JPS6330890B2 - - Google Patents
Info
- Publication number
- JPS6330890B2 JPS6330890B2 JP55094169A JP9416980A JPS6330890B2 JP S6330890 B2 JPS6330890 B2 JP S6330890B2 JP 55094169 A JP55094169 A JP 55094169A JP 9416980 A JP9416980 A JP 9416980A JP S6330890 B2 JPS6330890 B2 JP S6330890B2
- Authority
- JP
- Japan
- Prior art keywords
- molecular weight
- amino acid
- absorption
- low
- nutritional supplement
- 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.)
- Expired
Links
- 150000001413 amino acids Chemical class 0.000 claims description 44
- 239000000203 mixture Substances 0.000 claims description 39
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 34
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 32
- 235000015872 dietary supplement Nutrition 0.000 claims description 20
- 102000004169 proteins and genes Human genes 0.000 claims description 20
- 108090000623 proteins and genes Proteins 0.000 claims description 20
- 229910052757 nitrogen Inorganic materials 0.000 claims description 16
- 239000002994 raw material Substances 0.000 claims description 10
- 102000002322 Egg Proteins Human genes 0.000 claims description 7
- 108010000912 Egg Proteins Proteins 0.000 claims description 7
- 108010016626 Dipeptides Proteins 0.000 claims description 6
- 230000007071 enzymatic hydrolysis Effects 0.000 claims description 4
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 claims description 4
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 claims description 3
- 235000014103 egg white Nutrition 0.000 claims description 3
- 210000000969 egg white Anatomy 0.000 claims description 3
- 238000010521 absorption reaction Methods 0.000 description 26
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 10
- 102000004196 processed proteins & peptides Human genes 0.000 description 7
- 235000013305 food Nutrition 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 210000004369 blood Anatomy 0.000 description 5
- 238000000354 decomposition reaction Methods 0.000 description 5
- 230000000694 effects Effects 0.000 description 5
- 229940088598 enzyme Drugs 0.000 description 5
- 239000000047 product Substances 0.000 description 5
- 230000008485 antagonism Effects 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000007858 starting material Substances 0.000 description 4
- 230000004584 weight gain Effects 0.000 description 4
- 235000019786 weight gain Nutrition 0.000 description 4
- 238000004519 manufacturing process Methods 0.000 description 3
- 235000016709 nutrition Nutrition 0.000 description 3
- 241000700157 Rattus norvegicus Species 0.000 description 2
- 230000037213 diet Effects 0.000 description 2
- 235000005911 diet Nutrition 0.000 description 2
- 235000020776 essential amino acid Nutrition 0.000 description 2
- 239000003797 essential amino acid Substances 0.000 description 2
- 230000002496 gastric effect Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 210000002784 stomach Anatomy 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- FSXRLASFHBWESK-HOTGVXAUSA-N Phe-Tyr Chemical compound C([C@H](N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)C1=CC=CC=C1 FSXRLASFHBWESK-HOTGVXAUSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000003042 antagnostic effect Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 235000012888 dietary physiology Nutrition 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 230000001079 digestive effect Effects 0.000 description 1
- FSXRLASFHBWESK-UHFFFAOYSA-N dipeptide phenylalanyl-tyrosine Natural products C=1C=C(O)C=CC=1CC(C(O)=O)NC(=O)C(N)CC1=CC=CC=C1 FSXRLASFHBWESK-UHFFFAOYSA-N 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 230000037406 food intake Effects 0.000 description 1
- 235000012631 food intake Nutrition 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 230000014075 nitrogen utilization Effects 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 108010024951 plastein Proteins 0.000 description 1
- 210000003240 portal vein Anatomy 0.000 description 1
- 230000002980 postoperative effect Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000013585 weight reducing agent Substances 0.000 description 1
Classifications
-
- 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
-
- 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
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Food Science & Technology (AREA)
- Nutrition Science (AREA)
- Engineering & Computer Science (AREA)
- Polymers & Plastics (AREA)
- General Chemical & Material Sciences (AREA)
- Biochemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Mycology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
Description
本発明はデイペプチドおよびトリペプチドを主
構成分とする低分子ペプチド組成物を含有させた
経口、経胃腸栄養剤に関するものである。
従来、タンパク質を酵素で加水分解し、ペプチ
ドならびにアミノ酸を製造することは食品分野を
中心として行なわれてきている。
しかしながら、そこで目的としてきたものはタ
ンパク質を酵素で分解することによつて可溶化す
るとか、食品素材として適したものにするために
低分子化するとかのものばかりであり、分解生成
物の分子量を問題としたものは全くなかつた。従
来ペプチド化したものは分解度が低いものか遊離
アミノ酸含有が極めて高いものであり、すなわ
ち、分解度が不均一で分子量数万から遊離アミノ
酸までを含むものであり、平均分子量も数千以上
であるとか遊離アミノ酸が50%以上とかいつたも
のであつた。
本発明者等は、従来のような単なるタンパク質
の可溶化物あるいは分子量分布の広いペプチド混
合体あるいはアミノ酸混合物よりも分子量的にあ
る限定された小範囲にあるペプチド組成物の方が
消化吸収の面から、あるいは栄養生理面からみて
栄養剤として使用した時有利であることを確認し
た。本発明の栄養剤に含有させる低分子ペプチド
組成物は、タンパク質原料全体を窒素源とした酵
素的加水分解により得られたデイペプチドおよび
トリペプチドを主体とし、分子量700以上のペプ
チド含量が20wt%以下であり、しかも遊離アミ
ノ酸含量が20wt%以下のもので、平均分子量が
550〜300である。この組成物はタンパク原料を分
子量的に上記の如くコントロールして得たもので
ある。
最近では、シペプチド、トリペプチドが腸管か
らの吸収がはやいことが確実であると言われ、後
に詳述するように本発明者等がin vivoにおいて
初めて確認した。
また、遊離アミノ酸混合物は吸収に際して拮抗
作用あるいは溶解性小のために吸収のバラツキが
あるのに対して低分子ペプチドであればかかる吸
収のばらつきは見られないことを本発明者等は確
認した。従つて、栄養剤のタンパク源としては上
述したような低分子ペプチド組成物が好ましい。
本発明の目的はアミノ酸相互の吸収拮抗が少な
く、溶解性が高く、全窒素吸収速度が大きくなつ
て窒素収支の良い、すなわち、効率の高い窒素源
となるデイペプチドを主成分とする低分子ペプチ
ドを含有する栄養剤を提供しようとするにある。
本発明の他の目的は高い効率の窒素源として体
重増加をもたらすと同時に血中コレステロール値
を低下せしめる低ペプチド含有栄養剤を提供しよ
うとするにある。
本発明の更に他の目的は既にデイペプチドまた
はトリペプチドまでに低分子化されていることに
起因して吸収性が良いために消化負担を軽減する
経口栄養剤としても、あるいは体力の弱つている
人に直接経胃腸投与することもできる経胃腸栄養
剤を提供しようとするにある。
すなわち、本発明はタンパク質原料全体を窒素
源として酵素的加水分解により得た分子量700以
上のペプチド含量が20重量%以下、遊離アミノ酸
含量が20%以下のデイペプチドおよびトリペプチ
ドを主成分とする平均分子量が550〜300である低
分子ペプチド組成物を含有する栄養剤を提供す
る。
本発明の栄養剤に用いるデイペプチドおよびト
リペプチドを主構成分とする低分子ペプチド組成
物の作用効果ならびにその製造方法を以下に詳細
に説明する。
従来は本発明におけるように限定範囲で低分子
化を図つたペプチドは着目されておらず、その製
造方法も十分には開発されていないが、本発明者
等は以下製造例示するようにして安定的に高収率
で低分子化制御されたペプチド組成物を製造し
た。
〔製造例〕
タンパク質原料(卵白)を水に5〜20w/v%
の割合で溶解させ、酸でPHを1〜4に調整し、ペ
プシン、モルシン、サンプローゼFから選択した
いずれか二種の酵素を基質に対して0.5〜5wt%以
下の量を同時にまた遂次的に添加し、25〜60℃の
温度で20〜30時間反応させ、酵素を失活させた後
遠心分離後の上澄液を乾燥する。得られる生成物
の収率は原料タンパクに対して非常な高率で、平
均分子量は約550〜300、遊離アミノ酸の含量は約
5〜20wt%、分子量700以上のペプチド含量は
20wt%以下である。
なお、本明細書で使用しているタンパク質原料
とは、動植物、微生物等の起源のタンパク質の
他、プラステイン反応により特定のアミノ酸を付
加したタンパク質様物質をも含む。
かようにして得られる低分子ペプチド組成物を
本発明の栄養剤ではタンパク源(窒素源)として
使用する。実効性確認のため、同一アミノ酸組成
の窒素源を含むダイエツトを次表に示すような
組成で調整した。
The present invention relates to an oral or gastrointestinal nutrient containing a low-molecular-weight peptide composition containing dipeptides and tripeptides as main components. BACKGROUND ART Conventionally, peptides and amino acids have been produced by hydrolyzing proteins with enzymes, mainly in the food field. However, most of the objectives have been to solubilize proteins by decomposing them with enzymes, or to reduce the molecular weight of proteins to make them suitable as food materials, and to reduce the molecular weight of decomposition products. There were no problems at all. Conventional peptides have either a low degree of decomposition or an extremely high content of free amino acids.In other words, the degree of decomposition is uneven and the molecular weight ranges from tens of thousands to free amino acids, with an average molecular weight of several thousand or more. The amount of free amino acids was said to be 50% or more. The present inventors have found that peptide compositions with a narrow molecular weight range are better for digestion and absorption than conventional solubilized proteins or peptide mixtures or amino acid mixtures with a wide molecular weight distribution. It was confirmed that it is advantageous when used as a nutritional supplement from the viewpoint of nutrition and physiology. The low-molecular-weight peptide composition contained in the nutritional supplement of the present invention is mainly composed of deipeptides and tripeptides obtained by enzymatic hydrolysis using the whole protein raw material as a nitrogen source, and the content of peptides with a molecular weight of 700 or more is 20wt% or less. In addition, the free amino acid content is 20wt% or less, and the average molecular weight is
It is 550-300. This composition was obtained by controlling the molecular weight of the protein raw material as described above. Recently, it has been said that cypeptides and tripeptides are definitely absorbed quickly from the intestinal tract, and the present inventors confirmed this for the first time in vivo, as will be detailed later. In addition, the present inventors have confirmed that while free amino acid mixtures exhibit absorption variations due to antagonistic effects or low solubility, such absorption variations are not observed in the case of low-molecular-weight peptides. Therefore, the above-mentioned low-molecular-weight peptide composition is preferred as a protein source for nutritional supplements. The purpose of the present invention is to provide a low-molecular-weight peptide mainly composed of deipeptide, which has less mutual absorption antagonism among amino acids, has high solubility, and has a high total nitrogen absorption rate, resulting in a good nitrogen balance. We are trying to provide nutritional supplements containing. Another object of the present invention is to provide a low peptide-containing nutritional supplement that serves as a highly efficient nitrogen source to increase body weight and at the same time lower blood cholesterol levels. A further object of the present invention is to use the present invention as an oral nutritional supplement that reduces the digestive burden due to its low molecular weight, such as dipeptide or tripeptide, which has good absorption properties. The objective is to provide a gastrointestinal nutritional supplement that can be administered directly to humans. That is, the present invention provides an average amount of depeptides and tripeptides whose main components are peptides with a molecular weight of 700 or more and a free amino acid content of 20% or less and a free amino acid content of 20% or less obtained by enzymatic hydrolysis using the entire protein raw material as a nitrogen source. A nutritional supplement containing a low molecular weight peptide composition having a molecular weight of 550 to 300 is provided. The effects of the low-molecular-weight peptide composition containing dipeptide and tripeptide as main components used in the nutritional supplement of the present invention and the method for producing the same will be explained in detail below. Until now, attention has not been paid to peptides whose molecular weight is reduced within a limited range as in the present invention, and the production method thereof has not been sufficiently developed. A peptide composition with controlled molecular weight reduction was produced in high yield. [Production example] 5-20w/v% protein raw material (egg white) in water
Adjust the pH to 1 to 4 with acid, and simultaneously or sequentially dissolve any two enzymes selected from pepsin, morsin, and Sunprose F in an amount of 0.5 to 5 wt% or less based on the substrate. The enzyme is added to the solution and reacted at a temperature of 25 to 60°C for 20 to 30 hours to inactivate the enzyme, and the supernatant after centrifugation is dried. The yield of the product obtained is extremely high relative to the raw protein, with an average molecular weight of approximately 550 to 300, a free amino acid content of approximately 5 to 20 wt%, and a peptide content of 700 or more.
It is less than 20wt%. Note that the protein raw materials used in this specification include proteins originating from animals, plants, microorganisms, etc., as well as protein-like substances to which specific amino acids have been added by plastein reaction. The low-molecular-weight peptide composition thus obtained is used as a protein source (nitrogen source) in the nutritional supplement of the present invention. To confirm the effectiveness, a diet containing a nitrogen source with the same amino acid composition was prepared as shown in the table below.
【表】
上表における窒素源は次のようなものであ
る。
A… 卵白タンパク質
B… 本発明栄養剤に入れる平均分子量420、
遊離アミノ酸8wt%の低分子ペプチド組
成物
C… 遊離アミノ酸混合物
D… 平均分子量1400、遊離アミノ酸2wt%の
ペプチド組成物
表に示す組成のダイエツトをそれぞれ10匹の
ウイスター系ラツトに2週間自由摂取させた結果
は表に示す通りであつた。[Table] The nitrogen sources in the table above are as follows. A... Egg white protein B... Average molecular weight 420 to be added to the nutritional supplement of the present invention,
Low-molecular-weight peptide composition C containing 8 wt% free amino acids...Free amino acid mixture D...Peptide composition having an average molecular weight of 1400 and 2 wt% free amino acids Ten Wistar rats were each allowed to freely consume a diet with the composition shown in the table for two weeks. The results were as shown in the table.
【表】
上表において、Food efficiencyとはそれぞれ
のWeight gain/Food intakeの値のをベース
とした比を表示する。この試験結果から、デイペ
プチドおよびトリペプチドを主構成分とする低分
子ペプチド組成物を含有する本発明の栄養剤例
は以下に述べるような多くの実効性を有すること
が確認された。
(1) 窒素の体内保留量がおよび(従来のペプ
チド分解物)に比べて20%以上多く、(アミ
ノ酸混合物)と比較すると著しく高い。
(2) (1)で言及したように体内における有効窒素利
用率が高いためにFood efficiencyがでは他
のものに比して20%以上大きく、その結果、成
育が良くなり、体重増加も大きくなる。
(3) 血中のコレステロール値を見るとだけが著
しく低下しており、コレステロールを相対的に
低下せしめる効果を有するものと推論される。
上述の効果が何故でるかを追求するために窒素
源の違いによるin vivo吸収実験を行つた。
具体的には、窒素源だけをウイスター系ラツト
各5匹の胃にチユーブで強制的に注入して門脈か
ら採血して血中アミノ酸濃度上昇の切期速度の比
較試験を、前述したダイエツトに使用した窒素源
試料(),(),()および()間でアミノ
酸組成を同一にして行つた。その結果を次表に
示す。表の値は吸収量がピーク値に達するまで
の各アミノ酸の平均吸収速度である。また、ほぼ
理想アミノ酸組成の試料()と上記試料()
〜()とのアミノ酸吸収パターンの比較を第
表に示す。[Table] In the above table, Food efficiency indicates the ratio based on the respective Weight gain/Food intake values. From this test result, it was confirmed that the nutritional supplement of the present invention containing a low-molecular-weight peptide composition having dipeptides and tripeptides as main components has many efficacies as described below. (1) The amount of nitrogen retained in the body is more than 20% higher than that of (conventional peptide decomposition product) and significantly higher than that of (amino acid mixture). (2) As mentioned in (1), because the effective nitrogen utilization rate in the body is high, the food efficiency is more than 20% higher than other types, resulting in better growth and greater weight gain. . (3) When looking at the blood cholesterol level, it was found that it was significantly lowered, and it is inferred that it has the effect of relatively lowering cholesterol.
In order to investigate why the above-mentioned effects occur, we conducted in vivo absorption experiments using different nitrogen sources. Specifically, only a nitrogen source was forcibly injected into the stomachs of five Wistar rats through a tube, blood was collected from the portal vein, and a comparative test was conducted to determine the cut-off rate of increase in blood amino acid concentrations. The amino acid composition was made the same among the nitrogen source samples (), (), (), and () used. The results are shown in the table below. The values in the table are the average absorption rate of each amino acid until the absorption amount reaches its peak value. In addition, a sample with almost ideal amino acid composition () and the above sample ()
A comparison of amino acid absorption patterns with ~() is shown in Table 1.
【表】【table】
【表】
本発明の栄養剤に用いる低分子ペプチド組成物
は、上記試験結果(第および表)から以下に
述べるような効果を奏することが容易に理解でき
る。
(1) 本発明のペプチド組成物()は、卵白タン
パク質()のように吸収が不完全でなく、ア
ミノ酸混合物()のようにアミノ酸相互の吸
収拮抗が大きくなく、溶解性小ということもな
い。従来のタンパク質分解物()よりも吸収
性が良いために、それぞれのおよび総量のアミ
ノ酸初期吸収速度値が約1.5〜2.5倍になつてい
る。この吸収速度の違いはアミノ酸では主とし
て吸収拮抗とペプチド組成物の吸収ルートの違
いのため、卵白タンパク質では広い分子量分布
と吸収ルートの差によるものと推考され、ペプ
チド組成物では吸収速度が十分に低分子化され
ていることおよびアミノ酸相互の吸収拮抗が小
さいことのために吸収速度が大きくなつている
のを証明している。この結果として前述したよ
うに全窒素吸収量が増大し、Food efficiency
(体重増加)が向上するばかりか血中コレステ
ロール値の低下をももたらしているものと思わ
れる。
(2) アミノ酸吸収は理想アミノ酸投与パターン
()に近いのが好ましいが、卵白タンパク質
()およびアミノ酸混合物()においては
特にPhe−TyrおよびHisの理想吸収パターン
()からのカイ離率が大きい。これに反し、
本発明のペプチド組成物()は理想吸収パタ
ーン()に非常に近く、バランスのとれたア
ミノ酸吸収を実現することが確認された。
以上の試験結果よりデイペプチドおよびトリペ
プチドを主構成分とする低分子ペプチド組成物は
前述したような種々の効果を奏し、栄養剤の窒素
(タンパク)源として非常に有用であることが明
確に理解できる。
かかる低分子ペプチド組成物を任意のタンパク
質原料全体を窒素源として酵素的加水分解により
調製するのであるが、生成物は出発原料のアミノ
酸以外のものを含むことはできないし、出発原料
を検討しても卵白に勝るアミノ酸組成を有してい
るものはない。従つて、出発原料によつては、得
られた低分子ペプチド組成物のアミノ酸組成上理
想アミノ酸組成と比較してバランスをくずしてい
る場合がある。そのような場合には、本発明栄養
剤に用いる低分子ペプチド組成物には、使用目的
に応じて出発原料を選択したり、必要とされるア
ミノ酸を添加するのが好ましい。例えば、出発原
料に応じて必須アミノ酸が不足するものであれば
必要な必須アミノ酸を、特定のアミノ酸を必要と
する症状ではそのアミノ酸をというように所要に
応じアミノ酸組成を加減制御することができる。
また、組成物中の遊離アミノ酸の含有量はペプ
チド組成物の吸収速度の大きい特長を栄養生理学
に生かすために、あるいはアミノ酸吸収拮抗を生
じない程度に止めておくために、本発明者等はこ
れを約20wt%が上限であると考えている。分子
量が700以上の比較的大きなペプチドは初期吸収
速度を下げないようにその含有量は20wt%以下
に抑えておくのが好ましい。
また、平均分子量は550〜300の低分子量である
のが良い。
本発明による栄養剤には種々の用途が考えられ
る。経口的に投与する栄養剤として、あるいは胃
や腸に直接投与する栄養剤として、そのままある
いは他の栄養剤と混合して使用することもでき
る。風味、嗜好が問題となる場合には、そのよう
な添加物と混合して使用することができる。タン
パク質あるいはアミノ酸とは違つた吸収特異性を
持つことを生かせば、体力の弱つた人、劣えた
人、乳幼児には格好の素材となる。Food
efficiencyが高く、コレステロール値を下げるこ
とからみて中年以降の栄養素材としても有効であ
る。術前術後の栄養補給には従前のアミノ酸混合
物あるいは単に可溶化したタンパク質分解物より
も効率の高い素材として使用できる。[Table] It can be easily understood from the above test results (Table 1) that the low molecular weight peptide composition used in the nutritional supplement of the present invention has the following effects. (1) The peptide composition of the present invention () is not absorbed incompletely like egg white protein (), does not have significant absorption antagonism between amino acids like an amino acid mixture (), and does not have low solubility. . Because of its better absorption than conventional protein digests (), the initial absorption rate values for each and total amount of amino acids are about 1.5 to 2.5 times higher. This difference in absorption rate is thought to be due to differences in absorption routes for amino acids and peptide compositions, whereas for egg white proteins it is thought to be due to a wide molecular weight distribution and a difference in absorption routes. It has been proven that the absorption rate is high because it is molecularized and the absorption antagonism between amino acids is small. As a result, as mentioned above, total nitrogen uptake increases and food efficiency increases.
It is thought that this not only improves weight gain (weight gain) but also lowers blood cholesterol levels. (2) Amino acid absorption is preferably close to the ideal amino acid administration pattern (), but in egg white protein () and amino acid mixtures (), the chi separation rate from the ideal absorption pattern () is particularly large for Phe-Tyr and His. On the contrary,
It was confirmed that the peptide composition of the present invention () is very close to the ideal absorption pattern () and achieves balanced amino acid absorption. The above test results clearly demonstrate that low-molecular-weight peptide compositions containing dipeptides and tripeptides as main components exhibit the various effects mentioned above and are extremely useful as nitrogen (protein) sources for nutritional supplements. It can be understood. Such a low-molecular-weight peptide composition is prepared by enzymatic hydrolysis using the entire arbitrary protein raw material as a nitrogen source, but the product cannot contain anything other than the amino acids of the starting raw material, and it is difficult to consider the starting raw material. There is nothing that has a better amino acid composition than egg white. Therefore, depending on the starting material, the amino acid composition of the obtained low molecular weight peptide composition may be out of balance compared to the ideal amino acid composition. In such a case, it is preferable to select starting materials or add necessary amino acids to the low-molecular-weight peptide composition used in the nutritional supplement of the present invention depending on the purpose of use. For example, depending on the starting material, the amino acid composition can be controlled as needed, such as using the necessary essential amino acids if the starting material is lacking in essential amino acids, or using that amino acid if the condition requires a specific amino acid. In addition, the present inventors set the content of free amino acids in the composition in order to take advantage of the high absorption rate of the peptide composition in nutritional physiology, or to keep it to a level that does not cause amino acid absorption antagonism. The upper limit is considered to be approximately 20wt%. The content of relatively large peptides with a molecular weight of 700 or more is preferably kept at 20 wt% or less so as not to reduce the initial absorption rate. Further, the average molecular weight is preferably a low molecular weight of 550 to 300. Various uses are possible for the nutritional supplement according to the present invention. It can also be used as a nutritional supplement to be administered orally or directly to the stomach or intestines, either as it is or mixed with other nutritional supplements. If flavor or preference is an issue, it can be used in combination with such additives. Taking advantage of its absorption specificity, which is different from that of proteins or amino acids, it becomes an ideal material for people with weak physical strength, people with poor physical strength, and infants. Food
It has high efficiency and lowers cholesterol levels, making it an effective nutritional material for people from middle age onwards. It can be used as a more efficient material for pre- and post-operative nutritional support than conventional amino acid mixtures or simply solubilized protein decomposition products.
Claims (1)
水分解により得た分子量700以上のペプチド含量
が20wt%以下、遊離アミノ酸含量が20wt%以下
のデイペプチドおよびトリペプチドを主成分とす
る平均分子量が550〜300である低分子ペプチド組
成物を含有することを特徴とする栄養剤。 2 前記タンパク質原料が、卵白である特許請求
の範囲第1項に記載の栄養剤。[Scope of Claims] 1. The main components are dipeptides and tripeptides with a molecular weight of 700 or more, a peptide content of 20 wt% or less, and a free amino acid content of 20 wt% or less, obtained by enzymatic hydrolysis using the whole protein raw material as a nitrogen source. A nutritional supplement comprising a low molecular weight peptide composition having an average molecular weight of 550 to 300. 2. The nutritional supplement according to claim 1, wherein the protein raw material is egg white.
Priority Applications (7)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP9416980A JPS5718623A (en) | 1980-07-10 | 1980-07-10 | Nutrition supplement containing peptide oligomer |
US06/279,254 US4452888A (en) | 1980-07-10 | 1981-07-01 | Process for producing a low-molecular weight peptide composition and nutrient agent containing the same |
BE0/205335A BE889532A (en) | 1980-07-10 | 1981-07-07 | PROCESS FOR PRODUCING A COMPOSITION OF LOW MOLECULAR WEIGHT PEPTIDES AND NUTRIENT AGENT CONTAINING THE SAME |
EP81105302A EP0044032B2 (en) | 1980-07-10 | 1981-07-08 | Process for producing a low-molecular weight peptide composition and nutrient agent containing the same |
DE8181105302T DE3173244D1 (en) | 1980-07-10 | 1981-07-08 | Process for producing a low-molecular weight peptide composition and nutrient agent containing the same |
GB8121213A GB2079758B (en) | 1980-07-10 | 1981-07-09 | Process for producing a low-molecular weight peptide composition and nutrient agent containing the same |
CA000381510A CA1164377A (en) | 1980-07-10 | 1981-07-10 | Process for producing a low-molecular weight peptide composition and nutrient agent containing the same |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP9416980A JPS5718623A (en) | 1980-07-10 | 1980-07-10 | Nutrition supplement containing peptide oligomer |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS5718623A JPS5718623A (en) | 1982-01-30 |
JPS6330890B2 true JPS6330890B2 (en) | 1988-06-21 |
Family
ID=14102842
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP9416980A Granted JPS5718623A (en) | 1980-07-10 | 1980-07-10 | Nutrition supplement containing peptide oligomer |
Country Status (2)
Country | Link |
---|---|
JP (1) | JPS5718623A (en) |
BE (1) | BE889532A (en) |
Families Citing this family (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS58152498A (en) * | 1982-03-06 | 1983-09-10 | Terumo Corp | Production of low-molecular peptide mixture |
JPS58159422A (en) * | 1982-03-17 | 1983-09-21 | Kao Corp | Composition for supplying nutriment |
JPH0739351B2 (en) * | 1985-06-01 | 1995-05-01 | 森永乳業株式会社 | Method to increase water intake by boosting water intake of livestock or pets |
JPH0773507B2 (en) * | 1988-11-19 | 1995-08-09 | 森永乳業株式会社 | Low molecular weight peptide composition and method for producing the same |
JP3312944B2 (en) * | 1993-03-24 | 2002-08-12 | 伊藤ハム株式会社 | Adipocyte differentiation inhibitory peptide and adipocyte differentiation inhibitor comprising the peptide as active ingredient |
JPH08140585A (en) * | 1994-11-25 | 1996-06-04 | Hokuren Federation Of Agricult Coop:The | Production of low-molecular potato protein |
Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS5344661A (en) * | 1976-09-30 | 1978-04-21 | Kyupi Kk | Method of producing processed egg white liquid |
JPS5520668A (en) * | 1978-08-02 | 1980-02-14 | Nissan Eng Kk | Deodorizing method of waste gas of night soil treatment |
JPS5632488A (en) * | 1979-06-26 | 1981-04-01 | Agronomique Inst Nat Rech | Enzyme hydrolyzate obtained from milk serum protein and its manufacture |
-
1980
- 1980-07-10 JP JP9416980A patent/JPS5718623A/en active Granted
-
1981
- 1981-07-07 BE BE0/205335A patent/BE889532A/en not_active IP Right Cessation
Patent Citations (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS5344661A (en) * | 1976-09-30 | 1978-04-21 | Kyupi Kk | Method of producing processed egg white liquid |
JPS5520668A (en) * | 1978-08-02 | 1980-02-14 | Nissan Eng Kk | Deodorizing method of waste gas of night soil treatment |
JPS5632488A (en) * | 1979-06-26 | 1981-04-01 | Agronomique Inst Nat Rech | Enzyme hydrolyzate obtained from milk serum protein and its manufacture |
Also Published As
Publication number | Publication date |
---|---|
BE889532A (en) | 1981-11-03 |
JPS5718623A (en) | 1982-01-30 |
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