WO2013073648A1 - Agent fonctionnel anti-inflammatoire destiné à une application par voie orale - Google Patents

Agent fonctionnel anti-inflammatoire destiné à une application par voie orale Download PDF

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WO2013073648A1
WO2013073648A1 PCT/JP2012/079734 JP2012079734W WO2013073648A1 WO 2013073648 A1 WO2013073648 A1 WO 2013073648A1 JP 2012079734 W JP2012079734 W JP 2012079734W WO 2013073648 A1 WO2013073648 A1 WO 2013073648A1
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inflammatory
protein
pea protein
hydrolyzate
pea
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Japanese (ja)
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貴康 本山
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不二製油株式会社
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    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K36/00—Medicinal preparations of undetermined constitution containing material from algae, lichens, fungi or plants, or derivatives thereof, e.g. traditional herbal medicines
    • A61K36/18—Magnoliophyta (angiosperms)
    • A61K36/185—Magnoliopsida (dicotyledons)
    • A61K36/48—Fabaceae or Leguminosae (Pea or Legume family); Caesalpiniaceae; Mimosaceae; Papilionaceae
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/14—Vegetable proteins
    • A23J3/16—Vegetable proteins from soybean
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23J—PROTEIN COMPOSITIONS FOR FOODSTUFFS; WORKING-UP PROTEINS FOR FOODSTUFFS; PHOSPHATIDE COMPOSITIONS FOR FOODSTUFFS
    • A23J3/00—Working-up of proteins for foodstuffs
    • A23J3/30—Working-up of proteins for foodstuffs by hydrolysis
    • A23J3/32—Working-up of proteins for foodstuffs by hydrolysis using chemical agents
    • A23J3/34—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes
    • A23J3/346—Working-up of proteins for foodstuffs by hydrolysis using chemical agents using enzymes of vegetable proteins
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23K—FODDER
    • A23K10/00—Animal feeding-stuffs
    • A23K10/30—Animal feeding-stuffs from material of plant origin, e.g. roots, seeds or hay; from material of fungal origin, e.g. mushrooms
    • 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
    • A23L33/135—Bacteria or derivatives thereof, e.g. probiotics
    • 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
    • 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
    • A23L33/185—Vegetable proteins
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • A61K38/01—Hydrolysed proteins; Derivatives thereof
    • A61K38/011—Hydrolysed proteins; Derivatives thereof from plants
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
    • A23C19/00—Cheese; Cheese preparations; Making thereof
    • A23C19/02—Making cheese curd
    • A23C19/05—Treating milk before coagulation; Separating whey from curd
    • A23C19/054—Treating milk before coagulation; Separating whey from curd using additives other than acidifying agents, NaCl, CaCl2, dairy products, proteins, fats, enzymes or microorganisms
    • A—HUMAN NECESSITIES
    • A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
    • A23C—DAIRY PRODUCTS, e.g. MILK, BUTTER OR CHEESE; MILK OR CHEESE SUBSTITUTES; MAKING THEREOF
    • A23C9/00—Milk preparations; Milk powder or milk powder preparations
    • A23C9/12—Fermented milk preparations; Treatment using microorganisms or enzymes
    • A23C9/13—Fermented milk preparations; Treatment using microorganisms or enzymes using additives
    • A23C9/1322—Inorganic compounds; Minerals, including organic salts thereof, oligo-elements; Amino-acids, peptides, protein-hydrolysates or derivatives; Nucleic acids or derivatives; Yeast extract or autolysate; Vitamins; Antibiotics; Bacteriocins

Definitions

  • the present invention relates to a peptide having an anti-inflammatory function.
  • Inflammation is a proper defense reaction of the living body, but an excessive inflammatory reaction causes damage to the self-organization of the living body.
  • histamine and serotonin are first released from mast cells and platelets. Histamine and serotonin cause temporary vasoconstriction in a short time, dilate blood vessels in the inflamed area (arterioles, venules, and capillaries), increase blood flow, and cause heat and redness.
  • vascular permeability is increased (actin of vascular endothelial cells contracts), the interval between vascular endothelial cells is expanded, leukocytes are leached locally from the whole body (in blood), and protective factors such as plasma leak locally Causes swelling (edema).
  • factor 12 of blood coagulation is activated and bradykinin is produced in the kinin / caniclein system, causing pain. These reactions occur in the tissue, resulting in tissue dysfunction. These “fever, redness, swelling, pain, dysfunction” are called the five major signs of inflammation.
  • neutrophils treat bacteria, viruses, dead cells, and other foreign substances in the early stages of inflammation, but macrophages gather and treat dead cells and bacteria by phagocytosis at the later stage of inflammation.
  • Macrophages that encounter bacteria and dead cells are activated and release cytokines such as TNF- ⁇ , IL-1, and IL-6, and chemokines such as IL-8.
  • cytokines cause fever, redness, and swelling due to increased vascular permeability
  • chemokines increase leukocyte chemotaxis and cause swelling.
  • macrophages play an important role in maintaining homeostasis, but macrophage dysfunction such as excessive activation is involved in many diseases of the immune system and excessive inflammation.
  • the development of a drug that suppresses the reaction has been intensively studied.
  • Patent Document 1 describes many di- and tripeptides as peptides having an anti-inflammatory effect.
  • Patent Document 2 discloses a technique for obtaining an effect on gastrointestinal inflammation with a food-derived component, although it does not directly have an anti-inflammatory function.
  • this product is a hydrolyzate of cheese, its palatability is high due to its unique flavor.
  • Patent Document 3 discloses the anti-inflammatory function of soybean peptides, particularly Phe-Leu-Val and Val-Pro-Tyr, which are peptides derived from the 11S protein.
  • soybean peptides particularly Phe-Leu-Val and Val-Pro-Tyr
  • Patent Document 4 describes the anti-inflammatory function of pea protein, which is not a major food allergen, but there is no specific description as an example, and it is intended for skin application. Is not intended.
  • proteins contained in peas are composed of 11S (legmin), 7S (bicillin), combicillin and globulin from the sedimentation coefficient by ultracentrifugation analysis.
  • Pea 11S (Legmin) forms a hexamer with a molecular weight of 320,000 to 380,000, and like other legumins of seeds, acidic subunits and basic subunits are accumulated in a disulfide bond.
  • pea 7S (bicillin) forms a trimer with a molecular weight of 170,000 and is composed of subunits with molecular weights of 47,000, 50,000, 34,000 and 30,000.
  • Combicillin has a molecular weight of 290,000 and is composed of subunits with a molecular weight of 71,000.
  • combicilin is 9-12% in the isolated pea protein
  • 7S (bicillin) is 30-38%
  • 11S (legumin) is 28%- 33% included.
  • proteins contained in soybean are classified into 2S, 7S, 11S and 15S globulin fractions based on the sedimentation coefficient by ultracentrifugation analysis.
  • 7S and 11S are the main constituent proteins, 7S ( ⁇ -conglycinin) accounts for about 1/3, and 11S (glycinin) accounts for about 2/3.
  • the object of the present invention was to obtain an anti-inflammatory functional agent from a food material that does not contain major food allergens.
  • the present inventor diligently studied the pea protein, which has about 11% of the 11S component, which is less than 30% of the soy protein containing 1/3 of the 11S component, which is considered the main body of anti-inflammation.
  • the present inventors have found that a peptide obtained by hydrolyzing a protein composition containing pea protein as a main raw material has an anti-inflammatory effect equivalent to or higher than that of soybean protein, and completed the present invention.
  • the present invention is (1) an oral anti-inflammatory functional agent comprising pea protein hydrolyzate as an active ingredient.
  • the anti-inflammatory functional agent according to (1), wherein the di-tripeptide content in the hydrolyzate is 40% by weight or more.
  • an oral anti-inflammatory functional agent having an anti-inflammatory effect is obtained from pea, which is a food material that does not contain major food allergens, and is added to a form of a drug effective for inflammatory diseases, or to food or feed.
  • pea which is a food material that does not contain major food allergens
  • pea protein means each of the aforementioned pea protein subunits, or an aggregate thereof.
  • the pea protein material is a material derived from pea seeds and containing a large amount of pea protein, preferably contains 50% by weight or more of pea protein, more preferably contains 65% by weight or more, More preferably, it is contained by weight% or more.
  • Methods for preparing pea protein material from pea seeds are well known. Extracting and concentrating protein components from peas with a general composition using water, and pea seed material by pulverizing and classifying pea seeds. Methods for concentrating are known. Moreover, what mixed other components with the pea protein raw material with high protein contents, such as isolation
  • Pea protein hydrolyzate is a peptide mixture prepared by hydrolyzing a pea protein material.
  • the pea protein hydrolyzate preferably has a higher degree of degradation, and in particular, the proportion of dipeptides and tripeptides in the total amount of peptides and free amino acids in the hydrolyzate is preferably high.
  • the proportion of dipeptides and tripeptides in the total amount of peptides and free amino acids is preferably 40% by weight or more. It is more preferably 60% by weight or more, and most preferably 64% by weight or more.
  • dipeptides and tripeptides are defined as a fraction obtained by removing free amino acids from a fraction having a molecular weight of 500 or less. Therefore, the proportion of dipeptides and tripeptides in the total amount of peptides and free amino acids was measured by amino acid analysis after measuring the proportion of peptide fractions with a molecular weight of 500 or less in the hydrolyzate by gel filtration chromatography for peptides. It can be calculated by subtracting the free amino acid content in the hydrolyzate.
  • the content of free amino acids in the hydrolyzate is preferably 10% by weight or less, and more preferably 5% by weight or less.
  • the proportion of the fraction having a molecular weight of 500 or more in the total amount of peptide and free amino acid in the hydrolyzate is preferably 40% by weight or less, More preferably, it is not more than wt%.
  • protease Hydrolysis is preferably performed by protease treatment.
  • Protease treatment is carried out using the above-mentioned pea protein material slurry or aqueous solution as a substrate and the following proteases.
  • the protease used here is of animal origin, plant origin or microbial origin, and is classified into “metal protease”, “acidic protease”, “thiol protease”, “serine protease” in the classification of protease, preferably “metal” It can be appropriately selected from proteases classified as “protease”, “thiol protease”, and “serine protease”.
  • a degradation method in which enzymes belonging to two or more kinds or three or more kinds of different classes are acted on sequentially or simultaneously can increase the proportion of relatively low molecular weight peptides such as dipeptides and tripeptides.
  • protease is a classification method based on the type of amino acid at the active center, which is usually performed in the field of enzyme science.
  • Methodal Protease includes Bacillus Neutral Protease, Streptomyces Neutral Protease, Aspergillus Neutral Protease, “Samoase”, etc.
  • Protease includes bromelain, papain and the like
  • serine protease includes trypsin, chymotrypsin, subtilisin, Streptomyces alkaline protease, “Alcalase”, “Biolase” and the like.
  • the classification of other enzymes can also be confirmed by their pH and reactivity with inhibitors.
  • enzymes having different active centers differ greatly in the site of action on the substrate, it is possible to reduce the “uncut residue” and efficiently obtain an enzyme degradation product.
  • enzymatic degradation products can be more efficiently produced by using enzymes from different origins (origin organisms). Even in the same classification, if the origin is different, the site of action of the substrate protein is also different, and as a result, the proportion of dipeptides and tripeptides can be increased. These proteases preferably have low exo activity.
  • the reaction pH and reaction temperature of the protease treatment may be set in accordance with the characteristics of the protease to be used, and the reaction pH is usually carried out near the optimum pH, and the reaction temperature may be carried out around the optimum temperature. In general, the reaction can be carried out at a reaction temperature of 20 to 80 ° C, preferably 40 to 60 ° C. After the reaction, the enzyme is heated at a temperature sufficient to inactivate the enzyme (about 60 to 170 ° C.) to inactivate the remaining enzyme activity.
  • the reaction solution after the protease treatment can be used as it is or after being concentrated, but it can usually be used in the form of a dry powder by sterilization, spray drying, freeze drying or the like.
  • Sterilization is preferably heat sterilization, and the heating temperature is preferably 110 to 170 ° C, more preferably 130 to 170 ° C.
  • the heating time is preferably 3 to 20 seconds.
  • the reaction solution can be adjusted to an arbitrary pH, and precipitates and suspensions generated during pH adjustment can be removed by centrifugation, filtration, or the like. Furthermore, it can also refine
  • the hydrolyzate of the protein composition mainly composed of the pea protein hydrolyzate of the present invention can be widely used as a pharmaceutical form.
  • the oral form ie, food or As a form added to the feed, it can be appropriately mixed with other raw materials as necessary.
  • it can be used in various forms such as liquid, powder, tablet, capsule and the like.
  • When used as a mixed form in foods it can be used by mixing with solid foods such as biscuits, cakes, breads, etc., or it can be used for fluid or semi-solid foods such as bavaria, mousse or pudding. There is no problem with mixing. It can also be taken as a beverage by dissolving in water or the like.
  • the oral anti-inflammatory functional agent of the present invention can be used in combination with other foods and drinks and ingredients exhibiting an anti-inflammatory effect.
  • lactic acid bacteria fermentation for example, lactic acid bacteria drinks, yogurts, and cheeses
  • a particularly strong effect can be obtained.
  • other anti-inflammatory effects include polyphenols (tea catechin, anthocyanin, cyanidin, chlorogenic acid, etc.), carotenoids (astaxanthin, lycopene, lutein, etc.), glucosamine, chondroitin, curcumin, capsaicin, etc. Can be illustrated.
  • the peptide of the present invention may be denatured by decomposition or the like due to heat at the time of sterilization of food.
  • carbohydrates, vitamins, minerals and the like are mixed and used as a supplement.
  • it can be used by mixing with known feed without being limited to land and fishery.
  • lactic acid bacteria used for lactic acid bacteria fermented foods such as lactic acid bacteria beverages
  • lactic acid bacteria generally used as foods can be used.
  • Lactobacillus genus bacteria L.casei, L.plantarum, L.brevis, l.acidophilus, L.pentous etc.
  • Lactococcus genus bacteria L.lactis, L.cremoris etc.
  • Bifidobacterium genus bacteria B.bididum, B.adolescentis etc.
  • Example 1 Preparation of Isolated Pea Protein
  • a separated pea protein as a pea protein material was prepared as follows. That is, 50 g of pea seed pulverized product was dissolved and dispersed in 500 ml of water, and extracted at 50 ° C. for 1 hr under the condition of pH 9.0. The fiber fraction and pea soymilk were separated using a centrifuge. The pH of the obtained soymilk was adjusted to 4.5, and the precipitated curd fraction was collected with a centrifuge. This fraction was neutralized and sterilized by heating at 120 ° C. for 10 seconds to prepare a separated pea protein.
  • Example 2 Preparation of pea protein hydrolyzate
  • an enzymatic degradation product by protease was prepared as follows. To a 3% by weight separated pea protein solution, “Samoase” (origin; Bacillus thermoproteolyticus, metalloprotease, Daiwa Kasei) was added at 2% by weight per protein and allowed to act at pH 9.0, 58 ° C. for 60 minutes. Next, “Biolase” (origin; Bacillus sp., Serine protease, Nagase Chemtech) was added at 1% by weight per protein and allowed to act at pH 7.5 for 60 minutes at 58 ° C.
  • “Samoase” origin; Bacillus thermoproteolyticus, metalloprotease, Daiwa Kasei
  • Biolase origin; Bacillus sp., Serine protease, Nagase Chemtech
  • “Sumitum FP” (source: Aspergillus sp., Metalloprotease, Shin Nippon Chemical Industry) was added at 1% by weight per protein and allowed to act at pH 7.5, 58 ° C. for 60 minutes. After the above treatment, the reaction was stopped at 90 ° C. for 20 minutes, and then freeze-dried to obtain a pea protein hydrolyzate sample.
  • Example 3 Preparation of isolated soybean protein Isolated soybean protein was prepared from low-denatured defatted soybean as follows. A 1 kg kg of low-denatured defatted soybean was extracted with a hot water slurry to obtain defatted soymilk by removing the okara fraction with a centrifuge. Next, the pH of the obtained defatted soymilk was adjusted to 4.5 and subjected to isoelectric precipitation, and an acid precipitation card was obtained and neutralized with a centrifuge. Furthermore, each obtained fraction was neutralized and sterilized by heating at 120 ° C. for 10 seconds.
  • Example 4 Preparation of Soy Protein Hydrolyzate A sample obtained by treating the isolated soy protein obtained in Production Example 3 in the same manner as in Production Example 2 was used as a soy protein hydrolysate.
  • Example 5 Other food-derived protein hydrolysates For comparison with other food-derived protein hydrolysates, commercially available products were obtained. Casein hydrolyzate CE90M and Peptopro (manufactured by DMV) as whey protein hydrolysates, HW-3 (manufactured by Snow Brand Milk Products) and Thermox690 (manufactured by Glanbia), collagen hydrolysates as whey whey hydrolysates FSP-AS-L (Nippi) and Chicken collagen (Nippon Ham Health Create) were obtained as samples.
  • CE90M and Peptopro manufactured by DMV
  • HW-3 manufactured by Snow Brand Milk Products
  • Thermox690 manufactured by Glanbia
  • IL-6 concentration by ELISA In order to measure the IL-6 concentration in the culture medium by ELISA, Purified rat anti-mouse IL-6 (primary antibody), Biotinylated rat anti-mouse IL-6 (secondary antibody), Recombinant mouse IL-6 ( Standard IL-6) and Streptavidin-Alkalin Phosphate were all purchased from BD Pharmingen and used.
  • the plate was washed 3 times with PBS-Tween20 (PBS-T) and thoroughly drained. Thereafter, 3% BSA in PBS-T was added in an amount of 100 ⁇ l / well, and allowed to stand at room temperature for 1 hr, and then washed 3 times with PBS-T to thoroughly drain water. Samples diluted appropriately with PBS-T were added in an amount of 50 ⁇ l / well, and allowed to stand at 4 ° C. for 24 hours, and then washed 3 times with PBS-T to drain thoroughly.
  • PBS-Tween20 PBS-Tween20
  • the molecular weight distribution of each food-derived protein hydrolyzate was measured by the HPLC method using the following gel filtration column.
  • An HPLC system using a gel filtration column for peptides was assembled, a known peptide serving as a molecular weight marker was charged, and a calibration curve was obtained in relation to the molecular weight and the retention time.
  • the molecular weight markers are [ ⁇ -Asp] -Angiotensin II ⁇ -Asp-Arg-Val-Tyr-Ile-His-Pro-Phe (molecular weight 1046) as octapeptide and Angiotensin IV Val-Tyr- as hexapeptide.
  • the ratio (%) of the peptide fraction with a molecular weight of 500 or less to the total amount of peptide and free amino acid in the hydrolyzate is determined by the ratio of the area with a molecular weight of 500 or less (time range) to the total absorbance chart area. Determined (column used: Superdex Peptide 7.5 / 300GL (manufactured by GE Healthcare Japan). Solvent: 1% SDS / 10 mM phosphate buffer, pH 8.0, column temperature 25 ° C, flow rate 0.25 ml / min, detection Wavelength: 220 nm).
  • each food-derived protein hydrolyzate was measured by amino acid analysis.
  • Hydrolyzate (4 mg / ml) was added to an equal volume of 3% sulfosalicylic acid and shaken at room temperature for 15 minutes. Centrifugation was carried out at 10,000 rpm for 10 minutes, and the resulting supernatant was filtered through a 0.45 ⁇ m filter, and free amino acids were measured with an amino acid analyzer (JLC500V manufactured by JEOL Ltd.).
  • the free amino acid content in the protein was calculated as a ratio to the protein content obtained by the Kjeldahl method.
  • the value obtained by subtracting the “free amino acid content” from the “ratio of the peptide fraction having a molecular weight of 500 or less” obtained above was defined as the “dipeptide / tripeptide content” in the hydrolyzate.
  • Dr.SPSSII manufactured by SPSS was used for the significant difference test, and one-way analysis of variance between multiple groups was evaluated using the Turkey-Kramer method.
  • Example 6 Anti-inflammatory effect of each food-derived protein hydrolyzate on mouse macrophage cells Pea protein hydrolyzate obtained in Example 2, soybean protein hydrolyzate obtained in Example 4, and each food-derived In order to evaluate the anti-inflammatory effect of the protein hydrolyzate, mouse macrophage cell culture described in the measurement method and IL-6 concentration were measured by ELISA.
  • the anti-inflammatory effect by the cheese of patent document 2 has only a low effect compared with a pea, or originates in the metabolite of the lactic acid bacteria used at the time of cheese production.
  • the pea protein has less anti-inflammatory function than non-patent document 1 and non-patent document 2 because 11S type protein (legmin type) that exhibits anti-inflammatory function as described in patent document 3 is less than soybean protein.
  • the anti-inflammatory function exhibited by pea protein hydrolyzate was equivalent to or better than that of soybean protein hydrolyzate.
  • Example 7 Combined effect with lactic acid bacteria Regarding the anti-inflammatory effect on mouse macrophage cells, the combined effect of pea protein hydrolyzate and lactic acid bacteria was verified. Lactobacillus casei was used as the lactic acid bacterium, and mouse macrophage cell culture described in the measurement method and IL-6 concentration were measured by ELISA. Lactic acid bacteria were added at a concentration of 1 ⁇ 10 5 cells when CpG was added, and a system in which pea protein hydrolyzate was added and a system in which pea protein hydrolyzate was not added were set, and IL-6 concentration was measured. As a result, it was observed that IL-6 secreted by mouse macrophage cells was reduced even in the lactic acid bacteria addition system, but it was confirmed that the effect was increased by using it together with pea protein hydrolysate.
  • Example 8 Preparation of lactic acid bacteria beverage and anti-inflammatory effect
  • the above-mentioned pea protein hydrolysis was applied to the commercially available lactic acid bacteria beverage "Yakult" (manufactured by Yakult Honsha Co., Ltd.).
  • the sample was dissolved to a final concentration of 1% and used as a sample.
  • IL-6 secreted by mouse macrophage cells was reduced.

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Abstract

Le but de la présente invention est de produire un agent fonctionnel anti-inflammatoire à partir d'une matière première qui ne contient aucun allergène alimentaire majeur et qui peut être largement utilisée comme matière alimentaire. L'invention concerne ainsi un agent fonctionnel anti-inflammatoire destiné à une application par voie orale qui ne contient aucun allergène et qui a un effet puissant qui peut être produit en utilisant, comme ingrédient actif, un hydrolysat de protéines de pois qui est une matière alimentaire. Le produit de la présente invention peut être largement utilisé sous la forme d'un agent médicinal ou sous une forme telle qu'il peut être contenu dans un aliment destiné à l'alimentation humaine ou animale.
PCT/JP2012/079734 2011-11-18 2012-11-16 Agent fonctionnel anti-inflammatoire destiné à une application par voie orale WO2013073648A1 (fr)

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JP2011252120 2011-11-18
JP2011-252120 2011-11-18

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WO2013073648A1 true WO2013073648A1 (fr) 2013-05-23

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JP2021106624A (ja) * 2019-06-20 2021-07-29 ユニ・チャーム株式会社 ペットフード
CN117551171A (zh) * 2023-10-19 2024-02-13 湖北健肽生物科技有限公司 豌豆肽、修饰豌豆肽的制备方法及改善胃肠道功能的用途

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JP2019508054A (ja) * 2016-03-15 2019-03-28 ザ コカ・コーラ カンパニーＴｈｅ Ｃｏｃａ‐Ｃｏｌａ Ｃｏｍｐａｎｙ 加水分解エンドウ豆タンパク質を含有する冷凍飲料組成物
JP2021106624A (ja) * 2019-06-20 2021-07-29 ユニ・チャーム株式会社 ペットフード
JP7204816B2 (ja) 2019-06-20 2023-01-16 ユニ・チャーム株式会社 ペットフード
CN117551171A (zh) * 2023-10-19 2024-02-13 湖北健肽生物科技有限公司 豌豆肽、修饰豌豆肽的制备方法及改善胃肠道功能的用途

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