KR20130052910A - Silk peptide for improving hypercholesterolemia and hyperlipidemia - Google Patents
Silk peptide for improving hypercholesterolemia and hyperlipidemia Download PDFInfo
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- KR20130052910A KR20130052910A KR1020110118248A KR20110118248A KR20130052910A KR 20130052910 A KR20130052910 A KR 20130052910A KR 1020110118248 A KR1020110118248 A KR 1020110118248A KR 20110118248 A KR20110118248 A KR 20110118248A KR 20130052910 A KR20130052910 A KR 20130052910A
- Authority
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- Prior art keywords
- silk
- calcium salt
- decomposition
- improvement
- molecular weight
- Prior art date
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 45
- 208000035150 Hypercholesterolemia Diseases 0.000 title abstract description 14
- 208000031226 Hyperlipidaemia Diseases 0.000 title abstract description 14
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 claims abstract description 32
- 238000000034 method Methods 0.000 claims abstract description 26
- 239000000203 mixture Substances 0.000 claims abstract description 24
- 108010022355 Fibroins Proteins 0.000 claims abstract description 21
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 21
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 21
- 235000012000 cholesterol Nutrition 0.000 claims abstract description 15
- 238000000354 decomposition reaction Methods 0.000 claims abstract description 13
- 230000006872 improvement Effects 0.000 claims abstract description 13
- 159000000007 calcium salts Chemical class 0.000 claims abstract description 12
- 239000008280 blood Substances 0.000 claims abstract description 11
- 210000004369 blood Anatomy 0.000 claims abstract description 11
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims abstract description 10
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical group [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 claims abstract description 8
- 239000001110 calcium chloride Substances 0.000 claims abstract description 7
- 229910001628 calcium chloride Inorganic materials 0.000 claims abstract description 7
- 239000000243 solution Substances 0.000 claims abstract description 6
- 239000012266 salt solution Substances 0.000 claims abstract description 5
- 238000000108 ultra-filtration Methods 0.000 claims abstract description 5
- 238000000502 dialysis Methods 0.000 claims abstract description 4
- 201000010099 disease Diseases 0.000 claims abstract description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims abstract description 4
- 235000013376 functional food Nutrition 0.000 claims abstract description 4
- 238000005227 gel permeation chromatography Methods 0.000 claims abstract description 4
- 239000004480 active ingredient Substances 0.000 claims abstract description 3
- 150000002632 lipids Chemical class 0.000 claims abstract 3
- 238000005903 acid hydrolysis reaction Methods 0.000 claims abstract 2
- 238000008214 LDL Cholesterol Methods 0.000 claims description 6
- 206010012601 diabetes mellitus Diseases 0.000 claims description 5
- 150000003626 triacylglycerols Chemical class 0.000 claims description 5
- 230000015556 catabolic process Effects 0.000 claims 1
- 238000006731 degradation reaction Methods 0.000 claims 1
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 13
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 abstract description 3
- 102000007330 LDL Lipoproteins Human genes 0.000 abstract 2
- 108010007622 LDL Lipoproteins Proteins 0.000 abstract 2
- 238000011033 desalting Methods 0.000 abstract 1
- 229920000642 polymer Polymers 0.000 description 12
- 108010013296 Sericins Proteins 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 230000006870 function Effects 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 241000255789 Bombyx mori Species 0.000 description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 239000000835 fiber Substances 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 4
- 108010028554 LDL Cholesterol Proteins 0.000 description 3
- 241000382353 Pupa Species 0.000 description 3
- 230000003920 cognitive function Effects 0.000 description 3
- 230000007062 hydrolysis Effects 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 229910017053 inorganic salt Inorganic materials 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 238000007670 refining Methods 0.000 description 3
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 230000003301 hydrolyzing effect Effects 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- JIAARYAFYJHUJI-UHFFFAOYSA-L zinc dichloride Chemical compound [Cl-].[Cl-].[Zn+2] JIAARYAFYJHUJI-UHFFFAOYSA-L 0.000 description 2
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 238000009395 breeding Methods 0.000 description 1
- 230000001488 breeding effect Effects 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 235000012054 meals Nutrition 0.000 description 1
- 238000003359 percent control normalization Methods 0.000 description 1
- 239000000902 placebo Substances 0.000 description 1
- 229940068196 placebo Drugs 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 239000011592 zinc chloride Substances 0.000 description 1
- 235000005074 zinc chloride Nutrition 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
- A23L33/17—Amino acids, peptides or proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K8/00—Cosmetics or similar toiletry preparations
- A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
- A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
- A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2200/00—Function of food ingredients
- A23V2200/30—Foods, ingredients or supplements having a functional effect on health
- A23V2200/3262—Foods, ingredients or supplements having a functional effect on health having an effect on blood cholesterol
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2300/00—Processes
- A23V2300/28—Hydrolysis, degree of hydrolysis
Abstract
Description
The present invention relates to a silk peptide composition having a complex function of hypercholesterolemia and hyperlipidemia, and more particularly, to a silk protein hydrolyzed to have a weight average molecular weight of 10,000 to 50,000, and a combination of hypercholesterolemia and hyperlipidemia improvement. A silk peptide composition that functions.
Silk is a protein-based fiber composed of fibroin and sericin, which was previously used only for making fabrics, but recently has been manufactured and used as a functional food and cosmetics by research. In order to use such silk proteins as active ingredients of functional foods or pharmaceuticals, various methods for obtaining low molecular weight silk peptides from silk proteins have been proposed. For example, Korean Patent Registration No. 10-0443785 discloses a method for producing silk amino acids using hydrochloric acid, and Korean Patent Registration No. 10-0420824 discloses a method for preparing silk peptides using alkali, and Korea Patent Registration No. 10-0881210 discloses a method for producing silk peptides using enzymes.
In addition, the low molecular weight silk peptides having a molecular weight of about 100 to 2,000 thus produced have been shown to have various effects such as diabetes improvement and cognitive function. For example, Korean Patent Registration No. 10-0947547 discloses a silk peptide having a therapeutic and prophylactic effect of diabetes, and Korean Patent Registration No. 10-0494358 discloses a silk peptide effective for improving brain cognitive function. The contents are disclosed.
Conventional silk peptide production methods have been focused on developing a method of hydrolyzing a silk silk in the form of fiber using hydrochloric acid or an enzyme to decompose to a very low molecular weight peptide or amino acid level. Therefore, the molecular weight of the final product is mostly about 100 to 2,000 amino acids or about the size of the small molecule peptide, and the molecular weight of the large hydrolyzed products is composed of about 10,000. Since silk fiber cannot be digested and absorbed by itself, research has focused on how to lower the molecular weight by using various methods to increase digestive absorption rate, and the most representative method developed by using acid and enzyme It is a method of hydrolysis. Amino acids and low molecular weight peptides made by acids and enzymes could be absorbed by the human body more than 90%. The amino acids and low molecular weight peptides were found to be effective in improving diabetes and cognitive function. Further studies are underway to show this efficacy.
However, for the high molecular weight high molecular silk peptide of 10,000 or more, there is no manufacturing or research on this because of the fact that these substances are not absorbed in the human body.
The present inventors earnestly researched to develop a silk peptide composition having a complex function that can improve hypercholesterolemia and hyperlipidemia, and as a result, the polymer silk peptide having a weight average molecular weight of 10,000 or more obtained through hydrolysis has excellent complex functional activity. By confirming that the present invention has been completed, the present invention was completed.
Accordingly, it is an object of the present invention to provide a silk peptide composition having a multifunctional activity that improves hypercholesterolemia and hyperlipidemia.
According to an aspect of the present invention, the present invention provides a silk peptide composition hydrolyzing silk protein having a weight average molecular weight of 10,000-100,000 and having a combined activity of hypercholesterolemia and hyperlipidemia improvement.
A cocoon is used as starting material in the process of the invention. As used herein, the term "silk" means a fiber made by silkworm insects, and preferably means a silkworm sanded by a silkworm (Bombyx mori).
Silk cocoon silk protein consists of fibroin and sericin, fibroin and sericin are present on average 75% and 25%, respectively. Fibroin protein and sericin are different proteins with completely different amino acid compositions. According to recent research results, silk fibroin has a structure in which H-chain (350 kDa) and L-chain (26 kDa) are SS-bonded, and glycoprotein P25 (30 kDa) is non-covalently linked to the two chains. It was identified as a macromolecular protein having a mole composition of 6: 6: 1, and this structure has a polymer property of a block form in which crystalline and amorphous regions are continuously exchanged.
According to a preferred embodiment of the invention, the silk protein used is silk fibroin.
According to a preferred embodiment of the present invention, the hydrolysis of silk fibroin can be carried out through the method of (a) refining, (b) decomposition in inorganic salt solution, (c) removal of inorganic salt. The weight average molecular weight of the silk peptides produced by decomposition by the above method may range from about 10,000-100,000, and has a complex function of improving diabetes, hypercholesterolemia and hyperlipidemia.
The refining is carried out by heating the cocoon in hot water, preferably 80 to 130 ℃, more preferably at 120 ℃ to remove sericin. Moreover, it can also carry out by adding sodium carbonate and surfactant to hot water.
The decomposition in the inorganic salt solution is usually used hydrochloride, preferably calcium chloride, magnesium chloride, zinc chloride, more preferably calcium chloride. In addition, ethanol may be further mixed and used therein.
Step (b) is preferably performed by dissolving silk fibroin in a solution containing calcium chloride, water and ethanol at 60-95 ° C, more preferably 70-95 ° C, most preferably 75-85 Dissolve at ° C. By the decomposition in the calcium salt solution, silk fibroin is decomposed into a relatively high molecular peptide of about 10,000-50,000 molecular weight.
The method of removing the salt in step (c) may be carried out through various methods known in the art, for example, dialysis, ultrafiltration, gel filtration chromatography or electrodesalting, etc., and only a specific weight molecular weight range. These methods can be used in combination for selective separation.
Silk peptides prepared by the method of the present invention have a high molecular weight and are not well absorbed by the body. Silk fibroin's unique porous structure has high adsorption properties, so it can strongly adsorb fat components ingested with silk fibroin. As a result, the fat component adsorbed on silk fibroin is not excreted in the body and is excreted to inhibit the absorption of fat. As a result, it is possible to reduce blood fat concentration and lower blood cholesterol concentration.
The present invention provides a silk peptide composition having a combined activity of hypercholesterolemia and hyperlipidemia improvement. The present invention provides a high molecular weight silk peptide composition that is almost not absorbed into the body, having a combined activity of improving hypercholesterolemia and hyperlipidemia from silk proteins.
As illustrated in the examples below, silk peptides prepared by the methods of the present invention can be used for the treatment and prevention of hypercholesterolemia and hyperlipidemia.
Hereinafter, the present invention will be described in more detail with reference to Examples. These examples are only for illustrating the present invention more specifically, and the scope of the present invention is not limited by these examples according to the gist of the present invention.
Example 1 Refining Silk Fibroin
The silk protein used in the present invention was used after removing pupa from the cocoon obtained by breeding the gambo (Bombyx mori). 50 times of water was added to the cocoon from which the pupa was removed, heated at 120 degrees Celsius for 20 minutes, washed with clean water and dried to obtain pure silk fibroin protein from which sericin protein was removed.
Example 2. Preparation of Polymer Silk Peptides
The refined silk fibroin protein obtained in Example 1 was placed in a 5M calcium chloride solution, and ethanol was added while heating at 90 degrees Celsius to completely dissolve and hydrolyze the silk fibroin protein. Multiple layers of gauze were stacked to remove large foreign objects such as pupa pieces, and filter paper (Whatman No. 1) was used to remove insoluble matters. Calcium chloride was removed by using a) dialysis in water, b) using an electrodesulfate, c) using ultrafiltration, and d) using gel chromatography. Calcium chloride was well removed in all methods and the same result was obtained in subsequent work. However, the electrodesalter method has the advantage of being able to process a large amount of samples in a fast time, while there are many disadvantages of silk protein loss. The remaining methods had the disadvantages of being difficult and time-consuming to process a large amount of samples, while having the advantage of low loss of silk protein. The calcium chloride-free polymeric silk fibroin peptide solution was freeze-dried to prepare a powder.
Example 3. Determination of Molecular Weight of Polymer Silk Peptides
The molecular weight of the polymer silk peptide prepared in Example 2 was calculated by gel permeation chromatography. The polymer silk peptide was dissolved in 0.2 M sodium phosphate buffer and chromatographed to calculate the molecular weight distribution from the absorbance value of 280 nm. As a result, the weight average molecular weight of the polymer silk peptide was 26 kDa.
Example 4 Cholesterol and Triglyceride Improvement Effects of Polymer Silk Peptides
The investigator divided 20 obese men and women (8 males, 12 females, mean age 48.8 ± 6.5 years) into 5 control groups and 15 experimental groups. 500 mg of polymer silk peptide was taken 3 times a day, just before meals, and proceeded for 2 months. The control group received placebo instead of silk peptide. Before starting the clinical trial, each item was measured and then each item was measured on a monthly basis. The experimental results are shown in Table 1.
Total Cholesterol (%)
Total Cholesterol (%)
Total cholesterol, LDL cholesterol, and triglycerides exceeded the normal range at the start of the clinical trial, but there was no change in the control group for 2 months after ingesting the polymer silk peptide, whereas these levels gradually decreased in the experimental group. Total cholesterol, LDL cholesterol, and triglycerides were all improved to near normal levels. HDL cholesterol was in the normal range from the beginning, and remained in the normal range after 2 months, and the ratio of HDL cholesterol to total cholesterol improved from 23.5% to 25.1%.
From these results, it was confirmed that the polymer silk peptide is excellent in improving total cholesterol, LDL cholesterol, and triglyceride.
As described above, by ingesting the silk peptide of the polymer prepared according to the present invention, as a result, it has a combined function of improving hypercholesterolemia, hyperlipidemia can be used for the treatment and prevention of these diseases.
Claims (10)
Priority Applications (1)
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KR1020110118248A KR20130052910A (en) | 2011-11-14 | 2011-11-14 | Silk peptide for improving hypercholesterolemia and hyperlipidemia |
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KR1020110118248A KR20130052910A (en) | 2011-11-14 | 2011-11-14 | Silk peptide for improving hypercholesterolemia and hyperlipidemia |
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Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2015048805A1 (en) | 2013-09-30 | 2015-04-02 | Silk Therapeutics, Inc. | Silk potein fragment compositions and articles manufactured therefrom |
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2011
- 2011-11-14 KR KR1020110118248A patent/KR20130052910A/en active Search and Examination
Cited By (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2015048805A1 (en) | 2013-09-30 | 2015-04-02 | Silk Therapeutics, Inc. | Silk potein fragment compositions and articles manufactured therefrom |
US10987294B2 (en) | 2013-09-30 | 2021-04-27 | Evolved By Nature, Inc. | Stable silk fibroin based pharmaceutical formulations |
US11298311B2 (en) | 2013-09-30 | 2022-04-12 | Evolved By Nature, Inc. | Stable silk protein fragment compositions |
US11298310B2 (en) | 2013-09-30 | 2022-04-12 | Evolved By Nature, Inc. | Stable silk protein fragment compositions |
US11857663B2 (en) | 2013-09-30 | 2024-01-02 | Evolved By Nature, Inc. | Stable silk protein fragment compositions |
US11857664B2 (en) | 2013-09-30 | 2024-01-02 | Evolved By Nature, Inc. | Stable silk protein fragment compositions |
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