Collagen gel with congelation state

[0023] The present invention will be described below in conjunction with embodiments.

[0024] Collagen, also known as collagen, is a helical fibrous protein twisted by three peptide chains. After the collagen is hydrolyzed, the triple helix structure of collagen is completely loosened and becomes 3 free peptide chains. The non-helical terminal peptides of the collagen peptide chain include the N-terminal peptide and the C-terminal peptide. The C-terminal represents the carboxyl terminal and the N-terminal represents the amino terminal. In the application technology of collagen, some remove the telopeptide of collagen, that is, atelopeptide, and some retain the telopeptide of collagen. There are many types of collagen, such as Ⅰ, Ⅱ, Ⅲ, Ⅴ, Ⅸ, Ⅺ, Ⅻ, Ⅷ, etc. In the embodiment of the present invention, type I collagen and/or type I collagen hydrolysate are selected; atelopeptide type I collagen and/or atelopeptide type I collagen hydrolysate.

[0025] Type I collagen is the most abundant and widely distributed in organisms, accounting for more than 85% of all discovered collagen. Its related products have been widely used in the fields of biomaterials and biomedicine. Type I collagen is a fibrous collagen, white, transparent, and unbranched. The molecule is thin rod-shaped, with a length of 280nm, a diameter of 1.5nm, and a relative molecular weight of 300kDa. It is composed of two α1(Ⅰ) chains and one α2(Ⅰ) chain. Sometimes two α chains overlap each other to form a β chain, or three α chains overlap each other to form a γ chain. Therefore, it can be said that the collagen molecule is composed of three α chains, or one α chain and one β chain, or collagen is composed of one γ chain composition. There are about 1,000 amino acid residues on each α chain that make up a collagen molecule. The "Gly-XY" polypeptide fragment is its repeating unit and constitutes the basic unit of collagen. These three peptide chains form the unique collagen molecule through hydrogen bonds. Three-strand left-handed spiral rod-like structure. When many collagen molecules are together, the polar regions in one molecule and the non-polar regions in another molecule have electrostatic attraction to each other, causing them to aggregate with each other in a longitudinal dislocation manner, and the collagen molecules remain stable.

[0026] A collagen gel with a frozen state, which is characterized by comprising an aqueous collagen solution, the collagen being type I collagen and/or type I collagen hydrolysate, and the collagen aqueous solution can freeze as the temperature decreases In a semi-solid form, it is frozen. The temperature range at which the collagen aqueous solution is frozen is 0°C to 20°C. The weight content of collagen in the collagen aqueous solution is 0.1%-4%. The weight content of collagen in the collagen aqueous solution is 0.5%-2%. The type I collagen is the ateloceptide type I collagen after the ateloceptide treatment; the type I collagen hydrolysate is the atelopeptide type I collagen hydrolysate. The "Gly-X-Y" polypeptide fragment in the collagen molecule of the collagen is the repeating unit of the collagen molecule, that is, the "Gly-X-Y" polypeptide fragment constitutes the basic unit of the collagen molecule. The collagen is one of natural collagen or recombinant human type I collagen; the natural collagen is extracted from animal skin or animal Achilles tendon of pigs, cattle, sheep or horses.

[0027] The water is selected from one or more of the following substances: distilled water; deionized water; purified water; mineral water; the collagen aqueous solution includes a humectant and/or preservative; the humectant is selected from the following One or more of the substances: glycerin; sodium PCA; sodium hyaluronate; ethylene glycol; propylene glycol; 1,3-butanediol; rupa gum; rupa oil; the preservative is selected from the following substances One or more of: methyl paraben; ethyl paraben; propyl paraben; potassium sorbate; Gema BP; DMDM ​​hydantoin; imidazolidinyl urea; phenoxyethanol; p-hydroxyl Sodium benzoate. The collagen aqueous solution includes drugs or chemical components that promote epidermal growth and repair, ceramide or EGF epidermal growth factor, so as to increase the effect of the product in skin repair. The collagen is extracted from animal skin or animal Achilles tendon of pigs, cattle, sheep or horses, and the extraction methods include degreasing, enzymatic hydrolysis, salting out and dialysis purification.

[0028] A collagen gel with a frozen state, which is composed of atelocollagen type I collagen and/or a hydrolysate of atelocollagen type I collagen, preservatives and water. It is frozen at 0-20°C. It is a clear and transparent liquid between 21°C and 42°C; collagen is used as an effective ingredient in skin care cosmetics for moisturizing the epidermis and anti-wrinkle. The concentration of collagen ranges from 0.1% to 4%; the collagen is characterized in that the collagen is one of natural collagen or recombinant human type I collagen; wherein the natural collagen is extracted from The skin or Achilles tendon of pigs, cattle, sheep, horses and other animals are atelocollagen obtained through enzymatic hydrolysis, dialysis purification and other processes; collagen from animal skins and a small amount of type III collagen. The gel uses collagen as the body, and can add a moisturizing agent to increase the moisturizing effect of the gel. The moisturizer is selected from glycerin, PCA sodium, sodium hyaluronate, ethylene glycol, propylene glycol, 1,3-butane One or more of humectants such as alcohol, luba gum and luba oil. The humectant does not affect its freezing properties at 0-20°C. The water is selected from at least one of distilled water, deionized water, purified water and mineral water. The preservative is selected from methyl paraben, ethyl paraben, propyl paraben, potassium sorbate, Gema BP, DMDM ​​hydantoin, imidazolidinyl urea, phenoxyethanol, and p-hydroxyl One or more of sodium benzoate. The product can be packaged in glass ampoules, plastic bottles or other cosmetic packaging as medical devices or cosmetics and applied to the user's skin, allowing the user to receive the effects of epidermal repair and skin anti-wrinkle.

[0029] It is pointed out here that the above description is helpful for those skilled in the art to understand the invention, but it does not limit the protection scope of the invention. Any implementation of equivalent replacements, modifications and/or deletions of the above description without departing from the essential content of the present invention shall fall within the protection scope of the present invention.