WO2006132273A1 - Composition comprenant un peptide ayant pour effet de réduire la consommation d’aliments - Google Patents

Composition comprenant un peptide ayant pour effet de réduire la consommation d’aliments Download PDF

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Publication number
WO2006132273A1
WO2006132273A1 PCT/JP2006/311426 JP2006311426W WO2006132273A1 WO 2006132273 A1 WO2006132273 A1 WO 2006132273A1 JP 2006311426 W JP2006311426 W JP 2006311426W WO 2006132273 A1 WO2006132273 A1 WO 2006132273A1
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Prior art keywords
peptide
conglycinin
composition
activity
enzyme
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PCT/JP2006/311426
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English (en)
Japanese (ja)
Inventor
Toru Hira
Motohiko Hirotsuka
Toshihiro Nakamori
Hiroshi Hara
Kozo Asano
Hitoshi Chiba
Fusao Tomita
Original Assignee
A-Hitbio Inc.
National University Corporation Hokkaido University
Fuji Oil Co., Ltd.
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Application filed by A-Hitbio Inc., National University Corporation Hokkaido University, Fuji Oil Co., Ltd. filed Critical A-Hitbio Inc.
Priority to JP2007520140A priority Critical patent/JPWO2006132273A1/ja
Publication of WO2006132273A1 publication Critical patent/WO2006132273A1/fr

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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
    • 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
    • A23L33/30—Dietetic or nutritional methods, e.g. for losing weight
    • 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
    • A61K38/012—Hydrolysed proteins; Derivatives thereof from animals
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P3/00—Drugs for disorders of the metabolism
    • A61P3/04—Anorexiants; Antiobesity agents
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P3/00—Drugs for disorders of the metabolism
    • A61P3/06—Antihyperlipidemics
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P3/00—Drugs for disorders of the metabolism
    • A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
    • A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P9/00—Drugs for disorders of the cardiovascular system
    • A61P9/12—Antihypertensives
    • 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

Definitions

  • the present invention relates to a peptide that suppresses food intake and reduces hunger when taken orally, and various compositions containing the peptide.
  • the amphetamine class of mazindol has been put to practical use as a drug that suppresses appetite for the treatment of obesity.
  • due to the direct effects on the center and the habitual nature associated with this drug its use is limited only to highly obese patients, and a safer method is desired.
  • Non-Patent Documents 1 to 4 It is known that various hormones (gastrointestinal hormones) secreted from endocrine cells of the gastrointestinal tract have a function of suppressing appetite. Since these peptide hormones are easily degraded in the digestive tract lumen when administered orally, it is difficult to absorb them and exert their effects, and they must be administered in blood. Yes. In that case, there are high costs involved in peptide synthesis, complicated administration methods, and problems.
  • Cholecystokinin (hereinafter sometimes abbreviated as “CCK”) has been found to have an effect of suppressing appetite ahead of other gonadotropins (GLP-1, PYY) and the like. It is a gastrointestinal hormone and is caused by dietary lipids, proteins, amino acids, etc. Secretion is stimulated (Non-patent Document 2). However, in order to limit calorie intake, energy efficiency is high!
  • Patent Document 1 JP 2004-10569 A
  • Non-Patent Document 1 Woods SC, Am J Physiol Gastrointest Liver Physiol, 286 (1): G7-13, 2004
  • Non-Patent Document 2 Moran TH, et al, Am J Physiol Gastrointest Liver Physiol, 286 (2): G 183-8, 2004
  • Non-Patent Document 3 Moran TH, et al, Am J Physiol Gastrointest Liver Physiol, 286 (5): G 693-7, 2004
  • Non-Patent Document 4 Tso P, et al, Am J Physiol Gastrointest Liver Physiol, 286 (6): G885—90, 2004
  • Non-Patent Document 5 Nishi T, et al, J Nutr, 133 (2): 352-7, 2003
  • Non-Patent Document 6 Nishi T, et al, J Nutr, 133 (8): 2537-42, 2003
  • the present invention is a peptide having an anti-feeding action that can be orally administered or ingested and can also be applied to humans, in particular, a peptide that is low-cost and practical, less bitter and safe and easy to ingest. And an antifeedant, food, pharmaceutical composition, feed and the like containing the same.
  • the present inventor prepares a peptide composition by degrading soybean ⁇ -conglycinin, which is a food-derived protein, with various food-adding enzymes. By selecting a peptide composition with high CCK release activity, and further reducing the feeling of hunger and satiety due to actual ingestion in humans. By observing the triggering, the present invention was completed.
  • the present invention is a.
  • a peptide obtained by degrading ⁇ -conglycinin with an enzyme having an enzyme activity equivalent to that of bromelain or promelain, and contains a peptide having a cholecystocone secretion promoting activity or an antifeedant activity A composition to make;
  • composition according to (1) or (2), wherein the enzyme is bromelain
  • a cholecystokinin secretion promoter comprising the composition according to any one of (1) to (3) above;
  • a pharmaceutical composition comprising the antifeedant or cholecystokinin secretion promoter according to (4) or (5) above;
  • a peptide having cholecystokinin secretion-promoting activity or feeding-suppressing activity comprising a step of decomposing ⁇ -conglycinin by an enzyme that preferentially cleaves a peptide bond on the carboxyl group side of an arginine residue.
  • composition of the present invention an antifeedant, a cholecystocun secretion promoter, and a pharmaceutical composition, food, and feed containing these (hereinafter referred to as "the composition of the present invention") )
  • the composition of the present invention has the activity of stimulating the secretion of cholecystokinin, which has an appetite-suppressing effect, so that hunger can be reduced by taking it orally.
  • the composition of the present invention is obtained by treating a safe food material with an enzyme for food processing, so that the safety is high and the cost is low.
  • composition of the present invention can be taken not only in a solid form such as a capsule but also in a beverage or the like.
  • the effect of the composition of the present invention is exhibited about 15 minutes after ingestion, the user feels full before taking the peptide composition of the present invention about 15 minutes before eating. This can prevent excessive caloric intake thereafter.
  • a synergistic effect with the feeling of fullness caused by the actual meal can be expected.
  • FIG. 1 is a graph showing the amount of CCK released from gastrointestinal endocrine cell line STC-1 by various ⁇ -conglycinin degradation products. The value indicates the concentration of CCK released into the culture supernatant during 60 minutes.
  • FIG. 2 is a graph showing food intake from 30 minutes to 90 minutes after administration of a j8-conglycinin degradation product solution into the rat stomach.
  • the values are the average of 12 animals and the standard error. * Indicates that there is a significant difference (P ⁇ 0. 05) compared to the water-administered group.
  • FIG. 3 shows the total of 2 days after administration of
  • the numbers represent the mean (24-30) change from the pre-tasting value for each subject scored by the VAS method and the standard error.
  • ⁇ Hainu Mouth 3g (25 people) Mouth: High-Ute 1.5 g + ⁇ —Conglycine bromelain degradation product 1.5 g (24 people)
  • FIG. 5 is a graph showing changes in satiety after ingestion of ⁇ -conglycinin bromelain degradation product or soybean peptide solution.
  • the numerical value represents the average value (24-30 people) and standard error of changes in value before each tasting of each subject scored by the VAS method.
  • ⁇ High Newt 3g (25 people) Mouth: High-Ute 1.5g + ⁇ —Conglycine Bromelain Degradation Product 1.5g (24 people)
  • Plots with different alphabets indicate that they are significantly different from each other at the same time.
  • FIG. 6 is a graph showing changes in the allowable dietary intake after ingestion of ⁇ -conglycinin bromelain degradation product or soybean peptide solution.
  • the numbers represent the mean (24-30) change from the pre-tasting value for each subject scored by the VAS method and the standard error.
  • ⁇ High-yuteu 3g (25 people) Mouth: High-yute 1.5g + j8—Conglycine bromelain degradation product 1.5g (24 people)
  • Plots with different alphabets indicate that there is a significant difference from each other at the same time.
  • FIG. 7 is a diagram showing the CCK releasing activity of the active peptide fraction in ⁇ -conglycinin degradation product. Indicates that there is a significant difference between groups with different alphabets ( ⁇ ⁇ 0. 05).
  • the peptide of the present invention is obtained by degrading j8-conglycinin.
  • j8 Conglycinin is a major component of soy protein.
  • ⁇ -conglycinin except for soy allergies, is usually already eaten and has been confirmed to be safe by ingesting 5 grams a day for 3 months in humans. (Kanbara No. 2 ⁇ 16 ⁇ 17, Kanbara et al.) Has been confirmed to be safe.
  • ⁇ -conglycinin used in the present invention may be derived from soybeans or may be derived from natural raw materials such as other beans. It may be a thing. From the viewpoint of cost and the like, j8-conglycinin derived from soybean is preferable.
  • the enzyme used for the degradation of ⁇ -conglycinin is not particularly limited as long as it is an enzyme that preferentially cleaves the peptide bond on the carboxyl group side of the arginine residue in the polypeptide, such as bromelain.
  • an enzyme that preferentially cleaves the peptide bond on the carboxyl group side of the arginine residue in the polypeptide such as bromelain.
  • a peptide composition having little or no bitterness due to the presence of an aromatic amino acid at the end of the peptide can be obtained.
  • enzymes that preferentially cleave the peptide bond on the carboxyl side of the arginine residue in the polypeptide include thrombin, endoproteinase Arg-C, and cathebsin B1. From the viewpoints of safety, availability, cost, etc., bromelain is preferable.
  • Bromelain is a cystine protease derived from a plant belonging to the pineapple family (Bromeliaceae), and is mainly contained in pineapple rhizomes and fruits.
  • stem bromelain EC.3.4.22.4, EC.3.4.22.32
  • funolate bromelain EC.3.4.22.5, EC.3.4.22.33
  • bromelain derived from pineapple stem EC.3.4.22.4
  • Bromelain is an enzyme that has wide substrate recognition in proteolysis, but has high resolution against synthetic substrates including arginine. It is used for meat processing for food processing, and for inflammation for medical use. It is also used for improvement and has many advantages such as being easy to obtain and highly safe.
  • the degradation of ⁇ -conglycinin can be performed, for example, as follows.
  • ⁇ -Conglycinin is suspended in ion-exchanged water at a weight concentration of 10%, and ⁇ is adjusted to 6.0 with sodium hydroxide aqueous solution. Add bromelain to the substrate concentration of 0.1%, incubate at 50 ° C for 1 hour, and raise to 100 ° C to stop the enzyme reaction. The insoluble fraction is removed by centrifugation and filtration, and the resulting peptide solution is lyophilized to obtain a ⁇ -conglycinin bromelain degradation product. Any concentration of ⁇ -conglycinin can be used as long as it can be suspended (maximum 10%).
  • the concentration with respect to the substrate is 0.01% to 10%, 0.05 to 5% is preferred, and 0.05 to 1% is particularly preferred.
  • the optimum reaction temperature is 45 ° C to 60 ° C, with 50 ° C being optimal.
  • the reaction time is a force depending on the enzyme concentration'reaction temperature and the like. Generally, about 15 minutes to 20 hours is appropriate, and 30 minutes to 5 hours is preferable.
  • pH 4. 4. 0 to 7.0 force is preferred, 4. 0 to 6.5 force is particularly preferred, in vivo and in vitro tests Therefore, 6.0 was judged to be optimal.
  • the active peptide can be concentrated by treating the degradation product of ⁇ -conglycinin with a cation exchange resin under appropriate conditions.
  • the cation exchange resin used is preferably a weakly acidic cation exchange resin such as acrylic acid or methacrylic acid.
  • “Diaion” (registered trademark) WK series of Mitsubishi Igaku Co., Ltd., or commercially available products equivalent to them can be used.
  • the active peptide is recovered in the fraction adsorbed on the cation exchange resin, it is thought that it contains a large amount of basic amino acid such as arginine. Elution from the cation exchange resin is carried out using 0.7 to 0.9%, preferably 0.8% ammonia.
  • peptide is used as an encompassing term if it is composed of two or more amino acid residues and is smaller than the original protein or polypeptide.
  • the peptide is preferably a hydrolyzate having a molecular weight of about 200 to 20,000 (2 to 200 amino acid residues).
  • composition of the present invention means that it contains at least one component (may be another peptide! /) In addition to one kind of peptide.
  • cholecystocun secretion promoting activity can be examined as follows (CCK secretion test).
  • a mouse duodenum-derived cell line STC-1 widely used as a model of CCK-producing cells is used.
  • STC-1 cells cultured in 24-well plates were reacted in ⁇ -conglycinin hydrolyzate solution (lmg / ml) for 60 minutes, and the amount of CCK released into the supernatant was determined using Enzyme Immuno Assay (EIA). taking measurement.
  • EIA Enzyme Immuno Assay
  • 13-conglycinin hydrolyzate or a buffer not supplemented with its peptide (10 mM Hepes, pH 7.4) is used as a control.
  • cholecystocun secretion promoting activity means that cholecystocun secretion is significantly promoted as compared to the control when examined by the test method described above.
  • “having anti-feeding activity” means that, when examined by the above test method, it significantly inhibits feeding compared to the control.
  • composition and the like of the present invention can be administered orally orally.
  • the administration or ingestion amount can be 2 to 5 g, preferably 3 to 5 g, as the above-mentioned j8-conglycinin degradation product. Such intake is sufficiently safe.
  • the peptide-containing composition of the present invention can be used as an antifeedant or a cholecystoki secretion promoter containing the same.
  • the antifeedant or cholecystokinin secretion promoter of the present invention can be combined with components such as a pharmaceutically acceptable general carrier or excipient to form a pharmaceutical composition.
  • a pharmaceutically acceptable general carrier or excipient such as a pharmaceutically acceptable general carrier or excipient.
  • the term “medicine” is used as a concept encompassing not only those applied to humans but also those applied to animals (veterinary medicine).
  • the feeding inhibitor and the cholecystocun secretion promoter are effective for animals, they are combined with known general nutritional components. Or a feed containing the antifeedant or the secretecone secretion promoter of the present invention (pet food, livestock feed, etc.) in combination with other active ingredients.
  • Soybean j8 -.. The conglycinin was suspended in deionized water, pH was adjusted to 4 0-9 0 at Mizusani ⁇ sodium solution, which was used as a decomposition start P H. No buffer solution is used to eliminate the need for desalting.
  • Abbreviated names (labels) from A-1 to 14 were provided for the degradation products with different enzyme names and degradation pH.
  • the upper small intestinal brush border membrane soluble component of 3 & ⁇ -0 & ⁇ male rats aged 8-10 weeks was fixed on the sensor chip CM5 of the biomolecular interaction analyzer BIACORE3000.
  • Each type of conglycinin degradation product 500 / zg / ml was added as an analyte, and the binding amount (Resonance Unit: RU) to the small intestinal brush border membrane component on the sensor chip was measured.
  • Example 1 Specifically, using the mouse duodenum-derived cell line STC-1 widely used as a model for CCK-producing cells, various hydrolysates selected based on the binding test results of Example 1 (prepared in the same manner as in Example 1). The CCK release activity of the digestive tract endocrine cell strength of soybean ⁇ 8—conglycinin degradation product underlined in Table 1 was measured. STC-1 cells cultured in 24-well plates are reacted in the hydrolyzate solution (lmg / ml) for 60 minutes, and the amount of CCK released in the supernatant is determined using the Enzyme Immuno Assay (EIA) kit (Cholecystokinin Octapeptide EIA kit, Phenix Pharmaceuticals, EK-069-04).
  • EIA Enzyme Immuno Assay
  • the results are shown in Figure 1.
  • the vertical axis shows the concentration of CCK in the STC-1 cell supernatant 60 minutes after sample addition.
  • 9 hydrolysates excluding protease S hydrolyzate (“E-1” in Figure 1)
  • the product showed higher CCK release activity than the negative control without the hydrolyzate (“Blk” in FIG. 2).
  • pepsin decomposition product was used as a positive control in (in FIG. 2, "P mark ton e") the same extent showed the strongest ⁇ CCK releasing activity of 3-4 times that of the positive control It was decided to examine the feeding suppression effect of the thermolysin degradation product (“C-1” in FIG. 2) and bromelain degradation product (“G-1” in FIG. 1) in the rat feeding test.
  • a soy-conglycone bromelain degradation product 1.5 g or 3 g dissolved in 100 ml of low-calorie sports drinks sold on the market (“Pocari Sweat Stevia", Otsuka Pharmaceutical Co., Ltd., l lkcal / 100 ml) was used.
  • a commercially available soy peptide (“Hyute”, Fuji Oil Co., Ltd.) prepared at the same concentration was used.
  • the following three test samples (100 ml each) were prepared and tested by the double blind method. Each calorie intake is 23 kcal (protein 12 kcal, beverage l lkcal).
  • Group H High-Ute 3.
  • Group HB High-Ute 1.5 g + j8—Conglycine bromelain degradation product 1.5 g •
  • Group B j8—Conglycine bromelain degradation product 3.
  • Subjects were healthy men and women aged 21-35 years (19 men and 16 women). These subjects were fasted for 3 hours after lunch, had 100 ml of any of the above test samples taken, immediately before taking the test sample (set to 0 minutes), and every 15 minutes after ingestion (15, 30, 45 minutes later), appetite indicators (hunger, satiety, acceptable intake) were recorded on the Visual Analogue Scale (VAS). With the VAS method, the left end of the 100mm horizontal line is 0 (nothing at all) and the right end is 100 (very much), and each item is marked at any position with the degree of! Is the method.
  • VAS Visual Analogue Scale
  • the food intake group (Powder group) was always higher than the other two sample groups, and the mixed soy peptide and j8-conglycine bromelain degradation product group (HB group) was intermediate between the other two samples. Although there was a tendency to show a value, no significant change was seen.
  • Hungry sensation and tolerable intake remained lower than the initial values for 45 minutes in the ⁇ -conglycone bromelain degradation product intake group (group IV), but in the other two sample groups than before administration. But their degree increased.
  • the feeling of satiety remained higher in the ⁇ -conglycone bromelain-digested group (group IV) than the initial value for 45 minutes, and decreased in the other two groups compared to before administration. did.
  • the active peptide in the bromelain degradation product of ⁇ -conglycinin was concentrated by fractionation by batch method using cation exchange resin.
  • Peptide solution in weak cation exchange resin (Mitsubishi Chemical Diaion WK100), which was prepared in Example 1 from the bromelain degradation product of j8-conglycinin, conditioned to H + form with 1N hydrochloric acid tower and washed with demineralized water And stirred at 4 ° C. Thereafter, the non-adsorbed fraction was collected with demineralized water, and the adsorbed fraction was collected by eluting with 0.8 M and 1. OM ammonia. As for the ammonia elution fraction, the ammonia was removed by a rotary evaporator, and then freeze-dried powder was obtained. The non-adsorbed fraction was lyophilized without being concentrated.
  • weak cation exchange resin Mitsubishi Chemical Diaion WK100
  • the collected fraction was 59% in terms of dry matter weight ratio in the non-adsorbed fraction and 41% in the adsorbed fraction (0.8 M ammonia: 16%, 1. OM ammonia: 25%).
  • the CCK releasing activity of each of the above fractions was measured using a mouse small intestine-derived CCK producing cell line STC-1.
  • STC-1 cells cultured in a 48-well plate are reacted in a buffer containing the above peptide fractions for 60 minutes, and the amount of CCK released in the supernatant is used with a commercially available Enzyme 'Imnoassay' kit (Phoenix pharmaceutical). I made a mistake.
  • the bromelain degradation product of ⁇ -conglycinin prepared in Example 7 was fractionated with ion-exchange resin.
  • the 8% ammonia-eluted fraction was dissolved in demineralized water, and the residual ammonia concentration was measured using a kit (Ammonia Test Measured using Yakuhin Kogyo).

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Abstract

L'invention concerne un peptide ayant pour effet de diminuer la consommation d’aliments qui peut être administré ou pris oralement et est applicable à un organisme humain, en particulier le peptide qui est peu coûteux et utile au plan pratique, présente un goût peu amer, est fiable et facilement assimilable par un organisme ; et un agent diminuant la consommation d’aliments, un aliment, une composition pharmaceutique, un aliment animalier ou similaire comprenant le peptide. L'invention concerne également une composition comprenant un peptide qui peut être produit par digestion de la β-conglycinine par une enzyme capable de cliver de façon prédominante une liaison peptidique du côté carboxyle dans un résidu d'arginine et qui a une activité promotrice sur la sécrétion de cholécystokinine ou une activité réduisant la consommation d’aliments.
PCT/JP2006/311426 2005-06-08 2006-06-07 Composition comprenant un peptide ayant pour effet de réduire la consommation d’aliments WO2006132273A1 (fr)

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Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2009189276A (ja) * 2008-02-13 2009-08-27 Rohto Pharmaceut Co Ltd ダイズペプチド含有液状食品
JP2012513771A (ja) * 2008-12-31 2012-06-21 ソレイ リミテッド ライアビリティ カンパニー Ｃｃｋ放出能力が増強されたタンパク質加水分解組成物
WO2012137825A1 (fr) 2011-04-04 2012-10-11 味の素株式会社 Procédé de fabrication pour un aliment à goût renforcé, et procédé pour renforcer le goût d'aliment
JP2017528149A (ja) * 2015-04-30 2017-09-28 チャイナ ナショナル リサーチ インスティテュート オブ フード アンド ファーメンテーション インダストリーズ 低アレルギー誘発性で苦味の低下した大豆オリゴペプチド、その調製方法、およびその用途
JP2019530730A (ja) * 2016-09-07 2019-10-24 国立大学法人京都大学 精神疾患を治療するためのペプチドおよびペプチドコンジュゲート

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH06197788A (ja) * 1993-01-06 1994-07-19 Fuji Oil Co Ltd 蛋白質の製造法
JP2004010569A (ja) * 2002-06-10 2004-01-15 Kozo Asano コレシシトキニン分泌促進活性を有するアルギニン含有ペプチドおよびこれを含有する食品。
JP2005206545A (ja) * 2004-01-23 2005-08-04 Kyoto Univ 脂質代謝調節作用を有するダイズ由来ペプチド混合物およびその利用

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH03127958A (ja) * 1989-10-14 1991-05-31 Nakano Vinegar Co Ltd ペースト状食品素材
JP3726410B2 (ja) * 1997-03-28 2005-12-14 不二製油株式会社 大豆たん白含有飲料

Patent Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH06197788A (ja) * 1993-01-06 1994-07-19 Fuji Oil Co Ltd 蛋白質の製造法
JP2004010569A (ja) * 2002-06-10 2004-01-15 Kozo Asano コレシシトキニン分泌促進活性を有するアルギニン含有ペプチドおよびこれを含有する食品。
JP2005206545A (ja) * 2004-01-23 2005-08-04 Kyoto Univ 脂質代謝調節作用を有するダイズ由来ペプチド混合物およびその利用

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
MARUO F. ET AL.: "Koso Handbook", 1 March 1983, ASAKURA SHOTEN, pages: 545 - 546, XP003008017 *

Cited By (8)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2009189276A (ja) * 2008-02-13 2009-08-27 Rohto Pharmaceut Co Ltd ダイズペプチド含有液状食品
JP2012513771A (ja) * 2008-12-31 2012-06-21 ソレイ リミテッド ライアビリティ カンパニー Ｃｃｋ放出能力が増強されたタンパク質加水分解組成物
WO2012137825A1 (fr) 2011-04-04 2012-10-11 味の素株式会社 Procédé de fabrication pour un aliment à goût renforcé, et procédé pour renforcer le goût d'aliment
JP2017528149A (ja) * 2015-04-30 2017-09-28 チャイナ ナショナル リサーチ インスティテュート オブ フード アンド ファーメンテーション インダストリーズ 低アレルギー誘発性で苦味の低下した大豆オリゴペプチド、その調製方法、およびその用途
JP2019530730A (ja) * 2016-09-07 2019-10-24 国立大学法人京都大学 精神疾患を治療するためのペプチドおよびペプチドコンジュゲート
JP2020079266A (ja) * 2016-09-07 2020-05-28 国立大学法人京都大学 精神疾患を治療するためのペプチドおよびペプチドコンジュゲート
JP7061764B2 (ja) 2016-09-07 2022-05-02 国立大学法人京都大学 精神疾患を治療するためのペプチドおよびペプチドコンジュゲート
JP2022091961A (ja) * 2016-09-07 2022-06-21 国立大学法人京都大学 精神疾患を治療するためのペプチドおよびペプチドコンジュゲート

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