KR20220156317A - Method For Preparing Collagen Having Low Molecular Weight Derived From Antler - Google Patents

Abstract

One aspect of the present invention provides a method for manufacturing collagen having a lower molecular weight derived from antler comprising the following steps: reacting the remaining residue after extracting the antler by treating the same with an acid; obtaining a precipitate by treating the acid treatment reaction with a base; and adding a proteolytic enzyme to the precipitate. According to the present invention, antler-derived low molecular weight collagen can be obtained in high purity. In addition, since the antler-derived low molecular weight collagen manufactured by the method has a molecular weight in a lower range than that of conventional antler-derived collagen, there is an advantage in that usability thereof is increased in the manufacture of foods or cosmetics.

Description

Manufacturing method of deer antler-derived low-molecular collagen {Method For Preparing Collagen Having Low Molecular Weight Derived From Antler}

The present invention relates to a method for producing antler-derived low-molecular-weight collagen.

Deer antlers refer to freshly grown antlers of a stag, which are collected, processed, and dried. Every year in mid-March, deer lose their old antlers and start sprouting new ones. Amino acids, calcium phosphate, calcium carbonate, collagen, phospholipids, chondroitin, glucosamine, panthocrine, ganglioside, hyaluronic acid, etc. are known as pharmacologically active ingredients of antler. Deer antlers are especially rich in amino acids, and are known to help keep skin clear and healthy, strengthen immunity, protect the liver, and improve digestive functions.

As such, since antler is a valuable herbal medicine that contains a large amount of various ingredients effective for the human body, research on methods for extracting specific active ingredients of antler is continuously being conducted. According to the currently widely used hot water extraction method, water-soluble components are mainly extracted, protein insoluble precipitation appears, and the obtained extract has a phenomenon of gelation. In addition, when extracted with direct acid treatment such as hydrochloric acid, there is a problem that physiologically active components are easily destroyed and useful components are not sufficient.

Among the pharmacologically active components of deer antler, collagen is a protein found in most animals and is a major protein constituting the flesh and connective tissue of mammals. It is very abundant enough to account for 25% to 35% of the protein that makes up the body. Collagen in the form of thin and long fibers is mainly present in fibrous tissues such as tendons, ligaments, and skin, and also exists in corneas, cartilage tissues, bones, blood vessels, digestive tract, and spinal discs.

Collagen can be divided into high-molecular collagen and low-molecular collagen according to molecular weight. High-molecular collagen generally has a molecular weight of 5,000 Da. It refers to the above, but the higher the molecular weight, the lower the absorption rate in the body, and it is difficult to show functionality. Thus, a molecular weight of 5,000 Da. The above high-molecular collagen is mainly used for general food and the like. On the other hand, low-molecular-weight collagen has a molecular weight of 1,500 Da. The following materials have a high absorption rate in the body, and functionalities such as skin elasticity can be expected. Accordingly, in recent years, the development of health functional foods using low molecular weight collagen having a molecular weight of 2,000 Da or less, such as fish collagen or donkey-derived collagen, has been actively conducted (Patent Document 1).

While continuing research on a method for extracting collagen in the relatively low molecular weight range from deer antler-derived collagen, the present inventors performed acid treatment and base treatment on antler antler flakes and then treated them with proteolytic enzymes to obtain a 15-20 kDa range of collagen. It was confirmed that low-molecular-weight collagen could be obtained with high purity, and the present invention was completed.

Korean Patent No. 10-1841461 (March 19, 2018)

An object of the present invention is to provide a method for obtaining high purity collagen in the low molecular weight range from antler.

One aspect of the present invention is the step of reacting the residue remaining after extracting the antler by treating it with an acid; Obtaining a precipitate by treating the acid treatment reactant with a base; and adding a proteolytic enzyme to the precipitate.

Another aspect of the present invention provides an antler-derived low-molecular-weight collagen prepared according to the above production method.

According to the present invention, low-molecular-weight collagen derived from antler can be obtained in high purity. In addition, since the prepared low-molecular-weight collagen derived from antler has a molecular weight in a lower range than that of conventional collagen derived from antler, there is an advantage in that its usability is increased in the manufacture of foods or cosmetics.

1 is a result confirming that the antler-derived low-molecular-weight collagen prepared according to Preparation Examples 1 to 3 of the present invention has a low molecular weight in the range of 15 to 20 kDa.

Hereinafter, the present invention will be described in detail.

Terms or words used in this specification and claims should not be construed as being limited to ordinary or dictionary meanings, and the inventor may appropriately define the concept of terms in order to explain his or her invention in the best way. It should be interpreted as a meaning and concept consistent with the technical idea of the present invention based on the principle that there is.

1. Preparation of deer antler-derived low-molecular-weight collagen

One aspect of the present invention is the step of reacting the residue remaining after extracting the antler by treating it with an acid; Obtaining a precipitate by treating the acid treatment reactant with a base; and adding a proteolytic enzyme to the precipitate.

Deer antlers are cut and dried young antlers of plum blossoms, daeroks, or deer with thick hair and not yet ossified or slightly ossified. It refers to the horns of males that are evenly covered with hair. Deer antlers that are not keratinized are slightly soft, but in autumn, hard keratinization occurs and the effectiveness of the deer antler decreases, which is called deer antlers.

The antler includes both non-keratinized antler and keratinized antler.

The deer antler is obtained from marok, maehwarok, Siberian daerok, New Zealand jikdeok, reindeer, etc., depending on the place of origin and the type of deer, and these deer antlers can be applied to the present invention without limitation regardless of the type of deer.

Extraction conditions in the extraction of the deer antler may be in accordance with a conventional method, and are not particularly limited. As the extraction method, conventionally known extraction methods such as solvent extraction, ultrasonic extraction, filtration, and reflux extraction may all be used, and preferably, solvent extraction or reflux extraction may be used. The extraction process can be repeated several times. The extract also includes fractions obtained by further fractionating the extract.

At least one selected from the group consisting of water, organic solvents, supercritical fluids, and mixtures thereof may be used as an extraction solvent in the extraction of the antler. The organic solvent is an alcohol, preferably a C1-C4 lower alcohol, hexane (n-hexane), ether, glycerol, propylene glycol, butylene glycol, ethyl acetate, methyl acetate, dichloromethane, chloroform, ethyl acetate, benzene and It may be any one selected from the group consisting of these mixed solvents, preferably water.

The extraction temperature may be performed at 50 °C to 95 °C, or 55 °C to 92 °C, or 60 °C to 90 °C. The extraction time may be performed for 2 hours to 15 hours, or 5 hours to 12 hours, or 7 hours to 10 hours.

In the extraction of the deer antler, water is used as a solvent to extract most of the water-soluble components contained in the deer antler, and proteins, fat-soluble components, and the like remain in the remaining residue. The present invention is characterized in that low molecular weight collagen is obtained in high purity using antler residue.

Separation of the antler extract and the residue may be performed in a conventional manner using a filter or the like. In addition, the method of the present invention may further include drying the residue.

The temperature for drying the residue may be -50°C to 150°C, -30°C to 130°C, -10°C to 125°C, 10°C to 120°C, 50°C to 110°C, or 70°C to 100°C. When the drying temperature range is satisfied, the efficiency of the subsequent hydrolysis process using a proteolytic enzyme may be increased.

The drying time of the residue may be 40 hours to 130 hours, or 50 hours to 125 hours, or 60 hours to 120 hours, or 70 hours to 115 hours, or 80 hours to 110 hours, or 90 hours to 100 hours. When the drying time is satisfied, the efficiency of the subsequent hydrolysis process using a proteolytic enzyme may be increased.

Further, drying of the residue is such that the moisture content of the residue is 80% or less, or 70% or less, or 60% or less, or 50% or less, or 40% or less, or 30% or less, or 25% or less, or 15% or less, or 12% or less, or 9% or less, or 6% or less, or 3% or less. When the moisture content of the residue is controlled within the above range, the efficiency of a subsequent hydrolysis process using a proteolytic enzyme may be increased.

The drying step of the residue as described above may be selectively performed, and when the drying step of the residue is not separately performed, impurities other than collagen may be removed by washing the residue with water using a weak base solution. In addition, a step of pulverizing the residue may be additionally performed to facilitate the separation of collagen in a later step. At this time, pulverization may be performed so that the pulverized residue has a volume of 125 cm ³ or less, 91 cm ³ or less, or 64 cm ³ or less in the form of a hexahedron.

Next, acid is treated and reacted with the residue of the antler. The acid treatment may be performed using one or more acids selected from the group consisting of hydrochloric acid, nitric acid, perchloric acid, sulfuric acid, and acetic acid in a pH range of 2 to 3. During acid treatment, 3 to 20 parts by weight, or 5 to 17 parts by weight, or 7 to 15 parts by weight of an acid solution can be treated compared to antler antler. The concentration of the acid solution may be 0.1 to 3M, or 0.2 to 1.5M, or 0.3 to 1.0M.

The acid treatment reactant may include at least one type of collagen selected from the group consisting of hydroxyproline, hydroxylysine, proline, and glycine. The hydroxyproline and hydroxylysine are major index components of collagen. In the acid treatment reaction, the proportion of the collagen indicator component may be 30 to 70% by weight, or 40 to 60%.

A step of filtering the acid treatment reactant may be additionally performed. The filtration may be performed to obtain particles of 1-15 μm, or 2-10 μm, or 3-7 μm.

Next, a base treatment is performed on the acid-treated reactant. This allows the pH to be adjusted in the range of 5.5 to 7.0, or 5.5 to 6.5, or 5.5 to 6.0. When the above pH range is satisfied, the yield of protein precipitates obtained through base treatment, that is, neutralization, may be excellent.

The base treatment may be performed using at least one base selected from the group consisting of sodium hydroxide, potassium hydroxide, and potassium hydroxide. During the base treatment, 3 to 20 parts by weight, or 5 to 17 parts by weight, or 7 to 15 parts by weight of the base solution compared to the second extract may be treated, and the base solution is 1 to 3M, or 1.5 to 2.5M, 1.7 to It may be a 2.3M concentration.

When the base treatment is performed, a white protein precipitate may be formed. The precipitate thus produced may be separated out by a conventional method such as centrifugation, and optionally, a step of washing or whitening the precipitate may be additionally performed.

Next, the precipitate is dissolved in purified water to obtain an antler-derived collagen solution. At this time, the concentration of the solid content of the antler-derived collagen solution may be 3 to 30 brix%, or 4 to 27 brix%, or 5 to 22 brix%, or 7 to 20 brix%, or 9 to 15 brix%. When the antler-derived collagen solution has a solid concentration within the above numerical range, the efficiency of subsequent hydrolysis using a proteolytic enzyme may be increased.

Thereafter, a proteolytic enzyme is added to the precipitate to obtain low-molecular-weight collagen derived from antler through a hydrolysis reaction.

The proteolytic enzyme may include at least one selected from the group consisting of pancrypsin, FoodPro Alkaline Protease, and ProteAX, but is not limited thereto.

The hydrolysis reaction may be carried out in the range of pH 5.5 to 7.0, or pH 5.5 to 6.5, or pH 5.5 to 6.0. When the pH is less than 5.5, hydrolysis may not be performed well, and when the pH is higher than 7.0, the antler-derived low-molecular-weight collagen produced may not be smoothly filtered.

The hydrolysis reaction may be carried out at 38 to 60 °C, or 40 to 55 °C, or 42 to 53 °C, or 45 to 52 °C. In addition, the hydrolysis reaction may be carried out for 6 to 36 hours, or 12 to 32 hours, or 18 to 28 hours. When the above numerical range is satisfied, it may be easy to obtain antler-derived low-molecular-weight collagen having a desired average molecular weight.

Thereafter, the antler-derived low-molecular-weight collagen is inactivated by reacting at 90° C. or higher for 3 to 10 minutes.

In addition, the method of the present invention may further include filtering the antler-derived low-molecular-weight collagen. The filtration may be performed to obtain particles of 1-15 μm, or 2-10 μm, or 3-7 μm.

By further purifying the antler-derived low-molecular-weight collagen, high-purity antler-derived low-molecular-weight collagen can be obtained. As described above, according to the present invention, high-purity antler-derived low-molecular-weight collagen can be obtained through simple filtration or purification.

The antler-derived low-molecular-weight collagen produced according to the present invention may have an average molecular weight of 25 to 50 kDa or 15 to 20 kDa. The deer antler-derived low-molecular-weight collagen of the present invention has a relatively low molecular weight, so it has a good absorption rate in the body, so it can have excellent functionality such as skin elasticity.

2. Health functional food composition containing low-molecular-weight collagen derived from antler

Since the preparation method of the deer antler-derived low-molecular-weight collagen is the same as that described in " 1. Preparation of the deer-antler-derived low-molecular-weight collagen ", the description thereof is omitted.

The health functional food composition of the present invention may be for improving skin elasticity or preventing skin aging.

The antler-derived low-molecular-weight collagen is preferably contained in an amount of 0.005% to 20.0% by weight based on the total weight of the health functional food, and more preferably in an amount of 0.01% to 10.0% by weight, but is not limited thereto. don't If the effective content of the deer antler-derived low-molecular collagen is less than 0.005% by weight, the effect of improving skin elasticity or preventing skin aging may be insignificant, and if it exceeds 20% by weight, the effect of increasing the efficacy due to the increase in content is reduced, making it uneconomical. to be.

In addition to the antler-derived low-molecular-weight collagen of the present invention, the health functional food preferably contains other ingredients that can give a synergistic effect to the effect of the antler-derived low-molecular collagen within a range that does not impair the desired effect of the present invention. can contain. Conventional adjuvants such as, for example, stabilizers, solubilizers, vitamins, pigments and flavors, or carriers may be included.

In addition, it may include ingredients commonly added during food preparation, and include, for example, proteins, carbohydrates, fats, nutrients, seasonings, and flavoring agents. Examples of such carbohydrates include monosaccharides such as glucose, fructose, and the like; disaccharides such as maltose, sucrose, oligosaccharides and the like; and polysaccharides such as conventional sugars such as dextrins and cyclodextrins and sugar alcohols such as xylitol, sorbitol and erythritol. As the flavoring agent, natural flavoring agent thaumatin, stevia extract, and synthetic flavoring agent may be used. For example, when the health functional food of the present invention is prepared as a drink, citric acid, high fructose corn syrup, sugar, glucose, acetic acid, malic acid, fruit juice, natural extract, etc. may be further included in addition to the low-molecular-weight collagen derived from antler of the present invention.

There is no particular limitation on the type of health functional food. Examples of foods to which the deer antler-derived low-molecular-weight collagen of the present invention can be added include meat, sausages, bread, chocolates, candies, snacks, confectionery, pizza, ramen, other noodles, gums, dairy products including ice creams, various soups, and beverages , tea, drinks, alcoholic beverages and vitamin complexes, and includes all health functional foods in a conventional sense.

3. Cosmetic composition containing deer antler-derived low-molecular-weight collagen

Since the preparation method of the deer antler-derived low-molecular-weight collagen is the same as that described in " 1. Preparation of the deer-antler-derived low-molecular-weight collagen ", the description thereof is omitted.

The cosmetic composition of the present invention may be for improving skin elasticity or preventing skin aging.

The antler-derived low-molecular-weight collagen is 0.01% to 50% by weight, or 0.1% to 45% by weight, or 1% to 40% by weight, or 1% to 20% by weight, based on 100% by weight of the cosmetic composition, or It may be included in an amount of 1.5% to 15% by weight. When the content of the antler-derived low-molecular collagen in the cosmetic composition is less than 0.001% by weight, the effect of improving skin elasticity or preventing skin aging by the antler-derived low-molecular collagen may be low, and when it exceeds 60% by weight, the cost increases. The degree of improvement of the effect may not be high.

The cosmetic composition of the present invention may be prepared in liquid or solid form using bases, adjuvants and additives commonly used in the field of cosmetics. Cosmetics in liquid or solid form may include, but are not limited to, forms such as lotion, cream, lotion, and bath, for example. Bases, adjuvants and additives commonly used in the field of cosmetics are not particularly limited, and examples thereof include water, alcohol, propylene glycol, stearic acid, glycerol, cetyl alcohol, and liquid paraffin.

The cosmetic composition of the present invention may include not only the deer antler-derived low-molecular-weight collagen, but also components commonly used in cosmetic compositions, for example, antioxidants, stabilizers, solubilizers, conventional adjuvants such as vitamins, pigments and flavors, and carriers. can include

The cosmetic composition of the present invention may be prepared in any formulation commonly prepared in the art, for example, solution, suspension, emulsion, paste, gel, cream, lotion, powder, soap, surfactant-containing cleansing , It may be formulated as an oil, powder foundation, emulsion foundation, wax foundation and spray, but is not limited thereto. More specifically, it may be prepared in the form of softening lotion, nourishing lotion, nourishing cream, massage cream, essence, eye cream, cleansing cream, cleansing foam, cleansing water, pack, spray or powder.

When the formulation of the cosmetic composition of the present invention is a paste, cream or gel, animal oil, vegetable oil, wax, paraffin, starch, tracanth, cellulose derivative, polyethylene glycol, silicone, bentonite, silica, talc, zinc oxide, etc. this can be used

When the formulation of the cosmetic composition of the present invention is a powder or spray, lactose, talc, silica, aluminum hydroxide, calcium silicate or polyamide powder may be used as a carrier component, and in particular, in the case of a spray, additional chlorofluorohydro It may contain a propellant such as carbon, propane/butane or dimethyl ether.

When the formulation of the cosmetic composition of the present invention is a solution or emulsion, a solvent, solubilizing agent or 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-butylene glycol oil, glycerol aliphatic esters, polyethylene glycol or fatty acid esters of sorbitan.

When the formulation of the cosmetic composition of the present invention is a suspension, as a carrier component, a liquid diluent such as water, ethanol or propylene glycol, an ethoxylated isostearyl alcohol, a suspending agent such as polyoxyethylene sorbitol ester and polyoxyethylene sorbitan ester , microcrystalline cellulose, aluminum metahydroxide, bentonite, agar or tracanth, and the like can be used.

When the formulation of the cosmetic composition of the present invention is surfactant-containing cleansing, as carrier components, aliphatic alcohol sulfate, aliphatic alcohol ether sulfate, sulfosuccinic acid monoester, imidazolinium derivative, methyl taurate, sarcosinate, fatty acid amide ether Sulfates, alkylamidobetaines, fatty alcohols, fatty acid glycerides, fatty acid diethanolamides, vegetable oils, lanolin derivatives, or ethoxylated glycerol fatty acid esters may be used.

The cosmetic composition of the present invention may be used alone or overlappingly applied, or may be used overlappingly with other cosmetic compositions other than the present invention. In addition, the cosmetic composition according to the present invention can be used according to a conventional method of use, and the number of times of use can be varied according to the user's skin condition or taste.

When the cosmetic composition of the present invention is a soap, surfactant-containing cleansing or surfactant-free cleansing formulation, it may be applied to the skin and then wiped off, removed, or washed with water. As specific examples, the soap is liquid soap, powder soap, solid soap, and oil soap, the surfactant-containing cleansing formulation is a cleansing foam, cleansing water, cleansing towel, and a cleansing pack, and the surfactant-free cleansing formulation is a cleansing cream. , cleansing lotion, cleansing water and cleansing gel, but are not limited thereto.

Hereinafter, the present invention will be described in detail by production examples and examples.

However, the following Preparation Examples and Examples are only for exemplifying the present invention, and the contents of the present invention are not limited by the following Preparation Examples and Examples.

Preparation Example 1. Preparation of deer antler-derived low-molecular-weight collagen

1-1. Manufacture of dried deer antler foil

After pulverizing the raw material of the deer antler, water was added 8 times based on the weight of the raw material and extracted at 85° C. for 7 hours. Water was added 6 times to the residue remaining after extraction, and extraction was further performed at 85° C. for 5 hours. The residue generated after two extractions was dried with hot air at 70°C for 90 hours. The moisture content of the dried deer antler foil was approximately 4%.

1-2. Preparation of deer antler-derived collagen

500 g of the dried deer antler foil was put in an extractor, 5 kg of 0.5 N hydrochloric acid was added, and extraction was performed twice at 30 ° C for 4 hours. 4 L of the extract obtained as described above was filtered using a 5 μm sieve filter, and an appropriate amount of 2M sodium hydroxide was added to the filtrate to neutralize the pH to a pH in the range of 5.5 to 6.0.

The white precipitate produced during neutralization was separated by centrifugation at 3000 g for 20 minutes, washed with water, and centrifuged again to obtain a precipitate. 1% H ₂ O ₂ was added to the precipitate twice, whitened while stirring for about 10 hours, and centrifuged at 3000g for 20 minutes to obtain a precipitate. The precipitate was dissolved while adding purified water to obtain a antler collagen solution having a concentration of 10 brix%.

1-3. Preparation of deer antler-derived low-molecular-weight collagen

The pH of the antler collagen solution was adjusted to be in the range of 5.5 to 6.0. Thereafter, 0.1% of pancrypsin was added as a proteolytic enzyme, reacted at 50° C. for 24 hours, and then reacted at 90° C. or higher for 5 minutes to inactivate it. After filtering using a 5 μm sieve filter, the mixture was dried at room temperature to obtain 114 g of antler-derived low-molecular-weight collagen powder.

Production Example 2 and Production Example 3

Deer antler-derived low-molecular-weight collagen was prepared in the same manner as in Preparation Example 1, except that 0.1% of Alkaline Protease (Vision Biochem) and 0.1% (Danisco) were used as proteolytic enzymes, respectively.

Experimental Example 1. Confirmation of molecular weight of deer antler-derived low molecular weight collagen

In order to confirm the molecular weight of the antler-derived low-molecular-weight collagen obtained in Preparation Example 1, samples were prepared as shown in Table 1 below.

lane sample One protein markers 2 Untreated group* 3 Preparation Example 1 4 Preparation Example 2 5 Preparation Example 3

* Untreated group: powder prepared from the antler collagen solution of Preparation Example 1-2

For SDS-PAGE to confirm molecular weight, running gels containing 12% polyacrylamide and 0.1% SDS and stacking gels containing 4% polyacrylamide and 0.1% SDS were used. 100 μg of the antler-derived low-molecular-weight collagen was loaded onto the gel, subjected to electrophoresis at 100 volts, and then stained with Coomassie blue to confirm a protein band. The results are shown in FIG. 1 .

From the results of FIG. 1, it can be seen that the molecular weight of the antler-derived low-molecular-weight collagen of Preparation Examples 1 to 3 was 15 to 20 kDa, and the band moved to a lower molecular weight range than that of the untreated group (25 to 50 kDa). In particular, in the case of Preparation Example 2 using 0.1% of Food Pro alkaline protease as a proteolytic enzyme, it can be seen that a band in the low molecular weight range is clearly obtained. Due to the correlation between the proportion of protein components derived from antler and the proteolytic activity of the Foodpro alkaline protease 0.1% enzyme, in the case of Preparation Example 2, it seems that collagen in the lower molecular weight range was obtained.

Manufacturing Example 4. Manufacture of health functional food

4-1. Manufacture of Flour Food

0.5 to 5.0 parts by weight of the deer antler-derived low-molecular-weight collagen of the present invention was added to wheat flour, and bread, cakes, cookies, crackers, and noodles were prepared using the mixture.

4-2. Manufacture of health drinks

Instantaneous sterilization by homogeneously blending sub-materials such as high fructose (0.5%), oligosaccharide (2%), sugar (2%), salt (0.5%), and water (75%) and 5 g of the low-molecular-weight collagen derived from the antler of the present invention. After that, it was prepared by packaging it in a small container such as a glass bottle or a plastic bottle.

4-3. Preparation of vegetable juice

Vegetable juice was prepared by adding 5 g of the antler-derived low-molecular-weight collagen of the present invention to 1,000 ml of tomato or carrot juice.

4-4. manufacture of fruit juice

1 g of the antler-derived low-molecular-weight collagen of the present invention was added to 1,000 ml of apple or grape juice to prepare fruit juice.

Preparation Example 5. Preparation of cosmetic composition

5-1. Preparation of Essence

Using the antler-derived low-molecular-weight collagen of the present invention, an essence was prepared according to the contents (parts by weight) shown in Table 2 below.

Raw material Content (parts by weight) triethanolamine 0.25 carboxyvinyl polymer 0.22 glycerin 4 1,3-butylene glycol 2 Deer antler-derived low-molecular collagen 1.5 beeswax 0.5 Cetostearyl Alcohol One Glyceryl Monostearate One squalene 4 Purified water balance Sum 100

5-2. Manufacture of softening lotion

Softening lotion containing the antler-derived low-molecular-weight collagen as an active ingredient of the present invention was prepared as shown in Table 3 below.

Raw material Content (parts by weight) 1,3-butylene glycol 1.00 Disodium EDT 0.05 allantoin 0.10 dipotassium glycyrrhizate 0.05 Citric Acid 0.01 sodium citrate 0.02 glycereth-26 1.00 Arbutin 2.00 PEG-40 Hydrogenated Castor Oil 1.00 ethanol 30.00 Deer antler-derived low-molecular collagen 0.5 coloring agent a very small amount flavoring agent a very small amount Purified water balance Sum 100

5-3. Manufacture of nourishing cream

Nutritional cream containing the antler-derived low-molecular-weight collagen as an active ingredient of the present invention was prepared according to the composition shown in Table 4 below.

Raw material Content (parts by weight) 1,3-butylene glycol 7.0 glycerin 1.0 D-panthenol 0.1 Magnesium aluminum silicate 0.3 PEG-40 Stearate 1.2 Stearic Acid 2.0 polysorbate 60 1.5 Lipophilic Glyceryl Stearate 2.0 Sorbitan sesquioleate 1.5 Cetearyl Alcohol 3.0 mineral oil 4.0 squalene 3.8 Deer antler-derived low-molecular collagen 1.5 vegetable oil 1.8 dimethicone 0.4 dipotassium glycyrrhizate a very small amount allantoin a very small amount sodium hyaluronate a very small amount Tocopheryl Acetate Appropriate amount triethanolamine Appropriate amount flavoring agent Appropriate amount Purified water balance Sum 100

5-4. manufacture of lotion

A lotion containing the antler-derived low-molecular-weight collagen of the present invention as an active ingredient was prepared according to the composition shown in Table 5 below.

Raw material Content (parts by weight) Cetostearyl Alcohol 1.6 stearic acid 1.4 Glycerin lipophilic monostearate 1.8 PEG-100 Stearate 2.6 Sorbital Sesquioleate 0.6 squalene 4.8 macadamia oil 2 jojoba oil 2 Tocopherol Acetate 0.4 Methylpolysiloxane 0.2 Tocopherol Acetate 0.4 1,3-butylene glycol 4 xanthan gum 0.1 glycerin 4 d-pandenol 0.15 Deer antler-derived low-molecular collagen 1.0 allantoin 0.1 Carbomer (2% aq. Sol) 4 triethanolamine 0.15 ethanol 3 Purified water balance Sum 100

Claims (11)

Reacting the remaining residue after extracting the antler by treating it with an acid;
Obtaining a precipitate by treating the acid treatment reactant with a base; and
A method for producing antler-derived low-molecular-weight collagen comprising adding a proteolytic enzyme to the precipitate. The method of claim 1,
The acid treatment reactant is a method for producing low molecular weight collagen containing 30 to 70% by weight of hydroxyproline and hydroxylysine. The method of claim 1,
The precipitate is a method for producing low molecular weight collagen having an average molecular weight of 25 to 50 kDa. The method of claim 1,
The antler-derived low-molecular-weight collagen is a method for producing low-molecular collagen having an average molecular weight of 15 to 20 kDa. The method of claim 1,
The proteolytic enzyme is a method for producing low-molecular-weight collagen comprising at least one selected from the group consisting of pancrypsin, FoodPro Alkaline Protease, and ProteAX. The method of claim 1,
The base treatment is a method for producing low molecular weight collagen to neutralize so that the pH is in the range of 5.5 to 6.0. The method of claim 1,
A method for producing low-molecular-weight collagen in which a hydrolysis reaction is performed at 45 to 52 ° C. after the addition of the proteolytic enzyme. The method of claim 1,
A method for producing low-molecular-weight collagen in which a hydrolysis reaction is performed in the pH range of 5.5 to 6.0 after the addition of the proteolytic enzyme. The method of claim 1,
A method for producing low-molecular-weight collagen, further comprising filtering or purifying the antler-derived low-molecular-weight collagen obtained by hydrolysis after the addition of the proteolytic enzyme. A health functional food composition for improving skin elasticity or preventing skin aging, comprising the antler-derived low-molecular-weight collagen prepared by the method of any one of claims 1 to 9. A cosmetic composition for improving skin elasticity or preventing skin aging, comprising the antler-derived low-molecular-weight collagen prepared by the method of any one of claims 1 to 9.

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