KR101751617B1 - A composition comprising peptide extracts of ogye and method thereof - Google Patents
A composition comprising peptide extracts of ogye and method thereof Download PDFInfo
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- KR101751617B1 KR101751617B1 KR1020150174386A KR20150174386A KR101751617B1 KR 101751617 B1 KR101751617 B1 KR 101751617B1 KR 1020150174386 A KR1020150174386 A KR 1020150174386A KR 20150174386 A KR20150174386 A KR 20150174386A KR 101751617 B1 KR101751617 B1 KR 101751617B1
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Classifications
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- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/56—Materials from animals other than mammals
- A61K35/57—Birds; Materials from birds, e.g. eggs, feathers, egg white, egg yolk or endothelium corneum gigeriae galli
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- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/142—Amino acids; Derivatives thereof
- A23K20/147—Polymeric derivatives, e.g. peptides or proteins
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- 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
- A23L33/18—Peptides; Protein hydrolysates
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
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- 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
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
- A61Q19/00—Preparations for care of the skin
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- 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
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- 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
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- 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
- A23V2250/00—Food ingredients
- A23V2250/54—Proteins
- A23V2250/55—Peptide, protein hydrolysate
Abstract
The present invention relates to a composition comprising a pentapeptide extract as an active ingredient, and a composition comprising the pentapeptide extract of the present invention as an active ingredient inhibits the production of intracellular IL-6 and TNF- But also exhibits an antioxidative effect due to its excellent DPPH radical scavenging ability and is not toxic to cells, so that it is expected to be useful as a pharmaceutical composition, a food composition, a cosmetic composition and a feed composition.
Description
More particularly, the present invention relates to a composition comprising a pentapeptide extract as an active ingredient and a method for producing the same, more specifically, a method for optimizing a protein of breasts, legs or wings of Yeonsan Ogye through a hydrolysis process, A food composition, a cosmetic composition, and a feed composition which exhibit antioxidative and / or anti-inflammatory effects.
Inflammation is the immune response of the body in response to a wound or disease. Oxidative stresses such as ultraviolet rays, active oxygen, and free radicals activate inflammatory factors and cause aging of various diseases and skin. The vasoactive polypeptide, kinin, plasmin and complement, have vasodilatory and contraction and chemotaxis effects, as well as lymphokines such as interleukin-6 (IL-6) Phosphorus and arachidonic acid are responsible for inflammation. Arachidonic acid is metabolized through inflammatory mediators such as prostaglandin and lukotrienes via two pathways: cyclooxygenase or lipooxygenase, mediating a variety of inflammatory responses.
On the other hand, in order to eliminate inflammation, elimination of inflammation source, reduction of vital reaction and symptoms is called anti-inflammatory. To date, substances used for antiinflammatory purposes include flutenamic acid, ibuprofen, benzydamine, indomethacin, and steroids, prednisolone, , Dexamethasone, and the like. It is also known that allantoin, azene, hydrocortisone and the like are effective for antiinflammation. However, these materials are limited in their use due to safety of skin, .
An antioxidant is a substance which suppresses the oxidation reaction and includes a substance called a reactive oxygen or an oxygen free radical, such as a hydroxyl radical, a superoxide anion, hydrogen peroxide, etc., It means. As a low molecular weight compound, glutathione, N-acetylcysteine, ascorbic acid,? -Tocopherol, butylated hydroxyanilide (BHA), catechin, quercetin, uric acid, bilirubin, glucose and flavonoid are known. , Tomatoes, blueberries and other natural antioxidants.
Therefore, it is urgently required to develop an ingredient which is safe in living body, stable in its effective ingredient, and most effective than a substance having an existing anti-inflammatory effect.
As a substance having such antiinflammatory effect, Korean Patent Laid-open Publication No. 10-2015-0090295 discloses a composition for treating inflammation using an extract of Pyrrhizae extract as an active ingredient. In Korean Patent No. 10-1556773, Lt; RTI ID = 0.0 > of dietherpen < / RTI > compounds.
Accordingly, the inventors of the present invention have been continuing research to develop a substance which is safe for human body and has excellent anti-inflammatory effect as a natural substance, and the extract of DPPH peptide significantly reduced the production of cytokines in serum and excellently DPPH radical scavenging ability The present inventors have completed the present invention by discovering that they have excellent antiinflammatory and antioxidative effects as well as no cytotoxicity.
Accordingly, a technical problem to be solved by the present invention is to provide a composition which is safe as a natural edible material without cytotoxicity, and has excellent anti-inflammatory and antioxidative effects.
In order to solve the above-mentioned technical problems, the present invention provides a anti-inflammatory composition comprising an actinic factor peptide extract as an active ingredient.
Preferably, the present invention provides a pharmaceutical composition for anti-inflammation for the prevention or treatment of inflammatory diseases, which comprises an extract of Molecular Order Peptide as an active ingredient.
In addition, the present invention provides an antioxidant composition characterized by comprising an extract of Molecular Order Peptide as an active ingredient.
In addition, the present invention provides a food composition characterized by comprising an extract of Alchemical Peptide as an active ingredient.
In addition, the present invention provides a cosmetic composition characterized by comprising an extract of Calcification peptides as an active ingredient.
In addition, the present invention provides a feed composition characterized by comprising an extractant of Opuntia ficus-indica as an active ingredient.
(B) a step of homogenizing the chopped meat and adding a protein hydrolyzing enzyme to the chopped meat, and (c) the step of hydrolyzing , Adding 0.3 M TCA (Trichloroacetic acid) to the reaction mixture, precipitating the protein at room temperature, centrifuging at 3000 RPM, and taking only the supernatant, thereby producing a composition comprising the extract as an active ingredient to provide.
Generally, there are no large differences in appearance between the five and the chicken, but the head is small, and crests differ from chickens in that they usually have strawberry-shaped vessels. Sometimes chambers, stamens and roses are visible, It has a red color. Beak blue or black, face and body purple or blue white, eye iris brown or black, earlobe blue or blue white, legs color or yellow. The neck is short and feathery, and the tail is also short, with soft feathers. Legs are short and fine hairs are on the ankle. Skin, light and bone are all dark purple. Chickens have three toes on the front and one on the back, while the pussy has another long toe above the back toe. Feathers are mostly white, and rarely black and white and only red in the chest. Eggs are smaller than chickens.
The pentagram of the flower is characterized by a purple strawberry shape with varying concentration depending on the season and temperature. The toes are three in the front and one in the back like a regular chicken. The color of the feathers was originally red, white, black, yellow or hybrids, but only 20% of the single colors such as black and white were the result of efforts to fix the lineage such as separation breeding in 1973. Black, 5% white and 15% other mixed colors.
The active ingredient of the active ingredient of the antiinflammatory composition according to the present invention can be prepared by separating the meat from the ovary and hydrolyzing the protein using an enzyme and then centrifuging the obtained peptide.
The composition comprising the extract of the present invention of the present invention inhibits the production of intracellular cytokine IL-6 and intracellular cytokine TNF-a, thereby exhibiting excellent anti-inflammatory effects and being free from toxicity to cells.
In addition, the composition containing the extract of Molecular Order Peptide of the present invention can exhibit excellent antioxidative effect by eliminating the DPPH radical.
Accordingly, the present invention includes a pharmaceutical composition, a food composition, a cosmetic composition, and a feed composition which contain an extract of Molecular Order Peptide as an active ingredient.
According to one preferred embodiment of the present invention, the Pseudomonas exanthemum extract provides a pharmaceutical composition for the prevention or treatment of inflammatory diseases, which comprises as an active ingredient.
The pharmaceutical composition of the present invention may contain the extract of Opuntia ficus-indica in an amount of 0.01 to 80% by weight, preferably 0.1 to 60% by weight. However, this can be increased or decreased according to the need of the medicinal person, and it can be appropriately increased or decreased according to the situation such as the diet, nutritional status, disease progression, degree of inflammation.
The pharmaceutical composition of the present invention can be administered orally or parenterally and can be used in the form of a general pharmaceutical preparation. The preferred pharmaceutical preparations are those for oral administration such as tablets, hard or soft capsules, liquids, suspensions, etc. These pharmaceutical preparations can be prepared into conventional pharmaceutically acceptable carriers, for example, excipients such as excipients, Binders, disintegrators, lubricants, solubilizers, suspending agents, preservatives or extenders.
The dosage of the pharmaceutical composition containing the extract of the present invention may be determined by a specialist depending on various factors such as the patient's condition, age, sex, and complications, but is generally from 0.1 mg to 10 g per kg of the adult, Preferably in a dose of 10 mg to 5 g. Also, the daily dosage of the pharmaceutical composition per unit dosage form, or a half, 1/3, or 1/4 dose thereof, may be contained, and may be administered 1 to 6 times per day.
However, in the case of long-term intake for the purpose of health and hygiene or for the purpose of controlling health, the amount may be less than the above range, and the active ingredient may be used in an amount of more than the above range since there is no problem in terms of safety.
In the present invention, the inflammatory diseases are selected from the group consisting of edema, dermatitis, allergy, atopy, asthma, conjunctivitis, periodontitis, rhinitis, otitis, sore throat, tonsillitis, pneumonia, gastric ulcer, gastritis, Crohn's disease, colitis, hemorrhoids, Fibromyalgia, psoriatic arthritis, osteoarthritis, rheumatoid arthritis, shoulder periarthritis, tendonitis, nephritis, myositis, hepatitis, cystitis, nephritis, and multiple sclerosis.
The term antioxidative effect as used in the present invention refers to a substance which suppresses or suppresses the action of so-called oxide substances, including hydroxyl radicals, superoxide anions, hydrogen peroxide, etc., which are active oxygen or free radicals As used herein, the term " antioxidant composition ", " antioxidant ", " antioxidant composition "
According to one preferred embodiment of the present invention, there is provided an anti-inflammatory or antioxidant food composition comprising as an active ingredient an extract of Opuntia ficus-indica peptide.
The food of the present invention may be, but is not limited to, a health supplement food, a health functional food, a functional food, etc., and includes the addition of a compound of the present invention or an acceptable salt thereof to natural foods, processed foods, .
The food composition of the present invention can be used alone or in combination with other food or food compositions, and can be suitably used according to conventional methods. The amount of the active ingredient to be mixed can be suitably determined according to its intended use (prevention, improvement, or therapeutic treatment).
In general, the extract of Molecular Order Peptide of the present invention may be added in an amount of 0.1 to 70% by weight, preferably 2 to 50% by weight, based on 100% by weight of the raw material of food or beverage in the production of food or beverage.
The effective dose of the extract of Molecular Order Peptide of the present invention may be used in accordance with the effective dose of the pharmaceutical composition, but may be less than the above range for health and hygiene purposes or long-term consumption for health control purposes , The active ingredient can be used in an amount in the above range because there is no problem in terms of safety.
There is no particular limitation on the kind of the food. Examples of the food to which the extract of the present invention can be added include a dairy product including meat, sausage, bread, chocolate, candy, snack, confectionery, pizza, ramen, other noodles, gums, ice cream, , Tea, a drink, an alcoholic beverage and a vitamin complex, and other nutrients, but the present invention is not limited to these kinds of foods.
According to one preferred embodiment of the present invention, there is provided a cosmetic composition for anti-inflammation or antioxidation, which comprises an extract of Phragmites peptides as an active ingredient.
In the cosmetic of the present invention, the compounding ratio of the composition of the present invention can be appropriately selected depending on the type and the kind, quantity and form of other components to be compounded. Usually, with respect to the total amount of the cosmetic, To 20% by weight, preferably 0.01 to 10% by weight.
The cosmetic of the present invention may contain other various other ingredients as long as the desired effect of the present invention is not impaired. Examples of the other components include one or more selected from the group consisting of purified water, an emulsion, a surfactant, a lubricant, an alcohol, a gelling agent, a moisturizer, a buffering agent, an antiseptic, can do.
The cosmetic composition of the present invention may contain a skin penetration promoter for effective transdermal absorption. The skin penetration promoting agent is not particularly limited so long as it is a general skin penetration promoting agent used in the cosmetic composition in the art. For example, the skin penetration promoter of the present invention may be a fatty acid / ester compound such as dimethylsulfoxide, oleic acid, limonene, and the like.
The cosmetic composition of the present invention has anti-inflammatory and antioxidative properties, and can be used especially for troublesome skin, acne skin, atopic skin and the like.
The cosmetic composition of the present invention may be prepared in any of the formulations conventionally manufactured in the art and may be formulated as a solution, a suspension, an emulsion, a paste, a gel, a cream, a lotion, a powder, a soap, a surfactant-containing cleansing oil, Emulsion foundation, wax foundation, and spray, but are not limited thereto.
The cosmetic composition of the present invention may also be formulated as a softening agent, a nutritional lotion, a nutritional cream, a massage cream, an essence, an eye cream, a cleansing cream, a cleansing foam, a cleansing water, a pack, a spray or a powder.
When the cosmetic composition of the present invention is used, transdermal absorption may be promoted by using physical methods such as shock waves, iontophoresis, electrical invasion, and microinfiltration.
According to one preferred embodiment of the present invention, there is provided an anti-inflammatory or antioxidant feed composition comprising as an active ingredient an opioid peptide extract.
The feed composition of the present invention can be seeded with conventional feeds, and the feed composition of the present invention can be added to a conventional feed composition to prepare a functional feed composition. In addition, the feed composition of the present invention may further comprise a functional ingredient other than the extract of Peak Peptide. When preparing the functional feed composition comprising the conventional feed composition and the extract of the present invention, the extract of the present invention is added to the total feed composition in an amount of 0.01 to 30.00% by weight, preferably 0.01 to 20.00% by weight, By weight. Calculation of Feed Composition The effective dose of the five peptide extracts may be used in accordance with the effective dose of the food composition, but may be less than the above range for long-term intake intended for continuous health control, There is no problem, so that it can be used in an amount exceeding the above range as necessary.
The feed composition of the present invention is intended for livestock or poultry. The livestock or poultry may be any kind of animal such as cattle, pigs, chickens, horses, sheep, donkeys, mules, boars, rabbits, quail, ducks, fowls, poultry chickens, pigeons, turkeys, dogs, cats, monkeys, hamsters, , Parrots, parakeets, canaries, and the like, but are not limited to mammals or birds other than humans capable of breeding in the home.
As described above, the composition comprising the extract of the present invention as an active ingredient inhibits the production of intracellular cytokine IL-6 and intracellular cytokine TNF-a, thereby exhibiting excellent anti-inflammatory effects and also exhibiting DPPH radical scavenging ability And exhibits an antioxidative effect and is not toxic to cells, so that it is expected to be useful as a pharmaceutical composition, a food composition, a cosmetic composition and a feed composition for anti-inflammation or antioxidation.
BRIEF DESCRIPTION OF THE DRAWINGS FIG. 1 is a graph showing the effect of temperature and pH on the protein hydrolysis rate of the fifth breast of the present invention. FIG.
FIG. 2 is a graph showing the effect of temperature and enzyme amount on the protein hydrolysis degree of the fifth breast of the present invention.
FIG. 3 is a graph showing the effect of pH and enzyme amount on the protein hydrolysis rate of the fifth breast of the present invention.
Fig. 4 is a graph showing the optimum conditions for enzymatic hydrolysis of the five-pounded breast of the present invention.
FIG. 5 is a graph showing the results of Maldi-TOF analysis of the pentapeptide hydrolyzate of the present invention. FIG.
FIG. 6 is a graph showing the results of measurement of cytotoxicity in osteoblasts of the pentapeptide extract of the present invention. FIG. (A), (B), and (B), respectively.
FIG. 7 is a graph showing the DPPH radical scavenging activity of the pentapeptide extract of the present invention. FIG. (A) Peptide Peptide Extract, and (B) Peak Peptide Extract.
FIG. 8 is a graph showing the results of measurement of ABTS radical scavenging ability of the pentapeptide extract of the present invention. (A) breast muscle peptide extract, and (B) wing sesame peptide extract.
9 is a graph showing the ROS production amount of the pentapeptide extract of the present invention And FIG. (A) breast peptide peptide extract and (B) wing peptidic peptide extract. (**: p < 0.01, *: p < 0.05)
Figure 10 shows the amount of IL-6 produced by the pentapeptide extract of the present invention And FIG. (A), (B), and (B), respectively. (***: p < 0.001, **: p < 0.01)
Fig. 11 is a graph showing the amount of TNF-a produced in the pentapeptide extract of the present invention And FIG. (A) Peptide Peptide Extract, and (B) Peak Peptide Extract.
12 shows the ALP activity of the pentapeptide extract of the present invention And FIG. (A), (B), and (B), respectively.
13 shows the TRAP activity of the pentapeptide extract of the present invention And FIG. (A), (B), and (B), respectively.
Hereinafter, the present invention will be described in more detail with reference to Examples. It is to be understood by those skilled in the art that these embodiments are only for describing the present invention in more detail and that the scope of the present invention is not limited by these embodiments in accordance with the gist of the present invention .
Example 1
Materials and Experiments
1. Materials and reagents
The Folin ciocalteu`s phenol (FCP) reagent used in this experiment was purchased from Sigma Company (Seoul, Korea). Tri-chloro-acetic (TCA) acid was purchased from Sigma Company (Seoul, Korea). Proteolytic enzyme Bromelain 1200GDU (BM120 / Nobozyme0) was purchased from Daejong Sang (Seoul, Korea). The BM1200 enzyme is a plant protease obtained from pineapple. The protein for measuring enzyme activity was purchased from Daejon, Korea as casein. The oyster meat used in the experiment was provided by Jisan Plant (Nonsan, Choongnam, Korea).
2. Separation of the 5th breast
The pork provided by Jisan farm was supplied frozen without feather. The supplied oyster meat was stored in a laboratory freezer until the experiment. In order to isolate the poultry meat, the frozen pheasant was thawed in a constant temperature water bath at 40 ° C for 20 minutes. The thawed poultry meat was kept frozen at -20 ℃ until the experiment.
3. Chest chest chops
The frozen chest meat was frozen and stored at room temperature. The thawed breast meat was placed in a container, and the meat was evenly kneaded using a meat knife (Kenwood, Seoul, Korea). The thawed chest meat was put into a cutting material tray, cut into small pieces with a grinding blade, and then processed into a round and thin shaped meat. Chopped chest meat was placed in a zipper bag and the sample name and date of manufacture were filled in and stored frozen at -20 ° C.
4. Surface reaction experiment for optimal hydrolysis of 5th month chest muscle protein
In order to obtain optimum conditions for chest meat protein hydrolysis production, all experiments were performed with 3 independent variables: center reaction temperature, reaction pH, enzyme concentration (%) at 50 ℃,
In order to facilitate the statistical calculation, the independent variables were used as follows. The three variables are X 1 (temperature), X 2 (pH) and X 3 (enzyme concentration). The values of the standardization can be obtained by the following formula and the value is Z.
X o is the center value of the normalization value and X is the normalization value. DELTA X is the magnitude of the value that increases or decreases by one unit. The surface reaction analysis was used for the analysis of the experimental results. The multiple regression equation showing the optimal process conditions is as follows.
Here, Y is a predicted response, and if there are three variables as in this experiment, the value of k becomes 3 and ultimately expressed as
Statistical analysis of the results after the experiment was made using Design Expert (Couresy: Stat-ease Inc., Statistics Made Easy, Minneapolis, USA). The choice of values of the independent variable are selected from the results obtained in preliminary experiments to establish X 1 (C) is 40 ℃ (-1), 50 ℃ (0), 60 ℃ (+1), X 2 (pH) 5.0 (-1), 6.0 (0) 7.0 (+1) and X 3 (amount of enzyme) was 1% (-1), 2% (0) and 3% (+1) The production of breast meat peptide was carried out in a 250 ml Erlenmeyer flask containing 50 ml of PBS solvent, and the amount of enzyme was added to each flask solvent.
5. Protein hydrolysis
Enzymatic reaction 5 g of chestnut meat, which was stored frozen in the frozen state, was homogenized by using a homogenizer in a plastic beaker containing 50 ml of phosphate buffer solution. The homogenized breast milk was transferred to a 250 ml Erlenmeyer flask, Enzyme BM1200 was added, and incubated for 1 hour in an incubator. After reacting for 1 hour, 1 ml of the enzyme-hydrolyzed product was transferred to a tube, and 9 ml of water was added to dilute the solution. 2.5 ml of the diluted solution was transferred to another tube, and 5 ml of 0.3 M TCA (Trichloroacetic acid) was added. The protein was precipitated at room temperature for 20 minutes and then centrifuged at 3000 RPM for 10 minutes. Only the supernatant was removed, Hydrolyzate was obtained.
6. Measurement of Protein Hydrolysis of Five Chest Muscle
1 ml of 0.5 N NaOH was mixed with 1 ml of protein hydrolyzate of the poultry meat, 1 ml of 1 N FCP (Folin-Ciocalteu's penol reagent) was added, and the mixture was immediately mixed using a voltex. The mixture was incubated at 30 ° C for 15 minutes Followed by filtration. The filtered solution is measured for 578 nm Absorbance. The amount of protease hydrolysis was measured using a standard curve of L-Tyrosine, and a standard curve was obtained. Y = 0.0078X + 0.0182 After hydrolysis, the hydrolysis was calculated using the degree of hydrolysis of DH (%).
7. Five Chest Enzyme hydrolysis Peptides Analysis of constituent amino acids
0.1 g of the sample was weighed into an 18 ml test tube, 3 ml of 6 N HCl was added, and the sample was hydrolyzed in a heating block set at 110 ° C for more than 24 hours. The hydrolyzed samples were washed with 10 ml of sodium dilution buffer at 50 ° C with a rotary evaporator, and 1 ml of the solution was filtered through a membrane filter of 0.2 ㎛ to obtain an amino acid auto-analyzer (S433-H) .
8. Five Breast meat High-pressure liquefaction Peptides Free amino acid analysis
The sample (0.1 g) was weighed into an 18 ml test tube, and 3 ml of 6 N HCl was added, and the sample was hydrolyzed in a heating block set at 110 ° C for more than 24 hours. After hydrolysis, samples were removed by using a rotary evaporator at 50 ° C and then 10 ml of the solution was diluted with sodium dilution buffer. 1 ml of the solution was filtered through a 0.2 μm membrane filter, and analyzed by an automatic amino acid analyzer (S433-H ).
5 ml of 5% PBS broth was mixed with 50 ml of
9. Poultry meat peptide distribution (Maldi-TOF)
A-cyano-4-hydroxycinamic acid was used for molecular weight measurement of breast meat peptide, and a 10m / ml matrix sample was prepared with 70% ACN and 0.1% formic acid. 50-100 ppm of sample was prepared. matrix sample and the sample were mixed at a ratio of 1: 1. About 1 ml was dropped on a clean plate and hot air dried. After drying, samples with yellowish color were measured by laser irradiation with a mass spectrometer (MALDI-TOF, Voyager DE-STR, Applied Biosystems, USA). Laser measurements were made with Laser:> Nitrogen, 337 nm, 3 ns pulse.
Experiment result
1. Optimization of Peptide Production of the Five Chest Muscle by BM1200
The experimental results obtained by designing the experiment with the Box-Benken design for the three experimental parameters of temperature, pH, and enzyme amount, which are optimal conditions by enzymatic hydrolysis from the five-breasted muscle using the enzyme in BM1200, are shown in Table 3 below .
As a result of the enzyme hydrolysis experiment using the results of Table 3, when the optimum temperature was 50 ° C, the optimum pH was 6, and the amount of the enzyme was 3%, the results of the analysis of the regression equation were as follows: It indicates whether it is suitable or not. As a result of the surface reaction analysis, the stationary point was found to be the maximum point, and the predicted maximum enzyme hydrolysis was influenced by the higher temperature, the lower the pH, and the greater the amount of enzyme used in Table 2. The higher the temperature, the higher the temperature, but the higher the temperature, the better the hydrolysis. The pH showed the highest degree of hydrolysis at around 6 and the lower the pH, the lower the degree of hydrolysis.
Model determination coefficient R 2 value shows the degree of correlation between the observed value and the predicted value, and the degree of hydrolysis is 0.97. In the lack of fit test, no significance was observed and it was found that the model used in this experiment was very appropriate.
The regression equations for the three factors of hydrolysis are shown in Table 4 below. The amount of enzyme seemed to increase constantly at a rate of 3% more than 1%. Therefore, the optimum hydrolysis of the 5th stage chest was 37.14%.
Therefore, the most important factors affecting the amount of peptides in enzymatic hydrolysis of poultry meat were enzyme, followed by temperature and pH.
2. Optimal production conditions according to temperature and pH
As a result of analysis of optimal surface reaction according to temperature and pH, the maximum point of stationary point was found as predicted by peak hydrolysis of the 5th year old chick carcass. The reaction was found to be more affected by temperature. The degree of hydrolysis increased from 11.70 to 29.48% to pH 6-8 and then decreased. On the other hand, when the temperature was in the range of 40 to 60, the degree of hydrolysis was about 17.63% at 50.
As shown in FIG. 1, the degree of protein hydrolysis using temperature shows that the effect between temperature and pH is optimal at a pH of 7.5 and at a temperature of about 50. The degree of hydrolysis was 33.36%. Comprehensively, the optimal conditions for the hydrolysis of enzymes were temperature, pH, in order.
3. Optimal production conditions according to temperature and amount of enzyme
Analysis of optimal surface reaction according to temperature and enzyme amount of enzymatic hydrolysis using 5 year - old five - year - old breast meat revealed that the stationary point was found to be the maximum point. When the maximum peptide production was 50 at temperature, When the reaction was performed at 3% of the solvent, it was found to be more influenced by the amount of enzyme. % Of hydrolysis was continuously increased to 19.08 ~ 38.16% by 1 ~ 3% of enzyme. On the other hand, when the temperature was in the range of 40 to 60, the degree of hydrolysis was about 23.85% at around 50.
As shown in FIG. 2, the degree of protein hydrolysis using the temperature and the amount of enzyme shows that the degree of hydrolysis is optimal at an enzyme content of 3% and at a temperature of about 50 ° C. The degree of hydrolysis was 38.16%.
Overall, the optimum conditions for enzyme hydrolysis were temperature and enzyme order.
4. Optimal production conditions according to pH and amount of enzyme
Analysis of the optimum surface reaction according to the pH and the amount of enzyme showed that the maximum point was the stationary point. The maximum amount of peptide production was
As shown in FIG. 3, the degree of protein hydrolysis using the pH and the amount of enzyme shows that the effect of the pH and the amount of the enzyme is optimal at an enzyme content of 3% and at a pH of about 7.5. The degree of hydrolysis was 36.82%.
Comprehensively, enzymatic hydrolysis was the most effective factor in order of enzyme content and pH.
5. Optimum conditions depending on temperature, time and amount of enzyme
As shown in Fig. 4, enzymatic hydrolysis showed the highest enzyme hydrolysis as 37.14% as a result of hydrolysis of five - year - old chest carcass.
6. Five Chest Enzyme hydrolysis Peptides Analysis of constituent amino acids
The constituent amino acid compositions of the five-month-old chick carbohydrate hydrolyzate are shown in Table 5 below. The total content of constituent amino acids is 93.447 mg / 100g. Histidine 39.0% (36.429 mg / 100g) was the most abundant. Followed by leucine 9.5%, lysine 7.2%, glutamic acid 6.4%, and methionine 6.3%.
7. Analysis of Free Amino Acid Analysis of Enzyme Hydrolyzate of Five Chest Meat
Free amino acid content of the hydrolysates obtained by hydrolysis of the five muscle tissues was shown in Table 6 below. There were 26 kinds of free amino acids in the hydrolysates of the five pork chicks, and the total free amino acid content was 256.631 mg / 100g. Among the free amino acids, Carnosine (27.7%), Lysine (6.7%), Leucine (6.5%), Isoleucine (3.7%) and Phenylalanine (3.6%
8. Molecular weight distribution of peptides in the fifth breast
MALDI-TOP was used to analyze the molecular weight distributions of the products obtained by degrading the five-month-old breast meat using proteolytic enzymes. MALDI-TOF analyzes the mass of peptide fragments by treating a specific enzyme with PMF (Peptide Mass Fingerprint) analysis method and uses them to perform database search. Therefore, the PMF method is mainly used to identify proteins that have completed a genomic sequence or that have been listed in the NCBI. All amino acids in the protein have an average molecular weight of 138, but the weighted average is 128, and by condensation polymerization, the protein has an average molecular weight of 110 per unit. The unit to represent this is dalton (Dalton) and 1 kD is 1000 g / mol. For example, the average molecular weight of a protein having about 500 amino acids has a molecular weight of 55000 D, i.e. 55 kD.
As shown in FIG. 5, the molecular weight distribution of the peptides of the five-chain protein hydrolyzate was analyzed. In the graph of MALDI-TOP, the X axis represents mass (m / z) and the Y axis represents the intensity of the ionized substance. Most of the peptides showed a molecular weight distribution below m /
Example 2
1. Cytotoxicity measurement results
As shown in FIG. 6 (A), the cytotoxicity of osteoblast peptide extracts from osteoblast cells was measured to be 100.0 ± 5.0% for the control group. As a result, 1 year old rooster was 250, 500, 1000 (ug / ml The cell viability was 97.3 ± 3.1%, 114.5 ± 4.5% at the concentration of 250, 500 and 1000 (㎍ / ㎖) for the three year old rooster, respectively. The cell survival rate was 95.0 ± 6.5%, 101.4 ± 4.9% and 94.0 ± 5.0% The cell viability was 99.4 ± 6.9%. In addition, 3 year - old hen showed cell survival rate of 98.4 ± 7.9%, 105.1 ± 5.7% and 99.7 ± 13.2% at 250, 500 and 1000 (㎍ / ㎖) concentration, respectively.
As shown in FIG. 6 (B), the cytotoxicity of osteoblast cell extracts on the osteoblast cell lines was determined to be 100.0 ± 5.0% in the control group, and the 3-year-old rooster was 250, 500, 1000 (ug / Ml), cell viability was 96.0 ± 4.2%, 104.4 ± 1.2% and 98.7 ± 2.5%, respectively. In addition, the 3 year - old hen showed cell survival rate of 95.9 ± 8.4%, 107.3 ± 5.1%, and 95.0 ± 5.2% at 250, 500 and 1000 (㎍ / ㎖)
2. Measurement of DPPH radical scavenging ability
All living organisms using oxygen necessarily produce free radicals during oxidative metabolism, It is an unstable ion with one or more non-covalent electrons generated during normal body metabolism. It is closely related to aging and tissue damage associated with various inflammatory reactions such as DNA damage, protein peroxide generation and lipid peroxidation .
In the antioxidant assay, DPPH radical scavenging assay is a free radical reagent with strong oxidizing power. The antioxidative activity of DPPH by the compound donates electrons to the DPPH radical by contacting the electron donor antioxidant, Lt; / RTI > Since DPPH radicals have free radicals in their oxidized forms, it is known that when they come in contact with antioxidants, which are electron donors, they get electrons to be reduced, and that the greater the antioxidant effect, the greater the degree of decolorization.
As shown in FIG. 7 (A), the DPPH radical scavenging ability of the extracts of the 5th generation crest peptide was 12.3 ± 0.7% at 10, 20, 30, 40 and 50 (mg / , 20.4%, 40.4% and 50.4%, respectively, while the three year old rooster had a radical scavenging activity of 16.7 ± 2.0%, 32.4 ± 0.7%, 55.1 ± 3.6% and 59.3 ± 1.5% 0.6%, 14.5 ± 4.1%, 27.0 ± 3.3%, 50.6 ± 8.0% and 59.2 ± 4.9%, respectively. In addition, the 3 year - old hen had 6.8 ± 0.6%, 14.7 ± 0.1%, 25.9 ± 1.0%, 57.8 ± 2.5% and 76.8 ± 1.0% radical scavenging ability at concentrations of 10, 20, 30, 40 and 50 And the radical scavenging ability was increased in a concentration dependent manner.
These results indicate that the concentration of 50 ㎎ / ㎖ of 3 - year - old hen shows higher radical scavenging ability than the results of 1 - year - old and 3 - year - old rooster and is effective in product development related to aging and tissue damage.
As shown in FIG. 7 (B), the DPPH radical scavenging activity of the extract of Pseudomonas aeruginosa was measured to be 6.6 ± 3.1 at 10, 20, 30, 40, 50 (mg / , 3, 3, 5, 10, 20, 30, 40, 50 (㎎ / ㎖) showed the radical scavenging ability of 12.3 ± 0.6%, 31.4 ± 2.5%, 61.2 ± 3.1% and 76.7 ± 3.2% Radical scavenging activity was increased by 0.9%, 6.4 ± 1.3%, 12.7 ± 0.8%, 55.5 ± 3.0% and 73.7 ± 1.6%, respectively.
The results showed that there was no difference between sexes in the winged peptone extract, and the results were similar when compared with the 50 ㎎ / ㎖ concentration of 3 - year - old hen showing the highest DPPH radical scavenging ability of the breast peptide extract. In other words, the extract of winged peptides is considered to be effective in the development of products related to aging and tissue damage.
3. Measurement of ABTS radical scavenging ability
The method of measuring ABTS radical scavenging rate is based on the principle that the absorbance of cation radicals of ABTS is reduced by antioxidant. When ABTS + produced by mixing potassium persulphate with ABTS is cleared by antioxidant, . It is also useful in that both hydrophobic and hydrophilic samples can be measured.
As shown in FIG. 8 (A), the ABTS radical scavenging ability of the extracts of the 5 th row of breast muscle peptides was 27.0 ± 1.2% at 10, 20, 30, 40 and 50 (mg / , And 46.7 ± 3.5%, 49.6 ± 6.0%, 52.5 ± 1.7% and 56.5 ± 3.6%, respectively, and the 3 year old rooster showed 33.9 ± 5 at the concentration of 10, 20, 30, 40 and 50 0.9%, 48.6 ± 2.0%, 54.1 ± 5.2%, 59.6 ± 4.0% and 67.6 ± 1.1%, respectively. In addition, the 3 year - old hen had 29.0 ± 2.7%, 51.7 ± 1.9%, 51.7 ± 3.3%, 50.9 ± 1.6% and 56.2 ± 6.0% radical scavenging ability at concentrations of 10, 20, 30, 40 and 50 And the radical scavenging ability was increased in a concentration dependent manner.
These results show little difference between the gender and the expression of breast peptide extracts. When compared to DPPH radical scavenging ability, ABTS scavenging ability was higher at low concentration. In the case of radical scavenging ability, DPPH is free radical, but ABTS is cationic radical, or because phenolic substance is different in degree of binding to two substrates and different radical scavenging mechanism is active , Respectively.
As shown in FIG. 8 (B), the ABTS radical scavenging activity of the extracts of Pseudomonas aeruginosa was measured to be 37.3 ± 1.8 at the concentration of 10, 20, 30, 40, 50 (mg / The results showed that the 3 year old hen had a radical scavenging ability of 32.7% at the concentration of 10, 20, 30, 40, 50 (㎎ / ㎖), 53.5 ± 5.7%, 66.0 ± 1.6%, 64.6 ± 0.8% and 72.4 ± 0.6% The radical scavenging activity was increased by 5.7%, 54.1 ± 2.6%, 52.8 ± 2.3%, 67.2 ± 6.4% and 70.1 ± 6.1%, respectively.
The results showed that the wing peptidic extract showed little difference between genders and the results were higher than the results of DPPH radical scavenging at low concentrations, similar to that of the breast peptide extract.
4. Measuring ROS production
As shown in FIG. 9 (A), when the amount of ROS produced in the RAW 264.7 cells was measured as 100.0 ± 3.2% in the control group, 1-year-old rooster showed 1, 10, 100 (㎍ / ), Respectively. In the concentration of 1, 10, 100 (㎍ / ㎖) of 3 year - old rooster, the yields of 101.5 ± 3.1%, 87.1 ± 4.6 %, 94.7 ± 1.5%. The extracts of 3 year old hen shells showed 100.3 ± 9.9%, 87.7 ± 4.5% and 68.3 ± 5.6% at 1, 10 and 100 ㎍ / ㎖, respectively. ) And 100 ㎍ / ㎖ of 3 - year - old hen (**: p <0.01, *: p <0.05).
As shown in FIG. 9 (B), when the amount of ROS produced in the RAW 264.7 cells was measured as 100.0 ± 3.0% in the control group, the peel extract of the 3-year-old rooster was 1, 10, 100 (100 ㎍ / ㎖) concentration, and 109.3 ± 9.0%, 108.6 ± 10.9% and 100.4 ± 7.6%, respectively. The extracts of 3 - year - old hen had 95.3 ± 1.0% , 104.1 ± 3.7%, and 109.4 ± 1.7%, respectively.
5. IL -6 Measuring yield
As shown in FIG. 10 (A), when the amount of IL-6 produced in RAW 264.7 cells was measured as 92.3 ± 0.6 pg / ml, the 1-year- (50 μg / ml) and 44.0 ± 0.4 pg / ㎖ were obtained at the concentrations of 1, 10 and 100 (㎍ / ㎖) Concentration, 53.1 ± 1.0 pg / ml, 45.0 ± 1.1 pg / ml, and 35.3 ± 1.5 pg / ml, respectively. The extracts of 3 year - old hen showed 57.2 ± 2.1 pg / ㎖, 50.8 ± 1.4 pg / ㎖ and 95.6 ± 0.3 pg / ㎖ at 1, 10 and 100 ㎍ / (***: p <0.05) at the concentrations of 1, 10, 100 (㎍ / ㎖) and 3, 0.001, **: p < 0.01).
These results suggest that the extracts of human breast muscle peptides, as well as the extracts of leggroside peptides, show a remarkable reduction in LPS-induced IL-6 and are highly effective in diseases related to IL-6.
As shown in FIG. 10 (B), when the amount of IL-6 produced in RAW 264.7 cells was measured as 92.3 ± 0.6 pg / ㎖ in the control group, the extracts of 3-year- , 3, 5, 10, 100 (㎍ / ㎖), respectively. The extracts of 3-year-old hen shells were 1, 10, and 100 μg / The concentration of 1, 10, 100 (㎍ / ㎖) of 3 - year - old rooster and 3 - year - old hen showed the production of 54.8 ± 1.4 pg / ㎖, 57.2 ± 0.7 pg / ㎖ and 106.2 ± 0.6 pg / ( P <0.001, **: p <0.01) at the concentration of 1, 10 (㎍ / ㎖)
These results suggest that the wing peptidic extracts of Pseudomonas aeruginosa are also highly effective against IL-6-related diseases with a significant reduction in LPS-induced IL-6. However, the fact that there was no decrease in the concentration of 100 ㎍ / ㎖ of 3 - year - old hen, unlike the case where the peptide extract showed excellent reduction at all concentrations, will be revealed through in - depth studies in the future.
6. Measurement of TNF-α production
As shown in FIG. 11 (A), when the amount of TNF-α produced in RAW 264.7 cells was measured as 6985.0 ± 55.2 pg / ml in the control group, the 1-year- 10, and 100 (㎍ / ㎖), respectively, at 3 ㎍ / ㎖ concentration of the extracts of the three year old roosters showed 6612.3 ± 189.9 pg / ㎖, 6464.0 ± 39.6 pg / ㎖, 6453.0 ± 101.1 pg / At concentrations of 6559.8 ± 71.8 pg / ml, 6862.5 ± 23.3 pg / ml and 6643.8 ± 105.7 pg / ml, respectively. In addition, shell extracts of 3 - year - old hen showed 6898.8 ± 163.0 pg / ㎖, 6707.5 ± 152.0 pg / ㎖ and 6810.8 ± 6.7 pg / ㎖ at 1, 10 and 100 ㎍ /
As shown in FIG. 11 (B), when the amount of TNF-α produced in RAW 264.7 cells was measured as 6985.0 ± 55.2 pg / ml in the control group, the extracts of 3-year- , 10 and 100 (㎍ / ㎖), respectively. The extracts of 3-year-old hen shells showed 1, 10 and 100 (pg / Pg / ml) and 6943.3 + - 123.4 pg / ml at the concentration of 10 < 6 >
7. ALP Activity measurement
As shown in FIG. 12 (A), when ALP activity of osteoblast peptide extracts of osteoblast cells was measured, osteoclasts showed 250, 500 and 1000 (㎍ / ml) The activity of the three year old rooster was 105.2 ± 11.9%, 107.9 ± 7.8%, and 114.7 ± 5% at concentrations of 250, 500 and 1000 (㎍ / ㎖), respectively. And 11.8%, respectively. The activity of three year old hen was 91.7 ± 9.8%, 91.5 ± 10.9% and 76.0 ± 10.1% at the concentration of 250, 500 and 1000 (㎍ / ㎖), respectively.
As shown in FIG. 12 (B), when ALP activity of the extract of Pseudomonas aeruginosa was measured in the osteoblasts, when the control group was expressed as 100.0 ± 5.0%, the 3-year-old rooster was 250, 500, 1000 (㎍ / ), 93.7 ± 3.0% and 89.0%, respectively, at the concentrations of 250, 500 and 1000 (㎍ / ㎖) in the three year old hen, And the activity was ± 16.3%.
8. TRAP activity
As shown in FIG. 13 (A), when the TRAP activity of osteoblast peptide extracts of osteoblast cells was measured, 100.0 ± 5.0% of the control group showed 250, 500 and 1000 (ug / ml) , 53.6 ± 4.1%, and 40.5 ± 5.2%, respectively. The concentrations of the three year old rooster were 53.9 ± 3.1%, 43.8 ± 0.8% and 36.0 ± 0.5% at the concentration of 250, 500 and 1000 ㎍ / And 4.6%, respectively. In addition, the 3 year - old hen showed 47.3 ± 0.0%, 43.5 ± 4.9% and 41.4 ± 6.2% of activity at 250, 500 and 1000 (㎍ / ㎖) concentration, respectively.
As shown in FIG. 13 (B), when the TRAP activity of the extract of Pseudomonas aeruginosa was measured in the osteoblast cells, when the control group was expressed as 100.0 ± 5.0%, the 3-year-old rooster was 250, 500, 1000 ) Activity in the three year old hen were 56.3 ± 3.0%, 48.6 ± 3.4%, 41.9 ± 0.5% at the concentrations of 250, 500 and 1000 (㎍ / ㎖) ± 3.4%, respectively.
Claims (7)
(b) homogenizing the chopped meat product and adding a protein hydrolyzing enzyme; And
(c) adding 0.3 M TCA (Trichloroacetic acid) to the hydrolyzed reactant, precipitating the protein at room temperature, centrifuging at 3000 RPM, and taking only the supernatant, thereby producing an antioxidant activity Wherein the composition comprises an extract of a five-legged flesh, a winged flesh or a breast peptide as an active ingredient.
(b) homogenizing the chopped meat product and adding a protein hydrolyzing enzyme; And
(c) adding 0.3 M TCA (Trichloroacetic acid) to the hydrolyzed reactant, precipitating the protein at room temperature, centrifuging at 3000 RPM, and taking only the supernatant, thereby producing an antioxidant activity Wherein the composition comprises an extract of the five legged legged, winged or breasted peptides as an active ingredient.
(b) homogenizing the chopped meat product and adding a protein hydrolyzing enzyme; And
(c) adding 0.3 M TCA (Trichloroacetic acid) to the hydrolyzed reactant, precipitating the protein at room temperature, centrifuging at 3000 RPM, and taking only the supernatant, thereby producing an antioxidant activity Wherein the composition comprises an extract of the five legged legged, winged flesh or bovine peptides as an active ingredient.
(b) homogenizing the chopped meat product and adding a protein hydrolyzing enzyme; And
(c) adding 0.3 M TCA (Trichloroacetic acid) to the hydrolyzed reactant, precipitating the protein at room temperature, centrifuging at 3000 RPM, and taking only the supernatant, thereby producing an antioxidant activity Wherein the composition comprises an extract of a five-legged legged, winged or pectoral peptide as an active ingredient.
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Non-Patent Citations (2)
| Title |
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| 김진우 외 4인. 동의보감에 수재된 오계에 대한 생리활성 연구. 대한본초학회지, 2015.09., 제30권, 제5호, pp. 23-28* |
| 비특허문헌 1: 한국식품영양과학회 |
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