JPH04365444A - Antiallergic formulated milk - Google Patents
Antiallergic formulated milkInfo
- Publication number
- JPH04365444A JPH04365444A JP3039087A JP3908791A JPH04365444A JP H04365444 A JPH04365444 A JP H04365444A JP 3039087 A JP3039087 A JP 3039087A JP 3908791 A JP3908791 A JP 3908791A JP H04365444 A JPH04365444 A JP H04365444A
- Authority
- JP
- Japan
- Prior art keywords
- whey protein
- casein
- hydrolyzate
- purity
- protein
- 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
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- 239000005018 casein Substances 0.000 claims abstract description 62
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Abstract
Description
【０００１】0001
【産業上の利用分野】本発明は、抗原性が低く、食餌ア
レルギーの予防及び治療に有効であり、コレステロール
代謝、鉄吸収等の栄養面でも優れた作用を有する抗アレ
ルギー性調製乳に関する。TECHNICAL FIELD The present invention relates to an anti-allergic formula that has low antigenicity, is effective in preventing and treating food allergies, and has excellent nutritional effects such as cholesterol metabolism and iron absorption.
【０００２】0002
【従来の技術】乳児における食餌アレルギーの発生頻度
は、近年増加する傾向にあり、小児保健上重要な問題と
なっている。その予防及び治療には、一般に蛋白質の抗
原性を低減した抗アレルギー性調製乳が使用されている
。このため蛋白質源としては、蛋白質を加水分解して抗
原性を低減した分解物が主として使用されており、特に
、牛乳蛋白質の分解物である乳清蛋白質分解物又はカゼ
イン分解物が使用されている例が多い。しかしながら、
これらの抗アレルギー性調製乳は乳清蛋白質分解物又は
カゼイン分解物を単独に使用しており、通常の育児用調
製乳におけるように栄養学的な根拠に基づいて乳清蛋白
質とカゼインとを混合し、その混合比率を調整した抗ア
レルギー性調製乳は従来開発されていない。BACKGROUND OF THE INVENTION The frequency of food allergies in infants has been increasing in recent years, and has become an important problem in child health. For its prevention and treatment, antiallergic formula milk with reduced protein antigenicity is generally used. For this reason, as a protein source, hydrolyzed proteins with reduced antigenicity are mainly used, and in particular whey protein digests or casein digests, which are milk protein digests, are used. There are many examples. however,
These anti-allergic formulas use whey protein decomposition product or casein decomposition product alone, and whey protein and casein are mixed based on nutritional grounds like in regular infant formula milk. However, an anti-allergic formula with an adjusted mixing ratio has not been developed so far.
【０００３】このことは、通常の育児用調製乳において
はアミノ酸バランス、蛋白質利用効率、ミネラル吸収、
あるいはコレステロール代謝など乳児の栄養生理に与え
る影響等についての多くの研究に基づいて乳清蛋白質と
カゼインとの混合比率が設定されているのに対して、分
解物を用いた調製乳では、充分な栄養学的な研究がなさ
れていなかったことに起因している。[0003] This means that in normal infant formula, amino acid balance, protein utilization efficiency, mineral absorption,
Alternatively, the mixing ratio of whey protein and casein has been set based on many studies on the effects of cholesterol metabolism and other nutritional physiology in infants, whereas formula milk using decomposed products does not have enough This is due to the lack of nutritional research.
【０００４】したがって、従来から抗アレルギー用とし
て牛乳蛋白質の分解物を蛋白質源とした多くの調製乳及
びその製造法が報告されているが、それらの全ては、乳
清蛋白質分解物単独、カゼイン分解物単独、又は乳清蛋
白質とカゼインとを約２０：８０の割合で含む牛乳蛋白
質そのものを単に分解した牛乳蛋白質分解物を単独の蛋
白質源としたものであった。それらの幾つかを例示すれ
ば次の通りである。[0004] Therefore, many formulas and methods for producing the same have been reported for anti-allergy purposes, using decomposition products of cow's milk protein as the protein source, but all of them are based on whey protein decomposition products alone, casein decomposition products alone, and casein decomposition products. The sole protein source was either milk protein alone or a milk protein decomposition product obtained by simply decomposing milk protein itself containing whey protein and casein at a ratio of about 20:80. Some examples of them are as follows.
【０００５】特公昭４５ー３１９１２号公報には、牛乳
を放線菌蛋白質分解酵素のごとき、強い蛋白質分解作用
をもつ酵素を使用して分解し、パッシブ・キュタネアス
・アナフィラキシス（Ｐａｓｓｉｖｅ Ｃｕｔａｎｅ
ｏｕｓ Ａｎａｐｈｙｌａｘｉｓ）反応を陰性ならし
めることを特徴とする液状乳製品及び粉乳の製造方法が
開示されている。[0005] Japanese Patent Publication No. 45-31912 discloses that milk is decomposed using an enzyme with a strong proteolytic action such as actinomycete protease, and passive cutaneus anaphylaxis (Passive Cutaneus anaphylaxis) is produced.
Disclosed is a method for producing liquid dairy products and powdered milk, which is characterized by making the anaphylaxis reaction negative.
【０００６】特公昭５０ー１５６６６６号公報には、食
餌アレルギーの予防及び治療に有効な食品の蛋白質源と
して、苦味及び抗原性のない蛋白質分解物の製造法が開
示されている。[0006] Japanese Patent Publication No. 156666/1983 discloses a method for producing a protein decomposition product that is free from bitterness and antigenicity and is used as a food protein source effective for the prevention and treatment of food allergies.
【０００７】特公平１ー１８２７４５号公報には、乳清
蛋白質の部分加水分解物、同加水分解物を製造するため
の酵素的方法及び同加水分解物を含有する低アレルギー
性滋養特別食用乳製品が開示されている。[0007] Japanese Patent Publication No. 1-182745 describes a partial hydrolyzate of whey protein, an enzymatic method for producing the hydrolyzate, and a hypoallergenic nutritional special food dairy product containing the hydrolyzate. is disclosed.
【０００８】以上のように、抗原性が低く食餌アレルギ
ーの予防及び治療に有効であり、栄養学的にも優れた抗
アレルギー性調製乳及びその製造法について、乳清蛋白
質分解物とカゼイン分解物の配合比率を調製した調製乳
は従来知られていなかった。As described above, we have developed an anti-allergic formula that has low antigenicity, is effective in preventing and treating food allergies, and is nutritionally superior, as well as a method for producing the same. A formula prepared with a blending ratio of
【発明が解決しようとする課題】前記特公昭４５ー３１
９１２号公報の発明では、乳清蛋白質分解物とカゼイン
分解物との割合について栄養学的な見地からの配慮はな
されておらず、その割合について、何等言及されておら
ず、前記特公昭５０ー１５６６６６号公報の発明では、
蛋白質源の栄養学的意義についての考慮はされておらず
、前記特公平１ー１８２７４５号公報の発明では、加水
分解の対象は乳清蛋白質のみであり、乳清蛋白質分解物
とカゼイン分解物とを配合するという点については、何
等考慮されていなかった。[Problem to be solved by the invention] Said Japanese Patent Publication Publication No. 45-31
In the invention of Publication No. 912, no consideration was given to the ratio of whey protein decomposition product to casein decomposition product from a nutritional standpoint, and there was no mention of the ratio. In the invention of Publication No. 156666,
No consideration is given to the nutritional significance of protein sources, and in the invention of Japanese Patent Publication No. 1-182745, only whey protein is hydrolyzed, and whey protein decomposition products and casein decomposition products are hydrolyzed. No consideration was given to the addition of.
【０００９】本発明者等は、前記のような実情に鑑みて
、抗原性が低く、食餌アレルギーの予防及び治療に有効
であり、アミノ酸バランス、蛋白質利用効率、ミネラル
吸収、またはコレステロール代謝等、乳児の栄養生理上
、優れた抗アレルギー性調製乳を開発するために鋭意研
究を行い、本発明を完成した。In view of the above-mentioned circumstances, the present inventors have discovered that the present invention has low antigenicity, is effective in the prevention and treatment of food allergies, and improves amino acid balance, protein utilization efficiency, mineral absorption, cholesterol metabolism, etc. in infants. In order to develop an anti-allergic formula with excellent nutritional physiology, we conducted extensive research and completed the present invention.
【００１０】0010
【課題を解決するための手段】本発明によれば、下記の
（ａ）と（ｂ）との混合物を窒素源として含む抗アレル
ギー性調製乳が提供される。
（ａ） 少なくとも７０％（重量、以下とくに断りの
ない限り同じ）の純度の乳清蛋白質を加水分解して得ら
れ、抗乳清蛋白質血清を用いたエライザ（ＥＬＩＳＡ：
Ｅｎｚｙｍｅ ｌｉｎｋｅｄ ｉｍｍｕｎｏｓｏｒ
ｂｅｎｔ ａｓｓａｙ）抑制試験法により測定した残
存抗原活性が１０−４以下である乳清蛋白質加水分解物
、及び（ｂ） 少なくとも８０％の純度のカゼインを
加水分解物して得られ、抗カゼイン血清を用いたエライ
ザ抑制試験法により測定した残存抗原活性が１０−４以
下であるカゼイン加水分解物。According to the present invention, there is provided an anti-allergic formula containing a mixture of (a) and (b) below as a nitrogen source. (a) ELISA (ELISA) using anti-whey protein serum obtained by hydrolyzing whey protein with a purity of at least 70% (by weight, hereinafter the same unless otherwise specified):
Enzyme linked immunosor
(b) a whey protein hydrolyzate with a residual antigenic activity of 10-4 or less as measured by an inhibition test method; and (b) an anti-casein serum obtained by hydrolyzing casein with a purity of at least 80%. A casein hydrolyzate having a residual antigen activity of 10-4 or less as measured by the ELISA inhibition test method used.
【００１１】上記の（ａ）と（ｂ）との混合比率は、４
０〜８０％：６０〜２０％であることが望ましい。The mixing ratio of the above (a) and (b) is 4
0-80%: Desirably 60-20%.
【００１２】本発の抗アレルギー性調製乳の原料として
使用する抗乳清蛋白質血清を用いたエライザ抑制試験法
により測定した残存抗原活性が１０−４以下である乳清
蛋白質の加水分解物（以下、単に乳清蛋白質加水分解物
と記載する）及び抗カゼイン血清を用いたエライザ抑制
試験法により測定した残存抗原活性が１０−４以下であ
るカゼインの加水分解物（以下、単にカゼイン加水分解
物と記載する）は、それぞれ次のようにして製造される
。[0012] A hydrolyzate of whey protein (hereinafter referred to as a hydrolyzate of whey protein) having a residual antigenic activity of 10-4 or less as measured by the ELISA inhibition test method using anti-whey protein serum used as a raw material for the anti-allergic formula of the present invention. , simply referred to as whey protein hydrolyzate) and a casein hydrolyzate with a residual antigenic activity of 10-4 or less measured by the ELISA inhibition test method using anti-casein serum (hereinafter simply referred to as casein hydrolyzate). ) are manufactured as follows.
【００１３】乳清蛋白質加水分解物は、ホエー等から常
法（例えば、ウルトラフィルトレーションあるいはイオ
ン交換法等）により分離，精製した乳清蛋白質、望まし
くは純度が少なくとも７０％の乳清蛋白質を、１０％以
下の濃度で水又は精製水に溶解し、ｐＨを６．５〜１０
に調整し、通常使用されている蛋白質分解酵素を添加し
、常法により加水分解し、加熱して酵素を失活させるか
、またはウルトラフィルトレーションにより酵素を除去
し、残存抗原活性が１０−４以下の乳清蛋白質加水分解
物を得る。蛋白質分解酵素はパンクレアチン等の動物由
来の酵素、パパイン等の植物由来の酵素，細菌又は黴等
の微生物由来の酵素等、何れでも使用できる。[0013] Whey protein hydrolyzate is whey protein separated and purified from whey etc. by a conventional method (for example, ultrafiltration or ion exchange method), preferably whey protein with a purity of at least 70%. , dissolved in water or purified water at a concentration of 10% or less, and adjusted the pH to 6.5-10.
Add a commonly used protease, hydrolyze using a conventional method, heat to inactivate the enzyme, or remove the enzyme by ultrafiltration until the residual antigen activity is 10- A whey protein hydrolyzate of 4 or less is obtained. Any of the proteolytic enzymes can be used, such as animal-derived enzymes such as pancreatin, plant-derived enzymes such as papain, and enzymes derived from microorganisms such as bacteria or mold.
【００１４】特に望ましい実施態様では、使用する酵素
はトリプシンを主体とし、キモトリプシン及びエキソペ
プチダーゼを含むパンクレアチン、又はパパイン、又は
アスペルギルス・オリーゼ（Ａｓｐｅｒｇｉｌｌｕｓ
ｏｒｙｚａｅ）由来のエンドペプチダーゼ、又はバシ
ラス・サチリス（Ｂａｃｉｌｌｕｓ Ｓｕｂｔｉｌｉ
ｓ）由来のエンドペプチダーゼなどを用いる。これらの
酵素はいずれも市販品であって良い。In a particularly preferred embodiment, the enzymes used are trypsin-based, pancreatin, including chymotrypsin and exopeptidase, or papain, or Aspergillus oryzae.
endopeptidase from Bacillus subtili or Bacillus subtili.
Use endopeptidase derived from s). Any of these enzymes may be commercially available.
【００１５】これらの酵素の活性単位は、次の定義によ
る。ミルクカゼイン［ハマーシュタイン（Ｈａｍｍｅｒ
ｓｔｅｎ）、メルク社製］に酵素を作用させ、３０℃で
１分間に１μｇのチロシンに相当するアリルアミノ酸の
フォリン試薬での呈色反応を示す酵素活性度を１単位と
する（以下、この単位をＰＵＮ単位と記載する）。The activity units of these enzymes are defined as follows. Milk casein [Hammerstein
sten), manufactured by Merck & Co., Ltd.], and the enzyme activity that shows the color reaction with Folin's reagent of allyl amino acid corresponding to 1 μg of tyrosine per minute at 30°C is defined as 1 unit (hereinafter, this unit) (described as PUN unit).
【００１６】これらの酵素の使用量は、乳清蛋白質１ｇ
当たりパンクレアチンが２００〜２，０００ＰＵＮ単位
、望ましくは３００〜１，０００ＰＵＮ単位、パパイン
が２５０〜２，０００ＰＵＮ単位、望ましくは３００〜
１，０００ＰＵＮ単位、アスペルギルス・オリーゼ由来
のエンドペプチダーゼが２００〜２，０００ＰＵＮ単位
、望ましくは３００〜１，０００ＰＵＮ単位、バシラス
・サチリス由来のエンドペプチダーゼが２００〜２，０
００ＰＵＮ単位、望ましくは３００〜１，０００ＰＵＮ
単位が適当である。[0016] The amount of these enzymes used is 1 g of whey protein.
Pancreatin is 200 to 2,000 PUN units, preferably 300 to 1,000 PUN units, and papain is 250 to 2,000 PUN units, preferably 300 to
1,000 PUN units, endopeptidase derived from Aspergillus oryzae is 200 to 2,000 PUN units, preferably 300 to 1,000 PUN units, and endopeptidase derived from Bacillus subtilis is 200 to 2,0 PUN units.
00PUN unit, preferably 300-1,000PUN
The units are appropriate.
【００１７】前記乳清蛋白質の水溶液に、乳清蛋白質の
量に応じて前記の酵素の所定量を添加し、４５〜５２℃
の温度で３〜２４時間、望ましくは６〜２０時間加水分
解する。[0017] A predetermined amount of the enzyme described above is added to the aqueous solution of whey protein according to the amount of whey protein, and the mixture is heated at 45 to 52°C.
Hydrolysis is carried out at a temperature of 3 to 24 hours, preferably 6 to 20 hours.
【００１８】次いで加熱処理により酵素を失活させるか
又はウルトラフィルトレーション処理により酵素を除去
する。加熱処理は７０℃で１０分間から１４０℃で２秒
間までの範囲で適宜行う。ウルトラフィルトレーション
処理は酵素が透過せずペプチドが透過でき回収が容易な
分画分子量１５，０００から２，０００の範囲で行う。
その後セライト等により濾過し、噴霧乾燥又は凍結乾燥
し、乳清蛋白質加水分解物を得る。以上により得られた
乳清蛋白質加水分解物の残存抗原活性は１０−４以下で
ある。Next, the enzyme is inactivated by heat treatment or removed by ultrafiltration treatment. The heat treatment is appropriately carried out in the range from 70°C for 10 minutes to 140°C for 2 seconds. The ultrafiltration treatment is carried out at a molecular weight cut-off of 15,000 to 2,000, which allows the passage of enzymes but not peptides and is easy to recover. Thereafter, it is filtered through Celite or the like, and spray-dried or freeze-dried to obtain a whey protein hydrolyzate. The residual antigenic activity of the whey protein hydrolyzate obtained above is 10-4 or less.
【００１９】カゼイン加水分解物は、常法により分離，
精製された牛乳カゼイン、望ましくは純度が少なくとも
８０％のカゼインを１２％の濃度で水に溶解し、ｐＨを
７〜８．５に調整し、通常使用されている蛋白質分解酵
素を添加し、常法により加水分解し、残存抗原活性が１
０−４以下のカゼイン加水分解物を得る。使用する蛋白
質加水分解酵素は、パンクレアチン等の動物由来の酵素
、パパイン等の植物由来の酵素、細菌又は黴等の微生物
由来の酵素の単品又は混合物であって良い。[0019] The casein hydrolyzate is separated by a conventional method.
Purified milk casein, preferably with a purity of at least 80%, is dissolved in water at a concentration of 12%, the pH is adjusted to 7-8.5, commonly used proteolytic enzymes are added, and the hydrolyzed by the method, with residual antigenic activity of 1
A casein hydrolyzate of 0-4 or less is obtained. The proteolytic enzyme used may be an animal-derived enzyme such as pancreatin, a plant-derived enzyme such as papain, or an enzyme derived from a microorganism such as bacteria or mold, either singly or in a mixture.
【００２０】特に望ましい実施態様では、使用する酵素
はトリプシンを主体とし、キモトリプシン及びエキソペ
プチダーゼを含むパンクレアチン、又はパパイン、又は
アスペルギルス・オリーゼ（Ａｓｐｅｒｇｉｌｌｕｓ
ｏｒｙｚａｅ）由来のエンドペプチダーゼ、又はバシ
ラス・サチリス（Ｂａｃｉｌｌｕｓ ｓａｂｔｉｌｉ
ｓ）由来のエンドペプチダーゼなどが用いられる。これ
らの酵素は、何れも市販品であって良い。これらの酵素
の活性の単位は前記と同様の定義による。これらの酵素
使用量は、カゼイン１ｇ当たり、パンクレアチンが２０
０〜２，０００ＰＵＮ単位、望ましくは３００〜１，０
００ＰＵＮ単位、パパインが２５０〜２，０００ＰＵＮ
単位、望ましくは３００〜１，０００ＰＵＮ単位、アス
ペルギルス・オリーゼ由来のエンドペプチダーゼが２０
０〜２，０００ＰＵＮ単位、望ましくは３００〜１，０
００ＰＵＮ単位、バシラス・サチリス由来のエンドペプ
チダーゼが２００〜２，０００ＰＵＮ単位、望ましくは
３００〜１，０００ＰＵＮ単位が適当である。前記カゼ
インの水溶液に、カゼインの量に応じて前記酵素の所定
量を添加し、４５〜５２℃の温度で３〜２４時間、望ま
しくは６〜２０時間加水分解する。次いで、加熱処理に
より酵素を失活させるか又はウルトラフィルトレーショ
ン処理により酵素を除去する。加熱処理は、７０℃で１
０分間から１４０℃で２秒間までの範囲で適宜行う。ウ
ルトラフィルトレーション処理は、酵素が透過せずペプ
チドが透過でき回収が容易な分画分子量１５，０００か
ら２，０００の範囲で行う。その後セライト等により濾
過し、濾液を噴霧乾燥、あるいは凍結乾燥し、カゼイン
分解物粉末を得る。かくて得られたカゼイン分解物の残
存抗原活性は１０−４以下である。In a particularly preferred embodiment, the enzymes used are trypsin-based, pancreatin, including chymotrypsin and exopeptidase, or papain, or Aspergillus oryzae.
endopeptidase from Bacillus oryzae or Bacillus subtilis.
Endopeptidases derived from s) are used. Any of these enzymes may be commercially available. The units of activity of these enzymes are defined as above. The amount of these enzymes used is 20% of pancreatin per 1g of casein.
0 to 2,000 PUN units, preferably 300 to 1,0
00PUN unit, papain is 250-2,000PUN
unit, preferably 300 to 1,000 PUN units, endopeptidase derived from Aspergillus oryzae is 20
0 to 2,000 PUN units, preferably 300 to 1,0
00 PUN units, 200 to 2,000 PUN units, preferably 300 to 1,000 PUN units for endopeptidase derived from Bacillus subtilis. A predetermined amount of the enzyme is added to the casein aqueous solution depending on the amount of casein, and hydrolyzed at a temperature of 45 to 52°C for 3 to 24 hours, preferably 6 to 20 hours. Next, the enzyme is inactivated by heat treatment or removed by ultrafiltration treatment. Heat treatment was performed at 70°C.
The heating time is suitably carried out in the range from 0 minutes to 2 seconds at 140°C. The ultrafiltration treatment is performed at a molecular weight cutoff in the range of 15,000 to 2,000, where enzymes cannot pass through, peptides can pass through, and recovery is easy. Thereafter, it is filtered through Celite or the like, and the filtrate is spray-dried or freeze-dried to obtain casein decomposition product powder. The residual antigenic activity of the casein decomposition product thus obtained is 10-4 or less.
【００２１】次に調製乳の製造法について記載する。Next, a method for producing formula milk will be described.
【００２２】抗アレルギー性調製乳は、液状、粉末状の
何れでも良いが、特に望ましい粉末製品の製造法につい
て以下に例示する。前記により製造した乳清蛋白質加水
分解物とカゼイン加水分解物との比率が８０：２０〜４
０：６０であって、最終製品の全固形物中に占める蛋白
質（等量）が５〜２０％の割合にそれぞれの加水分解物
を計量し、水に５〜１５％の濃度で溶解し、所定のミネ
ラル類を加えて４０〜６５℃に加熱し、更に脂肪、糖、
ビタミン類の所定量を混合し、高圧ホモジナイザーによ
り乳化し、常法により加熱殺菌し、噴霧乾燥し、調製粉
乳を得る。[0022] The anti-allergic formula may be in either liquid or powder form, but a particularly desirable method for producing a powder product will be exemplified below. The ratio of whey protein hydrolyzate and casein hydrolyzate produced as above is 80:20 to 4.
Weigh each hydrolyzate to a ratio of 5 to 20% protein (equivalent) in the total solids of the final product, and dissolve it in water at a concentration of 5 to 15%. Add specified minerals and heat to 40-65℃, then add fat, sugar,
A predetermined amount of vitamins is mixed, emulsified using a high-pressure homogenizer, heat sterilized by a conventional method, and spray-dried to obtain a powdered milk.
【００２３】液状の抗アレルギー性調製乳についても、
粉末製品と同様に製造し得る。ただし、最終製品の濃度
が５〜４０％の液状物となるため、腐敗防止の点から加
水分解物を溶解する際の液量を増加すること、及び加熱
殺菌を１２０℃以上、望ましくは１３５℃以上の温度で
行う必要がある。Regarding the liquid anti-allergic formula,
It can be manufactured similarly to powdered products. However, since the final product will be a liquid product with a concentration of 5 to 40%, it is necessary to increase the amount of liquid when dissolving the hydrolyzate to prevent spoilage, and heat sterilization at 120°C or higher, preferably at 135°C. It is necessary to carry out the process at a temperature higher than that.
【００２４】かくて得られた本発明の抗アレルギー性調
製乳は、後述する試験によれば、アレルギーの予防及び
治療に有効な性質を有し、更にアミノ酸バランス、蛋白
質利用効率においても優れている。According to the tests described below, the antiallergic formula of the present invention thus obtained has properties that are effective in preventing and treating allergies, and is also excellent in amino acid balance and protein utilization efficiency. .
【００２５】次に試験例を示して本発明を詳述するが、
これら試験例において用いられた残存抗原活性の測定方
法及びアミノ酸組成測定方法の概要について先ず説明す
る。
（１）残存抗原活性の測定方法
エライザ抑制試験法により、次のようにして残存抗原活
性を測定した。９６穴プレート（ヌンク社製）に乳清蛋
白質をコーティングし、洗浄し、ウサギ抗乳清蛋白質血
清と加水分解物試料の混合液をプレートの穴に供給して
反応させ、洗浄後アルカリホスファターゼ標識ヤギ抗ウ
サギＩｇＧ抗体（ツァイメド・ラボラトリー社製）を反
応させ、のち洗浄し、ｐ−ニトロフェニル燐酸ナトリウ
ムを添加し、３０分後に５Ｎ水酸化ナトリウムを添加し
て反応を停止させ、反応生成物をマイクロプレートリー
ダーで測定した（日本小児アレルギー学会誌、第１巻、
第３６ページ、１９８７年）。
（２）アミノ酸組成の測定方法
トリプトファン、システイン及びメチオニン以外のアミ
ノ酸については、試料を６ＮのＨＣｌで１１０℃、２４
時間加水分解し、トリプトファンについては水酸化バリ
ウムで１００℃、２２時間アルカリ分解し、システイン
及びメチオニンについては過蟻酸処理後６ＮのＨＣｌで
１１０℃、１８時間加水分解し、夫々アミノ酸分析機（
日立製作所製：８３５型）により分析し、アミノ酸の質
量を求めた。
試験例１
この試験は乳清蛋白質分解物について残存抗原活性とア
レルギー性との関係を調べるために行われた。
（１）試料の調製
各種乳清蛋白質と酵素を用いて、種々の程度に抗原性を
残存する次の８種類の乳清蛋白質分解物を調製した。Next, the present invention will be explained in detail by showing test examples.
First, an overview of the method for measuring residual antigen activity and the method for measuring amino acid composition used in these test examples will be explained. (1) Method for Measuring Residual Antigen Activity Residual antigen activity was measured by the ELISA inhibition test method as follows. A 96-well plate (manufactured by Nunc) was coated with whey protein, washed, and a mixture of rabbit anti-whey protein serum and hydrolyzate sample was supplied to the wells of the plate for reaction. After washing, alkaline phosphatase-labeled goat Anti-rabbit IgG antibody (manufactured by Zeymed Laboratories) was reacted, then washed, sodium p-nitrophenyl phosphate was added, 30 minutes later, 5N sodium hydroxide was added to stop the reaction, and the reaction product was micro-incubated. Measured using a plate reader (Japanese Journal of Pediatric Allergy, Vol. 1,
p. 36, 1987). (2) Method for measuring amino acid composition For amino acids other than tryptophan, cysteine and methionine, the sample was diluted with 6N HCl at 110°C for 24 hours.
Tryptophan was alkaline decomposed with barium hydroxide at 100°C for 22 hours, and cysteine and methionine were treated with performic acid and then hydrolyzed with 6N HCl at 110°C for 18 hours.
Hitachi, Ltd.: Model 835) was used to determine the mass of the amino acid. Test Example 1 This test was conducted to investigate the relationship between residual antigen activity and allergic properties of whey protein decomposition products. (1) Preparation of Samples Using various whey proteins and enzymes, the following eight types of whey protein decomposition products, which retain antigenicity to varying degrees, were prepared.
【００２６】試料１：純度７５％の乳清蛋白質を１０％
の濃度で水に溶解し、水酸化ナトリウムでｐＨ８．０に
調整し、パンクレアチン（天野製薬社製）を乳清蛋白質
に対して１％の割合で添加し、５０℃で２時間加水分解
し、８５℃で１０分間加熱処理を行った。この溶液をハ
イフロースーパーセルを用いて濾過し、凍結乾燥した。
得られた分解物の残存抗原活性は１０−３．５であった
。Sample 1: 10% whey protein with a purity of 75%
It was dissolved in water at a concentration of , adjusted to pH 8.0 with sodium hydroxide, added pancreatin (manufactured by Amano Pharmaceutical Co., Ltd.) at a ratio of 1% to whey protein, and hydrolyzed at 50°C for 2 hours. , heat treatment was performed at 85° C. for 10 minutes. This solution was filtered using High Flow Super Cell and freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-3.5.
【００２７】試料２：純度７５％の乳清蛋白質を１０％
の濃度で水に溶解し、水酸化ナトリウムでｐＨ８．０に
調整し、パンクレアチン（天野製薬社製）を乳清蛋白質
に対して３％の割合で添加し、５０℃で６時間加水分解
し、８５℃で１０分間加熱処理した。この溶液をハイフ
ロースーパーセルを用いて濾過し、凍結乾燥した。この
分解物の残存抗原活性は１０−４．５であった。Sample 2: 10% whey protein with a purity of 75%
The solution was dissolved in water at a concentration of 1, adjusted to pH 8.0 with sodium hydroxide, pancreatin (manufactured by Amano Pharmaceutical Co., Ltd.) was added at a ratio of 3% to whey protein, and hydrolyzed at 50°C for 6 hours. , heat-treated at 85° C. for 10 minutes. This solution was filtered using High Flow Super Cell and freeze-dried. The residual antigenic activity of this decomposition product was 10-4.5.
【００２８】試料３：純度７５％の乳清蛋白質を１０％
の濃度で水に溶解し、水酸化ナトリウムでｐＨ７．０に
調整し、パパイン（長瀬生化学工業社製）を乳清蛋白質
に対して３％の割合で添加し、５０℃で６時間加水分解
し、８５℃で１０分間加熱処理を行った。この溶液をハ
イフロースーパーセルを用いて濾過し、凍結乾燥した。
この分解物の残存抗原活性は１０−５であった。Sample 3: 10% whey protein with a purity of 75%
The mixture was dissolved in water at a concentration of Then, heat treatment was performed at 85° C. for 10 minutes. This solution was filtered using High Flow Super Cell and freeze-dried. The residual antigenic activity of this decomposition product was 10-5.
【００２９】試料４：純度７５％の乳清蛋白質を１０％
の濃度で水に溶解し、水酸化ナトリウムでｐＨ７．５に
調整し、アクチナーゼ（科研製薬社製）を乳清蛋白質に
対して１％の割合で添加し、５０℃で２時間加水分解し
、８５℃で１０分間加熱処理した。得られた溶液をハイ
フロースーパーセルを用いて濾過し、凍結乾燥した。
得られた分解物の残存抗原活性は１０−４であった。Sample 4: 10% whey protein with a purity of 75%
It was dissolved in water at a concentration of Heat treatment was performed at 85° C. for 10 minutes. The resulting solution was filtered using High Flow Super Cell and freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-4.
【００３０】試料５：純度９０％の乳清蛋白質を１０％
の濃度で水に溶解し、水酸化ナトリウムでｐＨ７．５に
調整し、パンクレアチン（天野製薬社製）を乳清蛋白質
に対して１％の割合で添加し、５０℃で６時間加水分解
し、８５℃で１０分間加熱処理した。得られた溶液をハ
イフロースーパーセルを用いて濾過し、凍結乾燥した。
得られた分解物の残存抗原活性は１０−３．５であった
。Sample 5: 10% whey protein with a purity of 90%
It was dissolved in water at a concentration of , adjusted to pH 7.5 with sodium hydroxide, added pancreatin (manufactured by Amano Pharmaceutical Co., Ltd.) at a ratio of 1% to whey protein, and hydrolyzed at 50°C for 6 hours. , heat-treated at 85° C. for 10 minutes. The resulting solution was filtered using High Flow Super Cell and freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-3.5.
【００３１】試料６：純度９０％の乳清蛋白質を１０％
の濃度で水に溶解し、水酸化ナトリウムでｐＨ７．５に
調整し、パンクレアチン（天野製薬社製）を乳清蛋白質
に対して３％の割合で添加し、５０℃で６時間加水分解
し、８５℃で１０分間加熱処理した。得られた溶液をハ
イフロースーパーセルを用いて濾過し、凍結乾燥した。
得られた分解物の残存抗原活性は１０−４．５であった
。Sample 6: 10% whey protein with a purity of 90%
The mixture was dissolved in water at a concentration of , heat-treated at 85° C. for 10 minutes. The resulting solution was filtered using High Flow Super Cell and freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-4.5.
【００３２】試料７：純度９０％の乳清蛋白質を１０％
の濃度で水に溶解し、水酸化ナトリウムでｐＨ７．０に
調整し、パパイン（長瀬生化学工業社製）を乳清蛋白質
に対して３％の割合で添加し、５０℃で６時間加水分解
し、８５℃で１０分間加熱処理した。得られた溶液をハ
イフロースーパーセルを用いて濾過し、凍結乾燥した。
得られた分解物の残存抗原活性は１０−４であった。Sample 7: 10% whey protein with a purity of 90%
The mixture was dissolved in water at a concentration of and heat-treated at 85° C. for 10 minutes. The resulting solution was filtered using High Flow Super Cell and freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-4.
【００３３】試料８：純度９０％の乳清蛋白質を１０％
の濃度で水に溶解し、水酸化ナトリウムでｐＨ７．５に
調整し、アクチナーゼ（科研製薬社製）を乳清蛋白質に
対して３％の割合で添加し、５０℃で６時間加水分解し
、８５℃で１０分間加熱処理した。得られた溶液をハイ
フロースーパーセルを用いて濾過し、凍結乾燥した。
得られた分解物の残存抗原活性は１０−５であった。
（２）試験方法
アレルギー性の測定方法は次の通りである。生後３週齢
の雄モルモット５匹を１群とした複数群に、１日に体重
１００ｇ当たり５０ｍｇ、３週間連続的に各試料を経口
投与した。３週間後、静脈より純度９０％以上の乳清蛋
白質の１０％溶液を注入し、アナフィラキシーショック
の発現を観察し、次の基準によってアレルギー性を判定
した。Sample 8: 10% whey protein with a purity of 90%
It was dissolved in water at a concentration of Heat treatment was performed at 85° C. for 10 minutes. The resulting solution was filtered using High Flow Super Cell and freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-5. (2) Test method The method for measuring allergic properties is as follows. Each sample was orally administered at a dose of 50 mg per 100 g of body weight per day for 3 consecutive weeks to multiple groups each consisting of 5 male guinea pigs 3 weeks old. After 3 weeks, a 10% solution of whey protein with a purity of 90% or more was injected intravenously, the development of anaphylactic shock was observed, and the allergic nature was determined according to the following criteria.
【００３４】アレルギー性＋３：アナフィラキシーによ
りショック死。Allergic +3: Shock death due to anaphylaxis.
【００３５】アレルギー性＋２：ショックは起こすが死
には至らず。Allergic +2: Causes shock but does not lead to death.
【００３６】アレルギー性＋１：鼻擦りや立毛など弱い
症状を呈する。Allergy +1: exhibits weak symptoms such as nasal irritation and piloerection.
【００３７】アレルギー性０： 特に、変化を認めず
。
（３）試験結果
この試験の結果は表１に示すとおりであった。表１から
明らかなように、残存抗原活性が１０−４以下の乳清蛋
白質分解物にはアレルギー性がないことが判明した。Allergy 0: No particular change observed. (3) Test results The results of this test were as shown in Table 1. As is clear from Table 1, whey protein decomposition products with residual antigenic activity of 10-4 or less were found to be non-allergenic.
【表１】
試験例２
この試験はカゼイン加水分解物について残存抗原活性と
アレルギー性との関係を調べるために行われた。
（１）試料の調製
各種カゼインと酵素を用いて、種々の程度に抗原性を残
存する次の４種類のカゼイン分解物を調製した。試料１
：純度８５％の食用乳酸カゼイン（ニュージランド・デ
イリー・ボード製）を１０％の濃度で水に分散し、水酸
化ナトリウムでｐＨを８．０に調整しながら溶解し、パ
ンクレアチン（天野製薬社製）を食用乳酸カゼインにた
いして１％の割合で添加し、５０℃で２時間加水分解し
、８５℃で１０分間加熱して酵素を失活させた。この溶
液をハイフロースーパーセルを用いて濾過し、のち凍結
乾燥た。得られた分解物の残存抗原活性は１０−３．５
であった。試料２：純度８５％の食用乳酸カゼイン（ニ
ュージランド・デイリー・ボード製）を１０％の濃度で
水に分散し、水酸化ナトリウムでｐＨを８．０に調整し
ながら溶解し、パンクレアチン（天野製薬社製）を食用
乳酸カゼインにたいして１％の割合で添加し、５０℃で
６時間加水分解し、８５℃で１０分間加熱して酵素を失
活させた。この溶液をハイフロースーパーセルを用いて
濾過し、のち凍結乾燥した。得られた分解物の残存抗原
活性は１０−４．５であった。試料３：純度８５％の食
用乳酸カゼイン（ニュージランド・デイリー・ボード製
）を１０％の濃度で水に分散し、水酸化ナトリウムでｐ
Ｈを７．０に調整しながら溶解し、パパイン（長瀬生化
学工業社製）を食用乳酸カゼインにたいして１％の割合
で添加し、５０℃で６時間加水分解し、８５℃で１０分
間加熱して酵素を失活させた。この溶液をハイフロース
ーパーセルを用いて濾過し、のち凍結乾燥した。得られ
た分解物の残存抗原活性は１０−４であった。試料４：
純度８５％の食用乳酸カゼイン（ニュージランド・デイ
リー・ボード製）を１０％の濃度で水に分散し、水酸化
ナトリウムでｐＨを７．５に調整しながら溶解し、アク
チナーゼ（科研製薬社製）を食用乳酸カゼインに対して
１％の割合で添加し、５０℃で６時間加水分解し、８５
℃で１０分間加熱して酵素を失活させた。この溶液をハ
イフロースーパーセルを用いて濾過し、のち凍結乾燥し
た。得られた分解物の残存抗原活性は１０−４であった
。
（２）試験方法
アレルギー性の測定法は試験例１と同一の方法によった
。
（３）試験結果
この試験の結果は表２に示すとおりであった。表２から
明らかなように、残存抗原活性が１０−４以下のカゼイ
ン分解物にはアレルギー性がないことが判明した。[Table 1] Test Example 2 This test was conducted to investigate the relationship between residual antigenic activity and allergic properties of casein hydrolyzate. (1) Preparation of Samples Using various caseins and enzymes, the following four types of casein decomposition products, which retain antigenicity to varying degrees, were prepared. Sample 1
: Disperse 85% pure edible casein lactic acid (manufactured by New Zealand Dairy Board) in water at a concentration of 10%, dissolve it while adjusting the pH to 8.0 with sodium hydroxide, and add pancreatin (manufactured by Amano Pharmaceutical Co., Ltd.) to water. ) was added to edible lactic acid casein at a ratio of 1%, hydrolyzed at 50°C for 2 hours, and heated at 85°C for 10 minutes to inactivate the enzyme. This solution was filtered using High Flow Super Cell and then freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-3.5
Met. Sample 2: Edible casein lactate (manufactured by New Zealand Dairy Board) with a purity of 85% was dispersed in water at a concentration of 10%, and dissolved while adjusting the pH to 8.0 with sodium hydroxide. 1% of edible lactic acid casein, hydrolyzed at 50°C for 6 hours, and heated at 85°C for 10 minutes to deactivate the enzyme. This solution was filtered using High Flow Super Cell and then freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-4.5. Sample 3: Edible casein lactate (manufactured by New Zealand Dairy Board) with a purity of 85% was dispersed in water at a concentration of 10%, and purified with sodium hydroxide.
H was dissolved while adjusting it to 7.0, papain (manufactured by Nagase Seikagaku Kogyo Co., Ltd.) was added at a ratio of 1% to edible casein lactic acid, hydrolyzed at 50°C for 6 hours, and heated at 85°C for 10 minutes. The enzyme was inactivated. This solution was filtered using High Flow Super Cell and then freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-4. Sample 4:
Edible casein lactate (manufactured by New Zealand Dairy Board) with a purity of 85% was dispersed in water at a concentration of 10%, dissolved while adjusting the pH to 7.5 with sodium hydroxide, and actinase (manufactured by Kaken Pharmaceutical Co., Ltd.) was dissolved. It was added at a ratio of 1% to edible lactic acid casein and hydrolyzed at 50°C for 6 hours to give 85%
The enzyme was inactivated by heating at ℃ for 10 minutes. This solution was filtered using High Flow Super Cell and then freeze-dried. The residual antigenic activity of the obtained decomposition product was 10-4. (2) Test method The method for measuring allergic properties was the same as in Test Example 1. (3) Test results The results of this test were as shown in Table 2. As is clear from Table 2, it was found that casein decomposition products with residual antigenic activity of 10-4 or less were not allergic.
【表２】
試験例３
この試験は乳清蛋白質分解物とカゼイン分解物の配合比
率がコレステロール代謝に及ぼす影響を調べるために行
われた。
（１）飼料の調製
表３に示す乳清蛋白質加水分解物とカゼイン加水分解物
との配合比率が異なる６種類のコレステロール添加飼料
を調製した。[Table 2] Test Example 3 This test was conducted to examine the influence of the blending ratio of whey protein decomposition product and casein decomposition product on cholesterol metabolism. (1) Preparation of Feeds Six types of cholesterol-added feeds with different blending ratios of whey protein hydrolyzate and casein hydrolyzate shown in Table 3 were prepared.
【表３】
尚、乳清蛋白質加水分解物は、試験例１の試料６と同一
の方法で調製した試料を用いた。この乳清蛋白質加水分
解物の蛋白質含量（蛋白質量を窒素量×６．３８として
算出した値）は８１．０％であった。カゼイン加水分解
物は、試験例２の試料２と同一の方法で調製した試料を
用いた。このカゼイン加水分解物の蛋白質含量（蛋白質
量を窒素量×６．３８として算出した値）は８５．２％
であった。
（２）試験方法
生後１カ月のＳＤ系雄ラットの５匹を１群として６群に
分け、各群に、蛋白質源として乳清蛋白質加水分解物、
カゼイン加水分解物、又はそれらの各種比率の混合物を
用いたコレステロール添加飼料を３週間摂取させた。１
週間毎に３回採血し、血清中のコレステロール濃度を、
コレステロールＥテスト（和光純薬工業社製）を用いた
酵素法により測定した。各群、各週の血清中コレステロ
ール濃度の平均値を算出し、コレステロール値の変動を
試験した。
（３）試験結果
この試験の結果を表４に示した。飼料１、飼料２、飼料
３及び飼料４で飼育した群では、血清中のコレステロー
ル含量に顕著な増加は認められなかった。しかしながら
、飼料５及び飼料６で飼育した群ではコレステロールが
顕著に増加した。この試験の結果は、乳清蛋白質加水分
解物に血中コレステロール濃度の調節作用があること、
その効果は乳清蛋白質加水分解物が全窒素量の４０％以
上存在する場合に発揮されることを示している。
試験例４
この試験は乳清蛋白質加水分解物とカゼイン加水分解物
の配合比率が鉄の吸収に及ぼす影響を調べるために行わ
れた。
（１）飼料の調製
表５に示す乳清蛋白質加水分解物とカゼイン加水分解物
の配合比率が異なる６種類の飼料を調製した。[Table 3] As the whey protein hydrolyzate, a sample prepared in the same manner as Sample 6 of Test Example 1 was used. The protein content of this whey protein hydrolyzate (a value calculated by multiplying the amount of protein by the amount of nitrogen x 6.38) was 81.0%. As the casein hydrolyzate, a sample prepared in the same manner as Sample 2 of Test Example 2 was used. The protein content of this casein hydrolyzate (value calculated as protein amount x nitrogen amount x 6.38) is 85.2%.
Met. (2) Test method Five SD male rats, one month old, were divided into six groups, and each group was given whey protein hydrolyzate as a protein source;
Cholesterol supplemented feed using casein hydrolyzate or mixtures thereof in various ratios was fed for 3 weeks. 1
Blood was collected three times a week and the serum cholesterol concentration was determined.
Cholesterol was measured by an enzymatic method using Cholesterol E Test (manufactured by Wako Pure Chemical Industries, Ltd.). The average value of serum cholesterol concentration for each group and each week was calculated, and changes in cholesterol values were examined. (3) Test results The results of this test are shown in Table 4. In the groups fed Feed 1, Feed 2, Feed 3, and Feed 4, no significant increase in serum cholesterol content was observed. However, cholesterol levels significantly increased in the groups fed Feed 5 and Feed 6. The results of this test showed that whey protein hydrolyzate has a regulating effect on blood cholesterol concentration.
It has been shown that this effect is exhibited when whey protein hydrolyzate is present in an amount of 40% or more of the total nitrogen content. Test Example 4 This test was conducted to examine the effect of the blending ratio of whey protein hydrolyzate and casein hydrolyzate on iron absorption. (1) Preparation of Feeds Six types of feeds shown in Table 5 with different blending ratios of whey protein hydrolyzate and casein hydrolyzate were prepared.
【表５】
（２）試験方法
初体重約１００ｇのＳＤ系雄ラット８匹を１群として６
群に分け、各群に蛋白質源として乳清蛋白質加水分解物
、カゼイン加水分解物、又はそれらの各種比率の混合物
を用いた飼料を５０日間摂取させた。この間の糞尿中の
鉄量を原子吸光法により測定し、吸収率、尿中***量及
び体内保留率を求め、乳清蛋白質加水分解物とカゼイン
加水分解物の比率が鉄吸収に及ぼす影響を試験した。
（３）試験結果
この試験の結果を表６に示した。飼料１で飼育した群に
おける鉄の吸収率は他の群と比較して有意に低かった。
この試験の結果から、カゼイン加水分解物が鉄吸収に何
等かの効果を有すること、その効果を発現させるために
は、カゼイン加水分解物が少なくとも全窒素量の２０％
以上存在する必要があること、が判明した。[Table 5] (2) Test method A group of 8 SD male rats with an initial weight of approximately 100 g
The animals were divided into groups, and each group was fed a diet containing whey protein hydrolyzate, casein hydrolyzate, or mixtures thereof in various ratios as a protein source for 50 days. During this period, the amount of iron in the feces and urine was measured using atomic absorption spectrometry, and the absorption rate, urinary excretion amount, and retention rate in the body were determined, and the effect of the ratio of whey protein hydrolyzate and casein hydrolyzate on iron absorption was examined. did. (3) Test results The results of this test are shown in Table 6. The iron absorption rate in the group fed Feed 1 was significantly lower than in the other groups. The results of this test show that casein hydrolyzate has some effect on iron absorption, and in order to exhibit this effect, casein hydrolyzate must contain at least 20% of the total nitrogen content.
It turns out that there is a need for more than one.
【表６】[Table 6]
【実施例】次に実施例を示して本発明を更に詳述するが
、本発明は以下の実施例に限定されるものではない。
実施例１
試験例１の試料３と同一の方法で純度７５％の乳清蛋白
質を加水分解して得た残存抗原活性１０−４の乳清蛋白
質加水分解物（蛋白質等量７９．４％）１０．６Ｋｇ、
及び試験例２の試料３と同一の方法で純度８５％のカゼ
インを加水分解して得た残存抗原性１０−４のカゼイン
分解物（蛋白質等量８７．４％）１２．１Ｋｇを水１４
０Ｋｇに溶解し、５Ｋｇの水に溶解した所定量のミネラ
ル類を加え、６０℃に加熱し、植物性脂肪２５．０Ｋｇ
、マルツデキストリン５０．０Ｋｇ、砂糖５．０Ｋｇ、
及び所定量のビタミン類を混合し、この混合液を高圧ホ
モジナイザーで充分に乳化し、１２０℃で２秒間殺菌し
、噴霧乾燥し、約９６Ｋｇの粉末状の抗アレルギー性調
製乳を得た。この粉末抗アレルギー性調製乳の全蛋白質
等量に対する乳清蛋白質加水分解物の割合は６０％であ
り、カゼイン分解物の割合は４０％であった。また、常
法により測定した一般成分組成、及び前記の方法により
測定したアミノ酸組成の分析値は次のとおりであった。
一般成分組成
蛋白質（窒素量×６．３８） １４．５％脂
肪
２４．７％炭水化物
５５．３％灰分
２
．５％水分
３．０％ アミノ酸組成（粉末
１００ｇ中のｍｇ） Ｌ−アラニン
６１５ｍｇ Ｌ−ア
ルギニン
４４０ｍｇ
Ｌ−アスパラギン酸（Ｌ−アスパラギンを含む）
１４０５ｍｇ Ｌ−システイン
２９４ｍｇ Ｌ
−グルタミン酸（Ｌ−グルタミンを含む）
２８４０ｍｇ Ｌ−グリシン
２６８ｍｇ Ｌ−
ヒスチジン
３３３ｍｇ
Ｌ−イソロイシン
７７
２ｍｇ Ｌ−ロイシン
１６７７ｍｇ Ｌ−リジン
１３３９ｍｇ Ｌ−メ
チオニン
３００ｍｇ
Ｌ−フェニルアラニン
５７６ｍｇ
Ｌ−プロリン
９７７ｍｇ Ｌ−セリン
６６９ｍｇ Ｌ−スレ
オニン
６９６ｍｇ
Ｌ−トリプトファン
２６４ｍｇ
Ｌ−チロシン
４１４ｍｇ Ｌ−バリン
８５１ｍｇ実施例２
試験例１の試料８と同一の方法で純度９０％の乳清蛋白
質を加水分解して得た残存抗原活性１０−５の乳清蛋白
質分解物（蛋白質等量８５．１％）１１．４Ｋｇ、及び
試験例２の試料４と同一の方法で純度８５％のカゼイン
を加水分解して得た残存抗原活性１０−４のカゼイン分
解物（蛋白質等量８４．７％）１４．０Ｋｇを水１３０
０Ｋｇに溶解し、２５Ｋｇの水に溶解した所定量のミネ
ラル類を加え、６０℃に加熱し、植物性脂肪３７．５Ｋ
ｇ、マルツデキストリン１０５．０Ｋｇ、乳化剤、及び
所定量のビタミン類を混合し、この混合液を高圧ホモゲ
ナイザーで充分に乳化し、１５０℃で２．７秒間殺菌し
、２００ｍｌ容のアセプティク・パックに無菌的に充填
し、７３７０個の液状抗アレルギー性調製剤を得た。こ
の液状抗アレルギー性調製乳の全蛋白質等量に対する乳
清蛋白質加水分解物の割合は４５％であり、カゼイン加
水分解物の割合は５５％であった。また、常法により測
定した一般成分組成、及び前記の方法により測定したア
ミノ酸組成の分析値は次のとおりであった。
一般成分組成
蛋白質（窒素量×６．３８） １．４０％脂
肪
２．５９％炭水化物
６．９８％灰分
０．３
５％ アミノ酸組成（液体１００ｇ中のｍｇ）
Ｌ−アラニン
５
６．２ｍｇ Ｌ−アルギニン
４７．３ｍｇ Ｌ−アスパラギ
ン酸（Ｌ−アスパラギンを含む） １２５．
８ｍｇ Ｌ−システイン
２６．１ｍｇ Ｌ−グルタミン酸（
Ｌ−グルタミンを含む） ２９５．
４ｍｇ Ｌ−グリシン
２５．８ｍｇ Ｌ−ヒスチジン
３３．６ｍｇ Ｌ
−イソロイシン
７０．６ｍｇ
Ｌ−ロイシン
１
５６．４ｍｇ Ｌ−リジン
１２１．５ｍｇ Ｌ−メチオ
ニン
２８．２ｍｇ
Ｌ−フェニルアラニン
５７．０ｍｇ
Ｌ−プロリン
１０５．１ｍｇ Ｌ−セリン
６６．７ｍｇ Ｌ−ス
レオニン
６０．５ｍｇ
Ｌ−トリプトファン
２４．
９ｍｇ Ｌ−チロシン
３３．５ｍｇ Ｌ−バリン
８３．０ｍｇEXAMPLES Next, the present invention will be explained in more detail with reference to Examples, but the present invention is not limited to the following Examples. Example 1 Whey protein hydrolyzate with residual antigenic activity of 10-4 (protein equivalent 79.4%) obtained by hydrolyzing whey protein with a purity of 75% using the same method as Sample 3 of Test Example 1 10.6Kg,
Then, 12.1 kg of a casein decomposition product (protein equivalent: 87.4%) with residual antigenicity 10-4 obtained by hydrolyzing casein with a purity of 85% in the same manner as Sample 3 of Test Example 2 was added to 14 kg of water.
Add a predetermined amount of minerals dissolved in 5 kg of water, heat to 60°C, and make 25.0 kg of vegetable fat.
, maltdextrin 50.0Kg, sugar 5.0Kg,
and predetermined amounts of vitamins were mixed, and this mixed solution was thoroughly emulsified using a high-pressure homogenizer, sterilized at 120° C. for 2 seconds, and spray-dried to obtain about 96 kg of powdered anti-allergic formula milk. The ratio of whey protein hydrolyzate to the total protein equivalent of this powdered anti-allergic formula was 60%, and the ratio of casein decomposition product was 40%. In addition, the analytical values of the general component composition measured by a conventional method and the amino acid composition measured by the above-mentioned method were as follows. General composition Protein (nitrogen content x 6.38) 14.5% fat
24.7% carbohydrates
55.3% ash content
2
．． 5% moisture
3.0% Amino acid composition (mg in 100g powder) L-alanine
615mg L-Arginine
440mg
L-aspartic acid (contains L-asparagine)
1405mg L-cysteine
294mg L
-Glutamic acid (including L-glutamine)
2840mg L-glycine
268mg L-
histidine
333mg
L-isoleucine
77
2mg L-leucine
1677mg L-lysine
1339mg L-methionine
300mg
L-phenylalanine
576mg
L-proline
977mg L-serine
669mg L-threonine
696mg
L-tryptophan
264mg
L-tyrosine
414mg L-valine
851 mg Example 2 A whey protein decomposition product with a residual antigenic activity of 10-5 (protein equivalent: 85.1%) obtained by hydrolyzing whey protein with a purity of 90% using the same method as Sample 8 of Test Example 1. 11.4Kg, and 14.0Kg of a casein decomposition product (protein equivalent 84.7%) with residual antigenic activity of 10-4 obtained by hydrolyzing casein with a purity of 85% using the same method as Sample 4 of Test Example 2. water 130
Add a predetermined amount of minerals dissolved in 25Kg of water, heat to 60℃, and add 37.5K of vegetable fat.
Mix 105.0 kg of maltdextrin, an emulsifier, and a predetermined amount of vitamins, thoroughly emulsify this mixture using a high-pressure homogenizer, sterilize it at 150°C for 2.7 seconds, and aseptically pack it into a 200 ml aseptic pack. 7,370 liquid antiallergic preparations were obtained. The ratio of whey protein hydrolyzate to the total protein equivalent of this liquid anti-allergic formula was 45%, and the ratio of casein hydrolyzate was 55%. In addition, the analytical values of the general component composition measured by a conventional method and the amino acid composition measured by the above-mentioned method were as follows. General ingredient composition Protein (nitrogen amount x 6.38) 1.40% fat
2.59% carbohydrates
6.98% ash content
0.3
5% Amino acid composition (mg in 100g of liquid)
L-alanine
5
6.2mg L-arginine
47.3mg L-aspartic acid (contains L-asparagine) 125.
8mg L-cysteine
26.1mg L-glutamic acid (
(contains L-glutamine) 295.
4mg L-glycine
25.8mg L-histidine
33.6mg L
-isoleucine
70.6mg
L-leucine
1
56.4mg L-lysine
121.5mg L-methionine
28.2mg
L-phenylalanine
57.0mg
L-proline
105.1mg L-serine
66.7mg L-threonine
60.5mg
L-tryptophan
24.
9mg L-tyrosine
33.5mg L-valine
83.0mg
【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
。
（１）本発明の抗アレルギー性調製乳は、実質的にアレ
ルギー性がないので、食餌アレルギー疾患を有する乳幼
児の栄養補給に使用できる。
（２）本発明の抗アレルギー性調製乳は、実質的にアレ
ルギー性がないので、アレルギー素因を有する乳幼児の
食餌アレルギーの予防に使用できる。
（３）本発明の抗アレルギー性調製乳の摂取により、コ
レステロール値の上昇を防止することができる。
（４）本発明の抗アレルギー性調製乳の摂取により、ア
レルギー疾患を有する乳幼児における鉄の吸収率及び体
内保持率を正常に維持できる。[Effects of the Invention] The effects achieved by the present invention are as follows. (1) The anti-allergic formula of the present invention is substantially non-allergenic and can therefore be used for nutritional supplementation of infants with food allergy. (2) Since the anti-allergic formula of the present invention is substantially non-allergenic, it can be used to prevent food allergies in infants with allergic predispositions. (3) By ingesting the anti-allergic formula of the present invention, an increase in cholesterol levels can be prevented. (4) By ingesting the anti-allergic formula of the present invention, iron absorption and retention in the body can be maintained normally in infants with allergic diseases.
【表４】[Table 4]
Claims (2)
を窒素源とする抗アレルギー性調製乳、（ａ） 少な
くとも７０％（重量）の純度の乳清蛋白質を加水分解し
て得られ，抗乳清蛋白質血清を用いたエライザ（ＥＬＩ
ＳＡ：Ｅｎｚｙｍｅ ｌｉｎｋｅｄｉｍｍｕｎｏｓｏ
ｒｂｅｎｔ ａｓｓａｙ）抑制試験法により測定した
抗原残存活性が１０−４以下である乳清蛋白質加水分解
物、及び（ｂ） 少なくとも８０％（重量）の純度の
カゼインを加水分解物して得られ、抗カゼイン血清を用
いたエライザ抑制試験法により測定した残存抗原活性が
１０−４以下であるカゼイン加水分解物。Claim 1: An anti-allergic formula containing a mixture of (a) and (b) below as a nitrogen source, (a) obtained by hydrolyzing whey protein with a purity of at least 70% (by weight): , ELISA (ELI) using anti-whey protein serum
SA: Enzyme linkedimmunoso
(b) a whey protein hydrolyzate having an antigen residual activity of 10-4 or less as measured by an inhibition test method; and (b) a whey protein hydrolyzate obtained by hydrolyzing casein with a purity of at least 80% (weight); A casein hydrolyzate having a residual antigen activity of 10-4 or less as measured by the ELISA inhibition test method using casein serum.
を窒素源とし、それらの混合比率が４０〜８０％（重量
）：６０〜２０％（重量）である抗アレルギー性調製乳
、（ａ） 少なくとも７０％（重量）の純度の乳清蛋
白質を加水分解して得られ，抗乳清蛋白質血清を用いた
エライザ（ＥＬＩＳＡ：Ｅｎｚｙｍｅ ｌｉｎｋｅｄ
ｉｍｍｕｎｏｓｏｒｂｅｎｔ ａｓｓａｙ）抑制試験
法により測定した抗原残存活性が１０−４以下である乳
清蛋白質加水分解物、及び（ｂ） 少なくとも８０％
（重量）の純度のカゼインを加水分解物して得られ、抗
カゼイン血清を用いたエライザ抑制試験法により測定し
た抗原残存活性が１０−４以下であるカゼイン加水分解
物。2. Anti-allergic formula milk using a mixture of the following (a) and (b) as a nitrogen source and having a mixing ratio of 40 to 80% (by weight): 60 to 20% (by weight), (a) Enzyme linked ELISA (ELISA) obtained by hydrolyzing whey protein with a purity of at least 70% (by weight) using anti-whey protein serum.
(b) a whey protein hydrolyzate having an antigen residual activity of 10-4 or less as measured by an immunosorbent assay) inhibition test method; and (b) at least 80%
A casein hydrolyzate obtained by hydrolyzing casein with a purity of (weight) and having an antigen residual activity of 10-4 or less as measured by the ELISA inhibition test method using anti-casein serum.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP3039087A JP3061649B2 (en) | 1991-02-08 | 1991-02-08 | Antiallergic formula |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP3039087A JP3061649B2 (en) | 1991-02-08 | 1991-02-08 | Antiallergic formula |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH04365444A true JPH04365444A (en) | 1992-12-17 |
| JP3061649B2 JP3061649B2 (en) | 2000-07-10 |
Family
ID=12543305
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP3039087A Expired - Lifetime JP3061649B2 (en) | 1991-02-08 | 1991-02-08 | Antiallergic formula |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP3061649B2 (en) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0629350A1 (en) * | 1993-06-16 | 1994-12-21 | Sandoz Nutrition Ltd. | Milk protein hydrolysates |
| EP0979614A3 (en) * | 1998-08-11 | 2000-05-10 | Snow Brand Milk Products Co., Ltd. | Method of producing iron-whey-proteolysate complex |
| JP2010248136A (en) * | 2009-04-16 | 2010-11-04 | Snow Brand Milk Prod Co Ltd | Lipid metabolism-improving agent |
| JP2012231793A (en) * | 2006-08-30 | 2012-11-29 | Prolacta Bioscience Inc | Method of obtaining sterile milk and composition thereof |
| USRE48240E1 (en) | 2005-09-20 | 2020-10-06 | Prolacta Bioscience, Inc. | Methods for testing milk |
-
1991
- 1991-02-08 JP JP3039087A patent/JP3061649B2/en not_active Expired - Lifetime
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0629350A1 (en) * | 1993-06-16 | 1994-12-21 | Sandoz Nutrition Ltd. | Milk protein hydrolysates |
| EP0979614A3 (en) * | 1998-08-11 | 2000-05-10 | Snow Brand Milk Products Co., Ltd. | Method of producing iron-whey-proteolysate complex |
| US6139882A (en) * | 1998-08-11 | 2000-10-31 | Snow Brand Milk Products Co., Ltd. | Method of producing iron-whey-proteolysate complex |
| USRE48240E1 (en) | 2005-09-20 | 2020-10-06 | Prolacta Bioscience, Inc. | Methods for testing milk |
| JP2012231793A (en) * | 2006-08-30 | 2012-11-29 | Prolacta Bioscience Inc | Method of obtaining sterile milk and composition thereof |
| JP2010248136A (en) * | 2009-04-16 | 2010-11-04 | Snow Brand Milk Prod Co Ltd | Lipid metabolism-improving agent |
Also Published As
| Publication number | Publication date |
|---|---|
| JP3061649B2 (en) | 2000-07-10 |
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