JPS5814813B2 - Foaming agent and its manufacturing method - Google Patents

Foaming agent and its manufacturing method

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Publication number
JPS5814813B2
JPS5814813B2 JP51134435A JP13443576A JPS5814813B2 JP S5814813 B2 JPS5814813 B2 JP S5814813B2 JP 51134435 A JP51134435 A JP 51134435A JP 13443576 A JP13443576 A JP 13443576A JP S5814813 B2 JPS5814813 B2 JP S5814813B2
Authority
JP
Japan
Prior art keywords
molecular weight
foaming agent
peptide
foaming
foam stability
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
Application number
JP51134435A
Other languages
Japanese (ja)
Other versions
JPS5358982A (en
Inventor
光武広美
森憲一
前田聿紀
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Ajinomoto Co Inc
Original Assignee
Ajinomoto Co Inc
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Ajinomoto Co Inc filed Critical Ajinomoto Co Inc
Priority to JP51134435A priority Critical patent/JPS5814813B2/en
Publication of JPS5358982A publication Critical patent/JPS5358982A/en
Publication of JPS5814813B2 publication Critical patent/JPS5814813B2/en
Expired legal-status Critical Current

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  • Confectionery (AREA)
  • General Preparation And Processing Of Foods (AREA)
  • Emulsifying, Dispersing, Foam-Producing Or Wetting Agents (AREA)

Description

【発明の詳細な説明】 本発明は大豆たん白を用いて起泡性および気泡安定性に
すぐれ保存性もよく、また風味上もこのましい起泡剤及
びその製造法に関するものである。
DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a foaming agent that uses soybean protein and has excellent foaming properties and foam stability, good storage stability, and is also desirable in terms of flavor, and a method for producing the foaming agent.

更に詳しくは、従来品に比し気泡安定性が極めて優れた
起泡剤、及びその簡便な製法に関するものである。
More specifically, the present invention relates to a foaming agent with extremely superior foam stability compared to conventional products, and a simple method for producing the foaming agent.

従来より大豆たん白等の植物たん白を酵素で加水分解し
て起泡性物質を得る方法は知られておりたとえば米国特
許第2,4 8 9,1. 7 3、同3,814,8
16等がある。
Methods for obtaining foaming substances by hydrolyzing plant proteins such as soybean proteins with enzymes have been known, for example, as described in US Pat. No. 2,489,1. 7 3, 3,814,8
There is a 16th mag.

すなわち、脱指大豆をアルカリ抽出し次いで酸沈澱せし
め分離たん白を得、この酸沈澱カードを水に分散させ、
ペプシンで加水分解したのち濾過し、濾液を噴霧乾燥す
る等の方法である。
That is, the dedigitated soybeans are extracted with alkali, followed by acid precipitation to obtain separated proteins, and the acid-precipitated curd is dispersed in water.
This method includes hydrolysis with pepsin, filtration, and spray drying of the filtrate.

これらの方法にもとすいて得られる起泡性物質は気泡の
安定性、溶解性に問題があり、また呈味を有するという
欠点もあり、満足すべきものではない。
The foamable substances obtained by these methods also have problems with foam stability and solubility, and also have the disadvantage of having a taste, so they are not satisfactory.

またこれらの改良法もいくつか見られるが、かならずし
も充分とはいゝがたい。
Although some improvement methods are available, they are not always sufficient.

従来品はこれら欠点を有しつつもフラッペ、ヌガー、ス
ポンジケーキ、メレンゲ等の菓子製造用素材として広く
利用されてきたが、その改善が強く要望されて来た。
Although conventional products have these drawbacks, they have been widely used as materials for making confectionery such as frappes, nougat, sponge cakes, and meringues, but there has been a strong demand for improvements.

本発明者は大豆たん白の起泡性に関し研究を行ったとこ
ろ、たん白質の分解物の分子量が物性の発現に大きく影
響し、特に分子量で1,000〜6.000、好適には
1,500〜6,000の区分が起泡性および気泡安定
性が大きいという事実をゲルクロマトグラフイ等を用い
た研究により見い出し、本発明を完成するに至った。
The present inventor conducted research on the foaming properties of soybean protein and found that the molecular weight of the decomposed protein greatly influences the expression of physical properties, and in particular, the molecular weight is 1,000 to 6,000, preferably 1,000 to 6,000, preferably 1, Through research using gel chromatography, etc., the inventors discovered that the foaming property and foam stability are high in the 500 to 6,000 range, and have completed the present invention.

すなわち、本発明に係る起泡剤は実質的に分子量が1,
000乃至6,000、より好ましくは1,500乃至
6,000の大豆たん白加水分解ペプチドよりなるもの
であり、その製法としては種々の変法はあるが、大豆た
ん白又は同含有物をたん自分解酵素にて部分加水分解し
、実質的に上記範囲の分子量を有するペプチドを分取す
るのが効率的である。
That is, the foaming agent according to the present invention has a molecular weight of substantially 1,
000 to 6,000, more preferably 1,500 to 6,000, it is made of soy protein hydrolyzed peptide, and there are various methods for producing it. It is efficient to partially hydrolyze the peptide with an autolytic enzyme and separate the peptide having a molecular weight substantially within the above range.

原料大豆たん白としては待に制限はなく、脱脂大豆ある
いはそれから得られる濃縮たん白あるいは分離たん白等
の大豆たん白又は同含有物が用いられる。
The raw material soybean protein is not particularly limited, and soybean proteins such as defatted soybeans, concentrated proteins or isolated proteins obtained therefrom, or products containing the same can be used.

その形態はどのようなものであってもよく、例えば熱変
性、或いはアルコール変性したものでもよい。
It may be in any form, for example heat-denatured or alcohol-denatured.

しかし、大豆たん白以外では本法を適用して起泡性たん
白を得るには適当ではない。
However, this method is not suitable for obtaining foamable proteins other than soybean protein.

一方、酵素はヘフシン、パパイン、モルシン等如何なる
ものでもよく、動物、植物あるいは微生物起源のたん白
分解酵素が用いられる。
On the other hand, the enzyme may be any enzyme such as hefsin, papain, morsin, etc., and proteolytic enzymes of animal, plant or microbial origin are used.

本発明方法の第1段は、上記大豆たん白又は同含有物を
水性溶媒中にてたん白分解酵素にて部分加水分解するに
ある。
The first step of the method of the present invention is to partially hydrolyze the soybean protein or its containing material in an aqueous solvent using a proteolytic enzyme.

加水分解は、APL(平均ペプチド鎖長)4〜25程度
になるように行なわれる。
Hydrolysis is carried out so that the APL (average peptide chain length) is approximately 4 to 25.

加水分解条件は特に従来と変るところはなく、pHに関
しては使用酵素の至適領域であり、最も効率的に酵素が
作用する領域を原料の腐敗を考慮しつつ決定すればよく
、通常5°乃至60℃、好ましくは20°〜50℃が選
択される。
The hydrolysis conditions are not particularly different from conventional ones, and the pH is in the optimum range for the enzyme used, and the range where the enzyme acts most efficiently can be determined while taking into account the spoilage of the raw material, and it is usually between 5° and 60°C, preferably 20° to 50°C is selected.

加水分解時間は使用酵素活性及びその使用量により変化
するが、24時間以内となるよう設定するのが収率並び
に製品品質上好ましい。
Although the hydrolysis time varies depending on the enzyme activity and amount used, it is preferable to set it within 24 hours in terms of yield and product quality.

この加水分解反応中に、pEが至適域より大巾に変化す
る場合にはpHの調整を反応中に行うのが有効である。
If the pE changes more widely than the optimum range during this hydrolysis reaction, it is effective to adjust the pH during the reaction.

次いで、一般の酵素反応と同じく酵素活性を失活せしめ
反応を停止するのであるが、これには加熱失活が有効で
ある。
Next, the reaction is stopped by inactivating the enzyme activity as in general enzymatic reactions, and heat inactivation is effective for this purpose.

通常、70゜C以上に5分乃至30分加熱することによ
り失活は完了する。
Usually, deactivation is completed by heating to 70°C or higher for 5 to 30 minutes.

斯くして得られた反応液より目的とする分子量を有する
ペプチドを分取するのが本方法の第二段階である。
The second step of this method is to separate a peptide having the desired molecular weight from the reaction solution thus obtained.

原料大豆たん白に由来する高分子性不純物、例えば繊維
性物質(所謂オカラ)が存在する場合には、反応液より
まずそれら物質を除去するのが次後の処理効率等に於い
て望ましく、反応液のpHを7〜8に調整し不溶物を除
去するのが有利である。
If there are polymeric impurities derived from raw soy protein, such as fibrous substances (so-called okara), it is desirable to remove these substances from the reaction solution first in order to improve the efficiency of the subsequent reaction. It is advantageous to adjust the pH of the solution to 7-8 and remove insoluble matter.

次いで、たん白質及びペプチド等の低分子量部分及び高
分子量部分を除去するのであるが、高分子1分について
は酵素反応液のpHを4〜5に調整し、濾過、遠心、デ
カンテーション等により不溶物を除去することによりほ
ゞ達成することができる。
Next, low-molecular weight parts and high-molecular weight parts such as proteins and peptides are removed.For polymers, the pH of the enzyme reaction solution is adjusted to 4 to 5, and insoluble parts are removed by filtration, centrifugation, decantation, etc. This can be achieved mostly by removing things.

この操作にて不十分な場合には、限外濾過等によりより
精度を良くすることができる。
If this operation is insufficient, the accuracy can be improved by ultrafiltration or the like.

一方、低分子量部分の除去については、限外濾過あるい
はその他の適当な手段にて行うことができるが、限外濾
過が最も効率的である。
On the other hand, the removal of low molecular weight portions can be carried out by ultrafiltration or other suitable means, but ultrafiltration is the most efficient.

本限外濾過に使用する濾過膜としては分画分子量1,0
00〜10,000のもの、特に1,000〜5,00
0のものが好適であって、例えば米アミコン社製アミコ
ンUM2、ダイヤフローメンブレンDM5等市販の濾過
膜にて充分である。
The filtration membrane used for this ultrafiltration has a molecular weight cutoff of 1.0.
00 to 10,000, especially 1,000 to 5,000
For example, commercially available filtration membranes such as Amicon UM2 and Diaflow Membrane DM5 manufactured by Amicon Corporation of America are sufficient.

pH1圧力、温度等の膜処理条件は使用膜及びたん白溶
液の性質に応じその最適値は異るが、通常pHとしては
3〜8、圧力としては0.5kg/ffl〜7kg/C
r?L,瀧度としては0′C〜50゜Cの範囲内である
The optimal values for membrane treatment conditions such as pH 1 pressure and temperature vary depending on the properties of the membrane and protein solution used, but usually the pH is 3 to 8 and the pressure is 0.5 kg/ffl to 7 kg/C.
r? L and waterfall are within the range of 0'C to 50°C.

本処理中にペプチド等の腐敗が問題となる場合があるが
、この時には使用する膜の能力範囲内にてアルコールを
添加して処理してもよく、又予めソルビン酸等の防腐剤
を添加して処理に付するのも有効である。
Decomposition of peptides, etc. may become a problem during this treatment, but in this case, alcohol may be added within the capacity of the membrane used, or a preservative such as sorbic acid may be added in advance. It is also effective to subject it to treatment.

斯くして得られた実質的に分子量が1,000乃至6,
000、より好ましくは1,500乃至6,000より
なるペプチド含有液は水酸化ナ1〜リウム等のアルカリ
又は酸を添加しpH沓中性付近、より具体的には6〜7
に調整した後、濃縮物として、または凍結乾燥等により
乾燥し製品とすることができる。
The substantially molecular weight obtained in this way is 1,000 to 6,
000, more preferably 1,500 to 6,000, a peptide-containing solution is prepared by adding an alkali or acid such as sodium hydroxide to pH around neutrality, more specifically 6 to 7.
After adjusting the composition, it can be made into a product as a concentrate or dried by freeze-drying or the like.

本品は起泡性及び気泡安定性、特に後者の安定性が優れ
ており、その呈味もほとんどなく、所謂大豆臭やにが味
を感じさせない優れたものである。
This product has excellent foaming properties and foam stability, especially the latter stability, and has almost no taste, with no so-called soybean odor or bitter taste.

更に、乾燥品は吸湿性も少なく保存性にも優れたもので
ある。
Furthermore, the dried product has low hygroscopicity and has excellent storage stability.

ここで、参考のために分子量区分と起泡性及び気泡安定
性の関係をゲル濾過を用いて検討した結果を図1に示す
For reference, FIG. 1 shows the results of examining the relationship between molecular weight categories, foaming properties, and foam stability using gel filtration.

尚、起泡性及び気泡安定性の測定方法は後述する方法に
て行ったものであり、ゲル濾過はファルマシア社製Se
phadex G−50を使用した。
The foaming properties and foam stability were measured using the methods described below, and gel filtration was performed using Pharmacia Se.
Phadex G-50 was used.

図1より明らかな通り、起泡性、気泡安定性に関しては
分子量が1,000乃至6,000のペプチドが、特に
1,500乃至6,000のペプチドが好適であること
が明らかである。
As is clear from FIG. 1, it is clear that peptides with a molecular weight of 1,000 to 6,000, particularly 1,500 to 6,000, are suitable for foaming properties and foam stability.

特に気泡安定性は低分子物質の存在により大きく影響を
受けることが明白である。
In particular, it is clear that bubble stability is greatly affected by the presence of low molecular weight substances.

従って、本発明に係る起泡剤は実質的に分子量1,00
0〜6,000,好ましくは1.5000〜6,000
のペプチドよりなるものであるが、特に低分子量物質の
存在は可及的に少ないことが望ましく、分子量が1,0
00以下、より好ましくは1,500以下の物質は全重
量の5%以下、より好ましくは3%以下であることが肝
要である。
Therefore, the foaming agent according to the present invention has a molecular weight of substantially 1,000.
0 to 6,000, preferably 1.5000 to 6,000
However, it is particularly desirable that the presence of low molecular weight substances be as small as possible;
It is important that the substance having a molecular weight of 0.00 or less, more preferably 1,500 or less, accounts for 5% or less, more preferably 3% or less of the total weight.

一方、高分子量物質の存在は低分子量のものに比しその
影響はより少ないが、高品質の起泡剤としてはやはり可
及的に少ないことが望ましく、その上限は全重量の20
%以下である。
On the other hand, the presence of high molecular weight substances has less influence than low molecular weight substances, but as a high quality foaming agent it is still desirable to have as little as possible, and the upper limit is 20% of the total weight.
% or less.

以上の説明にて明らかな通り、本発明に係る起泡剤は起
泡剤に要求される種々の特性を高度に備えており、又そ
の製法も容易である。
As is clear from the above explanation, the foaming agent according to the present invention has various properties required for a foaming agent to a high degree, and its manufacturing method is also easy.

従って、本発明は起泡剤使用分野に大いに貢献するもの
である。
Therefore, the present invention makes a significant contribution to the field of foaming agent use.

以下に実施例をあげ本発明をより詳細に説明する。The present invention will be explained in more detail with reference to Examples below.

尚、実施例における起泡性および気泡安定性の測定法は
次の通りである。
The methods for measuring foamability and foam stability in Examples are as follows.

起泡性:a度1%の試料溶液100mlを起泡性測定用
シリンター(内径82mm,容 量1,000mA)にとり定速攪拌器(東京理化社製C
hemystirrer,B−100回転数2.80O
rpm)を用い て泡だたせ10分後に回転をとめ5分 後に泡の体積Aを測定する。
Foaming property: 100 ml of a sample solution with a degree of 1% was placed in a syringe for measuring foaming property (inner diameter 82 mm, capacity 1,000 mA), and a constant speed stirrer (C manufactured by Tokyo Rika Co., Ltd.) was used.
hemystirrer, B-100 rotation speed 2.80O
After 10 minutes, the rotation is stopped and the volume A of the foam is measured after 5 minutes.

この体積Aとはじめの溶液の液量(100ml) との比を起泡性とする。This volume A and the volume of the initial solution (100ml) The foaming property is defined as the ratio of

気泡安定性:上の方法で起泡性を測定したのちそのまま
2時間放置し、ふたゝび泡の体 積Bを測定する。
Foam stability: After measuring the foamability using the above method, the product is left to stand for 2 hours, and the volume B of the foam is measured again.

この体積Bと起泡性測定時の泡の体積Aから求めた泡の
減 少率(A−B/A×100)をもって気泡安定性とする
The foam stability is defined as the foam reduction rate (A-B/A×100) determined from this volume B and the foam volume A at the time of foamability measurement.

実施例 1 醸造用脱脂大豆(窒素含有率7.9%)100gを10
倍量の水に分散させ塩酸でpH1.5に調整した。
Example 1 100g of defatted soybeans for brewing (nitrogen content 7.9%)
It was dispersed in twice the amount of water and adjusted to pH 1.5 with hydrochloric acid.

これにペプシン(1:10,000)を脱脂大豆に対し
て1%(w/w)添加し40゜Cにて4時間加水分解し
たのち70゜C30分加熱して酵素を失活させた。
To this was added pepsin (1:10,000) at 1% (w/w) based on defatted soybean, hydrolyzed at 40°C for 4 hours, and then heated at 70°C for 30 minutes to inactivate the enzyme.

その後水酸化ナトリウムで溶液のpHを7.0に調整し
遠心分離により不溶物を除去し、上清は塩酸でpH4.
5にし生ずるたん白性沈澱を遠心分離によりのぞき清澄
液を得た。
Thereafter, the pH of the solution was adjusted to 7.0 with sodium hydroxide, insoluble matter was removed by centrifugation, and the supernatant was adjusted to pH 4.0 with hydrochloric acid.
The proteinaceous precipitate formed in step 5 was removed by centrifugation to obtain a clear solution.

この溶液を米国、アミコン社製アミコンUM10(分画
分子量10,000の限外濾過膜)を用いて限外濾過を
行ない濾過残液を凍結乾燥し製品27gを得た。
This solution was subjected to ultrafiltration using Amicon UM10 (ultrafiltration membrane with a molecular weight cutoff of 10,000) manufactured by Amicon, USA, and the filtration residue was freeze-dried to obtain 27 g of a product.

本品のうち分子量1,000以下の化合物は3%,1,
500以下のものは4%であり、6,000以上のもの
は約10%であった。
Compounds with a molecular weight of 1,000 or less in this product are 3%, 1,
4% had scores below 500, and about 10% had scores above 6,000.

このものの起泡性および気泡安定性は個々4.7及び7
2%で両特性はきわめて優れており、またほとんど無味
無臭であり呈味性の面からも好ましいものであった。
The foamability and foam stability of this product were 4.7 and 7, respectively.
At 2%, both properties were excellent, and it was almost tasteless and odorless, which was preferable from the standpoint of taste.

一方、上記方法に於いて得られた清澄液を限外濾過する
ことなく、そのまゝ凍結乾燥したところ、起泡性および
気泡安定性は個々4.6、及び45%と特にその安定性
が悪く、シかも極めてにが味を呈するものであった。
On the other hand, when the clear liquid obtained in the above method was directly freeze-dried without ultrafiltration, the foamability and foam stability were 4.6% and 45%, respectively. It was bad, and had a very bitter taste.

実施例 2 脱脂大豆より得た分離大豆蛋白(窒素含有率13.8%
)100gを20倍量の水に分散させ、水酸化ナl−I
JウムでpH7.0に調整した。
Example 2 Isolated soybean protein obtained from defatted soybeans (nitrogen content 13.8%)
) 100g was dispersed in 20 times the amount of water, and sodium hydroxide l-I
The pH was adjusted to 7.0 with Jum.

これにシステイン1gとパパイン1gを添加し、37°
Cにて8時間加水分解した。
Add 1 g of cysteine and 1 g of papain to this, and
Hydrolysis was carried out at C for 8 hours.

尚、この間2時間ごとに水酸化ナトリウムでpH調整を
行なった。
During this time, the pH was adjusted every 2 hours with sodium hydroxide.

加水分解後70℃30分加熱により酵素を失活させ、塩
酸でpH4.5に調整したのち遠心分離し、不溶物を除
去し得られた上清液を米国アミコン社製アミコンUM2
(分画分子量1,000の限外濾過膜)を用いて限外濾
過を行ない、残留液を凍結乾燥し製品54gを得た。
After hydrolysis, the enzyme was inactivated by heating at 70°C for 30 minutes, and the pH was adjusted to 4.5 with hydrochloric acid, followed by centrifugation, and insoluble materials were removed.
(An ultrafiltration membrane with a molecular weight cutoff of 1,000) was used to perform ultrafiltration, and the residual liquid was freeze-dried to obtain 54 g of a product.

本品のうち分子量1,000以下の化合物は2%,1,
500以下のものは8%であり、6,000以上のもの
は15%であった。
Compounds with a molecular weight of 1,000 or less in this product are 2%, 1,
8% had scores below 500, and 15% had scores above 6,000.

このものは起泡性および気泡安定性は個々4.8及び7
1%で両特性ともきわめて優れており、またほとんど無
味無臭であり呈味性の面からも好ましいものであった。
This product has foaming properties and foam stability of 4.8 and 7, respectively.
At 1%, both properties were excellent, and it was almost tasteless and odorless, which was preferable from the standpoint of taste.

【図面の簡単な説明】[Brief explanation of drawings]

図1は大豆たん自分解ペプチドの分子量と起泡性(実線
)及び気泡安定性(破線)を示す図である。
FIG. 1 is a diagram showing the molecular weight, foaming property (solid line), and foam stability (broken line) of soybean protein autolytic peptide.

Claims (1)

【特許請求の範囲】 1 実質的に分子量1,000万至6,000の大豆た
ん白加水分解ペプチドよりなる起泡剤。 2 ペプチドの分子量が実質的に1,500乃至6,0
00である特許請求の範囲第1項記載の起泡剤。 3 大豆たん白又は同含有物をたん白分解酵素にて部分
加水分解し、次いで実質的に分子量1,000.乃至6
,000よりなるペプチドを分取することを特徴とする
起泡剤の製造法。 4 ペプチドの分子量が実質的に1,500乃至6,0
00である特許請求の範囲第3項記載の製造法。
[Scope of Claims] 1. A foaming agent consisting essentially of a soybean protein hydrolyzed peptide having a molecular weight of 10 million to 6,000. 2 The molecular weight of the peptide is substantially 1,500 to 6,0
The foaming agent according to claim 1, which is 00. 3. Partially hydrolyze soybean protein or its contents with a proteolytic enzyme, and then reduce the molecular weight to substantially 1,000. to 6
A method for producing a foaming agent, which comprises separating a peptide consisting of ,000. 4 The molecular weight of the peptide is substantially 1,500 to 6,0
00. The manufacturing method according to claim 3.
JP51134435A 1976-11-09 1976-11-09 Foaming agent and its manufacturing method Expired JPS5814813B2 (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP51134435A JPS5814813B2 (en) 1976-11-09 1976-11-09 Foaming agent and its manufacturing method

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP51134435A JPS5814813B2 (en) 1976-11-09 1976-11-09 Foaming agent and its manufacturing method

Publications (2)

Publication Number Publication Date
JPS5358982A JPS5358982A (en) 1978-05-27
JPS5814813B2 true JPS5814813B2 (en) 1983-03-22

Family

ID=15128294

Family Applications (1)

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JP51134435A Expired JPS5814813B2 (en) 1976-11-09 1976-11-09 Foaming agent and its manufacturing method

Country Status (1)

Country Link
JP (1) JPS5814813B2 (en)

Families Citing this family (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
CH636248A5 (en) * 1979-03-09 1983-05-31 Nestle Sa PROCESS FOR THE PREPARATION OF A PURIFIED PROTEIN HYDROLYSATE.
JPH06101997B2 (en) * 1988-06-02 1994-12-14 不二製油株式会社 Manufacturing method of aerated fish paste products
JPH02286059A (en) * 1989-04-26 1990-11-26 Fuji Oil Co Ltd Preparation of processed meat food containing air
AU2017328480A1 (en) * 2016-09-14 2019-03-14 Ethicon, Inc. Stable pharmaceutical foam
JP7442777B2 (en) * 2019-02-20 2024-03-05 池田食研株式会社 protein hydrolyzate

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS5168486A (en) * 1974-12-10 1976-06-14 Kanegafuchi Chemical Ind

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS5168486A (en) * 1974-12-10 1976-06-14 Kanegafuchi Chemical Ind

Also Published As

Publication number Publication date
JPS5358982A (en) 1978-05-27

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