JP3274646B2 - Emulsifiable composition - Google Patents
Emulsifiable compositionInfo
- Publication number
- JP3274646B2 JP3274646B2 JP07306998A JP7306998A JP3274646B2 JP 3274646 B2 JP3274646 B2 JP 3274646B2 JP 07306998 A JP07306998 A JP 07306998A JP 7306998 A JP7306998 A JP 7306998A JP 3274646 B2 JP3274646 B2 JP 3274646B2
- Authority
- JP
- Japan
- Prior art keywords
- protein
- fraction
- insoluble fraction
- emulsifiable composition
- soluble
- 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 - Fee Related
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Landscapes
- Emulsifying, Dispersing, Foam-Producing Or Wetting Agents (AREA)
- Dairy Products (AREA)
- Grain Derivatives (AREA)
- General Preparation And Processing Of Foods (AREA)
Description
【０００１】[0001]
【発明の属する技術分野】本発明は、乳化性組成物に関
するものであり、更に詳細には、タンパク質をプロテア
ーゼによって酵素分解する際に発生する不溶性画分を有
効成分とする乳化性組成物に関するものである。The present invention relates to an emulsifying composition, and more particularly to an emulsifying composition containing, as an active ingredient, an insoluble fraction generated when a protein is enzymatically decomposed by a protease. It is.
【０００２】[0002]
【従来の技術】従来より、乳タンパク質その他のタンパ
ク質をプロテアーゼを用いて分解する際、不溶性画分が
生じることが知られている。従来この不溶性画分はケイ
ソウ土ろ過、膜分離等により、除去された後廃棄され、
可溶性画分のみを酵素分解物として利用することが一般
的である。しかし、この不溶性画分は、酵素分解の条件
によってはスタート時の乳タンパク質の約４０％に達す
ることがある。この為、実際の製造工程上、収率の悪化
によるコスト高、また環境汚染という問題点を抱えてい
る。2. Description of the Related Art It has been known that when a milk protein and other proteins are decomposed with a protease, an insoluble fraction is produced. Conventionally, this insoluble fraction is discarded after being removed by diatomaceous earth filtration, membrane separation, etc.
It is common to utilize only the soluble fraction as an enzymatic degradation product. However, this insoluble fraction can reach about 40% of the starting milk protein, depending on the conditions of the enzymatic degradation. For this reason, there is a problem in the actual manufacturing process that the cost is high due to the deterioration of the yield and that the environment is polluted.
【０００３】従来、この不溶性画分は、上記したよう
に、ケイソウ土ろ過、膜分離等によって除去した後に廃
棄され、可溶性画分のみを酵素分解物として利用するこ
とが一般的である。しかし、この沈殿物の発生は、上清
画分の回収率の低下がもたらす経済性の面のみならず、
分画に要する手間のほか、更に、産業廃棄物として環境
汚染にもつながる。Conventionally, as described above, the insoluble fraction is generally discarded after being removed by diatomaceous earth filtration, membrane separation, etc., and only the soluble fraction is used as an enzymatic degradation product. However, the generation of this precipitate is not only economical that the recovery rate of the supernatant fraction is reduced, but also
In addition to the labor required for fractionation, it also leads to environmental pollution as industrial waste.
【０００４】一方、従来から食品の乳化剤として、両親
媒性のシュガーエステルやリン脂質、あるいは一部のタ
ンパク質が用いられてきた。しかし、乳化剤の使用は、
コスト面や表示義務という問題があり、その利用には制
限がある。また、タンパク質の酵素分解物、いわゆるペ
プチド画分は、乳化性が著しく低いことから、このペプ
チド画分を用いた食品の乳化方法には問題が発生してい
る。On the other hand, amphiphilic sugar esters, phospholipids, or some proteins have been used as emulsifiers for foods. However, the use of emulsifiers
There are problems in terms of cost and display obligations, and their use is limited. In addition, enzymatic degradation products of proteins, so-called peptide fractions, have a remarkably low emulsifying property, and thus a problem has arisen in a method of emulsifying food using this peptide fraction.
【０００５】[0005]
【発明が解決しようとする課題】不溶性画分は、基質溶
解濃度と酵素分解条件によっては、出発物質であるタン
パク質の４０％に達する場合がある。低い溶解濃度での
酵素処理は、最終的に粉末乾燥する際に、水分を蒸発さ
せるためのエネルギー消費のコストが大きい。そのた
め、基質溶解濃度、酵素処理条件、不溶性画分発生量と
酵素分解後の処理コストを考慮に入れ、ペプチドの製造
を行う必要がある。従って、現状では、ペプチドの製造
時には、５〜３０％程度の不溶性画分が発生し、そのほ
とんどが利用されずに廃棄されている。そのため、廃棄
に要するコストはもちろん廃棄による環境汚染という重
大な問題が生じ、不溶性画分を回収してそれを有効利用
する新しいシステムの開発が当業界において強く希求さ
れている。The insoluble fraction may reach up to 40% of the starting protein, depending on the concentration of dissolved substrate and the conditions for enzymatic degradation. Enzymatic treatment at low dissolution concentrations is costly in terms of energy consumption to evaporate water during final powder drying. Therefore, it is necessary to produce the peptide in consideration of the substrate dissolution concentration, the enzyme treatment conditions, the amount of insoluble fraction generated, and the treatment cost after enzymatic decomposition. Therefore, at present, during the production of the peptide, an insoluble fraction of about 5 to 30% is generated, and most of the insoluble fraction is discarded without being used. Therefore, there is a serious problem of not only the cost required for disposal but also environmental pollution due to disposal, and there is a strong demand in the art to develop a new system that collects the insoluble fraction and uses it effectively.
【０００６】[0006]
【課題を解決するための手段】上記した技術の現状に鑑
み、本発明者らは、各方面から検討した結果、この不溶
性画分が疎水的性質を有することから、食用油脂との間
に乳化物を形成する性質を見いだした。つまり、通常、
酵素分解物の上清画分は元のタンパク質に比べ油脂との
乳化性が極めて劣っており、更に苦味が強い傾向をも
つ。これに対し、不溶性画分は苦味が少なく、強い乳化
性を示したことから様々な食品、又は飼料等の乳化剤と
して利用できることが分かった。In view of the above-mentioned state of the art, the present inventors have conducted various studies and found that the insoluble fraction has hydrophobic properties, so that the insoluble fraction is emulsified with edible oils and fats. I found the property of forming things. That is, usually
The supernatant fraction of the enzymatic degradation product has an extremely poor emulsifiability with fats and oils compared to the original protein, and tends to have a stronger bitter taste. On the other hand, the insoluble fraction had little bitterness and showed strong emulsifying properties, indicating that it can be used as an emulsifier for various foods or feeds.
【０００７】本発明は、上記した有用新知見に基づき、
更に研究した結果遂に完成されたものであって、タンパ
ク質を酵素分解した結果生成する不溶性画分を有効成分
とする乳化性組成物に関するものであって、本発明によ
れば、タンパク質の酵素分解液から不溶性画分を回収、
殺菌後、噴霧乾燥機あるいは凍結乾燥機によって水分を
除去し、粉末とする。この粉末を乳化性が求められる食
品のタンパク源として使用し、油との混合系で均質化処
理を行うことで、非常に安定した乳化物を形成すること
が可能である。以下、本発明について詳述する。The present invention is based on the above-mentioned useful new findings,
The present invention was finally completed as a result of further research, and relates to an emulsifying composition containing an insoluble fraction produced as a result of enzymatic degradation of a protein as an active ingredient. From the insoluble fraction,
After sterilization, water is removed by a spray drier or a freeze drier to obtain a powder. An extremely stable emulsion can be formed by using this powder as a protein source for foods requiring emulsifying properties and performing homogenization treatment in a mixed system with oil. Hereinafter, the present invention will be described in detail.
【０００８】本発明を実施するには、タンパク質あるい
はタンパク質含有物を原料とし、これをタンパク質分解
酵素で酵素分解し、可溶性画分には有効な用途が確立さ
れている可溶性ペプチドが含まれているので、これを濾
過、遠心分離、膜分離等によって分離して有効利用する
が、可溶性画分を除去した残りの画分である難溶性画分
及び／又は不溶性画分（以下、単に不溶性画分というこ
ともある）を、本発明に係る乳化性組成物の有効成分と
して利用するのである。In carrying out the present invention, a protein or a protein-containing substance is used as a raw material, which is enzymatically decomposed with a proteolytic enzyme, and the soluble fraction contains a soluble peptide for which an effective use has been established. Therefore, this is separated and effectively used by filtration, centrifugation, membrane separation or the like, but the remaining fraction from which the soluble fraction has been removed is a poorly soluble fraction and / or an insoluble fraction (hereinafter, simply referred to as an insoluble fraction). Is used as an active ingredient of the emulsifiable composition according to the present invention.
【０００９】本発明の原料としては、タンパク質及び／
又はタンパク質を含有する物質（タンパク質含有物）
（以下、これ（ら）を単にタンパク質ということもあ
る）を使用するが、タンパク質としては、乳、卵、肉
類、魚介類等の動物性タンパク質のほか、大豆、小麦等
の植物性タンパク質や微生物、各種細胞由来のタンパク
質が広く使用できる。例えば、乳由来のタンパク質とし
ては、カゼイン、ホエイ、ホエイタンパク質のほか、ナ
トリウムカゼイネート、ホエイタンパク質濃縮物（ＷＰ
Ｃ）、ホエイタンパク質分離物（ＷＰＩ）といった各種
処理物等、乳やホエイを原料とするタンパク質及び／又
はその処理物が広く包含される。The raw materials of the present invention include proteins and / or
Or substances containing proteins (protein-containing substances)
(Hereinafter, these are sometimes referred to simply as proteins.) Examples of proteins include animal proteins such as milk, eggs, meat and seafood, vegetable proteins such as soybeans and wheat, and microorganisms. In addition, proteins derived from various cells can be widely used. For example, milk-derived proteins include casein, whey, whey protein, sodium caseinate, whey protein concentrate (WP
C) and various processed products such as whey protein isolate (WPI), and proteins and / or processed products thereof derived from milk or whey are widely included.
【００１０】タンパク質分解酵素としては、ペプシン、
（キモ）トリプシン、カテプシン等の動物起源の酵素、
パパイン、ブロメリン、フィシン等の植物起源の酵素、
各種微生物由来のプロテアーゼ等既知の酵素が１種又は
２種以上使用される。また、市販されている各種プロテ
アーゼ製剤も有利に使用できる。As proteolytic enzymes, pepsin,
(Kimo) trypsin, cathepsin and other enzymes of animal origin,
Enzymes of plant origin, such as papain, bromelin, and ficin,
One or more known enzymes such as proteases derived from various microorganisms are used. Various commercially available protease preparations can also be used advantageously.
【００１１】本発明に係る組成物は、タンパク質を上記
した酵素を用いて常法にしたがって処理し、得られた酵
素分解液から可溶性画分を分離、除去した後の不溶性画
分を有効成分とするものである。不溶性画分は、そのま
ま用いてもよいし、必要あれば、濃縮物、ペースト化
物、乾燥物、希釈物等処理物として用いてもよい。乾燥
する場合、噴霧乾燥、凍結乾燥、減圧乾燥その他既知の
乾燥方法が適宜利用可能である。The composition according to the present invention is obtained by treating a protein with the above-mentioned enzyme according to a conventional method, separating and removing a soluble fraction from the obtained enzyme-decomposed solution, and treating an insoluble fraction as an active ingredient. Is what you do. The insoluble fraction may be used as it is, or, if necessary, may be used as a processed product such as a concentrate, a pasted product, a dried product, or a diluted product. In the case of drying, spray drying, freeze drying, drying under reduced pressure and other known drying methods can be appropriately used.
【００１２】本発明にしたがって乳化物を形成するに
は、この不溶性画分を乳化性が求められている対象物の
タンパク源として使用し、油との混合系で均質化処理す
ればよく、その結果、非常に安定した乳化物を形成する
ことができる。その際、グルコース、フラクトース、ガ
ラクトース、シュークロース、マルトース、ラクトース
等各種の糖を共存させると、更に良い結果が得られる。In order to form an emulsion according to the present invention, this insoluble fraction may be used as a protein source of the object for which emulsification is required, and homogenized in a mixed system with oil. As a result, a very stable emulsion can be formed. At this time, better results can be obtained by coexisting various sugars such as glucose, fructose, galactose, sucrose, maltose, and lactose.
【００１３】本発明に係る乳化性組成物は、乳化性にす
ぐれているだけでなく、安全性がきわめて高いので、食
品、飲料、飼料、魚介用餌料、化粧品、医薬品その他乳
化性を必要とする各種対象物の乳化剤として単独である
いは他の乳化剤とともに安心して使用することができ
る。The emulsifiable composition according to the present invention is not only excellent in emulsifiability, but also extremely safe, and thus requires emulsifiability in foods, beverages, feeds, foods for fish and shellfish, cosmetics, pharmaceuticals, and others. It can be safely used alone or with other emulsifiers as an emulsifier for various objects.
【００１４】本発明に係る乳化性組成物は、例えば調製
粉乳の乳化剤として好適であるし、また、ホイップ用ク
リームの配合において常用される脱脂粉乳の代りに使用
するのにもきわめて好適である。The emulsifiable composition according to the present invention is suitable, for example, as an emulsifier for milk powder, and is also very suitable for use in place of skim milk powder commonly used in formulating whipped creams.
【００１５】以下、本発明の実施例について述べるが、
実施例において、乳化性評価方法は次のとおりとした。Hereinafter, embodiments of the present invention will be described.
In the examples, the emulsifying property evaluation method was as follows.
【００１６】（乳化性評価方法について）乳化性の評価
は、各試料を水に分散後、油脂と乳化物を調製し、メス
シリンダーに移した後、一定の温度、時間で放置後、乳
化物の離水の状態（乳化安定性％＝乳化液分量／サンプ
ルの全容量×１００）によって評価した。(Emulsifying property evaluation method) Emulsifying properties were evaluated by dispersing each sample in water, preparing fats and oils and an emulsified product, transferring it to a measuring cylinder, leaving it to stand at a constant temperature and time, Of water (emulsion stability% = emulsion liquid content / total volume of sample × 100).
【００１７】また、各実施例において、各記号はそれぞ
れ次のことを表し、数値が高いほど乳化安定性が大きい
ことを示す。 ＷＰＣ−ＰＰＴ＝ＷＰＣを基質とした酵素分解物の不溶
性画分 ＣＮ−ＰＰＴ＝ＣＮを基質とした酵素分解物の不溶性画
分 ＷＰＣ−ＳＵＰ＝ＷＰＣを基質とした酵素分解物の可溶
性画分 ＣＮ−ＳＵＰ＝ＣＮを基質とした酵素分解物の可溶性画
分In each example, each symbol represents the following, and the higher the numerical value, the higher the emulsion stability. WPC-PPT = insoluble fraction of enzymatic degradation product using WPC as a substrate CN-PPT = insoluble fraction of enzymatic degradation product using CN as a substrate WPC-SUP = soluble fraction of enzymatic degradation product using WPC as a substrate CN- SUP = soluble fraction of enzymatic degradation product using CN as a substrate
【００１８】[0018]
【実施例１】市販のホエータンパク質濃縮物（ＷＰＣ）
２０ｋｇを水１８０ｋｇに溶解し、ｐＨを７．８に調製
し、９０℃、１５分間加熱変性させた。５０℃に冷却
後、市販酵素剤（プロテアーゼＮ「アマノ」、天野製薬
（株）製）を基質／酵素（Ｅ／Ｓ）＝１／１００となる
ように添加し、５時間保持後、９０℃、１５分間の条件
で加熱失活した。３０℃に冷却後、限外ろ過（分画範囲
０．４５μｍ）により透過画分を回収後、非透過画分を
回収、凍結乾燥し、粉末６ｋｇを得た。Example 1 Commercially available whey protein concentrate (WPC)
20 kg was dissolved in 180 kg of water to adjust the pH to 7.8 and denatured by heating at 90 ° C. for 15 minutes. After cooling to 50 ° C., a commercially available enzyme agent (Protease N “Amano”, manufactured by Amano Pharmaceutical Co., Ltd.) was added so that substrate / enzyme (E / S) = 1/100, and after keeping for 5 hours, 90 ° C. For 15 minutes. After cooling to 30 ° C., a permeated fraction was collected by ultrafiltration (fractionation range: 0.45 μm), and a non-permeated fraction was collected and lyophilized to obtain 6 kg of powder.
【００１９】[0019]
【実施例２】市販品のナトリウムカゼイネート（Ｎａ−
ＣＮ）１０ｋｇを水４９０ｋｇに溶解し、ｐＨを７．４
に調製し、１２１℃、１５分加熱する。４５℃に冷却
後、市販酵素剤（プロテアーゼＮ「アマノ」、天野製薬
（株）製）を基質／酵素（Ｅ／Ｓ）＝１／２５０となる
ように添加し、２４時間保持後、９０℃、１５分間の条
件で加熱失活した。３０℃に冷却後、限外ろ過（分画範
囲０．１μｍ）により透過画分を回収後、非透過画分を
回収、凍結乾燥し、粉末２ｋｇを得た。Example 2 Commercially available sodium caseinate (Na-
CN) 10 kg was dissolved in 490 kg of water, and the pH was 7.4.
And heated at 121 ° C. for 15 minutes. After cooling to 45 ° C., a commercially available enzyme preparation (Protease N “Amano”, manufactured by Amano Pharmaceutical Co., Ltd.) was added so that the substrate / enzyme (E / S) = 1/250, and after holding for 24 hours, 90 ° C. For 15 minutes. After cooling to 30 ° C., a permeated fraction was collected by ultrafiltration (fractionation range: 0.1 μm), and a non-permeated fraction was collected and lyophilized to obtain 2 kg of powder.
【００２０】[0020]
【実施例３】実施例１で得られたＷＰＣ由来不溶性画分
凍結乾燥物１５０ｇを、１５ｋｇの水で溶解後、市販植
物油を１５ｋｇ添加する（固形分４０％）。室温下で、
ホモミキサーにより１７０００ｒｐｍ、３０秒の条件で
乳化し、１００ｃｃのメスシリンダーに移した後、４０
℃で４時間放置し、乳化安定性を求めた。その結果、乳
清タンパク質の酵素分解時に生じる可溶性画分（ホエイ
可溶性ペプチド）がほとんど乳化性を示さなかったのに
対し、不溶性画分はＷＰＣあるいは分離乳清タンパク質
（ＷＰＩ）に匹敵する乳化性を示した。得られた結果を
表１に示す。Example 3 150 g of the freeze-dried WPC-derived insoluble fraction obtained in Example 1 is dissolved in 15 kg of water, and 15 kg of a commercially available vegetable oil is added (solid content: 40%). At room temperature,
The mixture was emulsified by a homomixer at 17000 rpm for 30 seconds and transferred to a 100 cc measuring cylinder.
The emulsion was left at 4 ° C. for 4 hours to determine emulsion stability. As a result, the soluble fraction (whey soluble peptide) generated during the enzymatic degradation of whey protein showed almost no emulsifiability, whereas the insoluble fraction had an emulsifiability comparable to WPC or separated whey protein (WPI). Indicated. Table 1 shows the obtained results.
【００２１】[0021]
【表１】 [Table 1]
【００２２】[0022]
【実施例４】実施例１あるいは２で得られた不溶性画分
の凍結乾燥物５ｋｇを、４０ｋｇの水で溶解後、市販乳
糖を１５ｋｇ添加し、植物油脂８．２ｋｇと混合した
（固形分４０％）。ホモミキサーにて１７０００ｒｐ
ｍ、５分間乳化後、１００ｃｃのメスシリンダーに移し
た後、４０℃で一昼夜保持し、乳化安定性を求めた。そ
の結果、ホエイ可溶性ペプチド、あるいはカゼインの酵
素分解時に生じる可溶性画分（カゼイン可溶性ペプチ
ド）はほとんど乳化性を示さなかったのに対し、各不溶
性画分はＷＰＣあるいはＷＰＩに匹敵する乳化性を示し
た。得られた結果を表２に示す。Example 4 5 kg of a freeze-dried product of the insoluble fraction obtained in Example 1 or 2 was dissolved in 40 kg of water, 15 kg of commercial lactose was added, and the mixture was mixed with 8.2 kg of vegetable oil (solid 40). %). 17000 rpm with a homomixer
After emulsification for 5 minutes, the mixture was transferred to a 100 cc measuring cylinder, and kept at 40 ° C. for 24 hours to determine the emulsion stability. As a result, the whey soluble peptide or the soluble fraction (casein soluble peptide) generated during enzymatic degradation of casein showed almost no emulsifiability, whereas each insoluble fraction showed emulsifiability comparable to WPC or WPI. . Table 2 shows the obtained results.
【００２３】[0023]
【表２】 [Table 2]
【００２４】[0024]
【実施例５】各不溶性画分の凍結乾燥物１ｋｇを、８０
ｋｇの水で溶解後、市販乳糖を３０ｋｇ溶解した。植物
油脂１６．４ｋｇと混合した（固形分４０％）。ホモミ
キサーにて１７０００ｒｐｍ、５分間の予備乳化後、ホ
モジナイザーにて１５０ｃｍ2／ｋｇの圧力で乳化物を
調製した。４０℃で一昼夜保持し、乳化安定性を求め
た。その結果、ホエイ可溶性ペプチド、あるいはカゼイ
ン可溶性ペプチドがほとんど乳化性を示さなかったのに
対し、各不溶性画分はＷＰＣあるいはＷＰＩに匹敵する
乳化性を示した。得られた結果を表３に示す。Example 5 1 kg of the lyophilized product of each insoluble fraction was
After dissolution with kg of water, 30 kg of commercial lactose was dissolved. It was mixed with 16.4 kg of vegetable oil (solid content 40%). After preliminary emulsification for 5 minutes at 17000 rpm using a homomixer, an emulsion was prepared using a homogenizer at a pressure of 150 cm 2 / kg. The emulsion was kept at 40 ° C. for a day and night to determine the emulsion stability. As a result, whey soluble peptide or casein soluble peptide showed little emulsifiability, whereas each insoluble fraction showed emulsifiability comparable to WPC or WPI. Table 3 shows the obtained results.
【００２５】[0025]
【表３】 [Table 3]
【００２６】[0026]
【実施例６】各不溶性画分の凍結乾燥物５ｋｇを、１６
０ｋｇの水で溶解後、市販乳糖を１５ｋｇ溶解する。植
物油脂８．２ｋｇと混合する（固形分１４％）。ホモミ
キサーにて１７０００ｒｐｍ、５分間の予備乳化後、ホ
モジナイザーにて１５０ｃｍ2／ｋｇの圧力で乳化物を
調製した。４０℃で一昼夜保持し、乳化安定性を求め
た。その結果、ホエイ可溶性ペプチド、あるいはカゼイ
ン可溶性ペプチドがほとんど乳化性を示さなかったのに
対し、各不溶性画分はＷＰＣあるいはＷＰＩに匹敵する
乳化性を示した。得られた結果を表４に示す。Example 6 5 kg of the lyophilized product of each insoluble fraction was
After dissolving with 0 kg of water, 15 kg of commercial lactose is dissolved. Mix with 8.2 kg of vegetable oil (solids 14%). After preliminary emulsification for 5 minutes at 17000 rpm using a homomixer, an emulsion was prepared using a homogenizer at a pressure of 150 cm 2 / kg. The emulsion was kept at 40 ° C. for a day and night to determine the emulsion stability. As a result, whey soluble peptide or casein soluble peptide showed little emulsifiability, whereas each insoluble fraction showed emulsifiability comparable to WPC or WPI. Table 4 shows the obtained results.
【００２７】[0027]
【表４】 [Table 4]
【００２８】[0028]
【実施例７】各不溶性画分の凍結乾燥物とホエイ不溶性
ペプチド、あるいはカゼイン可溶性ペプチドを様々な比
率で混合し、実施例５に準じた系で乳化物を調製した
（固形分４０％）。その結果、各可溶性ペプチドに対す
る各不溶性ペプチドの混合比が高いほど乳化性が改善さ
れることが分かった。得られた結果を表５に示す。Example 7 A freeze-dried product of each insoluble fraction and a whey insoluble peptide or casein soluble peptide were mixed at various ratios, and an emulsion was prepared in a system similar to Example 5 (solid content: 40%). As a result, it was found that the higher the mixing ratio of each insoluble peptide to each soluble peptide, the more the emulsifiability was improved. Table 5 shows the obtained results.
【００２９】[0029]
【表５】 [Table 5]
【００３０】[0030]
【実施例８】各不溶性画分４００ｇ及び乳化剤（ショ糖
脂肪酸エステル）２０ｇを水５．０３ｋｇに溶解後、食
品用レシチン４０ｇを溶解した油脂４．５ｋｇを加え
た。この溶液をホモミキサーにて１００００ｒｐｍ、５
分間予備乳化後、１０％メタヘキサリン酸ナトリウムを
１００ｍｌ加え１０分間攪拌した。これを、ホモジナイ
ザーにて８０ｋｇ／ｃｍ2で均質化し、５℃に急冷後一
晩放置した後、約５℃でホイッパーにてホイップする。
２０℃で一昼夜保持後、ホイップクリーム保形性を観察
した。その結果、各可溶性ペプチドがほとんど乳化性を
示さなかったのに対し、各不溶性画分は市販の脱脂粉乳
に匹敵するホイップ性を示した。得られた結果を表６に
示す。Example 8 400 g of each insoluble fraction and 20 g of an emulsifier (sucrose fatty acid ester) were dissolved in 5.03 kg of water, and 4.5 kg of fat or oil in which 40 g of lecithin for food was dissolved was added. This solution was mixed with a homomixer at 10,000 rpm for 5 minutes.
After the preliminary emulsification for 10 minutes, 100 ml of 10% sodium metahexaphosphate was added and the mixture was stirred for 10 minutes. This is homogenized with a homogenizer at 80 kg / cm 2 , rapidly cooled to 5 ° C., left overnight, and then whipped at about 5 ° C. with a whipper.
After keeping at 20 ° C. for one day, the whipped cream shape retention was observed. As a result, each soluble peptide showed little emulsifying property, whereas each insoluble fraction showed a whipping property comparable to commercially available skim milk powder. Table 6 shows the obtained results.
【００３１】[0031]
【表６】 [Table 6]
【００３２】[0032]
【発明の効果】本発明により、（１）不溶性画分の廃棄
が不要になり、廃棄にかかるコスト、環境汚染の低減と
いった効果が奏され、（２）安全性の高い天然物由来の
乳化剤として飲食品、飼餌料、化粧品、医薬品等に有利
に利用できる。According to the present invention, (1) there is no need to dispose of insoluble fractions, the effects of reducing disposal costs and environmental pollution are exhibited, and (2) a highly safe natural product-derived emulsifier. It can be advantageously used for foods and drinks, feedstuffs, cosmetics, pharmaceuticals and the like.
───────────────────────────────────────────────────── フロントページの続き (56)参考文献 特開 平11−221024（ＪＰ，Ａ) (58)調査した分野(Int.Cl.7，ＤＢ名) B01F 17/30 ────────────────────────────────────────────────── ─── Continuation of the front page (56) References JP-A-11-221024 (JP, A) (58) Field surveyed (Int. Cl. 7 , DB name) B01F 17/30
Claims (7)
タンパク質分解酵素によって酵素分解し、生成した分解
物から可溶性画分を濾過、遠心分離、膜分離等によって
分離した後に残った難溶性ないし不溶性画分を有効成分
としてなること、を特徴とする乳化性組成物。1. A protein or a protein-containing substance is enzymatically decomposed by a protease, and a soluble fraction is separated from a produced decomposed product by filtration, centrifugation, membrane separation, etc., and a hardly soluble or insoluble fraction remaining after the separation is effectively used. An emulsifiable composition characterized by being a component.
動物性、植物性又は微生物由来の少なくともひとつであ
ること、を特徴とする請求項１に記載の乳化性組成物。2. The emulsifiable composition according to claim 1, wherein the protein or the protein-containing substance is at least one of animal, vegetable or microbial origin.
乳タンパク質、ホエイタンパク質、これ（ら）の含有
物、これ（ら）の処理物の少なくともひとつであるこ
と、を特徴とする請求項１又は２に記載の乳化性組成
物。3. The protein according to claim 1, wherein the protein or the protein-containing substance is at least one of a milk protein, a whey protein, a substance contained therein, and a processed product thereof. Emulsifiable composition.
は微生物由来の少なくともひとつであること、を特徴と
する請求項１〜３のいずれか１項に記載の乳化性組成
物。4. The emulsifiable composition according to claim 1, wherein the proteolytic enzyme is at least one of animal, vegetable or microbial origin.
る請求項１〜４のいずれか１項に記載の乳化性組成物。5. The emulsifiable composition according to claim 1, further comprising a sugar.
化性組成物を含有してなること、を特徴とする飲食品及
び／又は飼餌料。6. A food or drink and / or feedstuff comprising the emulsifiable composition according to any one of claims 1 to 5.
を特徴とする請求項６に記載の飲食品。7. The food or beverage is whipped cream,
The food or drink according to claim 6, characterized in that:
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP07306998A JP3274646B2 (en) | 1998-03-09 | 1998-03-09 | Emulsifiable composition |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP07306998A JP3274646B2 (en) | 1998-03-09 | 1998-03-09 | Emulsifiable composition |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH11253783A JPH11253783A (en) | 1999-09-21 |
| JP3274646B2 true JP3274646B2 (en) | 2002-04-15 |
Family
ID=13507689
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP07306998A Expired - Fee Related JP3274646B2 (en) | 1998-03-09 | 1998-03-09 | Emulsifiable composition |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP3274646B2 (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP5380649B2 (en) * | 2007-03-16 | 2014-01-08 | 株式会社アップウェル | Milk component hydrolyzate |
| JP6429372B2 (en) * | 2014-10-03 | 2018-11-28 | 国立大学法人 宮崎大学 | Dispersant for poorly water-soluble substances containing hydrophobic peptides |
-
1998
- 1998-03-09 JP JP07306998A patent/JP3274646B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JPH11253783A (en) | 1999-09-21 |
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