Wrinkle-improving cosmetics using ultra-low molecular collagen peptides

KR1020260122002APending Publication Date: 2026-08-11고광희
View PDF 0 Cites 0 Cited by

Patent Information

Application Number
KR1020250013446
Authority / Receiving Office
KR · KR
Patent Type
Applications
Current Assignee / Owner
Filing Date
2025-02-04
Publication Date
2026-08-11

Smart Images

  • Figure PAT00001_ABST
    Figure PAT00001_ABST
Patent Text Reader

Abstract

The present invention relates to a cosmetic composition for improving wrinkles using ultra-low molecular weight collagen peptides, wherein the ultra-low molecular weight collagen peptides are characterized by having a content of 90% or more of collagen peptides with a molecular weight of 180 Da or less and an average molecular weight of 175 Da or less. By utilizing ultra-low molecular weight collagen peptides as active ingredients, an economical and efficient ultra-low molecular weight collagen peptide can be obtained. The ultra-low molecular weight collagen peptides have excellent skin penetration delivery efficiency and an effect of improving wrinkles or elasticity, and are safe for the skin while having an excellent effect of improving skin condition.
Need to check novelty before this filing date? Find Prior Art

Description

Technology Field

[0001] The present invention relates to a cosmetic composition for improving wrinkles using ultra-low molecular weight collagen peptides, wherein an economical and efficient ultra-low molecular weight collagen peptide can be obtained by utilizing the ultra-low molecular weight collagen peptide as an active ingredient, and the ultra-low molecular weight collagen peptide has excellent skin penetration delivery efficiency and an effect of improving wrinkles or elasticity, thereby relating to a cosmetic composition for improving wrinkles using ultra-low molecular weight collagen peptides that is safe for the skin and has an excellent effect of improving skin condition. Background Technology

[0003] Collagen is a structural protein found in most animals, constituting the flesh and connective tissue of mammals in particular. Protein makes up approximately 20% of our body's composition, with collagen accounting for 30% of this (LC. Junqueira and J. Carneiro 1983). It is also found in large quantities in the bones and skin of animals such as cows, pigs, chickens, and fish. Currently, collagen is utilized in a wide range of products, from health foods to cosmetics and pharmaceuticals. Based on molecular weight, collagen can generally be classified into high molecular weight collagen (over 5,000 daltons) and low molecular weight collagen (under 1,500 daltons). Low molecular weight collagen is known to have a relatively higher absorption rate in the body compared to high molecular weight collagen, and is therefore used in health functional foods, cosmetics, and over-the-counter medicines.

[0004] Collagen, a major protein that makes up the skin, is a fibrous protein that accounts for about 90% of the dermal components. Along with elastin, it provides skin tension and elasticity, and functions to protect the skin from ultraviolet rays and prevent wrinkles. It is known that collagen can be delivered to the dermal layer through the epidermis only when its molecular weight is at least 500 Da or less. Although various studies on this are being conducted, the current situation is insufficient.

[0005] Meanwhile, when collagen peptides are manufactured using proteolytic enzymes, the usual method involves simply mixing the substrate, a high-molecular-weight collagen-containing material, with the proteolytic enzyme to react them. However, in this case, the enzyme remains after the reaction and may cause side effects, requiring a separate inactivation or removal process. Furthermore, since the enzyme cannot be reused, it is time-consuming and thus uneconomical.

[0006] Collagen, which generally makes up about 90% of the dermis, plays a role in protecting the skin from external stimuli or forces by providing strength and tensile strength to the skin. Therefore, a decrease in collagen within the skin is closely related to skin aging.

[0007] Collagen, the matrix substance that constitutes the skin, is broken down by external stress such as ultraviolet rays or internal oxidative damage. As collagen breakdown progresses, wrinkles deepen and elasticity decreases, leading to sagging skin or a rough surface. Therefore, efforts are being made to protect skin cells by inhibiting the biosynthesis or inhibiting the activity of enzymes that break down collagen (matrix metalloproteinases, MMPs), or by using antioxidant and anti-aging substances.

[0008] Peptides are known to have lipid metabolism-promoting functions and are currently being applied in diet foods. Milk, fish meat, and soybean gluten are used as raw protein sources for functional peptides that improve lipid metabolism. Silk peptides, which are hydrolysates of silkworm cocoons, consist of 18 types of amino acids and peptides, and have antioxidant and immune-related effects. Hydrolysates or peptides of casein protein in milk have been reported as acting as opioid peptides that promote calcium absorption, lower blood pressure, immune function, gastric juice secretion, emotional function, anesthesia, and stress reduction, as well as growth-promoting factors (Registered Patent 10-0844386) and antioxidant factors.

[0009] Recently, research has been actively conducted to isolate peptides with bio-regulatory functions for such adult diseases from the degradation products of various food ingredients. In particular, peptides present in food proteins such as milk, bovine blood, pork, beef, pollack, mackerel, soybeans, wheat, and barley are mostly produced by enzymatic treatment in vitro and are known to have excellent bio-regulatory functions, although they are composed of relatively simple amino acid bonds. The problem to be solved

[0011] The present invention was devised to improve the above-mentioned disadvantages, and by utilizing ultra-low molecular weight collagen peptides as active ingredients, it is possible to obtain economical and efficient ultra-low molecular weight collagen peptides. Since the ultra-low molecular weight collagen peptides have excellent skin penetration delivery efficiency and wrinkle or elasticity improvement effects, the invention provides a wrinkle-improving cosmetic product using ultra-low molecular weight collagen peptides that are safe for the skin and have excellent skin condition improvement effects. means of solving the problem

[0013] To achieve the above objective, the present invention provides a wrinkle-improving cosmetic composition using ultra-low molecular weight collagen peptides, characterized in that the ultra-low molecular weight collagen peptides have a collagen peptide content of 3 to 5% of 180 Da or less and an average molecular weight of 175 Da or less.

[0014] The above ultra-low molecular weight collagen peptide is,

[0015] It is extracted from hibiscus, a plant of the Malvaceae family and the genus Asteraceae, and has skin barrier strengthening, whitening, anti-aging, and antioxidant functions. Effects of the invention

[0017] The anti-wrinkle cosmetic composition using the ultra-low molecular weight collagen peptide of the present invention can obtain an economical and efficient ultra-low molecular weight collagen peptide by utilizing the ultra-low molecular weight collagen peptide as an active ingredient, and the ultra-low molecular weight collagen peptide has excellent skin penetration delivery efficiency and an effect of improving wrinkles or elasticity, so it is safe for the skin and has an excellent effect of improving skin condition. Brief explanation of the drawing

[0018] Figure 1 is a graph showing the efficacy of hibiscus as an ultra-low molecular weight collagen peptide of the present invention. Specific details for implementing the invention

[0019] The following detailed description of the invention refers to the accompanying drawings, which illustrate specific embodiments in which the invention may be practiced. These embodiments are described in sufficient detail to enable those skilled in the art to practice the invention. It should be understood that various embodiments of the invention are different but need not be mutually exclusive. For example, specific shapes, structures, and characteristics described herein may be implemented in other embodiments without departing from the spirit and scope of the invention in relation to one embodiment. It should also be understood that the location or arrangement of individual components within each disclosed embodiment may be changed without departing from the spirit and scope of the invention. Accordingly, the following detailed description is not intended to be limiting, and the scope of the invention is limited only by the appended claims, including all equivalents to those claimed therein, provided they are appropriately described. Similar reference numerals in the drawings refer to the same or similar functions across various aspects.

[0020] Hereinafter, preferred embodiments of the present invention will be described in more detail.

[0021] The method for manufacturing ultra-low molecular weight collagen peptides according to the present invention is described.

[0022] Specifically, the method for producing ultra-low molecular weight collagen peptides may comprise: (a) a step of immobilizing carboxypeptidase and dipeptidylaminopeptidase on a carrier; (b) a step of primary enzymatic treatment by mixing the carboxypeptidase immobilized on the carrier with collagen; and (c) a step of secondary enzymatic treatment by mixing the dipeptidylaminopeptidase immobilized on the carrier with the collagen treated with primary enzyma.

[0023] Collagen is a fibrous protein found in abundance in most animals, particularly mammals. It constitutes the majority of all connective tissues in the body, including skin and cartilage, and is produced and secreted by fibroblasts, the most common cells in the body. Since a decrease in collagen is a primary cause of wrinkles and reduced skin elasticity, collagen synthesis is essential for wrinkle improvement and elasticity enhancement.

[0024] Collagen peptides refer to the degradation products of collagen that have been hydrolyzed.

[0019] Collagen peptides can contribute to shortening the time required to repair damaged collagen tissue by reconnecting with each other immediately after penetrating the skin.

[0025] The ultra-low molecular weight collagen peptide of the present invention may have a collagen peptide content of 3 to 5% or more with a molecular weight of 180 Da or less, and may be a combination with an average molecular weight of 175 Da, but is not limited thereto. Specifically, the ultra-low molecular weight collagen peptide of the present invention may have a collagen peptide content of 90% or more, 93% or more, or 95% or more with a molecular weight of 180 Da or less, 177 Da or less, 176 Da or less, or 1755 Da or less, and may be a combination of collagen peptides with an average molecular weight of 175 Da, 170 Da to 173 Da, 171 Da, or 172 Da, but is not limited thereto.

[0026] The above ultra-low molecular weight collagen peptide is,

[0027] It is extracted from hibiscus, a plant of the Malvaceae family and the genus Asteraceae, and has skin barrier strengthening, whitening, anti-aging, and antioxidant functions.

[0028] Figure 1 is a graph showing the efficacy of hibiscus as an ultra-low molecular weight collagen peptide of the present invention.

[0029] As a process for manufacturing the ultra-low molecular weight collagen peptide of the present invention,

[0030] (a) Step is to immobilize carboxypeptidase and dipeptidyl-aminopeptidase on a carrier.

[0031] The term "carrier" in the present invention refers to a carrier having a chemical functional group attached to the surface of a gel used in chromatography, or having such a chemical functional group activated. The gel of the present invention may be a silica gel, and the chemical functional group may include one or more selected from epoxy groups, amino groups, carboxyl groups, aldehydes, hydroxyl groups, allyl groups, thiol groups, phenyl groups, sulfonic acid groups, acrylic groups, methacrylic groups, and halogen groups, and specifically may be an aldehyde group, but is not limited thereto.

[0032] The term "enzyme immobilization" in the present invention refers to artificially restricting the mobility of an enzyme using chemical or physical methods. In the present invention, the enzyme is not particularly limited as long as it has proteolytic activity. Specifically, it may be an enzyme having carboxypeptidase activity that degrades the carboxy terminal portion of a protein as a substrate, or an enzyme having aminopeptidase activity that degrades the amino terminal portion of a protein as a substrate. Specifically, the enzyme having aminopeptidase activity may be dipeptidyl-aminopeptidase that degrades into dipeptides, but is not limited thereto.

[0033] In one embodiment of the present invention, an activated silica gel was prepared as a carrier, and carboxypeptidase and dipeptidyl-aminopeptidase enzymes were added to the silica gel at a concentration of 0.5% to 5%, specifically 1% to 4%, and more specifically 15% to 3%, respectively, to immobilize them. The present invention solves the conventional problem of enzymes remaining after the reaction by immobilizing proteolytic enzymes on a carrier, and not only is there no need for a separate additional process to inactivate or remove the remaining enzymes, but the enzymes can also be reused, thus providing economic advantages.

[0034] Step (b) of the present invention is a step of primary enzymatic treatment by mixing collagen with carboxypeptidase immobilized on the carrier.

[0035] In the present invention, the enzyme reaction may be carried out at 45°C to 60°C for 13 to 17 hours, but is not limited thereto.

[0036] After the first enzyme treatment in step (b) above, a step of centrifuging to recover the supernatant may be additionally included, but is not limited thereto.

[0037] Step (b) above may additionally include a freeze-drying step, but is not limited thereto.

[0038] The supernatant of the present invention refers to the clear liquid above the insoluble components, such as precipitates, in a liquid.

[0039] In one embodiment of the present invention, collagen was mixed with a gel immobilized with carboxypeptidase and subjected to an enzymatic reaction. After the enzymatic reaction, the supernatant was recovered by centrifugation, and then the collagen was obtained by freeze-drying.

[0040] Step (c) of the present invention is a step of secondarily enzymatically treating the primary enzymatically treated collagen by mixing it with

[0037] dipeptidyl-aminopeptidase immobilized on the carrier.

[0041] In the present invention, the enzyme reaction may be carried out at 45°C to 60°C for 13 to 17 hours, but is not limited thereto.

[0042] After secondary enzyme treatment in step (c) above, a step of centrifuging to recover the supernatant may be additionally included, but is not limited thereto.

[0043] Step (c) above may additionally include a freeze-drying step, but is not limited thereto.

[0044] In one embodiment of the present invention, freeze-dried collagen was dissolved in purified water and mixed with a gel immobilized with dipeptidyl-aminopeptidase to perform an enzymatic reaction. After the enzymatic reaction, the supernatant was recovered by centrifugation, and then freeze-dried to obtain ultra-low molecular weight collagen peptides.

[0045] It was confirmed that the proportion of low molecular weight collagen peptides produced gradually increased when collagen was not treated with enzymes, when collagen was reacted with a primary enzyme immobilized on a carrier (step (b)), and when collagen was reacted with primary and secondary enzymes (step (c)).

[0046] A dipeptide refers to a peptide composed of two amino acid residues, and collagen produces the dipeptides glycylproline or hydroxyglycylproline as breakdown products. Dipeptides are broken down again into proline or hydroxyproline by the hydrolytic enzyme prolidase, thereby being recycled into collagen and potentially improving skin elasticity.

[0047] In the present invention, the dipeptide content of the ultra-low molecular weight collagen peptide may be about 80% or more, about 83% or more, about 85% or more, or about 86% or more, and the dipeptide may be glycyl-proline, but is not limited thereto.

[0048] As a result of analyzing the ultra-low molecular weight collagen peptide of the present invention, it was confirmed that collagen peptides of 172 Da accounted for 64% and collagen peptides of approximately 1753 Da accounted for 21%, with 951% being 176 Da or less (Fig. 2). As a result of analyzing the above ultra-low molecular weight collagen peptide using GC / MS, it was confirmed that the main peak was glycyl-proline, a dipeptide, and that it accounted for the largest content in the ultra-low molecular weight collagen peptide of the present invention.

[0049] Another aspect of the present invention provides an ultra-low molecular weight collagen peptide prepared by the above method.

[0050] The present invention provides a cosmetic composition comprising an ultra-low molecular weight collagen peptide prepared by the above method as an active ingredient.

[0051] Since the cosmetic composition of the present invention is basically applied to the skin, it can be prepared in any formulation conventionally manufactured by referring to cosmetic compositions in the art. For example, it can be prepared in a formulation selected from the group consisting of solutions, topical ointments, creams, nourishing lotions, softening lotions, packs, emulsions, makeup bases, foundations, essences, soaps, liquid cleansers, bath additives, sun creams, sun oils, suspensions, gels, lotions, powders, surfactant-containing cleansers, patches, and sprays, but is not limited thereto.

[0052] In addition to the ultra-low molecular weight collagen peptide of the present invention, the above cosmetic composition may further include conventional auxiliary agents and carriers such as oxidizing agents, stabilizers, solubilizing agents, vitamins, pigments, fragrances, etc., which are commonly used in cosmetic compositions. For example, the above cosmetic composition may further include auxiliary ingredients such as glycerin, butylene glycol, polyoxyethylene hydrogenated castor oil, tocopheryl acetate, citric acid, panthenol, squalane, sodium citrate, and allantoin.

[0053] The cosmetic composition of the present invention may additionally include one or more cosmetically acceptable carriers that are incorporated into general skin cosmetics, and may appropriately incorporate common ingredients such as oils, water, surfactants, moisturizers, lower alcohols, thickeners, chelating agents, colorants, preservatives, fragrances, etc. The cosmetically acceptable carriers included in the cosmetic composition of the present invention vary depending on the formulation.

[0054] In the case where the formulation of the present invention is an ointment, paste, cream, or gel, animal oil, vegetable oil, wax, paraffin, starch, tracanth, cellulose derivative, polyethylene glycol, silicone, bentonite, silica, talc, zinc oxide, or a mixture thereof may be used as a carrier component.

[0055] When the formulation of the present invention is a powder or a spray, lactose, talc, silica, aluminum hydroxide, calcium silicate, polyamide powder, or a mixture thereof may be used as a carrier component, and in particular, in the case of a spray, it may additionally include a propellant such as chlorofluorohydrocarbon, propane / butane, or dimethyl ether.

[0056] In the case where the formulation of the present invention is a solution or an emulsified liquid, a solvent, a solubilizing agent, or an emulsifying agent is used as a carrier component, such as water, ethanol, isopropanol, ethyl carbonate, ethyl acetate, benzyl alcohol, benzyl benzoate, propylene glycol, 1,3-butyl glycol oil, and in particular, cottonseed oil, peanut oil, corn germ oil, olive oil, castor oil and sesame oil, glycerol aliphatic ester, polyethylene glycol or fatty acid ester of sorbitan may be used.

[0057] In the case where the formulation of the present invention is a suspension, liquid diluents such as water, ethanol, or propylene glycol, ethoxylated isostearyl alcohol, polyoxyethylene sorbitol ester, and polyoxyethylene sorbitan ester, microcrystalline cellulose, aluminum metahydroxide, bentonite, agar, or tracant, etc. may be used as carrier components.

[0058] Meanwhile, when the formulation of the present invention is a capsule, it may be formulated in the form of an alginate capsule, an agar capsule, a gelatin capsule, a wax capsule, or a double capsule, but is not particularly limited thereto.

[0059] In one embodiment of the present invention, it was confirmed that there was cytotoxicity at 10 µg / ml to 200 µg / ml when human fibroblasts were treated with unenzyme-treated collagen, whereas the ultra-low molecular weight collagen peptide of the present invention was confirmed to have no cytotoxicity at 01 µg / ml to 100 µg / ml.

[0060] The cosmetic composition of the present invention is for improving skin wrinkles or elasticity.

[0062] The present invention is not limited to the aforementioned embodiments and can be implemented with various modifications within the scope permissible to the technical concept of the present invention.

Claims

Claim 1 A wrinkle-improving cosmetic using ultra-low molecular weight collagen peptides, characterized by having an ultra-low molecular weight collagen peptide content of 3-5% of collagen peptides with a molecular weight of 180 Da or less and an average molecular weight of 175 Da or less. Claim 2 A wrinkle-improving cosmetic composition using ultra-low molecular weight collagen peptides according to claim 1, wherein the ultra-low molecular weight collagen peptide is extracted from hibiscus, a plant of the genus *Mallow* in the family Malvaceae, and is characterized by having skin barrier strengthening / whitening / anti-aging / antioxidant functions.