] 1. The present invention assembles fish type I collagen molecules with positive charge and sodium alginate molecules with negative charge into fish type I collagen sodium alginate supramolecular assembly through electrostatic interaction. The reaction system does not contain organic solvents, so it is safe and non-toxic, has low production cost, is easy to control, and is suitable for large-scale production.

[0027] 2. The fish type I collagen sodium alginate supramolecular assembly prepared by the present invention maintains the triple helix structure of type I collagen, exhibits good biocompatibility, and solves the application bottleneck problems of poor solubility and stability of fish type I collagen.

[0028] 3. The fish type I collagen sodium alginate supramolecular assembly prepared by the present invention has excellent solubility and high thermal stability, significant anti-wrinkle and moisturizing effects, and good safety, and is therefore very suitable for application in the field of general anti-aging cosmetics. BRIEF DESCRIPTION OF THE DRAWINGS

[0029] Figure 1 The diagram shows the bonding mode between the fish type I collagen molecule and the sodium alginate molecule obtained in Example 1 of the present invention.

[0030] Figure 2 The X-ray diffraction diagram of the fish type I collagen and the supramolecular assembly prepared in Example 1 of the present invention is shown.

[0031] Figure 3 The thermal denaturation temperature of the fish type I collagen and the supramolecular assembly prepared in Example 1 of the present invention is shown. DETAILED DESCRIPTION

[0032] The technical solution of the present invention is further illustrated and described below through specific implementation modes in combination with the accompanying drawings.

[0033] The pretreatment in the following examples uses immersion in a sodium bicarbonate solution to remove impurities such as fat and melanin.

[0034] Example 1

[0035] (1) 10 g of the pretreated fish skin is added to a reaction kettle, and 100 g of a 0.5 M acetic acid solution is added and stirred for extraction at a temperature below 10° C. The extraction time is 10 h. After the extract is centrifuged to remove solid impurities, a type I collagen crude extract solution is obtained.

[0036] (2) The crude collagen extract solution was salted out by adding 3% (W / V) sodium chloride and then centrifuged to obtain a precipitate.

[0037] (3) After adding 0.1 M acetic acid to the precipitate and stirring to dissolve it, the inorganic salts were removed using ion exchange resin at a flow rate of 10 m 3 / h to obtain type I collagen solution.

[0038] (4) freeze-drying the type I collagen solution obtained in step (3) to obtain fish type I collagen.

[0039] (5) Adding the sodium alginate solution into a reactor, and then adding the fish type I collagen obtained in step (4), and performing a composite reaction at a temperature below 10° C., wherein the mass ratio of fish type I collagen to sodium alginate in the reaction system is 4:1, the pH value of the reaction system is 4, and the reaction time is 2 h. After the solution after the reaction is centrifuged to remove impurities, a mixed solution containing fish type I collagen, sodium alginate, and fish type I collagen sodium alginate supramolecular assembly is obtained.

[0040] (6) Add 3% (W / V) sodium chloride to the mixed solution obtained in step (5) for salting out, centrifuge to remove fish type I collagen precipitate, remove sodium alginate from the clear solution using an ultrafiltration membrane with a cutoff relative molecular mass of 200-350 kD, freeze-dry the material solution after membrane separation, and obtain a freeze-dried sample of fish type I collagen sodium alginate supramolecular assembly.

[0041] [Structural characterization]

[0042] The binding type of fish type I collagen and sodium alginate molecules in the supramolecular assembly prepared in this embodiment was detected by using an isothermal titration instrument. The fish type I collagen solution was titrated into the sodium alginate solution as a titrant, and the titration curve was analyzed by the "One binding sites" model to obtain the fitting curve and related thermodynamic parameters: stoichiometric binding ratio (N), enthalpy change value (ΔH), entropy change value (ΔS) and Gibbs free energy (ΔG). The test results show that the composite reaction of fish type I collagen molecules and sodium alginate molecules is spontaneous. During the composite process, every 0.823 fish type I collagen molecules can bind to one sodium alginate molecule, and the binding mode is mainly driven by the negative enthalpy of electrostatic interaction ( Figure 1 ).

[0043] The structure of the fish type I collagen and the supramolecular assembly prepared in this embodiment was detected by X-ray diffraction. The detection results showed that the distance between the fiber molecular chains of the fish type I collagen was The distance between the collagen backbones is In the supramolecular assembly, the distance between collagen fibers is The distance between collagen backbones is The distance between fiber molecules and the distance between skeletons of supramolecular assemblies are lower than those of fish type I collagen, indicating that the electrostatic interaction between fish type I collagen molecules and sodium alginate molecules changes the crystallinity and molecular arrangement conformation of supramolecular assemblies, making the distance between collagen molecules and skeletons closer, but does not destroy the triple helix structure of collagen. (e.g. Figure 2 (shown)

[0044] [Characterization of physical and chemical properties]

[0045] The thermal denaturation temperature (Td) is used to characterize the thermal stability of the sample. The Td of fish type I collagen is 12.01°C, and the Td of the fish type I collagen sodium alginate supramolecular assembly prepared in this example is 35.11°C. The Td of the assembly is 23.1°C higher than that of fish type I collagen, indicating that the electrostatic interaction between fish type I collagen molecules and sodium alginate molecules makes the intermolecular chimera of the assembly more tightly, thereby improving the thermal stability of the product. (e.g. Figure 3 (shown)

[0046] The fish type I collagen sodium alginate supramolecular assembly prepared in this example was dissolved in water to prepare a solution with a mass volume ratio of 30% without any particle impurities visible to the naked eye.

[0047] [Human efficacy evaluation]

[0048] The fish type I collagen sodium alginate supramolecular assembly prepared in this example was made into an essence, and the human efficacy was evaluated and compared with the blank group and the control group. The specific test method is as follows:

[0049] The ingredients of the essence in the experimental group are: 60% water, 10% glycerin, 4.6% butylene glycol, 2% tert-butyl alcohol, 2% 1,3-propylene glycol, 1% acryloyldimethyl taurateuramine, 1,2-ethylene glycol, 1%, betaine, 1% glycosyl trehalose, 1% hyaluronic acid, 0.6% sodium benzoate, 0.4% phenoxyethanol, 0.3% ethylhexylglycerin, 0.1% sodium lysine, and 15% fish type I collagen sodium alginate supramolecular assembly.

[0050] The difference between the blank group essence and the test group essence is that fish type I collagen sodium alginate supramolecular assembly is not added, and the other ingredients are consistent with the formula of the experimental group essence.

[0051] The difference between the essence of the control group and the essence of the experimental group is that the fish type I collagen was not added to replace the fish type I collagen sodium alginate supramolecular assembly in equal parts by weight, and the other ingredients were consistent with the formula of the essence of the experimental group.

[0052] The subjects used the essence for 56 consecutive days, with a daily dosage of 1 mL. The skin of the subjects was tested and evaluated at 8 hours, 28 days and 56 days to detect the skin elasticity value (R 2 ) and the increase rate of skin moisture content, and the decrease rate of nasolabial fold volume and eye wrinkle volume. Increase rate = (value after use - value before use) / value before use × 100%. Decrease rate = (value before use - value after use) / value before use × 100%

[0053] The experimental results show that the fish type I collagen sodium alginate supramolecular assembly essence significantly improved the skin elasticity of the subjects, increased the skin moisture content, and reduced the volume of nasolabial folds and caudal wrinkles. The effect was better than that of the blank group and the fish type I collagen essence control group (see Table 1). It can be used in the field of high-end anti-aging cosmetics.

[0054] Table 1. Human efficacy evaluation

[0055]

[0056] Example 2

[0057] (1) 50 g of pretreated fish scales were added to a reactor, and 150 g of 1 M acetic acid solution was added for extraction under stirring at a temperature below 10° C. The extraction time was 15 h. After the solid impurities were removed from the extract by centrifuge, a crude type I collagen extract solution was obtained.

[0058] (2) The crude collagen extract solution was salted out by adding 4% (W / V) sodium chloride and then centrifuged to obtain a precipitate.

[0059] (3) After adding 0.5M acetic acid to the precipitate and stirring to dissolve it, the inorganic salts were removed using ion exchange resin at a flow rate of 30m 3 / h to obtain type I collagen solution.

[0060] (4) freeze-drying the type I collagen solution obtained in step (3) to obtain fish type I collagen.

[0061] (5) The sodium alginate solution is added to the reactor, and then the fish type I collagen prepared in step (4) is added to carry out a composite reaction at a temperature below 10° C. In the reaction system, the mass ratio of fish type I collagen to sodium alginate is 1:1, the pH value of the reaction system is 6, and the reaction time is 5 h. After the solution after the reaction is centrifuged to remove impurities, a mixed solution containing fish type I collagen, sodium alginate and fish type I collagen sodium alginate supramolecular assembly is obtained.

[0062] (6) Add 4% (W / V) sodium chloride to the mixed solution obtained in step (5) for salting out, centrifuge to remove fish type I collagen precipitate, remove sodium alginate from the clear solution using an ultrafiltration membrane with a cutoff relative molecular mass of 200-350 kD, freeze-dry the material solution after membrane separation, and obtain a freeze-dried sample of fish type I collagen sodium alginate supramolecular assembly.

[0063] [Structural characterization]

[0064] The binding type of fish type I collagen and sodium alginate molecules in the supramolecular assembly prepared in this embodiment was detected by using an isothermal titration measuring instrument. The fish type I collagen solution was titrated into the sodium alginate solution as a titrant, and the titration curve was analyzed by the "One binding sites" model to obtain the fitting curve and related thermodynamic parameters: stoichiometric binding ratio (N), enthalpy change value (ΔH), entropy change value (ΔS) and Gibbs free energy (ΔG). The test results show that the composite reaction of fish type I collagen molecules and sodium alginate molecules is spontaneous. During the composite process, every 0.914 fish type I collagen molecules can bind to one sodium alginate molecule, and the binding mode is mainly driven by the negative enthalpy of electrostatic interaction.

[0065] The structure of the fish type I collagen and the supramolecular assembly prepared in this embodiment was detected by X-ray diffraction. The detection results showed that the distance between the fiber molecular chains of the fish type I collagen was The distance between the collagen backbones is In the supramolecular assembly, the distance between collagen fibers is The distance between collagen backbones is The distances between fiber molecules and skeletons of the supramolecular assembly are lower than those of fish type I collagen, indicating that the electrostatic interaction between fish type I collagen molecules and sodium alginate molecules changes the crystallinity and molecular arrangement conformation of the supramolecular assembly, making the distances between collagen molecules and skeletons closer, but does not destroy the triple helix structure of collagen.

[0066] [Characterization of physical and chemical properties]

[0067] The thermal denaturation temperature (Td) was used to characterize the thermal stability of the sample. d The T of the fish type I collagen sodium alginate supramolecular assembly prepared in this example was 12.13°C. d The T of the assembly is 36.25°C. d It is 23.95℃ higher than that of fish type I collagen, indicating that the electrostatic interaction between fish type I collagen molecules and sodium alginate molecules makes the intermolecular integration of the assembly more compact, thus improving the thermal stability of the product.

[0068] The fish type I collagen sodium alginate supramolecular assembly prepared in this example was dissolved in water to prepare a solution with a mass volume ratio of 30% without any particle impurities visible to the naked eye.

[0069] [Human efficacy evaluation]

[0070] The fish type I collagen sodium alginate supramolecular assembly prepared in this example was made into an essence, and the human efficacy was evaluated and compared with the blank group and the control group. The specific test method is as follows:

[0071] The ingredients of the essence in the experimental group are: 60% water, 10% glycerin, 4.6% butylene glycol, 2% tert-butyl alcohol, 2% 1,3-propylene glycol, 1% acryloyldimethyl taurateuramine, 1,2-ethylene glycol, 1%, betaine, 1% glycosyl trehalose, 1% hyaluronic acid, 0.6% sodium benzoate, 0.4% phenoxyethanol, 0.3% ethylhexylglycerin, 0.1% sodium lysine, and 15% fish type I collagen sodium alginate supramolecular assembly.

[0072] The difference between the blank group essence and the test group essence is that fish type I collagen sodium alginate supramolecular assembly is not added, and the other ingredients are consistent with the formula of the experimental group essence.

[0073] The difference between the essence of the control group and the essence of the experimental group is that the fish type I collagen was not added to replace the fish type I collagen sodium alginate supramolecular assembly in equal parts by weight, and the other ingredients were consistent with the formula of the essence of the experimental group.

[0074] The subjects used the essence for 56 consecutive days, with a daily dosage of 1 mL. The skin of the subjects was tested and evaluated at 8 hours, 28 days and 56 days to detect the skin elasticity value (R2 ) and the increase rate of skin moisture content, and the decrease rate of nasolabial fold volume and eye wrinkle volume. Increase rate = (value after use - value before use) / value before use × 100%. Decrease rate = (value before use - value after use) / value before use × 100%

[0075] The experimental results show that the fish type I collagen sodium alginate supramolecular assembly essence significantly improved the skin elasticity of the subjects, increased the skin moisture content, and reduced the volume of nasolabial folds and caudal wrinkles. The effect was better than that of the blank group and the fish type I collagen essence control group (see Table 2). It can be used in the field of high-end anti-aging cosmetics.

[0076] Table 2. Human efficacy evaluation

[0077]

[0078]

[0079] Example 3

[0080] (1) 100 g of pretreated fish maw was added to a reaction kettle, and 500 g of 0.8 M acetic acid solution was added for extraction under stirring at a temperature below 10° C. The extraction time was 20 h. After the solid impurities were removed from the extract by centrifuge, a crude type I collagen extract solution was obtained.

[0081] (2) The crude collagen extract solution was salted out by adding 5% (W / V) sodium chloride and then centrifuged to obtain a precipitate.

[0082] (3) After adding 0.3M acetic acid to the precipitate and stirring to dissolve it, the inorganic salts were removed using ion exchange resin at a flow rate of 20m 3 / h to obtain type I collagen solution.

[0083] (4) freeze-drying the type I collagen solution obtained in step (3) to obtain fish type I collagen.

[0084] (5) The sodium alginate solution is added to the reactor, and then the fish type I collagen obtained in step (4) is added to carry out a composite reaction at a temperature below 10° C. In the reaction system, the mass ratio of fish type I collagen to sodium alginate is 10:1, the pH value of the reaction system is 3, and the reaction time is 8 h. After the solution after the reaction is centrifuged to remove impurities, a mixed solution containing fish type I collagen, sodium alginate and fish type I collagen sodium alginate supramolecular assembly is obtained.

[0085] (6) Add 5% (W / V) sodium chloride to the mixed solution obtained in step (5) for salting out, centrifuge to remove fish type I collagen precipitate, remove sodium alginate from the clear solution using an ultrafiltration membrane with a cutoff relative molecular mass of 200-350 kD, freeze-dry the material solution after membrane separation, and obtain a freeze-dried sample of fish type I collagen sodium alginate supramolecular assembly.

[0086] [Structural characterization]

[0087] The binding type of fish type I collagen and sodium alginate molecules in the supramolecular assembly prepared in this embodiment was detected by using an isothermal titration instrument. The fish type I collagen solution was titrated into the sodium alginate solution as a titrant, and the titration curve was analyzed by the "One binding sites" model to obtain the fitting curve and related thermodynamic parameters: stoichiometric binding ratio (N), enthalpy change value (ΔH), entropy change value (ΔS) and Gibbs free energy (ΔG). The test results show that the composite reaction of fish type I collagen molecules and sodium alginate molecules is spontaneous. During the composite process, every 0.724 fish type I collagen molecules can bind to one sodium alginate molecule, and the binding mode is mainly driven by the negative enthalpy of electrostatic interaction.

[0088] The structure of the fish type I collagen and the supramolecular assembly prepared in this embodiment was detected by X-ray diffraction. The detection results showed that the distance between the fiber molecular chains of the fish type I collagen was The distance between the collagen backbones is In the supramolecular assembly, the distance between collagen fibers is The distance between collagen backbones is The distances between fiber molecules and skeletons of the supramolecular assembly are lower than those of fish type I collagen, indicating that the electrostatic interaction between fish type I collagen molecules and sodium alginate molecules changes the crystallinity and molecular arrangement conformation of the supramolecular assembly, making the distances between collagen molecules and skeletons closer, but does not destroy the triple helix structure of collagen.

[0089] [Characterization of physical and chemical properties]

[0090] The thermal denaturation temperature (Td) was used to characterize the thermal stability of the sample. d The Td of the fish type I collagen sodium alginate supramolecular assembly prepared in this example is 34.82°C. d It is 22.67℃ higher than that of fish type I collagen, indicating that the electrostatic interaction between fish type I collagen molecules and sodium alginate molecules makes the intermolecular integration of the assembly more compact, thus improving the thermal stability of the product.

[0091] The fish type I collagen sodium alginate supramolecular assembly prepared in this example was dissolved in water to prepare a solution with a mass volume ratio of 30% without any particle impurities visible to the naked eye.

[0092] [Human efficacy evaluation]

[0093] The fish type I collagen sodium alginate supramolecular assembly prepared in this example was made into an essence, and the human efficacy was evaluated and compared with the blank group and the control group. The specific test method is as follows:

[0094] The ingredients of the essence in the experimental group are: 60% water, 10% glycerin, 4.6% butylene glycol, 2% tert-butyl alcohol, 2% 1,3-propylene glycol, 1% acryloyldimethyl taurateuramine, 1,2-ethylene glycol, 1%, betaine, 1% glycosyl trehalose, 1% hyaluronic acid, 0.6% sodium benzoate, 0.4% phenoxyethanol, 0.3% ethylhexylglycerin, 0.1% sodium lysine, and 15% fish type I collagen sodium alginate supramolecular assembly.

[0095] The difference between the blank group essence and the test group essence is that fish type I collagen sodium alginate supramolecular assembly is not added, and the other ingredients are consistent with the formula of the experimental group essence.

[0096] The difference between the essence of the control group and the essence of the experimental group is that the fish type I collagen was not added to replace the fish type I collagen sodium alginate supramolecular assembly in equal parts by weight, and the other ingredients were consistent with the formula of the essence of the experimental group.

[0097] The subjects used the essence for 56 consecutive days, with a daily dosage of 1 mL. The skin of the subjects was tested and evaluated at 8 hours, 28 days and 56 days to detect the skin elasticity value (R 2 ) and the increase rate of skin moisture content, and the decrease rate of nasolabial fold volume and eye wrinkle volume. Increase rate = (value after use - value before use) / value before use × 100%. Decrease rate = (value before use - value after use) / value before use × 100%

[0098] The experimental results show that the fish type I collagen sodium alginate supramolecular assembly essence significantly improved the skin elasticity of the subjects, increased the skin moisture content, and reduced the volume of nasolabial folds and caudal wrinkles. The effect was better than that of the blank group and the fish type I collagen essence control group (see Table 2). It can be used in the field of high-end anti-aging cosmetics.

[0099] Table 3. Human efficacy evaluation

[0100]

[0101] The above description is only a preferred embodiment of the present invention, and therefore cannot be used to limit the scope of the present invention. That is, equivalent changes and modifications made according to the patent scope of the present invention and the contents of the specification should still fall within the scope of the present invention.

Claims

1. A method for preparing a fish type I collagen sodium alginate supramolecular assembly, characterized in that: The steps include: (1) mixing the fish processing byproducts after pretreatment and impurity removal with an acetic acid solution with a concentration of 0.5-1 M, stirring and extracting at a temperature below 10° C. for 10-20 hours, and then performing solid-liquid separation to obtain a crude type I collagen extract solution; (2) adding sodium chloride having a final concentration of 3-5% by weight volume to the crude type I collagen extract solution obtained in step (1) for salting out, and then centrifuging to obtain a precipitate; (3) adding 0.1-0.5 M acetic acid to the precipitate obtained in step (2), stirring and dissolving the mixture, and removing inorganic salts using an ion exchange resin to obtain a type I collagen solution; (4) freeze-drying the type I collagen solution obtained in step (3) to obtain fish type I collagen; (5) adding the sodium alginate solution to a reaction kettle, and then adding the fish type I collagen obtained in step (4), and performing a composite reaction at a temperature below 10° C., wherein the mass ratio of fish type I collagen to sodium alginate is 1-10:1, the pH value of the reaction system is 3-6, and the reaction time is 2-8 h. After the reaction, the solution is centrifuged to remove impurities, thereby obtaining a mixed solution containing fish type I collagen, sodium alginate, and fish type I collagen sodium alginate supramolecular assembly; (6) Adding sodium chloride with a final concentration of 3-5% by mass volume to the mixed solution obtained in step (5) for salting out, centrifuging to remove the fish type I collagen precipitate, removing sodium alginate from the obtained clear solution using an ultrafiltration membrane, and then freeze-drying to obtain a fish type I collagen sodium alginate supramolecular assembly.

2. The preparation method according to claim 1, characterized in that: The fish processing by-products include at least one of fish scales, fish skin and fish bladder.

3. The preparation method according to claim 1, characterized in that: The flow rate of the ion exchange resin is 10-30m 3 / h.

4. The preparation method according to claim 1, characterized in that: The cut-off relative molecular mass of the ultrafiltration membrane is 200-350 kD.

5. The preparation method according to any one of claims 1 to 4, characterized in that: In the step (1), the mass ratio of the pretreated fish processing by-product to the acetic acid solution is 1:3-10.

6. Use of the fish type I collagen sodium alginate supramolecular assembly obtained by the preparation method according to any one of claims 1 to 5 in the preparation of an anti-aging cosmetic composition.

7. The use according to claim 6, characterized in that: The anti-aging cosmetic composition is in the form of an essence.

8. An anti-aging cosmetic composition, characterized in that: The effective components thereof include the fish type I collagen sodium alginate supramolecular assembly prepared by the preparation method described in any one of claims 1 to 5.

9. An anti-aging cosmetic composition according to claim 8, characterized in that: The effective component is the fish type I collagen sodium alginate supramolecular assembly prepared by the preparation method.

10. An anti-aging cosmetic composition according to claim 8 or 9, characterized in that: It comes in the form of a serum.

Images