KR102100866B1 - Manufacturing method of pig skin collagen using natural proteinase solution - Google Patents

Abstract

The present invention relates to a method for effectively producing a collagen protein derived from livestock products, and more particularly, to a method for producing low molecular weight water-soluble collagen (soluble collagen) from pig skin using a natural protease solution. The method for extracting collagen from donpi of the present invention can effectively manufacture low molecular weight water-soluble collagen from donpi when using a specific combination of natural protease solution with optimized treatment conditions, and various industrial fields (food , Medicine, cosmetics, etc.). In particular, the natural protease solution used in the present invention is a natural enzyme, unlike the chemical enzyme used in the conventional collagen extraction, is harmless to the human body, and the collagen produced therefrom has a safe advantage when used in food or cosmetics.

Description

Production method of pig skin collagen using natural protease solution {Manufacturing method of pig skin collagen using natural proteinase solution}

The present invention relates to a method for effectively producing a collagen protein derived from livestock products, and more particularly, to a method for producing low molecular weight water-soluble collagen (soluble collagen) from pig skin using a natural protease solution.

Collagen is a structural protein that forms the structure of tissues distributed throughout biological tissues, such as shells, cartilage, bones, ligaments, blood vessels, fascia of mammals and other marine animals, rodents and birds. The most important function of collagen in vivo is mucopolysaccharide, which consists of a polymer matrix with chondroitin sulfate and maintains a specific structure of each organ. Although it differs in molecular weight or content with other mucopolysaccharides, it is the same tissue in mammals. In the same form and proportions exist.

In particular, about 20% of the protein is contained in our body, of which 30% is collagen (L.C.Junqueira and J.carneiro1983). Collagen is the same in other animals, so it is also contained in bones and skin of cattle, pigs, chickens, and fish. Currently, such collagen is used in various products ranging from health foods to cosmetics and medicines.

Collagen is a protein, so when consumed in food, it is broken down into amino acids in the body and resynthesized into various proteins as needed. For this reason, even if you consume collagen from food, it is not necessarily that it remains collagen in your body. However, according to a recent study, it is known that when collagen is ingested, the metabolism of collagen is improved and the probability of being synthesized into collagen increases again. Therefore, in order to maintain the health of the skin, bones, and joints, it is recommended that the research site actively ingest collagen from food. Ingestion and supplementation of collagen stops aging and gives the skin shine and elasticity.

On the other hand, collagen is divided into two types: water-soluble collagen (or soluble collagen) that is soluble in water and insoluble collagen that is insoluble in water. And wrinkles increase. Soluble collagen can be extracted with acids from connective tissues, such as the skin of young animals, but in this case there is also a safety problem and also a small and expensive problem.

Under this background, the present inventors studied to derive a method capable of extracting and preparing low molecular weight water-soluble collagen effective for ingestion or skin penetration from the body, and as a result, natural proteolytic enzyme solution in a specific combination with optimized treatment conditions. In the case of using, the present invention was completed by confirming that low molecular weight water-soluble collagen derived from donpi can be effectively produced.

Korean Registered Patent No. 10-1361060

Accordingly, an object of the present invention is to provide a method for effectively producing collagen in donpi.

Another object of the present invention is to provide donpi collagen prepared by the above method.

Another object of the present invention is to provide a composition comprising the donpi collagen as an active ingredient.

In order to achieve the object of the present invention as described above,

The present invention comprises the steps of: (a) putting the pig skin in a pressure extractor and extracting it for 4-8 hours at 60-100 ° C; And (b) hydrolyzing the protease extract after treating the protease solution with natural protease.

In one embodiment of the present invention, step (a) can be put in a pressure extractor in a pressure extractor and extracted at 80 ° C. for 8 hours.

In one embodiment of the present invention, the natural protease solution may be one or more juices selected from the group consisting of kiwi, pineapple and figs.

In one embodiment of the present invention, the natural protease solution may be a mixed juice of two kinds of pineapple and fig.

In one embodiment of the present invention, the mixed juice solution may be a juice solution in which pineapple and figs are mixed in a weight ratio of 2: 1.

In addition, the present invention provides a donpi collagen prepared by the above method.

In addition, the present invention provides a composition comprising the donpi collagen as an active ingredient.

In one embodiment of the present invention, the composition may be a food composition, a pharmaceutical composition or a cosmetic composition.

The method for extracting collagen from donpi of the present invention can effectively manufacture low molecular weight water-soluble collagen from donpi when using a specific combination of natural protease solution with optimized treatment conditions, and various industrial fields (food , Medicine, cosmetics, etc.). In particular, the natural protease solution used in the present invention is a natural enzyme, unlike the chemical enzyme used in the conventional collagen extraction, is harmless to the human body, and the collagen produced therefrom has a safe advantage when used in food or cosmetics.

1 is an electrophoresis photograph showing the molecular weight pattern of donpi collagen extracted by the method of the present invention (S: Standard, Con: Control, T15: Papain, T16: Kiwi, T17: Pineapple, T18: Fig, T19: Leek, T20 : Pepper, T21: ginger).

The present invention relates to a method for producing donpi collagen.

The method for producing collagen derived from donpi of the present invention comprises the steps of (a) putting the donpi into a pressure extractor and extracting it at 60 to 100 ° C. for 4 to 8 hours; And (b) treating the protease extract with a natural protease solution, followed by hydrolysis.

The step (a) of the present invention is a step of putting the donpi into a pressure extractor and extracting it, and in detail, it may be a step of putting the donpi into a pressure extractor and extracting it at 60 to 100 ° C. for 4 to 8 hours, preferably a pressure extractor. It can be added to the pig skin and extracted at 80 ° C for 8 hours.

In the following examples of the present invention, as a result of examining the water-soluble collagen content using a freeze-dried product of a donpi extract obtained at various temperature and time conditions as a sample, it showed a remarkably high water-soluble collagen content in a treatment extracted at 80 ° C for 8 hours.

Step (b) of the present invention is a step of hydrolyzing the donpi extract, and in detail, is a step of hydrolyzing the donpi extract obtained through the step (a) by treating the natural protease solution.

In one embodiment of the present invention, the natural protease solution may be one or more juice juices selected from the group consisting of kiwi, pineapple and figs, preferably a mixed juice juice of two pineapples and figs.

In another embodiment of the present invention, the mixed juice solution may be a juice solution in which pineapple and figs are mixed in a weight ratio of 2: 1.

The juice of the present invention can be used to extract the obtained fruit by removing the peel and seeds of the target fruit, followed by filtration, or, by crushing the target fruit and adding 2 times distilled water to homogenize it and filtering. After centrifugation, only the supernatant can be taken and used.

In the following examples of the present invention, water-soluble collagen produced by treating natural proteolytic enzymes derived from various fruits (kiwi, pineapple, figs) or vegetables (ketchup, red pepper, ginger) to the donpi extract obtained through step (a) above As a result of measuring the content and molecular weight of collagen, the decomposition effect was better in fruits than in vegetables. In addition, it was confirmed that the water-soluble collagen content was significantly increased in the treatment mixture of pineapple and fig 2: 1 in the enzyme solution in which two or more of these fruit juices were mixed.

In addition, the present invention provides a donpi collagen prepared by the above method.

The donpi collagen produced by the method of the present invention has a low molecular weight with a molecular weight of 130 kD or less, and has a feature of containing a large amount of water-soluble collagen.

Water-soluble collagen having a low molecular weight as described above is excellent in the absorption rate and skin permeability in the body, health functional food products; Cosmetics such as cream, latex, and lotion; It can be useful as a material for medicines such as regeneration patches.

In addition, the present invention provides a composition comprising the donpi collagen as an active ingredient.

In one embodiment of the invention, the composition may be a food composition, pharmaceutical composition or cosmetic composition.

Hereinafter, the present invention will be described in more detail through examples. These examples are intended to illustrate the present invention more specifically, but the scope of the present invention is not limited to these examples.

< Example >

Preparation of disclosure materials

The ox, crucible, cow head, chicken feet, and donpi used in the experiment were all supplied from Hansalim livestock.

< Example  1>

Investigation of ingredients and characteristics of 5 livestock products

In this experiment, the general components, storage characteristics, and collagen content of extracts obtained from 5 livestock products (cow, cow, crucible, donpi, chicken feet) were investigated. To this end, extraction (100 ° C, 12H, no pressure) was performed using a full-automatic pressure extractor (Gyeongseo ENP Co., Ltd., model name KS220S). The extract was extracted by putting 1 kg of raw meat and 5 L of water into a fully automatic pressure extractor.

T1 T2 T3 T4 T5 Woo Crucible Cow head Chicken feet Don blood

<1-1> General ingredients

Analysis of the general components of the sample extracts for each treatment group measured moisture, protein, fat and ash (%) according to the AOAC method (1990), and the results are shown in Table 1 below.

General ingredients (%) of extracts extracted from raw meat Treatment T1 T2 T3 T4 T5 moisture 98.24
± 0.11 ^b 98.20
± 0.00 ^b 98.90
± 0.00 ^a 98.27
± 0.11 ^b 95.56
± 0.05 ^c Fat 0.01
± 0.00 ^c 0.07
± 0.00 ^b 0.17
± 0.00 ^a 0.02
± 0.00 ^c 0.02
± 0.00 ^c Ash 0.04
± 0.00 ^d 0.09
± 0.00 ^a 0.08
± 0.00 ^b 0.06
± 0.00 ^c 0.08
± 0.00 ^b protein 1.70
± 0.11 ^b 1.62
± 0.00 ^b 0.83
± 0.00 ^c 1.63
± 0.11 ^b 4.32
± 0.05 ^a T1: Woori, T2: Crucible, T3: Cow head, T4: Chicken feet, T5: Donpi
^{a- d} There are significant differences in the number of heads in each treatment section (p <0.05).

<1-2> Chemical properties

The pH was measured by taking a sample of 10 g and homogenizing it with a stomacher (400 lab blender, seward, London, England) for 30 seconds with 100 ml of distilled water and measuring it with a pH-meter (WTW pH 720, Germany). The repetition was averaged in 3 iterations.

For volatile basic nitrogen (VBN), 90 ml of distilled water was added to 10 g of the sample using the method of 高 坂 (1975), homogenized for about 30 seconds at 10,000 rpm, and the homogenate was added to Whatman No. 2 Filter paper was used to filter, 3 ml of the filtrate was placed in the outer chamber of the Conway unit, and 1 ml of 0.01 N boric acid solution and 3 drops of indicator (0.066% methyl red + 0.066% bromocresol green) were added to the inner chamber. Glycerine was applied to the adhesive portion with the lid, the lid was closed, and then 1 ml of 50% K2CO3 was injected into the outer chamber, immediately sealed, and then the vessel was horizontally stirred and incubated at 37 ° C for 120 minutes. After incubation, the borate solution in the boudoir was titrated with 0.02NH ₂ SO ₄ . The value of volatile basic nitrogen (VBN) was expressed in terms of mg (mg%) per 100 g sample.

VBN = ((a-b) * F * 28.014 * 100) / Amount of sample

-a: amount of sulfuric acid injected (ml)

-b: amount of sulfuric acid injected in the blank (ml)

-f: 0.02NH ₂ SO ₄ standardization index

-28.014 = 0.02NH ₂ SO ₄ 1ml The amount of N needed to consume

Fatty acid dominance (TBA, 2-thiobarbituric acid) was expressed as TBA (2-thiobarbituric acid) by slightly modifying the extraction method of Witte et al. (1970) .In 10 g of sample, 15 ml of cold 10% perchloric acid and 25 ml of tertiary distilled water were added. Homogenize and homogenize for 10 seconds at 10,000 rpm. The homogenate is whatman No. 2 Filtered using filter paper, 5 ml of filtrate and 5 ml of 0.02M thiobarbituric acid (TBA) solution were mixed thoroughly, and then allowed to stand for 16 hours in a cool dark place using Spectrophotometer (DU-650, Beckman, USA) to 529nm Absorbance at the wavelength of was measured. As the blank, tertiary distilled water was used. TBA values were expressed as mg malonaldehyde / mg malonaldehyde / kg per 1,000 g of sample. The standard curve used was y = 0.1975x-0.0011 (r = 0.999), and y = absorbance and x = TBA value were calculated.

The detailed results are shown in Table 3 below.

Chemical Characteristics of Extracts Extracted from Raw Meat Treatment T1 T2 T3 T4 T5 pH 7.52
± 0.04 ^a 7.25
± 0.03 ^c 6.31
± 0.07 ^d 7.36
± 0.04 ^b 7.55
± 00 ^a VBN
(mg%) 8.59
± 0.54 ^c 9.05
± 0.27 ^c 11.34
± 0.57 ^b 9.17
± 0.96 ^c 13.45
± 0.47 ^a TBA
(mg malonaldehyde / 1,000 g) 0.23
± 0.00 ^c 0.17
± 0.05 ^c 0.19
± 0.03 ^c 0.63
± 0.05 ^b 1.57
± 0.16 ^a T1: Woori, T2: Crucible, T3: Cow head, T4: Chicken feet, T5: Donpi
^{a- e} There is a significant difference in the number of heads in each treatment section (p <0.05).

As shown above, in the case of 5 kinds of livestock products used in this experiment (cow head, oxen, crucible, pig skin, chicken feet), it was confirmed that pH, VBN and TBA values were safe tolerances for use as food.

<1-3> Collagen content

To measure the collagen content of the sample for each treatment group, add about 4 g of sample to the Erlenmeyer flask, add 30 ml of sulfuric acid solution, cover the lid, and heat it for 16 hours in a 105 ° C dry oven into a 500 ml volume flask. Diluted with tertiary distilled water and homogenized to obtain Whatman No. 2 Filtered using a φ150mm filter paper. After adding 5 ml of the filtrate and diluting to 100 ml, add 2 ml of the diluent to the test tube, add 1 ml of the oxidant solution, shake it, and leave it at room temperature for 20 minutes. Then, after adding and mixing 1 ml of color reagent to each test tube, soak it in a water bath at 60 ° C for 15 minutes, cool it in running water for 3 minutes or more, and use a Spectrophotometer to measure a fixed wavelength (absorbance) at 558 nm. It was measured. The standard curve was analyzed for collagen content (g / 100g) by applying 2 ml of a working standard solution to the absorbance after color development and measurement, and then substituting it into a regression equation.

The detailed results are shown in Table 4 below.

Collagen content of extract extracted from raw meat Treatment T1 T2 T3 T4 T5 Collagen (g / 100g) 1.79
± 0.03 ^a 1.14
± 0.01 ^d 1.74
± 0.00 ^b 1.66
± 0.00 ^c 1.82
± 0.00 ^a Water soluble collagen 0.25
± 0.02 ^a 0.17
± 0.00 ^b 0.12
± 0.02 ^b 0.16
± 0.01 ^b 0.15
± 0.01 ^b T1: Woori, T2: Crucible, T3: Cow head, T4: Chicken feet, T5: Donpi
^{a- d} There are significant differences in the number of heads in each treatment section (p <0.05).

As shown above, among the five livestock products used in this experiment (cow head, ox, crucible, donpi, chicken feet), the donpi showed the highest collagen content, and the ox group showed the highest water-soluble collagen content.

As a result of comprehensively examining the contents of collagen and water-soluble collagen, it was confirmed that the oxtail showed a somewhat higher water-soluble collagen content compared to donpi, but because the difference was not so great, it was judged that donpi is a useful material for collagen extraction in terms of price and efficiency of the material. .

< Example  2>

Development of optimal extraction method for collagen

In this experiment, the optimal extraction conditions for obtaining collagen from donpi among livestock products were identified. To this end, extraction (65 to 100 ° C, 4 to 12H, no pressure) was performed using a full-automatic pressure extractor.

Treatment Temperature / hour 4H 8H 12H 65 ℃ T6 T7 T8 80 ℃ T9 T10 T11 100 ℃ T12 T13 T14

<2-1> Don blood  General ingredients according to extraction time and temperature of extract

In the general component analysis of the sample extract for each treatment, moisture, protein, fat and ash (%) were measured according to the AOAC method (1990), and the results are shown in Table 6 below.

General ingredients according to extraction time and temperature of donpi extract (%) Treatment T6 T7 T8 T9 T10 T11 T12 T13 T14 moisture 99.13 ±
0.05 ^b 99.73 ±
0.11 ^a 99.39 ±
0.43 ^ab 98.70 ±
0.00 ^c 98.30 ±
0.17 ^d 96.91 ±
0.29 ^e 98.71 ±
0.17 ^c 96.34 ±
0.10 ^f 96.27 ±
0.22 ^f Fat 0.00 ±
0.00 ^b 0.00 ±
0.00 ^b 0.00 ±
0.00 ^b 0.02 ±
0.00 ^b 0.03 ±
0.01 ^b 0.02 ±
0.01 ^b 0.04 ±
0.06 ^b 0.19 ±
0.11 ^a 0.14 ±
0.06 ^a Ash 0.07 ±
0.00 ^a 0.01 ±
0.00 ^d 0.01 ±
0.00 ^d 0.05 ±
0.00 ^b 0.06 ±
0.00 ^ab 0.05 ±
0.01 ^b 0.02 ±
0.00 ^c 0.03 ±
0.00 ^c 0.05 ±
0.01 ^b protein 0.78 ±
0.05 ^e 0.25 ±
0.11 ^f 0.58 ±
0.43 ^ef 1.21 ±
0.00 ^d 1.60 ±
0.17 ^c 3.00 ±
0.30 ^b 1.19 ±
0.21 ^d 3.48 ±
0.09 ^a 3.52 ±
0.17 ^a T6: 65 ° C-4h, T7: 65 ° C-8h, T8: 65 ° C-12h, T9: 80 ° C-4h, T10: 80 ° C-8h, T11: 80 ° C-12h, T12: 100 ° C-4h, T13 : 100 ℃ -8h, T14: 100 ℃ -12h
^{a- i} There is a significant difference in the number of heads in each treatment section (p <0.05).

<2-2> Don blood  Depending on the extraction time and temperature of the extract Chemical properties

The storage characteristics of the sample extract for each treatment group were investigated. As a chemical property, pH, VBN and TBA measurements were performed in the same manner as in Example <1-2>.

Chemical Characteristics of Donpi Extract according to Extraction Time and Temperature Treatment T6 T7 T8 T9 T10 T11 T12 T13 T14 pH 7.26
± 0.02 ^c 7.16
± 0.03 ^c 7.18
± 0.02 ^c 7.45
± 0.04 ^b 7.60
± 0.06 ^b 7.74
± 0.02 ^b 8.39
± 0.51 ^a 7.75
± 0.01 ^b 6.64
± 0.01 ^d VBN
(mg%) 7.68
± 1.92 ^c 4.30
± 0.31 ^d 6.68
± 1.40 ^c 19.03 ± 0.88 ^a 19.58 ± 0.83 ^a 6.95
± 1.14 ^c 20.22 ± 1.65 ^a 10.61 ± 0.41 ^b 20.95 ± 0.96 ^a TBA
(mg malonaldehyde / 1,000 g) 0.18
± 0.02 ^f 0.18
± 0.04 ^f 0.11
± 0.00 ^f 0.83
± 0.11 ^c 0.75
± 0.06 ^c 0.55
± 0.12 ^d 3.03
± 0.06 ^a 0.42
± 0.06 ^e 1.04
± 0.12 ^b T6: 65 ° C-4h, T7: 65 ° C-8h, T8: 65 ° C-12h, T9: 80 ° C-4h, T10: 80 ° C-8h, T11: 80 ° C-12h, T12: 100 ° C-4h, T13 : 100 ℃ -8h, T14: 100 ℃ -12h
^{a- f} There is a significant difference in the heading of each treatment section (p <0.05).

<2-3> Don blood  Collagen content according to extraction time and temperature of extract

The collagen content of the sample extract for each treatment group was investigated. The collagen content was measured in the same manner as in Example <1-3>.

Collagen content according to extraction time and temperature of donpi extract Treatment T6 T7 T8 T9 T10 T11 T12 T13 T14 Collagen 0.96
± 0.04 ^d 1.16
± 0.01 ^c 0.65
± 0.03 ^f 1.22
± 0.05 ^c 0.93
± 0.02 ^d 2.04
± 0.01 ^a 0.80
± 0.02 ^e 1.40
± 0.03 ^c 1.20
± 0.01 ^b Water soluble collagen 0.16
± 0.04 ^c 0.14
± 0.00 ^a 0.02
± 0.03 ^e 0.02
± 0.05 ^cd 0.26
± 0.02 ^b 0.04
± 0.01 ^e 0.14
± 0.02 ^c 0.05
± 0.03 ^e 0.14
± 0.01 ^d T6: 65 ° C-4h, T7: 65 ° C-8h, T8: 65 ° C-12h, T9: 80 ° C-4h, T10: 80 ° C-8h, T11: 80 ° C-12h, T12: 100 ° C-4h, T13 : 100 ℃ -8h, T14: 100 ℃ -12h
There are significant differences in the headings of the ^{a- f} treatment sections (p <0.05).

As shown above, it showed the highest water-soluble collagen content in the T10 treatment group.

< Example  3>

Discover natural proteolytic enzymes

In this experiment, in order to discover natural proteolytic enzymes useful for extracting donpi collagen, the molecular weight of collagen produced by hydrolysis after treatment with natural proteases at 60 ° C for 24 hours in 50 g of donpi extract (extracted for 8 hours at 80 ° C) Was measured. The natural protease added at this time is 1% by weight of the extract of donpi.

The molecular weight size of the resulting collagen was confirmed through an electrophoretic pattern. SDS-PAGE was used by partially modifying the method of Laemmli (1970). Prosi prestained protein marker (GenDEPOT, USA) was used to make and use 5% stacking gel and 12% separating gel. After the protein content was quantified, the mixture was mixed 1: 1 with 2X sample buffer and then 5 min at 95 ° C. It was used by heat treatment. Electrophoresis was performed at 100 V using an electrophoresis device (page Run, AE-6531, ATTO, Japan), and a gel staining solution (0.25% Coomassie brilliant blue R-250, 5% methanol and 7.5% acetic acid) was used. And decolorized with 7.5% acetic acid and 25% methanol to confirm the separated protein band.

At this time, a control (no additive) was used to confirm the difference between the existing extract and the sample to which the natural protease was added, while papain (to confirm the difference between the conventionally known protease and the natural protease of the present invention) Biocis, Papain T 100MG) was used. At this time, the papain treatment amount is 1% by weight of the extract of pig skin.

Treatment Treatments T15 T16 T17 T18 T19 T20 T21 Treatment Papain Kiwi pineapple FIG chives pepper ginger

The coenzyme solution (natural protease) used in this experiment can be prepared by the following method.

After grinding only the edible portion of the sample, add 2 times of distilled water, homogenize it for 2 minutes, filter twice with double gauze, and centrifuge the filtrate at 3,000 rpm (2200 X g) for 30 minutes at 5 ° C. The supernatant can be used as the basic coenzyme solution.

As a result, the natural protease showed a better effect on fruits than vegetables, and among them, kiwi, pineapple, and figs showed relatively good effects (see FIG. 1). In the control (no treatment), the collagen molecular weight of 130 kD was confirmed, and in the kiwi, pineapple and figs, the molecular weight was confirmed to be less than 130 kD.

In addition, Table 10 below shows the content of water-soluble collagen for each treatment group, and the content of water-soluble collagen in fruit is higher than that of vegetables.

Collagen content by type of natural protease Treatment T15 T16 T17 T18 T19 T20 T21 Collagen 1.88
± 0.01 ^c 1.98
± 0.01 ^b 2.12
± 0.01 ^a 1.18
± 0.02 ^e 1.98
± 0.02 ^b 1.50
± 0.05 ^e 1.82
± 0.01 ^d Water soluble collagen 0.28
± 0.01 ^c 0.30
± 0.00 ^b 0.32
± 0.00 ^a 0.28
± 0.02 ^c 0.26
± 0.05 ^e 0.27
± 0.02 ^d 0.28
± 0.02 ^c T15: papain, T16: kiwi, T17: pineapple, T18: fig, T19: leek, T20: red pepper, T21: ginger
There are significant differences in the headings of the ^{a- f} treatment sections (p <0.05).

< Example  4>

Optimization of natural protease

In this experiment, the content of Soluble Collagen according to the combination of kiwi, pineapple, and fig as a natural protease was investigated. The molecular weight of collagen produced by treating hydrophilic acid after treatment with natural protease at 60 ° C. for 24 hours in a pig skin extract (extracted at 80 ° C. for 8 hours) was measured. The natural protease added at this time is 1% by weight of the extract of donpi.

Treatment Subsidy / Combination Kiwi + Pineapple Pineapple + Fig Kiwi + Fig 1: 1 T22 T23 T24 2: 1 T25 T26 T27 1: 2 T28 T29 T30

Collagen content according to natural protease combination Treatment T22 T23 T24 T25 T26 T27 T28 T29 T30 Collagen 2.08
± 0.01 ^a 2.01
± 0.00 ^bc 2.02
± 0.01 ^b 1.80
± 0.05 ^e 2.08
± 0.01 ^a 1.82
± 0.01 ^d 2.08
± 0.01 ^a 1.98
± 0.02 ^c 2.00
± 0.02 ^bc Soluble Collagen 0.30
± 0.01 ^d 0.32
± 0.00 ^c 0.28
± 0.00 ^e 0.30
± 0.05 ^c 0.59
± 0.02 ^a 0.30
± 0.01 ^d 0.36
± 0.02 ^b 0.32
± 0.01 ^c 0.28
± 0.02 ^e T22: Kiwi + pineapple (1: 1), T23: Pineapple + fig (1: 1), T24: Kiwi + fig (1: 1), T25: Kiwi + pineapple (2: 1), T26: Pineapple + fig ( 2: 1), T27: Kiwi + Fig (2: 1), T28: Kiwi + Pineapple (1: 2), T29: Pineapple + Fig (1: 2), T30: Kiwi + Fig (1: 2)
There are significant differences in the headings of the ^{a- f} treatment sections (p <0.05).

As a result, as shown in Table 12, it showed a significantly higher water-soluble collagen content in the treatment group (T 26) mixed with pineapple and figs in a weight ratio of 2: 1 compared to other treatment groups. Therefore, it was confirmed that a mixture of pineapple + figs in a weight ratio of 2: 1 can be useful as an optimized protease for collagen extraction from donpi.

So far, the present invention has been focused on the preferred embodiments. Those skilled in the art to which the present invention pertains will understand that the present invention may be implemented in a modified form without departing from the essential characteristics of the present invention. Therefore, the disclosed embodiments should be considered in terms of explanation, not limitation. The scope of the present invention is shown in the claims rather than the foregoing description, and all differences within the equivalent range should be interpreted as being included in the present invention.

Claims (8)

(a) putting donpi into a pressure extractor and extracting it at 60 to 100 ° C. for 4 to 8 hours; And
(b) treating the protease extract with a natural protease solution and then hydrolyzing it,
The natural protease solution is characterized in that the pineapple and figs are juice juice mixed in a weight ratio of 2: 1, the method of producing donpi collagen. According to claim 1,
The step (a) is a method of manufacturing donpi collagen, characterized in that the step of putting the donpi into a pressure extractor and extracting it at 80 ° C for 8 hours. delete delete delete Pigpi collagen prepared by the method of claim 1 or 2. Food composition comprising the donpi collagen of claim 6 as an active ingredient. Cosmetic composition comprising the donpi collagen of claim 6 as an active ingredient.

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