JPH02300137A - Peptide mixture - Google Patents
Peptide mixtureInfo
- Publication number
- JPH02300137A JPH02300137A JP1119194A JP11919489A JPH02300137A JP H02300137 A JPH02300137 A JP H02300137A JP 1119194 A JP1119194 A JP 1119194A JP 11919489 A JP11919489 A JP 11919489A JP H02300137 A JPH02300137 A JP H02300137A
- Authority
- JP
- Japan
- Prior art keywords
- casein
- peptide mixture
- sample
- minutes
- rennet
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 239000000203 mixture Substances 0.000 title claims abstract description 44
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 42
- 239000005018 casein Substances 0.000 claims abstract description 34
- 235000020244 animal milk Nutrition 0.000 claims abstract description 11
- 108091005804 Peptidases Proteins 0.000 claims abstract description 10
- 239000004365 Protease Substances 0.000 claims abstract description 10
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims abstract description 10
- 235000016709 nutrition Nutrition 0.000 abstract description 13
- 229940108461 rennet Drugs 0.000 abstract description 10
- 108010058314 rennet Proteins 0.000 abstract description 10
- 102000004190 Enzymes Human genes 0.000 abstract description 9
- 108090000790 Enzymes Proteins 0.000 abstract description 9
- 229940088598 enzyme Drugs 0.000 abstract description 9
- 108010019160 Pancreatin Proteins 0.000 abstract description 7
- 208000019423 liver disease Diseases 0.000 abstract description 7
- 230000035764 nutrition Effects 0.000 abstract description 7
- 229940055695 pancreatin Drugs 0.000 abstract description 7
- 238000006243 chemical reaction Methods 0.000 abstract description 6
- 238000000354 decomposition reaction Methods 0.000 abstract description 6
- 239000000706 filtrate Substances 0.000 abstract description 6
- 238000010521 absorption reaction Methods 0.000 abstract description 4
- 108010059378 Endopeptidases Proteins 0.000 abstract description 3
- 102000005593 Endopeptidases Human genes 0.000 abstract description 3
- 235000019640 taste Nutrition 0.000 abstract description 3
- 239000003814 drug Substances 0.000 abstract description 2
- 208000034657 Convalescence Diseases 0.000 abstract 1
- 230000001737 promoting effect Effects 0.000 abstract 1
- 210000000664 rectum Anatomy 0.000 abstract 1
- 238000012360 testing method Methods 0.000 description 27
- 239000000243 solution Substances 0.000 description 19
- 150000001413 amino acids Chemical class 0.000 description 18
- 238000000034 method Methods 0.000 description 18
- 102000011632 Caseins Human genes 0.000 description 15
- 108010076119 Caseins Proteins 0.000 description 15
- 239000000796 flavoring agent Substances 0.000 description 15
- 235000019634 flavors Nutrition 0.000 description 15
- 235000021240 caseins Nutrition 0.000 description 14
- 102000004196 processed proteins & peptides Human genes 0.000 description 14
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 13
- 239000000843 powder Substances 0.000 description 11
- 239000006228 supernatant Substances 0.000 description 9
- 229920001184 polypeptide Polymers 0.000 description 8
- 235000018102 proteins Nutrition 0.000 description 8
- 102000004169 proteins and genes Human genes 0.000 description 8
- 108090000623 proteins and genes Proteins 0.000 description 8
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 7
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 235000013336 milk Nutrition 0.000 description 6
- 239000008267 milk Substances 0.000 description 6
- 210000004080 milk Anatomy 0.000 description 6
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 5
- 239000007864 aqueous solution Substances 0.000 description 5
- 239000011575 calcium Substances 0.000 description 5
- 229910052791 calcium Inorganic materials 0.000 description 5
- 239000001110 calcium chloride Substances 0.000 description 5
- 229910001628 calcium chloride Inorganic materials 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 238000010438 heat treatment Methods 0.000 description 5
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 208000024891 symptom Diseases 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- 108090000746 Chymosin Proteins 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 235000015872 dietary supplement Nutrition 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 238000001914 filtration Methods 0.000 description 3
- 238000006460 hydrolysis reaction Methods 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 230000003908 liver function Effects 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 230000035484 reaction time Effects 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- 102100030840 AT-rich interactive domain-containing protein 4B Human genes 0.000 description 2
- 101000792935 Homo sapiens AT-rich interactive domain-containing protein 4B Proteins 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- -1 aromatic amino acids Chemical class 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 230000007515 enzymatic degradation Effects 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 208000007386 hepatic encephalopathy Diseases 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 235000014655 lactic acid Nutrition 0.000 description 2
- 239000004310 lactic acid Substances 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 235000020183 skimmed milk Nutrition 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 238000010998 test method Methods 0.000 description 2
- WBQJTPDOGLYTBE-VIFPVBQESA-N 1-nitroso-L-tryptophan Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CN(N=O)C2=C1 WBQJTPDOGLYTBE-VIFPVBQESA-N 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- 206010013911 Dysgeusia Diseases 0.000 description 1
- 206010016654 Fibrosis Diseases 0.000 description 1
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 235000019658 bitter taste Nutrition 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 230000007882 cirrhosis Effects 0.000 description 1
- 208000019425 cirrhosis of liver Diseases 0.000 description 1
- 239000003240 coconut oil Substances 0.000 description 1
- 235000019864 coconut oil Nutrition 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 239000002285 corn oil Substances 0.000 description 1
- 235000005687 corn oil Nutrition 0.000 description 1
- 239000012043 crude product Substances 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- 230000037213 diet Effects 0.000 description 1
- 235000005911 diet Nutrition 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 1
- 235000019256 formaldehyde Nutrition 0.000 description 1
- 229960004279 formaldehyde Drugs 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 230000002414 glycolytic effect Effects 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 239000002075 main ingredient Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 102000036068 sialic acid binding proteins Human genes 0.000 description 1
- 108091000315 sialic acid binding proteins Proteins 0.000 description 1
- 229940080237 sodium caseinate Drugs 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
Landscapes
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
Description
【発明の詳細な説明】
産業上の利用分野
本発明は、肝疾患あるいはその他の医療分野において、
経口栄養剤または経腸栄養剤として用いられ得る、風味
及び吸収が良好でかつフィッシャー値が高いペプチド混
合物に関する。[Detailed Description of the Invention] Industrial Application Field The present invention is applicable to liver diseases or other medical fields.
The present invention relates to a peptide mixture with good flavor and absorption and a high Fisher value that can be used as an oral or enteral nutrition.
従来技術の問題点
近年、肝炎あるいは肝硬変等の肝機能疾患の罹患率が増
加しつつある。この肝機能疾患に伴って発症する肝性脳
症は、現在肝疾患の最も重大な症状の一つであるとされ
ており、その症状の軽減方法及び治療方法の開発が望ま
れている。Problems with the Prior Art In recent years, the prevalence of liver function diseases such as hepatitis and cirrhosis has been increasing. Hepatic encephalopathy, which occurs with liver function disease, is currently considered to be one of the most serious symptoms of liver disease, and there is a desire to develop methods for alleviating and treating the symptoms.
その一つの治療方法として、栄養改善がある。One treatment method is nutritional improvement.
この目的のために、従来、経腸栄養剤が使用されている
が、その主成分はアミノ酸混合物、特に芳香族アミノ酸
（以下ＡＡＡと略称する）を全く含まず、分校アミノ酸
（以下、ＢＣＡＡと略称する）を比較的多量に含有する
混合物であった。For this purpose, enteral nutrition has conventionally been used, but its main ingredient is a mixture of amino acids, especially aromatic amino acids (hereinafter abbreviated as AAA), which do not contain any branched amino acids (hereinafter abbreviated as BCAA). The mixture contained a relatively large amount of
病態栄養において、食餌中のＡＡＡのモル含量でＢＣＡ
Ａのそれを除した値をフィッシャー値といい、高フィッ
シャー値のアミノ酸混合物が肝疾患治療に有効であると
されている（サージエリ−１第８缶、第１号、７７頁、
１９７６年；臨床栄養。In pathonutrition, the molar content of AAA in the diet
The value obtained by dividing that of A is called the Fisher value, and amino acid mixtures with high Fisher values are said to be effective in treating liver diseases (Surgery-1 No. 8 Can, No. 1, p. 77,
1976; Clinical Nutrition.
第７０巻、第７号、７９９頁、１９８７年参照）。(see Vol. 70, No. 7, p. 799, 1987).
ちなみに、世界各国で肝性脳症の治療に用いられている
経腸栄養剤のフィッシャー値は２０〜４５程度であり、
有効性が認められている。By the way, the Fisher value of enteral nutrition used in the treatment of hepatic encephalopathy in various countries around the world is around 20 to 45.
Recognized as effective.
従来の遊離アミノ酸混合物においては、必要な高フィッ
シャー値を得るために、アミノ酸を自由に配合できる利
点を有する。しかしながら、遊離アミノ酸は、風味、消
化、吸収の面で問題があった。詳述すれば、遊離アミノ
酸は風味が悪く、比較的軽症の患者あるいは回復期にあ
る患者に投与する経口栄養剤としては使用できないのが
実態であった。しかも、遊離アミノ酸の消化、吸収はペ
プチドのそれよりも劣り、また遊離アミノ酸は腸管にお
ける浸透圧を高め、それによって下痢症状を引き起こす
等の問題が指摘されていた。Conventional free amino acid mixtures have the advantage that amino acids can be incorporated freely in order to obtain the required high Fisher values. However, free amino acids have problems in terms of flavor, digestion, and absorption. Specifically, free amino acids have a bad taste and cannot be used as oral nutritional preparations for patients with relatively mild symptoms or patients in the recovery period. Moreover, it has been pointed out that the digestion and absorption of free amino acids is inferior to that of peptides, and that free amino acids increase the osmotic pressure in the intestinal tract, thereby causing diarrhea symptoms.
また、一般にペプチドは高分子量のポリペプチドおよび
蛋白質と比較して、消化、吸収が容易であって、経口栄
養剤および経腸栄養剤として最も優れていることが知ら
れている（栄養と食糧、第３１巻、２４７頁、１９７８
年）。 ′一方、ｋ−カゼインは、哺乳類の乳中
に存在するシアル酸結合蛋白質であり、例えば牛乳では
全カゼインの約１３％を占めており、その−次構造は既
に明らかにされている。In addition, peptides are generally easier to digest and absorb than high-molecular-weight polypeptides and proteins, and are known to be the best for oral and enteral nutrition (Nutrition and Food, Volume 31, page 247, 1978
Year). 'On the other hand, k-casein is a sialic acid-binding protein present in mammalian milk. For example, it accounts for about 13% of the total casein in milk, and its secondary structure has already been clarified.
しかしながら、一般に蛋白質をプロテアーゼで酵素分解
し、得られた分解物中の遊離したＡＡＡを除去する方法
において、ＡＡＡの完全な除去が困難であるために、フ
ィッシャー値の高いペプチドを得ることができず、また
回収率も低かった。However, in the general method of enzymatically decomposing proteins with protease and removing free AAA in the resulting decomposition product, it is difficult to completely remove AAA, making it impossible to obtain peptides with a high Fisher value. , and the recovery rate was also low.
また、分解率を高くする程、風味が悪化する等の欠点が
あった。In addition, there was a drawback that the higher the decomposition rate, the worse the flavor.
従って、軽症または回復期の肝疾患患者に経口投与でき
るペプチド混合物、換言すれば、風味が良好であり（遊
離アミノ酸が少ない）、且つフィッシャー値が高い（Ａ
ＡＡ含量が少ない）ペプチド混合物（比較的低分子量の
ペプチド）を得ることはできなかった。Therefore, a peptide mixture that can be orally administered to patients with mild or convalescent liver disease, in other words, has a good flavor (low free amino acids) and a high Fisher value (A
It was not possible to obtain a peptide mixture (relatively low molecular weight peptides) with low AA content.
本発明者等は、前記のような従来技術の現状に鑑みて、
研究を重ねた結果、獣乳由来のｋ−カゼインにレンネッ
トを作用させて得られたグリコポリペプチドにレンニン
以外のプロテアーゼを作用させると、ＡＡＡを含まず、
フィッシャー値が高く、且つ風味が良好なペプチド混合
物が得られることを見いだし、本発明を完成するに至っ
た。In view of the current state of the prior art as described above, the present inventors have
As a result of repeated research, we found that when a protease other than rennin is applied to a glycopolypeptide obtained by applying rennet to k-casein derived from animal milk, it does not contain AAA.
It was discovered that a peptide mixture with a high Fisher value and good flavor could be obtained, and the present invention was completed.
問題点を解決する手段
本発明は、獣乳のｋ−カゼインに由来するグリコポリペ
プチドのプロテアーゼ処理物であって、フィッシャー値
が３０から６０の範囲であることを特徴とするペプチド
混合物である。Means for Solving the Problems The present invention is a protease-treated glycopolypeptide derived from animal milk k-casein, and is a peptide mixture characterized by having a Fisher value in the range of 30 to 60.
かかるポリペプチド混合物は、獣乳から公知の方法によ
って、純度５０％以上（５０〜７０％で良い）のに−カ
ゼインを精製し、得られたｋ−カゼインの溶液に、塩化
カルシウムとレンネットを添加して、分解してグリコポ
リペプチドを分離し、得られたグリコポリペプチドをプ
ロテアーゼで加水分解させて精製分離することによって
得られる。Such a polypeptide mixture is obtained by purifying k-casein from animal milk to a purity of 50% or more (50 to 70% is fine) by a known method, and adding calcium chloride and rennet to the resulting solution of k-casein. The glycopolypeptides are added, decomposed and separated into glycopolypeptides, and the resulting glycopolypeptides are hydrolyzed with protease and purified and separated.
作 用
本発明によるポリペプチド混合物は、風味が良好で、フ
ィッシャー値が高いので、軽症又は回復期の肝疾患患者
に経口的に投与できる。Effect The polypeptide mixture according to the present invention has a good taste and a high Fisher value, so it can be administered orally to patients with mild or convalescent liver disease.
しかも、本発明のポリペプチド混合物は、獣乳から比較
的簡単な処理によって得られ、従って廉価に提供できる
。Moreover, the polypeptide mixture of the present invention can be obtained from animal milk through relatively simple processing, and therefore can be provided at low cost.
発明の目的
本発明の目的は、フィッシャー値が高く、風味が良好な
ポリペプチド混合物を提供することである。OBJECTS OF THE INVENTION An object of the invention is to provide a polypeptide mixture with a high Fisher value and good taste.
本発明の他の目的は、肝疾患の治療用に有効なペプチド
混合物を提供することである。Another object of the invention is to provide an effective peptide mixture for the treatment of liver diseases.
実 施 例
本発明のペプチド混合物は下記の方法によって製造でき
る。EXAMPLE The peptide mixture of the present invention can be produced by the following method.
獣乳から純度５０％（重量、以下、特記しない場合は同
じ）以上（５０〜７０％で良い）のに−カゼインを公知
の方法で分離する。Casein having a purity of 50% (by weight, the same applies hereinafter unless otherwise specified) or more (50 to 70% is fine) is separated from animal milk by a known method.
原料となる獣乳は、牛、羊、山羊等の乳、あるいはそれ
らの加工品（例えば、カゼイン、その塩。The raw material animal milk is milk from cows, sheep, goats, etc., or processed products thereof (e.g. casein, its salt).
濃縮乳、粉乳、脱脂乳、脱脂粉乳等）、またはそれらの
混合物であって良い（以下、これらを総称して獣乳と記
載する）。(concentrated milk, milk powder, skim milk, skim milk powder, etc.), or a mixture thereof (hereinafter, these are collectively referred to as animal milk).
獣乳からｋ−カゼインを得る公知の方法としては、下記
の方法がある。Known methods for obtaining k-casein from animal milk include the following methods.
ナトリウムカゼイネートを低イオン強度下で、ゲル濾過
して分画する方法（特開昭５９−９１４８４８号）。A method of fractionating sodium caseinate by gel filtration under low ionic strength (Japanese Unexamined Patent Publication No. 59-914848).
全カゼイン溶液に７５ｍＭのカルシウムを添加して分画
する方法（特公昭５９−４８９６４号）。A method of fractionating by adding 75mM calcium to a total casein solution (Japanese Patent Publication No. 59-48964).
全カゼイン溶液に５００ｍＭのカルシウムを添加して分
画する方法（ジャーナル・オブ・７−ド・サイエンス、
第４３巻、３９７頁、１９７８年）。A method of fractionation by adding 500mM calcium to a total casein solution (Journal of Seventh Science,
Volume 43, page 397, 1978).
得られたｋ−カゼイン粉末を５〜１０％の濃度で、ｐＨ
５，５〜７．０の溶液となるように溶解し、得られた溶
液にレンネットを蛋白質１ｇ当たり１０００〜ｌ１００
ＯＯｐｐ （望ましくは２０００〜６０００ｐｐｍ）と
塩化カルシウムをレンネット添加料の１−１０倍（望ま
しくは２〜５倍）の割合で添加し、３０〜４５℃（望ま
しくは３５〜４０°Ｃ）の温度で、３０〜１５０分間（
望ましくは３０〜６０分間）反応させる。反応液を加熱
して（例えば８０°Ｃ，ｔＯ分間）酵素を失活させ、後
に遠心分離して、上澄液を常法のウルトラフィルトレー
ジョンによって脱塩、濃縮し、凍結乾燥してグリコポリ
ペプチドを得る。この工程は、本発明者等の下記の発見
に基づくものである。The obtained k-casein powder was adjusted to a concentration of 5 to 10% at pH
5.5 to 7.0, and add 1000 to 1100 rennet per 1 g of protein to the resulting solution.
Add OOpp (preferably 2000-6000 ppm) and calcium chloride at a ratio of 1-10 times (preferably 2-5 times) the rennet additive, and at a temperature of 30-45°C (preferably 35-40°C). , for 30 to 150 minutes (
(preferably for 30 to 60 minutes). The enzyme is inactivated by heating the reaction solution (e.g., 80°C for tO minutes), followed by centrifugation, and the supernatant is desalted and concentrated by conventional ultrafiltration, and lyophilized to remove the glycolytic acid. Obtain a polypeptide. This step is based on the following discovery by the present inventors.
即ち、本発明者等は、ｋ−カゼインにレンネットを作用
させると、ｋ−カゼインのＮ末端から１０５番目と１０
６番目のアミノ酸であるフェニルアラニンとメチオニン
との間のペプチド結合を特異的に切断し、その結果、ｋ
−カゼインはパラに−カゼインと、糖鎖を有するグリコ
ポリペプチドとの二つの断片に分解され、疎水性の高い
パラｋ−カゼインは凝集沈澱し、グリコポリペプチドは
溶液中に残ること、得られるグリコポリペプチドは６４
個のアミノ酸残基からなるポリペプチドであり、構成ア
ミノ酸中にＡＡＡであるフェニルアラニン、チロシン、
トリプトファン、を全く含んでいないことを発見したの
である。この際、塩化カルシウムを添加するとパラｋ−
カゼインの凝固性が増加する。尚、市販のレンネットは
レンニン以外のプロテアーゼ活性を有するクルードな製
品であるので、不純物として含まれる他のカゼイン成分
をも多少分解し、ＡＡＡを含むペプチド及び遊離アミノ
酸の生成が見られる。従って、ｋ−カゼインの純度は５
０％以上、望ましくは５０〜７０％の純度の物を用いる
のが良い。That is, the present inventors found that when rennet was applied to k-casein, the 105th and 10th positions from the N-terminus of k-casein
Specifically cleaves the peptide bond between the 6th amino acid phenylalanine and methionine, resulting in k
-Casein is decomposed into two fragments: para-casein and a glycopolypeptide having a sugar chain, the highly hydrophobic para-k-casein aggregates and precipitates, and the glycopolypeptide remains in solution. Glycopolypeptide is 64
It is a polypeptide consisting of AAA amino acid residues such as phenylalanine, tyrosine,
They discovered that it contained no tryptophan at all. At this time, if calcium chloride is added, para-k-
The coagulability of casein increases. Since commercially available rennet is a crude product that has protease activity other than rennin, other casein components contained as impurities are also degraded to some extent, and peptides containing AAA and free amino acids are produced. Therefore, the purity of k-casein is 5
It is preferable to use a product with a purity of 0% or more, preferably 50 to 70%.
得られたグリコポリペプチド画分を５％の濃度。The resulting glycopolypeptide fraction at a concentration of 5%.
ｐＨ６，０〜９．０となるよう溶解し、市販のプロテア
ーゼ（レンニン以外の）を蛋白質１ｇ当たり１００〜２
０００単位（望ましくは５００〜１０００単位）の割合
で添加し、５０°Ｃに保持して加水分解を行い、分解率
が５〜２５％となった時点で加熱処理して酵素を失活さ
せる。尚、分解率はホルモル滴定法（蛋白質化学１．赤
堀四部・水島三一部編１株式会社共立出版刊、昭和２９
年）で測定できる。得られた反応液を冷却、濾過し、濾
液を凍結乾燥して、フィッシャー値の高いペプチド混合
物粉末を得る。なお、上記濾液を活性炭で吸着処理する
ことによりフィッシャー値を上昇させることができる。Dissolve the protein to a pH of 6.0 to 9.0, and add commercially available protease (other than rennin) at a concentration of 100 to 2 ml per gram of protein.
000 units (preferably 500 to 1000 units), hydrolysis is carried out by holding at 50°C, and when the decomposition rate reaches 5 to 25%, heat treatment is performed to deactivate the enzyme. The decomposition rate was determined by the formol titration method (Protein Chemistry 1. Edited by Shibu Akahori and Sanichi Mizushima 1, published by Kyoritsu Shuppan Co., Ltd., 1952).
year). The resulting reaction solution is cooled and filtered, and the filtrate is freeze-dried to obtain a peptide mixture powder with a high Fisher value. Note that the Fisher value can be increased by adsorbing the filtrate with activated carbon.
使用するプロテアーゼはパンクレアチン等のエンドペプ
チダーゼが望ましい。エンドペプチダーゼの使用はアミ
ノ酸の遊離率を抑制する効果がある。The protease used is preferably an endopeptidase such as pancreatin. The use of endopeptidase has the effect of suppressing the release rate of amino acids.
かくて得られたペプチド混合物を、所定量（例えば２５
ｇ）密封し、水に溶解して使用する粉末状の経口栄養剤
とすることができる。The peptide mixture thus obtained is added to a predetermined amount (for example, 25
g) It can be made into a powdered oral nutritional preparation that is sealed and dissolved in water.
まｊ；得られたペプチド混合物を、所定濃度の水溶液（
例えば５％）として、殺菌、密封し、液状のペプチド混
合物経口栄養剤とすることもできる。Add the obtained peptide mixture to an aqueous solution of a predetermined concentration (
For example, 5%) can be sterilized and sealed to form a liquid peptide mixture oral nutritional preparation.
勿論、その液状栄養剤は、経腸栄養剤として使用するこ
とができる。Of course, the liquid nutritional supplement can be used as an enteral nutritional supplement.
あるいはまた、糖質（デキストリン、蔗糖）２８．０ｇ
、脂質（コーン油、ココナツ油）６．２ｇ、及びビタミ
ン、ミネラルと本発明のペプチド混合物８６０ｇとを２
００ｍＱ中に含む、ＩＫｃａＱ／ｍＱの経口栄養剤とし
ても良い。Alternatively, carbohydrates (dextrin, sucrose) 28.0g
, 6.2 g of lipids (corn oil, coconut oil), and 860 g of the peptide mixture of the present invention with vitamins and minerals.
It may also be used as an oral nutritional supplement containing IKcaQ/mQ in 00mQ.
以上に本発明の詳細な説明したが、以下に試験例を示し
て、本発明を詳述する。Although the present invention has been described in detail above, the present invention will be explained in detail by showing test examples below.
［試験例１］分子量に関する試験
下記の方法により６種類の試料（試料１〜６）を夫々調
整した。[Test Example 1] Test regarding molecular weight Six types of samples (Samples 1 to 6) were prepared by the following method.
市販の乳酸カゼインにュージーランド産）２０００ｇを
０．５％水酸化ナトリウム溶液に１２％の濃度となるよ
う加温しながら溶解し、得られた溶液をｐＨ８，０に調
製した。この溶液に４０％塩化カルシウム溶液２４８ｇ
を加え（最終濃度０．３Ｍ）、６０°Ｃで１５．〜３０
分間撹拌撹拌力ルシウムと充分反応させ、溶液が均一状
態となっだ後、連続遠心分離機を用いて上澄液を分離し
た。2000 g of commercially available lactic acid casein (produced in New Zealand) was dissolved in a 0.5% sodium hydroxide solution with heating to a concentration of 12%, and the resulting solution was adjusted to pH 8.0. Add 248g of 40% calcium chloride solution to this solution.
(final concentration 0.3M) and incubated at 60°C for 15. ~30
Stirring power for 1 minute After the solution was sufficiently reacted with lucium and the solution became homogeneous, the supernatant liquid was separated using a continuous centrifuge.
この上澄液を分画分子量約６０００のウルトラフィルト
レージョンモジュール（旭化成工業社製）によってカル
シウム濃度が初濃度の１％以下となるまで脱塩し、凍結
乾燥して、純度約７０％のｋ−カゼイン粉末約１２０ｇ
を得た。This supernatant was desalted using an Ultrafiltration module (manufactured by Asahi Kasei Industries, Ltd.) with a molecular weight cutoff of approximately 6,000 until the calcium concentration was 1% or less of the initial concentration, and then freeze-dried to obtain a calcium concentration of approximately 70% purity. - Casein powder approx. 120g
I got it.
得られたｋ−カゼイン粉末１００ｇを、５％の濃度で水
に溶解し、ｐＨを６．３に調整した後、塩化カルシウム
１２００ｍｇを含む水溶液を添加し、均一に混合し、市
販のカーフ由来レンネット（ハンセン社製）を６００ｍ
ｇ添加し、３５°Ｃで３０分間反応させた後、６０°Ｃ
で１０分間加熱して酵素を失活させ、遠心して上澄液を
分離した。After dissolving 100 g of the obtained k-casein powder in water at a concentration of 5% and adjusting the pH to 6.3, an aqueous solution containing 1200 mg of calcium chloride was added and mixed uniformly. 600m of net (manufactured by Hansen)
g and reacted at 35°C for 30 minutes, then at 60°C.
The enzyme was inactivated by heating for 10 minutes, and the supernatant was separated by centrifugation.
この上澄液を分画分子量約３０００のウルトラフィルト
レージョンモジュールを用いて脱塩、濃縮し、凍結乾燥
してグリコポリペプチド粉末約１．５ｇを得た。This supernatant was desalted and concentrated using an Ultrafiltration module with a molecular weight cutoff of about 3000, and lyophilized to obtain about 1.5 g of glycopolypeptide powder.
得られたグリコポリペプチドの５％溶液（ｐＨ９，０）
に市販のパンクレアチン（大野製薬社製）及びスミチー
ム（新日本化学工業社製）を各々基質の０．１％の割合
で添加し、５０°Ｃで試料に応じて異なった時間に亙り
反応させた後、反応液を８０°Ｃで１０分間加熱して酵
素を失活させ、４°Ｃで２時間冷却し、生じた沈澱物を
濾過、除去した。5% solution of the obtained glycopolypeptide (pH 9,0)
Commercially available pancreatin (manufactured by Ohno Pharmaceutical Co., Ltd.) and Sumiteim (manufactured by Shin Nihon Kagaku Kogyo Co., Ltd.) were each added at a ratio of 0.1% of the substrate and allowed to react at 50°C for different times depending on the sample. After that, the reaction solution was heated at 80°C for 10 minutes to inactivate the enzyme, cooled at 4°C for 2 hours, and the resulting precipitate was filtered and removed.
更に濾液の５％（ｗ／ｖ）にあたる量の粉末活性炭を加
え、４℃で１時間撹拌し、濾過後、濾液を凍結乾燥し、
６種類のペプチド混合物粉末試料を得 ｔこ。Furthermore, powdered activated carbon in an amount equivalent to 5% (w/v) of the filtrate was added, stirred at 4 ° C. for 1 hour, and after filtration, the filtrate was freeze-dried.
Six types of peptide mixture powder samples were obtained.
各試料に含まれるペプチドの分子量分布を、セファデッ
クスＧ−１５，Ｇ−２５，あるいはＴ。The molecular weight distribution of the peptides contained in each sample was determined using Sephadex G-15, G-25, or T.
ｙｏｐｅａｒｌ ＨＷ−４０等を用いて常法により測
定した。測定結果は表１に示されている。また、参考の
ために、それらの試料におけるグリコポリペプチドの分
解率をも示しである。It was measured by a conventional method using Yopearl HW-40 or the like. The measurement results are shown in Table 1. For reference, the degradation rates of glycopolypeptides in those samples are also shown.
各試料の調製におけるグリコポリペプチドのパンクレア
チン及びスミチームによる加水分解反応時間と試料番号
との対応関係もまた表１に示されている。Table 1 also shows the correspondence between the hydrolysis reaction time of the glycopolypeptide with pancreatin and sumizyme and the sample number in the preparation of each sample.
ｌ（対照） ０ ０ ８００
０２ ３０ ３ ２
０００〜６０００３ ６０
５ １０００〜２５００４ ９０
１０ ３００〜１５００５
１２０ ２２ １００〜５００６
１５０ ２５ １
００〜３００表１の結果から、反応時間が３０〜９０分
の試料は、分子量の分布が６０００〜３００であること
が判明した。l (control) 0 0 800
02 30 3 2
000-60003 60
5 1000-25004 90
10 300~15005
120 22 100~5006
150 25 1
00-300 From the results in Table 1, it was found that the samples whose reaction time was 30-90 minutes had a molecular weight distribution of 6000-300.
一般に、加水分解の進行は、使用する酵素の種類、使用
量、反応温度等によって影響されるので、使用される酵
素に関して、前記の諸国子を決定（確認）してこくのが
良い。Generally, the progress of hydrolysis is affected by the type of enzyme used, the amount used, the reaction temperature, etc., so it is best to determine (confirm) the above-mentioned factors regarding the enzyme used.
［試験例２］フィッシャー値の試験（１）試験例１にお
ける試料４と同一の方法で新たに調製した試料４及び後
述の試験例３における試料。[Test Example 2] Fisher value test (1) Sample 4 newly prepared in the same method as Sample 4 in Test Example 1 and the sample in Test Example 3 described below.
ｌＯと同一の方法で別個に調製した試料ｌＯのアミノ酸
組成を常法（改定日本食品アミノ酸組成表。The amino acid composition of sample IO, which was prepared separately using the same method as IO, was determined using the conventional method (Revised Japanese Food Amino Acid Composition Table).
科学技術庁編、１９８６年）により分析し、これに基づ
いてＢＣＡＡ、ＡＡＡ及びフィッシャー値を計算し、表
に示した。尚、比較対照のため、牛乳中の各カゼイン画
分のアミノ酸組成（ジャーナル・オブ・ディリー・サイ
エンス、第５９巻、７９５頁、１９７６年）に基づいて
、同様に上記各数値を算出し、表２に示した。Based on this analysis, BCAA, AAA, and Fisher values were calculated and shown in the table. For comparison purposes, the above numerical values were calculated in the same way based on the amino acid composition of each casein fraction in milk (Journal of Daily Science, Vol. 59, p. 795, 1976), and the values are shown in the table. Shown in 2.
全カゼイン ２１．１ ８．５
２．５ａｓ、−力ゼイン−Ｂ １９．６ １０
．０ ２．０β−カゼイン−Ａ２ ２３．９
６．７ ３．６ｋ−カゼイン８ １８
．９ ８．３ ２．３試料４
１７．６ ０．３ ５８．７試料１０
１７．３ ０．５ ３４．６表２の結
果から、試料４及び試料ｌＯのペプチド混合物のフィッ
シャー値は、対照として示した全カゼイン、及び各カゼ
イン画分のフィッシャー値と比して、かなり高いことが
明らかである。Total casein 21.1 8.5
2.5as, -forcezein-B 19.6 10
．． 0 2.0β-casein-A2 23.9
6.7 3.6k-casein 8 18
．． 9 8.3 2.3 Sample 4
17.6 0.3 58.7 sample 10
17.3 0.5 34.6 From the results in Table 2, the Fisher values of the peptide mixtures of Sample 4 and Sample 1O are significantly higher than those of the total casein and each casein fraction shown as controls. That is clear.
［試験例３］フィッシャー値の試験（２）試験例１にお
ける試料ｌ〜６と同一の方法で新たに試料１〜６を調製
した。[Test Example 3] Fisher Value Test (2) Samples 1 to 6 were newly prepared in the same manner as Samples 1 to 6 in Test Example 1.
また、下記の方法により更に４種類の試料（試料７〜１
０）を調製した。In addition, four more types of samples (Samples 7 to 1) were prepared using the following method.
0) was prepared.
市販の乳酸カゼインにュージーランド産）２０００ｇを
、０．３％水酸化ナトリウム溶液に３％の濃度となるよ
う加温しながら溶解し、ｐＨを６．０に調整した。この
溶液に４０％塩化カルシウム溶液５７ｇ（最終濃度０．
０７５Ｍ） を加ｔ、４５°Ｃで３０分間撹拌し、連続
遠心分離機を用いて上澄液を分離した。この上澄液を分
画分子量約６０００のウルトタフイルトレーションモジ
ュール（旭化成工業社製）を用いてカルシウム濃度が初
濃度の１％以下となるまで脱塩し、凍結乾燥して、純度
約５０％のｋ−カゼイン粉末約４００ｇを得た。2000 g of commercially available lactic acid casein produced in New Zealand) was dissolved in a 0.3% sodium hydroxide solution with heating to a concentration of 3%, and the pH was adjusted to 6.0. Add 57 g of 40% calcium chloride solution to this solution (final concentration 0.
075M) was added and stirred at 45°C for 30 minutes, and the supernatant was separated using a continuous centrifuge. This supernatant was desalted using an Ultofiltration module (manufactured by Asahi Kasei Industries, Ltd.) with a molecular weight cutoff of approximately 6000 until the calcium concentration was 1% or less of the initial concentration, and then lyophilized to a purity of approximately 50%. About 400 g of k-casein powder was obtained.
得られたｋ−カゼイン粉末１００ｇを５％濃度で水に溶
解し、ｐＨを６，３に調整した後、塩化カルシウム４０
０ｍｇを含む水溶液を添加し均一に混合し、市販の微生
物由来レンネット（明糖社製）を２００ｍｇ添加し、３
５℃で３０分間反応させ、その後８０°Ｃで１０分間加
熱して酵素を失活させ遠心１分離した。得られた上澄液
をウルトタフィルトレーションモジュールを用いて脱塩
。100 g of the obtained k-casein powder was dissolved in water at a concentration of 5%, the pH was adjusted to 6.3, and then calcium chloride 40 g was dissolved in water at a concentration of 5%.
Add an aqueous solution containing 0 mg, mix uniformly, add 200 mg of commercially available microorganism-derived rennet (manufactured by Meito Co., Ltd.),
The mixture was reacted at 5°C for 30 minutes, and then heated at 80°C for 10 minutes to inactivate the enzyme, followed by centrifugation. The resulting supernatant was desalted using an Urutafiltration module.
濃縮し、凍結乾燥してグリコポリペプチド粉末約２０ｇ
を得を二。Concentrate and lyophilize to obtain approximately 20g of glycopolypeptide powder
Get two.
上記グリコポリペプチドの５％溶液（ｐＨ７゜０）に市
販のバンクレアチン（大野製薬社製）及びスミチーム（
新日本化学工業社製）を各々基質の０．２％の割合で添
加し、５０℃で各試料に応じて異なった時間に亙り反応
させた後、反応液を８０℃で１０分間加熱して酵素を失
活させ、４℃で２時間冷却し、生じた沈澱物を濾過によ
り除去した。更に濾液の１０％（Ｗ／Ｖ）にあたる量の
粉末活性炭を加え、４°Ｃ″′ｃ１時間撹拌し、癲過後
、上澄液を凍結乾燥して、ペプチド混合物を得た。A 5% solution (pH 7°0) of the above glycopolypeptide was added with commercially available vancreatin (manufactured by Ohno Pharmaceutical Co., Ltd.) and Sumiteem (
(manufactured by Shin Nihon Kagaku Kogyo Co., Ltd.) was added at a ratio of 0.2% of the substrate and allowed to react at 50°C for different times depending on each sample, and then the reaction solution was heated at 80°C for 10 minutes. The enzyme was inactivated, cooled at 4°C for 2 hours, and the resulting precipitate was removed by filtration. Further, powdered activated carbon was added in an amount corresponding to 10% (W/V) of the filtrate, and the mixture was stirred at 4°C for 1 hour. After filtration, the supernatant was freeze-dried to obtain a peptide mixture.
試料７におけるパンクレアチン及びスミチームによる酵
素加水分解反応時間は、０分（対照）であり、試料８〜
１０では、それぞれ３０．６０゜９０分である。The enzymatic hydrolysis reaction time with pancreatin and Sumiteem in Sample 7 was 0 minutes (control), and in Samples 8 to 8.
10, it is 30.60°90 minutes, respectively.
かくてえられた合計１０種類の試料（試料１〜１０）の
ペプチド混合物についてアミノ酸組成を試験例２記載の
方法に従って分析し、これに基づいてフィッシャー値を
算出した。その結果を表３に示す。The amino acid composition of the peptide mixtures of a total of 10 types of samples (Samples 1 to 10) thus obtained was analyzed according to the method described in Test Example 2, and the Fisher value was calculated based on this. The results are shown in Table 3.
表 ３
試料 １ ２ ３ ４ ５ ６
７ ８ ９ １０フィッンヤ−６１′＋ ４０
．６４５．１４６．２５ｇ、７５７．５５８，２３４．
６３５．２４０，５４１．２表３及び前記表１の結果か
ら、使用されたレンネットの種類にかかわらず実施例１
及び実施例２における酵素分解条件で６０分以上分解し
た試料のフイッンヤー値はそれ以下のものに比較して高
かった。Table 3 Sample 1 2 3 4 5 6
7 8 9 10 Finnya-61'+ 40
．． 645.146.25g, 757.558,234.
635.240, 541.2 From the results in Table 3 and Table 1 above, Example 1 was obtained regardless of the type of rennet used.
Furthermore, the heat value of the sample degraded for 60 minutes or more under the enzymatic degradation conditions in Example 2 was higher than that of samples of less than 60 minutes.
［試験例４１風味試験（１）
試験例１と同一の方法によって得た試料ｌ及び４の各５
％溶液を調整し、男女各２０名からなるテストパネルに
より昭和３６年６月南江堂発行「推計学の化学及び生物
学への応用、第３集」 １４５頁記載の方法で、先ず３
点識別試験法を行った。[Test Example 41 Flavor Test (1) 5 samples each of Samples 1 and 4 obtained by the same method as Test Example 1
% solution was prepared, and a test panel consisting of 20 men and 20 men was tested using the method described on page 145 of "Applications of Stochastics to Chemistry and Biology, Volume 3" published by Nankodo in June 1960.
A point discrimination test method was performed.
次に正解者（男性１６名、女性１７名をパネルとして２
点試験法により試料ｌと試料４°の水溶液の風味を試験
した。その結果は表４の通りであり、試験例１で９０分
間酵素分解したペプチド混合物（分子量範囲３００〜１
５００． 試料４）は、分解していないグリコポリペプ
チド（試料ｌ）と比較して苦味等の風味上の差は認めら
れなかった。Next, those who answered correctly (16 men and 17 women as a panel)
The flavor of the aqueous solutions of Sample 1 and Sample 4° was tested using the point test method. The results are shown in Table 4, and the peptide mixture (molecular weight range 300-1
500. Sample 4) showed no difference in flavor such as bitterness compared to the undegraded glycopolypeptide (sample 1).
なお、試料２（３０分）試料３（６０分）について同様
の試験を行ったところ、試料１ （対照）に比較して風
味上の差が認められなかった。When a similar test was conducted on Sample 2 (30 minutes) and Sample 3 (60 minutes), no difference in flavor was observed compared to Sample 1 (control).
男 ７人 ９人
［試験例５］風味試験（２）
試験例１における試料ｌ及び５と同一の方法によって新
たに調製した試料ｌ及び試料５の各５％水溶液を調整し
、試験例４と同様の方法で先ず３点試験法を行い、次に
正解した男性１８名１女性１９名をパネルとして２点試
験法で風味を試験した。結果は表５の通りであり、試料
５のポリペプチド（試験例１と同一の方法で１２０分間
酵素分解、分子量範囲１００〜５００）は、試料ｌ（分
解しないグリコポリペプチド）と比較して好ましくない
ことが明らかになった。Male 7 people 9 people [Test Example 5] Flavor test (2) 5% aqueous solutions of each of Sample 1 and Sample 5, which were newly prepared in the same manner as Samples 1 and 5 in Test Example 1, were prepared. In the same manner, a 3-point test was first conducted, and then the flavor was tested using a 2-point test using a panel of 18 men and 19 women who answered correctly. The results are shown in Table 5, and the polypeptide of Sample 5 (enzymatically degraded for 120 minutes in the same manner as Test Example 1, molecular weight range 100-500) is preferable compared to Sample 1 (glycopolypeptide that is not degraded). It became clear that there was no.
男 １５人 ３人
なお、同じパネルによって試料ｌと試料６（試験例１と
同一の方法で１５０分間酵素分解、分子量範囲１００〜
３００）とについて同様の試験を行った結果、同様の結
果が得られた。Male: 15 3: Sample 1 and Sample 6 (enzymatically degraded for 150 minutes using the same method as Test Example 1, molecular weight range 100~
300), similar results were obtained.
上記の結果から、遊離アミノ酸（平均分子量１００）は
、栄養学的見地のみならず風味上の見地からも好ましく
ないことが判明した。The above results revealed that free amino acids (average molecular weight 100) are unfavorable not only from a nutritional standpoint but also from a flavor standpoint.
［実施例１］
グリコポリペプチドのパンクレアチン及びスミチームに
よる酵素分解時間を１２０分間とした以外は、試験例１
と同一の方法でペプチド混合物約３０ｇを得た。[Example 1] Test Example 1 except that the enzymatic decomposition time of the glycopolypeptide with pancreatin and sumizyme was 120 minutes.
Approximately 30 g of the peptide mixture was obtained in the same manner as described above.
得られたペプチド混合物を試験例２及び４と同一の方法
で試験した結果フィッシャー値が５８゜７と高く、風味
は良好であった。The obtained peptide mixture was tested in the same manner as in Test Examples 2 and 4, and as a result, the Fisher value was as high as 58.7, and the flavor was good.
［実施例２］
グリコポリペプチドのパンクレアチン及びスムチームに
よる酵素分解時間を１２０分間とした以外は、試験例３
と同一の方法でペプチド混合物約２５ｇを得た。[Example 2] Test Example 3 except that the enzymatic degradation time of the glycopolypeptide with pancreatin and sumzyme was 120 minutes.
Approximately 25 g of the peptide mixture was obtained in the same manner as above.
得られたペプチド混合物を試験例２と同一の方法で試験
しｔ；結果、フィッシャー値は３４．６であり、風味も
良好であった。The obtained peptide mixture was tested in the same manner as in Test Example 2; as a result, the Fisher value was 34.6 and the flavor was good.
発明の効果 本発明によって奏せられる効果は次のとおりである。Effect of the invention The effects achieved by the present invention are as follows.
（１）本発明のペプチド混合物はフィッシャー値が３０
〜６０と一般の蛋白質に比較して高値であり、肝機能疾
患用の治療職として有効である。(1) The peptide mixture of the present invention has a Fisher value of 30
~60, which is higher than that of general proteins, and is effective as a therapeutic agent for liver function diseases.
（２）本発明のペプチド混合物は、風味が量恋いであり
、かつ分子量が一般の蛋白質に比較して小さいため、吸
収され易く、経口栄養剤として有効である。(2) The peptide mixture of the present invention has a rich flavor and a molecular weight smaller than that of general proteins, so it is easily absorbed and effective as an oral nutritional agent.
Claims (1)
ロテアーゼ加水分解物であつて、フィッシャー値が３０
から６０の範囲であることを特徴とするペプチド混合物
。[1] A protease hydrolyzate of glycopolypeptide derived from animal milk k-casein, with a Fisher value of 30
A peptide mixture characterized in that it ranges from .
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1119194A JP2785956B2 (en) | 1989-05-12 | 1989-05-12 | Peptide mixture |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1119194A JP2785956B2 (en) | 1989-05-12 | 1989-05-12 | Peptide mixture |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH02300137A true JPH02300137A (en) | 1990-12-12 |
| JP2785956B2 JP2785956B2 (en) | 1998-08-13 |
Family
ID=14755251
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP1119194A Expired - Fee Related JP2785956B2 (en) | 1989-05-12 | 1989-05-12 | Peptide mixture |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP2785956B2 (en) |
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007080962A1 (en) * | 2006-01-13 | 2007-07-19 | Meiji Dairies Corporation | Anti-inflammatory composition and method for production of anti-inflammatory composition |
| CN103461985A (en) * | 2013-07-18 | 2013-12-25 | 浙江劲膳美生物科技有限公司 | Special diet for patient with hepatopathy |
| WO2021024622A1 (en) * | 2019-08-02 | 2021-02-11 | 味の素株式会社 | Method for producing glycomacropeptide |
-
1989
- 1989-05-12 JP JP1119194A patent/JP2785956B2/en not_active Expired - Fee Related
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2007080962A1 (en) * | 2006-01-13 | 2007-07-19 | Meiji Dairies Corporation | Anti-inflammatory composition and method for production of anti-inflammatory composition |
| JP5025491B2 (en) * | 2006-01-13 | 2012-09-12 | 株式会社明治 | Anti-inflammatory composition and method for producing anti-inflammatory composition |
| CN103461985A (en) * | 2013-07-18 | 2013-12-25 | 浙江劲膳美生物科技有限公司 | Special diet for patient with hepatopathy |
| WO2021024622A1 (en) * | 2019-08-02 | 2021-02-11 | 味の素株式会社 | Method for producing glycomacropeptide |
Also Published As
| Publication number | Publication date |
|---|---|
| JP2785956B2 (en) | 1998-08-13 |
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