JP2003333997A - Method for production of hydrolysate of soy protein - Google Patents

Method for production of hydrolysate of soy protein

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Publication number
JP2003333997A
JP2003333997A JP2002141999A JP2002141999A JP2003333997A JP 2003333997 A JP2003333997 A JP 2003333997A JP 2002141999 A JP2002141999 A JP 2002141999A JP 2002141999 A JP2002141999 A JP 2002141999A JP 2003333997 A JP2003333997 A JP 2003333997A
Authority
JP
Japan
Prior art keywords
component
soybean protein
hydrolyzate
solution
reaction
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
Application number
JP2002141999A
Other languages
Japanese (ja)
Other versions
JP5183006B2 (en
Inventor
Yasushi Nakamura
靖 中村
Kazunobu Tsumura
和伸 津村
Eiji Iwaoka
栄治 岩岡
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.)
Fuji Oil Co Ltd
Original Assignee
Fuji Oil Co Ltd
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Filing date
Publication date
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Priority to JP2002141999A priority Critical patent/JP5183006B2/en
Publication of JP2003333997A publication Critical patent/JP2003333997A/en
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Publication of JP5183006B2 publication Critical patent/JP5183006B2/en
Anticipated expiration legal-status Critical
Expired - Fee Related legal-status Critical Current

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  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Emulsifying, Dispersing, Foam-Producing Or Wetting Agents (AREA)

Abstract

<P>PROBLEM TO BE SOLVED: To provide a method for production of hydrolysate of soy protein achieving both quality and productivity, having emulsifying property and foaming property equal or more than that of a product obtained in a fractionation process, without requiring the fractionation process in producing the polypeptide containing both hydrolysates obtained by separated hydrolysis of 7S component (β-conglycinin) and 11S component (glycinin) of the soy protein. <P>SOLUTION: The method produces the hydrolysate of protein originating from 7S component (β-conglycinin) and 11S component (glycinin) by selectively hydrolyzing (a first hydrolyzing step) either one of the 7S component (β- conglycinin) and 11S component (glycinin) of the soy protein, and then hydrolyzing (a second hydrolyzing step) without fractionating the hydrolyzed fraction and the unhydrolyzed fraction to obtain the both hydrolysates, and then subjecting them to a heating process under ≤pH 4.3 and ≥100°C of temperature. <P>COPYRIGHT: (C)2004,JPO

Description

【発明の詳細な説明】Detailed Description of the Invention

【0001】[0001]

【発明の属する技術分野】本発明は、乳化力や起泡力が
高い、機能性の大豆蛋白加水分解物の製造法に関し、特
に、乳化性や起泡性の高い加水分解物を効率よく得る蛋
白加水分解物の製造方法に関する。
TECHNICAL FIELD The present invention relates to a method for producing a functional soybean protein hydrolyzate having high emulsifying ability and foaming ability, and particularly, to efficiently obtain a hydrolyzate having high emulsifying ability and foaming ability. The present invention relates to a method for producing a protein hydrolyzate.

【0002】[0002]

【従来の技術】近年、食品において消費者の天然素材へ
の志向が高まり、合成乳化剤および起泡剤に代わる天然
素材の開発が強く要望されている。天然素材としての大
豆蛋白は、従来から乳化剤、起泡剤原料として過去より
検討されてきた。(特開昭56−26171号公報、特
開昭57−16674号公報、特開平6−197788
号公報、特開昭49−109551号公報、特開昭53
−58982号公報、特開昭58−36347号公報、
特開昭60−176549号公報、特開昭60−184
372号公報、特開昭61−216646号公報、特開
平4−311354号公報、US−2502482、US−381
4816、US−4409248、US−4370267、US−463290
3)しかしながら、いずれの方法とも得られた物の機能
特性、作業性(工程の簡素さ)、歩留まりの全てを満足
することは困難であった。
2. Description of the Related Art In recent years, consumers have become increasingly interested in natural materials in foods, and there is a strong demand for the development of natural materials that replace synthetic emulsifiers and foaming agents. Soybean protein as a natural material has been studied as a raw material for emulsifiers and foaming agents from the past. (JP-A-56-26171, JP-A-57-16674, JP-A-6-197788)
JP-A-49-109551 and JP-A-53
-58982, JP-A-58-36347,
JP-A-60-176549, JP-A-60-184
372, JP 61-216646, JP 4-311354, US-2502482, US-381.
4816, US-4409248, US-4370267, US-463290
3) However, it was difficult to satisfy all of the functional characteristics, workability (simpleness of the process), and yield of the product obtained by either method.

【0003】これに対し、本発明者らは特開平2001-069
920号公報において、大豆蛋白中の7S成分(β−コン
グリシニン)及び11S成分(グリシニン)を別途に加
水分解し、且つ両方の加水分解物を含んだポリペプチド
(以降本明細書では「両加水分解物」と表現することが
ある。)が乳化力及び起泡力に優れた性質を有すること
見出し、合成乳化剤及び起泡剤に代わる天然素材及びそ
の製造方法の提案を行っている。しかしながら、この技
術でのポリペプチドは、それ以前の方法によって得られ
る物に比して、乳化力及び起泡力に顕著に優れる特徴が
あるものの、その品質と収率は、ポリぺプチドの製造条
件に大きく影響を受け、品質と歩留まり、また作業性の
面で完全に満足できるまでには、なお改良の余地があっ
た。具体的に述べると該公報の製造法において、作業
性、歩留まりで最も効率の良い、非分離での調製法で
は、使用濃度により機能特性の影響を受け易く、3%を
下回る低濃度条件では濃度低下に従い機能性も低下傾向
となる欠点があり、低濃度条件でも乳化力及び起泡力に
極めて優れているポリペプチドを得る為には、その製造
工程中で物性に悪影響を及ぼす不溶物の画分を除去する
分画操作が必要となっていた。従って、低濃度条件にお
いても高い機能を有したポリペプチドを求める場合、分
画による歩留まり低下、分画工程が入ることによる生産
性の低下、分画操作のバイプロとして生じる分離残渣の
処理問題等が派生してくる為、これらの課題解決が望ま
れていた。
On the other hand, the inventors of the present invention disclosed in Japanese Patent Laid-Open No. 2001-069.
No. 920, a polypeptide that separately hydrolyzes the 7S component (β-conglycinin) and the 11S component (glycinin) in soybean protein and contains both hydrolysates (hereinafter referred to as “both hydrolysates”). It is sometimes referred to as "a thing".) Has excellent properties of emulsifying power and foaming power, and proposes natural materials replacing synthetic emulsifiers and foaming agents and a method for producing the same. However, while the polypeptide obtained by this technique is characterized by significantly superior emulsifying power and foaming ability as compared with the product obtained by the previous method, its quality and yield are not so high. It was greatly affected by the conditions, and there was still room for improvement before being completely satisfied in terms of quality, yield, and workability. Specifically, in the production method of the publication, in the non-separation preparation method, which is the most efficient in terms of workability and yield, the functional characteristics are easily influenced by the concentration used, and the concentration is reduced under a low concentration condition of less than 3%. There is a drawback that the functionality tends to decrease with the decrease, and in order to obtain a polypeptide having excellent emulsifying power and foaming power even under low concentration conditions, in order to obtain a polypeptide, it is difficult to obtain A fractionation operation for removing the fraction was required. Therefore, when a polypeptide having a high function even in a low concentration condition is sought, there are problems such as a decrease in yield due to fractionation, a decrease in productivity due to the inclusion of a fractionation step, a treatment problem of a separation residue generated as a bipro in fractionation operation, etc. Since they are derived, it is desired to solve these problems.

【0004】[0004]

【発明が解決しようとする課題】本発明は、乳化性や起
泡性に優れた大豆蛋白加水分解物を得る製法において、
大豆蛋白中の7S成分(β−コングリシニン)及び11
S成分(グリシニン)を別途に加水分解し、且つ両方の
加水分解物を含んだポリペプチドの製造に関して、それ
ぞれの加水分解において分画操作を行わないと、乳化性
や起泡性の機能が高い分解物が得難いところを、分画操
作の有無に関わらず、従来法の分画操作処理品と同等以
上の優れた乳化力及び起泡力を持つ改良された大豆蛋白
加水分解物の製造方法を提供することにある。
DISCLOSURE OF THE INVENTION The present invention provides a method for producing a soybean protein hydrolyzate excellent in emulsifying property and foaming property,
7S component (β-conglycinin) in soybean protein and 11
With respect to the production of a polypeptide that separately hydrolyzes the S component (glycinin) and that contains both hydrolysates, unless the fractionation operation is performed in each hydrolysis, the emulsifying and foaming functions are high. Where a degradable product is difficult to obtain, a method for producing an improved soybean protein hydrolyzate having excellent emulsifying power and foaming power equivalent to or better than the conventional fractionated processed product, regardless of the presence or absence of a fractionation operation, is provided. To provide.

【0005】[0005]

【課題を解決するための手段】本発明者らは、以上の目
的を達成するため鋭意研究した結果、大豆蛋白中の7S
成分(β−コングリシニン)または11S成分(グリシ
ニン)のいずれかを選択的に加水分解し、次いで、未分
解の画分を更に加水分解することで「両加水分解物」を
調製し、本加水分解物を酸性下で加熱処理を施すことに
より、加水分解物の分画操作の有無に関わらず、乳化性
および起泡性が極めて優れた品質の蛋白加水分解物が得
られることを見出し、本発明を完成するに至ったもので
ある。
Means for Solving the Problems As a result of intensive studies to achieve the above object, the present inventors have found that 7S in soybean protein is
Selectively hydrolyze either the component (β-conglycinin) or the 11S component (glycinin), and then further hydrolyze the undecomposed fraction to prepare a “both hydrolyzate”, and carry out the main hydrolysis By subjecting the product to a heat treatment under acidic conditions, it was found that a protein hydrolyzate having extremely excellent emulsifying property and foaming property can be obtained regardless of the presence or absence of a fractionation operation of the hydrolyzate, and the present invention Has been completed.

【0006】即ち、本発明は、大豆蛋白中の7S成分
(β−コングリシニン)または11S成分(グリシニ
ン)のいずれかを選択的に加水分解し、加水分解された
画分と未分解の画分とを一旦分離して或いは分離しない
でそのままに、未分解の画分を更に加水分解することで
「両加水分解物」を得、これをpH4.3以下で、10
0℃以上の酸性加熱処理を施すことを特徴とする大豆蛋
白加水分解物の製造方法である。
That is, the present invention selectively hydrolyzes either the 7S component (β-conglycinin) or the 11S component (glycinin) in soybean protein to obtain a hydrolyzed fraction and an undegraded fraction. The unhydrolyzed fraction is further hydrolyzed with or without being separated once to obtain a "both hydrolyzate".
A method for producing a soybean protein hydrolyzate, which comprises performing an acidic heat treatment at 0 ° C. or higher.

【0007】また本発明は、上記の製造法において加水
分解物の加熱処理の前にフィターゼを用いて大豆蛋白中
のフィチン酸の低減化を行うことができ、あるいはまた
加熱処理前に加水分解物の固形物重量に対して0.1〜
10%のキトサンを添加しておくこともできる。
In the present invention, the phytase can be used to reduce the phytic acid in the soybean protein before the heat treatment of the hydrolyzate in the above production method, or alternatively, the hydrolyzate before the heat treatment. 0.1 to the solid weight of
It is also possible to add 10% chitosan.

【0008】さらに本発明は、低変性の大豆蛋白を原料
として、11S成分の選択加水分解を反応時間4時間以
内、反応pH3.0以下、反応温度45℃以下にて行
い、それから未分解の画分を45℃を超える温度、pH
が3.0より高いpHで行う大豆蛋白加水分解物の製造
法である。
Further, in the present invention, the low-denaturation soybean protein is used as a raw material to selectively hydrolyze the 11S component within a reaction time of 4 hours at a reaction pH of 3.0 or less and a reaction temperature of 45 ° C. or less, and then undecomposed Minutes, temperature over 45 ℃, pH
Is a method of producing a soybean protein hydrolyzate at a pH higher than 3.0.

【0009】一方で本発明は、低変性の大豆蛋白を原料
とし、7S成分の選択加水分解を反応時間2時間以内、
pH3.0〜8.0、反応温度50℃以上で行い、それ
から未分解の画分を45℃以下、pH3.0以下で加水
分解を行うことによる、蛋白加水分解物の製造法であ
る。
On the other hand, the present invention uses low-denaturation soybean protein as a raw material, and selectively hydrolyzes the 7S component within a reaction time of 2 hours,
It is a method for producing a protein hydrolyzate, which is carried out at pH 3.0 to 8.0 at a reaction temperature of 50 ° C. or higher, and then hydrolyzing the undecomposed fraction at 45 ° C. or lower and pH 3.0 or lower.

【0010】[0010]

【発明の実施の形態】本発明は、大豆蛋白中の構成成分
である7S成分(β−コングリシニン)または11S成
分(グリシニン)のいずれかを選択的に加水分解し、加
水分解された画分と未分解の画分とを分離して或いは分
離せずにそのまま、未分解の画分を更に加水分解するこ
とで「両加水分解物」調製する工程をへて、これをpH
4.3以下、100℃以上の酸性加熱処理を施す工程を含むこ
とを特徴とする製造法である。そして更に好ましい実施
形態として、前述の両加水分解物を調製する課程におい
て、混在するフィチン酸をフィターゼにより低フィチン
化する処理および叉はキトサン添加を行う処理工程を行
った後、これをpH4.3以下、100℃以上の酸性加熱処理
を施すことが良い。
BEST MODE FOR CARRYING OUT THE INVENTION The present invention selectively hydrolyzes either 7S component (β-conglycinin) or 11S component (glycinin), which is a constituent of soybean protein, to obtain a hydrolyzed fraction. Separate the undegraded fraction or leave it as it is and further hydrolyze the undegraded fraction to prepare a "both hydrolyzate".
The manufacturing method is characterized by including a step of subjecting to an acidic heat treatment at 100 ° C or higher at 4.3 or lower. And as a further preferred embodiment, in the process of preparing both of the above-mentioned hydrolysates, after performing a treatment process of reducing phytic acid mixed phytic acid with phytase and / or a process of adding chitosan, this is adjusted to pH 4.3. Hereinafter, it is preferable to perform an acidic heat treatment at 100 ° C. or higher.

【0011】7Sおよび11S由来の両加水分解物調製
工程について説明する。これは、大豆蛋白の主構成成分
である7S成分、11S成分を共に含む大豆蛋白質を基
質に用い、蛋白分解酵素を作用させることにより、第一
段分解反応(選択分解)にて11S成分を選択的に、第
二段分解反応によって未分解の7S成分を、或いはその
逆に第一段分解反応にて7S成分を選択的に、第二段分
解反応によって未分解の11S成分をそれぞれ加水分解
する分解工程からなる。本発明では、第一段分解反応
後、分解物を分画回収せず、引き続いて第二段分解反応
を行い「両加水分解物」調製しても、第一段反応の後に
分画して第二段反応を行う場合と乳化性や起泡性の機能
で差異のない加水分解物が得られる。従って、分画をし
ない場合、第二段分解に当たって遠心分離等による第一
段分解物の分画操作を取り入れる必要がないので生産工
程が効率的で、歩留まりでのロスを生じない特徴があ
る。
The steps for preparing both hydrolysates derived from 7S and 11S will be described. This is soy protein that contains both 7S and 11S components, which are the main constituents of soybean protein, is used as a substrate, and a proteolytic enzyme acts to select the 11S component in the first-stage decomposition reaction (selective decomposition). Specifically, the undecomposed 7S component is hydrolyzed by the second-stage decomposition reaction, or conversely, the 7S component is selectively hydrolyzed by the first-stage decomposition reaction, and the undecomposed 11S component is hydrolyzed by the second-stage decomposition reaction. It consists of a decomposition process. In the present invention, after the first-stage decomposition reaction, the decomposed product is not fractionally collected, and the second-stage decomposition reaction is subsequently performed to prepare “both hydrolysates”, but the fraction is also fractionated after the first-stage reaction. A hydrolyzate having no difference in emulsifying property and foaming function from the case of performing the second-step reaction can be obtained. Therefore, when the fractionation is not performed, it is not necessary to incorporate the fractionation operation of the first-stage decomposed product by centrifugation or the like in the second-stage decomposition, so that the production process is efficient and the loss in yield does not occur.

【0012】本発明に用いる原料大豆蛋白は、未変性あ
るいは低変性のものが好ましい。丸大豆もしくはヘキサ
ン等の溶剤で脱脂された低変性脱脂大豆または、これら
を水抽出した豆乳もしくは脱脂豆乳、更にはこれに酸を
用いて等電点沈澱させて沈澱画分を回収する低変性の分
離大豆蛋白や脱脂大豆からホエー成分を除いた低変性コ
ンセントレートから、おからの除去により得られる分離
大豆蛋白等が例示できる。用いる低変性脱脂大豆は、N
SI60以上、好ましくはNSI80以上である。また、これ
らの蛋白質が加熱等により変性を受けているか否かは、
蛋白質のDSC(Differential Scanning Calorimetry)
分析にて判別可能である。(Nagano et al.,J.Agric.Fo
od Chem.,40,941-944(1992))
The raw soybean protein used in the present invention is preferably undenatured or low-denatured. Low-denaturation defatted soybeans that have been defatted with a solvent such as whole soybeans or hexane, or soybean milk or defatted soybean milk obtained by extracting them with water, and isoelectric focusing using an acid to this to recover a precipitated fraction Examples thereof include isolated soybean protein and isolated soybean protein obtained by removing okara from a low-denaturation concentrate obtained by removing whey components from defatted soybean. The low-denaturation defatted soybean used is N
It is SI60 or more, preferably NSI80 or more. Whether these proteins have been denatured by heating, etc.
DSC (Differential Scanning Calorimetry) of protein
It can be determined by analysis. (Nagano et al., J. Agric.Fo
od Chem., 40,941-944 (1992))

【0013】11S成分を第一段分解反応により選択的
加水分解する場合は、上記の大豆蛋白を基質とし、1%
〜30%蛋白濃度の溶液に対して、蛋白加水分解酵素を
基質固形分に対して0.001〜1%、好ましくは0.0
1〜0.5%の範囲で添加し、45℃以下、好ましくは
30〜40℃においてpH3.0以下、好ましくはpH
1.8〜2.5で、反応時間4時間以内の短時間、好まし
くは10分〜2時間に0.22MTCA 可溶率で10〜50
となるまで反応するのが良い。反応温度が45℃を超え
ると11S成分以外に7S成分も同時に分解を受け易く
なり11S成分の選択的な分解が困難となり、また11
S成分の分解物自体もより低分子化する為、乳化性や起
泡性の機能が低下する。反応pHが3.0より高くなる
と、分解の選択性が低くなり分子量的に適正な分子量か
ら外れた低分子物や高分子物が多く発生し、乳化や起泡
の機能が低下し好ましくないし、pHが低すぎても選択
性の低下や後の中和での塩の増加等好ましくない。ま
た、反応時間が長すぎても11S成分の分解物がより低
分子化する為前記同様に品質低下が起り好ましくない。
When the 11S component is selectively hydrolyzed by the first-step decomposition reaction, 1% of the soybean protein is used as a substrate.
Proteolytic enzyme is added to the solution having a protein concentration of ˜30% in an amount of 0.001-1% with respect to the substrate solid content, preferably 0.0.
It is added in the range of 1 to 0.5%, and at 45 ° C. or lower, preferably 30 to 40 ° C., pH 3.0 or lower, preferably pH
The reaction time is 1.8 to 2.5, and the reaction time is within a short period of 4 hours, preferably 10 minutes to 50 hours at a solubility of 0.22 MTCA in 2 hours.
It is good to react until it becomes. If the reaction temperature exceeds 45 ° C., the 7S component as well as the 11S component is susceptible to decomposition at the same time, making it difficult to selectively decompose the 11S component.
Since the decomposed product of the S component itself has a lower molecular weight, the functions of emulsifying property and foaming property are deteriorated. When the reaction pH is higher than 3.0, the selectivity of decomposition is lowered and a large amount of low molecular weight compounds and high molecular weight substances deviating from the proper molecular weight in terms of molecular weight are generated, and the functions of emulsification and foaming are deteriorated, which is not preferable. If the pH is too low, the selectivity is lowered and the salt is increased in the subsequent neutralization, which is not preferable. Further, if the reaction time is too long, the degradation product of the 11S component becomes lower in molecular weight, and the quality is deteriorated as described above, which is not preferable.

【0014】ここで用いられる蛋白加水分解酵素はpH
3.0以下で活性を示す蛋白加水分解酵素全般が適当で
あり、動物由来のペプシン、カセプシンや微生物由来の
一連のアスパルチックプロテアーゼ類、例えば「ニュー
ラーゼF」、「プロテアーゼM」(天野製薬株式会社
製)、「スミチームLP」、「スミチームAP」(新日本化
学株式会社製)等の市販酵素剤を用いることが出来る。
中でもペプシンは好適である。
The proteolytic enzyme used here has a pH of
All protein hydrolases that show activity at 3.0 or less are suitable, and a series of aspartic proteases derived from animal-derived pepsin and capssin and microorganisms, such as "Neulase F" and "Protease M" (Amano Pharmaceutical Co., Ltd. Commercially available enzyme preparations such as "Company", "Sumiteam LP", "Sumiteam AP" (produced by Shin Nippon Kagaku Co., Ltd.) can be used.
Of these, pepsin is preferable.

【0015】7S成分を第一段分解反応により選択加水
分解するには、上記の大豆蛋白基質とし、0.5%〜2
0%蛋白濃度の溶液に対して、蛋白加水分解酵素を基質
固形分に対して0.001〜0.5%、好ましくは0.0
1〜0.5%の範囲で添加し、反応温度50℃以上、好
ましくは55〜85℃においてpH3.0より高いp
H、好ましくはpH3.5〜8.0で、反応時間2時間以
内の短時間、好ましくは10分〜30分程度で、0.2
2MTCA 可溶率で10〜50%となるまで反応すること
で実施できる。反応温度とpHがこの範囲を外れると、
7Sの選択分解性が低下し、11Sの分解が併発して好
ましくない。また反応時間が長くなっても、必要以上に
加水分解が進み、加水分解物の機能を低下させることに
なり好ましくない。ここで用いられる蛋白加水分解酵素
は、50℃を超え90℃未満、好ましくは55〜85℃
において蛋白質分解活性を有する酵素剤であることが必
要である。これらは植物や動物臓器或いは微生物起源の
市販酵素剤等その起源は特に限定されない。
In order to selectively hydrolyze the 7S component by the first-step decomposition reaction, the above soybean protein substrate is used, and 0.5% to 2% is used.
Proteolytic enzyme is added to the solution having a protein concentration of 0% in an amount of 0.001 to 0.5%, preferably 0.0 to 0.1%, based on the solid content of the substrate.
It is added in the range of 1 to 0.5%, and at a reaction temperature of 50 ° C. or higher, preferably 55 to 85 ° C., the pH is higher than 3.0.
H, preferably pH 3.5-8.0, reaction time within a short time of 2 hours, preferably about 10-30 minutes, 0.2.
It can be carried out by reacting until the solubility of 2MTCA becomes 10 to 50%. If the reaction temperature and pH are outside this range,
The selective decomposability of 7S decreases, and the decomposition of 11S also occurs, which is not preferable. Further, even if the reaction time becomes long, hydrolysis proceeds more than necessary and the function of the hydrolyzate is deteriorated, which is not preferable. The protein hydrolase used here is more than 50 ° C and less than 90 ° C, preferably 55 to 85 ° C.
It is necessary that the enzyme agent has proteolytic activity. The origins of these are commercially available enzyme agents of plant or animal organs or microbial origin, and the origin is not particularly limited.

【0016】第一段分解反応の未分解の画分は、遠心分
離等による分画回収をせず、第一段分解物を含んだ状態
のまま第二段の分解に供する。例えば11S成分を第一
段分解反応した後であると、45℃より高い反応温度で
任意のpH範囲、またはpHが3より高いpHで温度は
任意の反応温度で7S成分に富んだ画分を第二段分解反
応する。中でも反応温度が50℃以上かつpH3.0以
下で行うのが効率的で好都合である。7S成分を第一段
分解反応した後であると、11S成分に富んだ画分を第
二段分解反応する。この場合特にpH3.0以下、反応
温度45℃以下で行うことが好適である。第二段分解反
応で用いる蛋白分解酵素は第一段分解で使用した酵素の
残存活性を考慮して添加の必要性を判断すれば良い。添
加に当たっては反応pHで活性を持つものであれば良く
前述した酵素が例示される。反応時間は2時間以内の短
時間、好ましくは10分〜30分程度で、0.22MTCA
可溶率で30〜90%程度、好ましくは40〜65%と
なるように分解する。このようにして「両加水分解物」
調製し、この分解物を酸性下での加熱処理を行う。
The undecomposed fraction of the first-stage decomposition reaction is subjected to the second-stage decomposition in the state of containing the first-stage decomposed product without collecting the fraction by centrifugation or the like. For example, after the first-stage decomposition reaction of the 11S component, a reaction temperature higher than 45 ° C. in an arbitrary pH range, or a pH higher than 3 at a reaction temperature, a fraction rich in the 7S component is obtained. Second stage decomposition reaction. Above all, it is efficient and convenient to carry out the reaction at a temperature of 50 ° C. or higher and a pH of 3.0 or lower. After the 7S component is subjected to the first stage decomposition reaction, the 11S component-rich fraction is subjected to the second stage decomposition reaction. In this case, it is particularly preferable to carry out at a pH of 3.0 or lower and a reaction temperature of 45 ° C. or lower. The proteolytic enzyme used in the second-step decomposition reaction may be judged to be necessary in consideration of the residual activity of the enzyme used in the first-step decomposition. In addition, the above-mentioned enzyme is exemplified as long as it has activity at the reaction pH. The reaction time is as short as 2 hours or less, preferably about 10 to 30 minutes and 0.22 MTCA.
It is decomposed to have a solubility of about 30 to 90%, preferably 40 to 65%. In this way, "both hydrolysates"
It prepares and heat-processes this decomposition product under acidic condition.

【0017】酸性加熱の条件は、「両加水分解物」の溶
液を固形分5重量%〜20重量%、好ましくは7重量%
〜14重量%の濃度、pHを2〜4.3、好ましくはp
H2.5〜3.8の範囲に調製し、100℃〜160℃、
好ましくは105℃〜140℃で数秒間〜5分間程度の
加熱を行う。固形分が5重量%未満だと、加熱効果は得
られるものの作業効率が悪く適切ではない。一方、20
重量%を超える場合、分解率の低い蛋白加水分解物の処
理において蛋白溶液の粘度上昇が大きくなり過ぎ、流動
性の低下による作業性の悪化を招く危険もあるため好ま
しくない。加熱時のpHが2未満では、加熱の間に蛋白
加水分解物が更に酸加水分解を受けてしまい乳化性や起
泡性の機能の低下に繋がる。また、pH4.3を超える
条件での加熱処理では上記機能の低下を来たす場合あ
る。加熱温度が、100℃未満の場合では蛋白加水分解
物の機能は不充分にしか発現しない、160℃を超える
場合では、加熱時の酸加水分解を受け易くなるので機能
の低下に繋がってしまう。加熱時間は、加熱温度と酸加
水分解の程度により調整を行う。具体的には、加熱温度
が高くなる程、酸加水分解が進行し易くなるので、加熱
時間は短時間で処理する必要がある。スチームインジェ
クション方式の連続式直接加熱殺菌装置であれば、瞬間
的に100℃以上の高温加熱処理が可能であり、好適な
加熱装置として例示できる。
The condition of acidic heating is that the solution of "both hydrolysates" has a solid content of 5 to 20% by weight, preferably 7% by weight.
-14% by weight concentration, pH 2-4.3, preferably p
H range from 2.5 to 3.8, 100 ℃ ~ 160 ℃,
Preferably, heating is performed at 105 ° C. to 140 ° C. for several seconds to 5 minutes. When the solid content is less than 5% by weight, the heating effect is obtained but the work efficiency is poor and it is not suitable. On the other hand, 20
When the content is more than 5% by weight, the viscosity of the protein solution increases excessively in the treatment of a protein hydrolyzate having a low decomposition rate, and there is a risk of deterioration of workability due to deterioration of fluidity, which is not preferable. If the pH during heating is less than 2, the protein hydrolyzate will be further subjected to acid hydrolysis during heating, leading to a reduction in the functions of emulsification and foamability. Moreover, the above-mentioned function may be deteriorated in the heat treatment under the condition that the pH exceeds 4.3. When the heating temperature is lower than 100 ° C, the function of the protein hydrolyzate is insufficiently expressed. When the heating temperature is higher than 160 ° C, acid hydrolysis during heating is likely to occur, which leads to deterioration of the function. The heating time is adjusted depending on the heating temperature and the degree of acid hydrolysis. Specifically, the higher the heating temperature, the easier the acid hydrolysis progresses, so the heating time must be shorter. If it is a steam injection type continuous direct heat sterilizer, it is possible to instantaneously perform high-temperature heat treatment at 100 ° C. or higher, and it can be exemplified as a suitable heating device.

【0018】本発明では、pH4.3以下での酸性条件
下で加熱することが重要であるが、この理由はpH4.
3を超えるpH環境では蛋白加水分解物が加熱により疎
水相互作用やSS交換反応による分解物間の相互作用を
受け易くなり、会合度が増すことで溶解性の低下に繋が
り、蛋白加水分解物としての乳化性や起泡性の機能が低
下するのに対して、pH4.3より低いpH環境では、
SS交換反応は促進されず、分解物の会合化も抑制され
る為、高い溶解性が維持され機能性の低下に至らないも
のと推定される。
In the present invention, it is important to heat under acidic conditions at a pH of 4.3 or less, and the reason for this is that the pH is 4.3.
In a pH environment above 3, the protein hydrolyzate becomes more susceptible to hydrophobic interaction and interaction between the hydrolyzates due to SS exchange reaction due to heating, leading to a decrease in solubility due to an increased degree of association. While the emulsifying and foaming functions of are reduced, in a pH environment lower than pH 4.3,
Since the SS exchange reaction is not promoted and the association of degradation products is suppressed, it is presumed that the high solubility is maintained and the functionality is not deteriorated.

【0019】また、酸性加熱処理の前のいずれかの段階
で以下に述べる処理工程を行うことが、最終調製される
蛋白加水分解物の乳化力、起泡力をより高める上で有効
な操作になり、組み入れることが好ましい。
Further, it is effective to carry out the treatment steps described below at any stage before the acidic heat treatment in order to further enhance the emulsifying power and foaming power of the finally prepared protein hydrolyzate. , And preferably incorporated.

【0020】その操作の一つは、大豆由来の混在するフ
ィチン酸を除去または分解しておくことである。フィチ
ン酸を除去する方法としては、電気透析、膜分離、イオ
ン交換樹脂等処理などが例示でき、フィチン酸の分解に
ついては、フィターゼ(広義にはフィチン酸分解活性を
有する酵素)による酵素反応にてフィチン酸を加水分解
する方法である。特に後者のフィターゼを用いた酵素分
解処理が、生産コスト面から最も有利な方法である。使
用するフィターゼは、大豆蛋白加水分解物の物性への影
響を避ける為にプロテアーゼ活性の低い酵素または酵素
剤を選定することが好ましい。フィターゼ処理は、原料
の分解前、選択分解の後、未分解画分の分解後のいずれ
の段階で実施してもよい。但し反応条件は、大豆蛋白基
質での実施の場合7S、11Sの加熱変性を避ける為、
50℃以下、好ましくは40℃以下で反応するべきであ
る。
One of the operations is to remove or decompose the mixed phytic acid derived from soybean. As a method for removing phytic acid, electrodialysis, membrane separation, treatment with an ion exchange resin, etc. can be exemplified. For the decomposition of phytic acid, an enzymatic reaction by phytase (enzyme having a phytic acid decomposing activity in a broad sense) is used. This is a method of hydrolyzing phytic acid. In particular, the latter enzymatic decomposition treatment using phytase is the most advantageous method from the viewpoint of production cost. As the phytase to be used, it is preferable to select an enzyme or enzyme agent having a low protease activity in order to avoid affecting the physical properties of the soybean protein hydrolyzate. The phytase treatment may be carried out at any stage before the decomposition of the raw material, after the selective decomposition, and after the decomposition of the undecomposed fraction. However, the reaction conditions are to avoid heat denaturation of 7S and 11S when carried out with a soy protein substrate,
The reaction should be below 50 ° C, preferably below 40 ° C.

【0021】またフィターゼ処理の反応pHも、酵素活
性を有するpHであれば何れのpH条件でも可能である
が、後でpH4.3以下で加熱処理を実施する為、pH調
製操作や灰分含量の上昇を考慮するとpH4.3以下で
処理した方が好ましい。フィチン酸の除去または分解程
度の目安は、対蛋白重量当たり0.5重量%以下、好ま
しくは0.3重量%以下にまで低減することが望まし
い。
The reaction pH of the phytase treatment can be any pH condition as long as it has enzymatic activity, but since the heat treatment is performed at pH 4.3 or less later, the pH adjustment operation and the ash content Considering the increase, it is preferable to treat at pH 4.3 or less. It is desirable to reduce the level of removal or decomposition of phytic acid to 0.5% by weight or less, preferably 0.3% by weight or less, based on the weight of protein.

【0022】別の好ましい操作として、7Sおよび11
S由来の両加水分解物の加熱処理の前の段階で蛋白加水
分解物の固形物重量に対してキトサンを0.1〜10重
量%、好ましくは0.5〜3重量%を添加しておくこと
が効果ある。キトサンは、エビ、カニなどの甲殻類の殻
を原料として製造されるキチンの脱アセチル化物が好適
に用いられ、通常水溶性のグルコサミンのポリマーを主
成分とする。キトサン添加量が、0.1重量%未満だと
期待する物性の向上が僅かしか得られず、逆に10重量
%を超えると製品の溶液粘度が高くなり、起泡性の低下
に繋がるなど品質低下が生じてくるので好ましくない。
用いるキトサンは、分子量3000以上、好ましくは1
万以上のタイプで脱アセチル化度80%以上のグレード
が好適で、添加時期はフィターゼ処理同様、酸性加熱前
の段階であれば何れの時期でも構わない。但し、キトサ
ンは、pH5以上では溶解性が低く溶解し難い為、pH5
以下の酸性条件で分解物溶液に添加、溶解することが良
い。
Another preferred operation is 7S and 11
Before the heat treatment of both hydrolyzates derived from S, chitosan is added in an amount of 0.1 to 10% by weight, preferably 0.5 to 3% by weight, based on the solid weight of the protein hydrolyzate. Is effective. Chitosan is preferably a deacetylated product of chitin produced from shells of crustaceans such as shrimp and crab, and usually contains a water-soluble glucosamine polymer as a main component. If the amount of chitosan added is less than 0.1% by weight, the expected improvement in physical properties can be obtained only slightly. On the contrary, if it exceeds 10% by weight, the solution viscosity of the product becomes high, leading to a decrease in foamability. This is not preferable because it causes a decrease.
The chitosan used has a molecular weight of 3000 or more, preferably 1
A grade of 10,000 or more types with a deacetylation degree of 80% or more is suitable, and the addition time may be any time as long as it is a stage before acid heating, similar to the phytase treatment. However, chitosan has low solubility above pH 5 and is difficult to dissolve, so pH 5
It is preferable to add and dissolve in the decomposed product solution under the following acidic conditions.

【0023】以上述べたように酸性加熱処理の前の段階
でフィターゼ処理やキトサン添加、好ましくはフィター
ゼ処理およびキトサン添加の両方を行うことが、酸性条
件下での加熱処理の効果をより引き出し、最終調製され
る蛋白加水分解物の乳化力、起泡力がより高められる。
As described above, performing phytase treatment or chitosan addition, preferably both phytase treatment and chitosan addition, in the stage before the acidic heat treatment brings out the effect of the heat treatment under acidic conditions more, The emulsifying power and foaming power of the prepared protein hydrolyzate are further enhanced.

【0024】酸性加熱処理の前の段階でフィターゼ処理
やキトサン添加の処理理由は、これらの操作が蛋白加水
分解物の酸性域での溶解性向上に寄与し、後の酸性加熱
処理における蛋白間の相互作用がより低減され、機能性
の高い加水分解物を得る効果が高まるものと推定され
る。このようにして酸性加熱処理した7Sおよび11S
由来の両加水分解物溶液は、液体のままや噴霧乾燥等の
乾燥により粉体として製品化ができる。
The reason why the phytase treatment or the addition of chitosan is added before the acidic heat treatment is that these operations contribute to the improvement of the solubility of the protein hydrolyzate in the acidic region, and that the protein hydrolyzate in the subsequent acidic heat treatment is It is presumed that the interaction is further reduced and the effect of obtaining a highly functional hydrolyzate is enhanced. 7S and 11S acid-heat-treated in this way
Both derived hydrolyzate solutions can be commercialized as a powder as a liquid or by drying such as spray drying.

【0025】本発明により得られる蛋白加水分解物は、
これまで述べたように乳化性や起泡性が優れており、こ
れらの機能を用いる食品に利用されるが、本発明品は酸
性域においてもこれらの機能が顕著であり、酸性の乳化
食品には特に好適に用いられる。
The protein hydrolyzate obtained by the present invention is
As described above, the emulsifying property and the foaming property are excellent, and it is used for foods using these functions, but the product of the present invention has these functions remarkably even in the acidic range, and is suitable for acidic emulsified foods. Is particularly preferably used.

【0026】[0026]

【実施例】以下、実施例により本発明の実施様態を具体
的に説明するが、本発明がこれらの実施例によってその
技術範囲が限定されるものではない。
EXAMPLES Hereinafter, the embodiments of the present invention will be specifically described with reference to Examples, but the technical scope of the present invention is not limited by these Examples.

【0027】(分離大豆蛋白カードの調製)不二製油
(株)製の低変性脱脂大豆フレーク(NSI:90)に
40℃の温水10倍量を加え、これにNaOH溶液を加えて
そのpHを7.0に調整した。これを緩やかに撹拌して
1時間抽出し、遠心分離にて不溶画分のオカラと可溶画
分の脱脂豆乳とに分離した。得られた脱脂豆乳に塩酸を
加えてそのpHを4.5に調整し、生じた蛋白質沈澱物
を遠心分離にて回収し分離大豆蛋白カードを得た。な
お、この分離大豆蛋白カードにおいては、固形分が40
重量%であり、この固形分中における粗蛋白質純度が9
5重量%であった。また、DSC分析を行った結果、7S
成分、11S成分に由来するそれぞれの吸熱ピークが認
められた。
(Preparation of isolated soybean protein curd) 10 times amount of warm water at 40 ° C. was added to low-denaturation defatted soybean flakes (NSI: 90) manufactured by Fuji Oil Co., Ltd., and NaOH solution was added thereto to adjust the pH. Adjusted to 7.0. This was gently stirred, extracted for 1 hour, and separated by centrifugation into an insoluble fraction of okara and a soluble fraction of defatted soymilk. Hydrochloric acid was added to the defatted soymilk thus obtained to adjust its pH to 4.5, and the resulting protein precipitate was recovered by centrifugation to obtain a separated soybean protein curd. In this isolated soy protein curd, the solid content was 40%.
% By weight, and the crude protein purity in this solid content is 9%.
It was 5% by weight. In addition, as a result of DSC analysis, 7S
Endothermic peaks derived from the component and the 11S component were observed.

【0028】〔製造例1〕分離大豆蛋白カードに水及び
リン酸を加えてpH2.5、分離大豆蛋白濃度を10重
量%に調製し、この溶液2Lに対してフィターゼ(新日
本化学工業社製「スミチームPHY」)を1gを加え、
37℃で30分間フィターゼ処理を行った。次いで、3
7℃、pH2.5のままペプシン(日本バイオコン社
製)800mgを加え、1時間加水分解した(第一段分
解:選択分解)。反応液を電気泳動で分析した結果、大
豆蛋白中の11S成分のみ選択的に加水分解され、11
S成分に相当する移動度のバンドは消失していた。その
後、第一段反応液を分離することなく、そのままのpH
の状態で溶液温度のみ70℃まで昇温させ、昇温過程中
で未分解で残る7S成分を酵素加水分解(第二段分解)
し、「両加水分解物」調製した。なお、第一段反応液の
0.22M TCA可溶率は、33%であり、第二段反応液の
0.22M TCA可溶率は、44%であった。
[Production Example 1] Water and phosphoric acid were added to the isolated soybean protein curd to adjust the pH to 2.5 and the isolated soybean protein concentration to 10% by weight, and 2 L of this solution was mixed with phytase (manufactured by Shin Nippon Chemical Industry Co., Ltd.). "Sumiteam PHY") 1g,
Phytase treatment was performed at 37 ° C. for 30 minutes. Then 3
800 mg of pepsin (manufactured by Nippon Biocon Co., Ltd.) was added at 7 ° C. and pH 2.5, and hydrolysis was carried out for 1 hour (first stage decomposition: selective decomposition). As a result of analyzing the reaction solution by electrophoresis, only the 11S component in soybean protein was selectively hydrolyzed.
The mobility band corresponding to the S component disappeared. Then, without separating the first-stage reaction solution,
In this state, only the solution temperature is raised to 70 ° C, and the 7S component that remains undecomposed during the heating process is enzymatically hydrolyzed (second stage decomposition).
Then, “both hydrolysates” were prepared. The solubility of 0.22M TCA in the first-step reaction solution was 33%, and the solubility of 0.22M TCA in the second-step reaction solution was 44%.

【0029】前記で調製された蛋白加水分解物溶液を二
等分し、一方はそのまま、残り一方の溶液には、キトサ
ン(焼津水産化学工業社製「キトサンLL」)を1g添加
し、完全に溶解するまで撹拌溶解させ、各々の溶液を連
続式直接加熱殺菌装置にて120℃、7秒間加熱処理を
行った後、そのまま噴霧乾燥を行い、キトサン無添加の
大豆蛋白加水分解物(T−1a)およびキトサン添加し
た大豆蛋白加水分解物(T−1b)を調製した。なお、
両者とも加熱前の溶液pHはpH3であり、その0.2
2M TCA可溶率は、51%であった。
The protein hydrolyzate solution prepared above was divided into two equal parts, one was left as it was, and 1 g of chitosan (“Chitosan LL” manufactured by Yaizu Suisan Chemical Co., Ltd.) was added to the other solution to completely After stirring and dissolving until dissolved, each solution was subjected to heat treatment at 120 ° C. for 7 seconds in a continuous direct heat sterilizer, and then spray-dried as it was, soybean protein hydrolyzate containing no chitosan (T-1a). ) And chitosan were added to prepare a soybean protein hydrolyzate (T-1b). In addition,
In both cases, the solution pH before heating is pH 3, which is 0.2
The 2M TCA solubility was 51%.

【0030】〔製造例2〕分離大豆蛋白カードに水及び
リン酸を加えてpH2.5、分離大豆蛋白濃度を10重
量%に調製し、この溶液2Lに対してペプシン(日本バ
イオコン社製)800mgを加え、37℃で1時間加水分
解した(第一段分解)。反応液を電気泳動で分析した結
果、大豆蛋白中の11S成分のみ選択的に加水分解され
ていた。その後、第一反応液を分離することなく、その
ままのpHの状態で溶液温度のみ70℃まで昇温させ、
昇温過程中で未分解で残る7S成分を酵素加水分解(第
二段分解)し、「両加水分解物」調製した。なお、第一
段分解反応液の0.22M TCA可溶率は、30%であり、
第ニ段分解反応液の0.22M TCA可溶率は、40%であ
った。
[Production Example 2] Water and phosphoric acid were added to the isolated soybean protein curd to adjust the pH to 2.5 and the isolated soybean protein concentration to 10% by weight, and 800 mg of pepsin (manufactured by Nippon Biocon) was added to 2 L of this solution. Was added and the mixture was hydrolyzed at 37 ° C. for 1 hour (first stage decomposition). As a result of analyzing the reaction solution by electrophoresis, only the 11S component in soybean protein was selectively hydrolyzed. Then, without separating the first reaction liquid, only the solution temperature is raised to 70 ° C. in the same pH state,
The 7S component that remained undecomposed during the temperature rising process was enzymatically hydrolyzed (second-stage decomposition) to prepare a “both hydrolyzate”. The solubility of 0.22 M TCA in the first-stage decomposition reaction solution was 30%,
The second-stage decomposition reaction solution had a solubility of 0.22 M TCA of 40%.

【0031】調製された蛋白加水分解物を含む溶液をニ
等分し、一つはそのままの状態で、残りの一方は、キト
サン(焼津水産化学工業社製「キトサンLL」)を1g添
加し、完全に溶解するまで撹拌溶解させた。キトサン無
添加およびキトサン添加の溶液はそれぞれ、そのまま連
続式直接加熱殺菌装置にて120℃、7秒間加熱処理を
行い、これを粉霧乾燥した。これによりキトサン無添加
の大豆蛋白加水分解物(T−2a)、及びキトサン添加
の大豆蛋白加水分解物(T−2b)を得た。なお、両者
とも加熱前の溶液pHはpH3であり、T−2a、bの
0.22M TCA可溶率は、48%であった。
The prepared solution containing protein hydrolyzate was divided into two equal parts, one was left as it was, and the other was added with 1 g of chitosan (“Chitosan LL” manufactured by Yaizu Suisan Chemical Co., Ltd.), It was stirred and dissolved until completely dissolved. The chitosan-free solution and the chitosan-containing solution were directly subjected to heat treatment at 120 ° C. for 7 seconds in a continuous direct heat sterilizer, which was then atomized and dried. As a result, a soybean protein hydrolyzate containing no chitosan (T-2a) and a soybean protein hydrolyzate containing chitosan (T-2b) were obtained. In both cases, the solution pH before heating was pH 3, and the T2a and b solubility of 0.22M TCA was 48%.

【0032】比較製造例1 分離大豆蛋白カードに水及びリン酸を加えてpH2.
5、分離大豆蛋白濃度を10重量%に調製し、この溶液
3Lに対してフィターゼ(新日本化学工業社製「スミチ
ームPHY」)を1.5gを加え、37℃で30分間フィ
ターゼ処理を行った。次いで、37℃、pH2.5のま
まペプシン(日本バイオコン社製)1.2gを加え、1時
間加水分解した(第一段分解)。反応液を電気泳動で分
析した結果、大豆蛋白中の11S成分のみ選択的に加水
分解され、11S成分に相当する移動度のバンドは消失
していた。その後、第一反応液を分離することなく、そ
のままのpHの状態で溶液温度のみ70℃まで昇温さ
せ、昇温過程中で未分解で残る7S成分を酵素加水分解
(第二段分解)し、「両加水分解物」調製した。なお、
第一反応液の0.22M TCA可溶率は、33%であり、第
ニ反応液の0.22M TCA可溶率は、45%であった。
Comparative Production Example 1 Water and phosphoric acid were added to the isolated soybean protein curd to obtain a pH of 2.
5. The isolated soybean protein concentration was adjusted to 10% by weight, and 1.5 g of phytase (“Sumiteam PHY” manufactured by Shin Nippon Chemical Industry Co., Ltd.) was added to 3 L of this solution, and phytase treatment was performed at 37 ° C. for 30 minutes. . Next, 1.2 g of pepsin (manufactured by Nippon Biocon Co., Ltd.) was added at 37 ° C. and pH 2.5, and hydrolysis was carried out for 1 hour (first stage decomposition). As a result of analyzing the reaction solution by electrophoresis, only the 11S component in soybean protein was selectively hydrolyzed, and the mobility band corresponding to the 11S component disappeared. Then, without separating the first reaction liquid, only the solution temperature is raised to 70 ° C. in the same pH state, and the 7S component that remains undecomposed during the temperature raising process is enzymatically hydrolyzed (second stage decomposition). "Both hydrolysates" were prepared. In addition,
The solubility of 0.22M TCA in the first reaction solution was 33%, and the solubility of 0.22M TCA in the second reaction solution was 45%.

【0033】調製された蛋白加水分解物溶液を三等分
し、各々の溶液に対してキトサン(焼津水産化学工業社
製「キトサンLL」)を1g添加し、完全に溶解するまで
撹拌溶解させた。その後、一つはそのままのpH3、残
りの二つはNaOH溶液を用いてpH4.5、およびpH6.
5に調整した。各々の溶液を連続式直接加熱殺菌装置に
てpH3調整溶液は、95℃、1分間、他のpH4.5
およびpH6.5調整溶液については120℃、7秒間
加熱処理を行った後、そのまま噴霧乾燥を行い、pH3
加熱処理の大豆蛋白加水分解物(C−1a)、pH4.
5加熱処理の大豆蛋白加水分解物(C−1b)およびp
H6.5加熱処理の大豆蛋白加水分解物(C−1c)を
調製した。なお、C−1aの0.22M TCA可溶率は、5
3%、C−1b,C−1Cの0.22M TCA可溶率は、5
0%であった。
The prepared protein hydrolyzate solution was divided into three equal parts, and 1 g of chitosan (“Chitosan LL” manufactured by Yaizu Suisan Kagaku Kogyo Co., Ltd.) was added to each solution and dissolved by stirring until completely dissolved. . After that, one is pH 3 as it is, and the other two are pH 4.5 and pH 6 with NaOH solution.
Adjusted to 5. Each solution is adjusted to pH 3 with a continuous direct heat sterilizer at 95 ° C for 1 minute.
And for the pH 6.5 adjusted solution, after heat treatment at 120 ° C. for 7 seconds, spray drying is performed as it is, and the pH is adjusted to 3
Heat-treated soy protein hydrolyzate (C-1a), pH 4.
5 Heat-treated soybean protein hydrolyzate (C-1b) and p
H6.5 heat-treated soybean protein hydrolyzate (C-1c) was prepared. The solubility of C-1a at 0.22M TCA was 5
3%, C-1b, C-1C 0.22M TCA solubility is 5
It was 0%.

【0034】〔比較製造例2〕分離大豆蛋白カードに水
及び塩酸を加えてpH2.0、分離大豆蛋白濃度を10
重量%に調製し、この溶液1Lに対してペプシン(日本
バイオコン社製)200mgを加え、37℃で30分間加
水分解した(第一段分解)。反応液を電気泳動で分析し
た結果、大豆蛋白中の11S成分のみ選択的に加水分解
されていた。第一反応液は、NaOHを用いてpH4.5に
調整し生じてくる沈澱を遠心分離にて11S成分の分解
物を含んだ上清画分と未分解の7S成分を含んだ沈澱画
分とに分離した。なお、第一段反応の反応液の0.22M
TCA可溶率は、24%であった。沈澱画分は、水及び塩
酸を加えてpH2.0、固形分7重量%に調整し、この
溶液1Lに対してペプシン100mgを加え、60℃で2
0分間再度加水分解を行った(第二段反応)。反応液の
0.22M TCA可溶率は44%であった。第二段反応液
は、前記第一段反応の上清画分と混合し、この混合液の
固形分に対して3重量%の水酸化Caを添加し、更にNaOH
溶液を用いてpH6.5に調整、これを連続式直接加熱
殺菌装置にて120℃、7秒間の加熱処理を行った後室
温まで冷却した。冷却後、5000Gにて10分間遠心
分離して不溶成分を除去し、「両加水分解物」含む上清
画分を得、これを噴霧乾燥し、不溶成分を除去した大豆
蛋白加水分解物(C−2)を調製した。なお、C−2の
0.22M TCA可溶率は、73%であり、固形分回収率は
70%であった。
[Comparative Production Example 2] Water and hydrochloric acid were added to the isolated soybean protein curd to adjust the pH to 2.0 and the isolated soybean protein concentration to 10.
The concentration was adjusted to 200% by weight, 200 mg of pepsin (manufactured by Nippon Biocon Co., Ltd.) was added to 1 L of this solution, and the mixture was hydrolyzed at 37 ° C. for 30 minutes (first stage decomposition). As a result of analyzing the reaction solution by electrophoresis, only the 11S component in soybean protein was selectively hydrolyzed. The first reaction solution was adjusted to pH 4.5 with NaOH, and the resulting precipitate was centrifuged to separate a supernatant fraction containing a degradation product of the 11S component and a precipitation fraction containing an undegraded 7S component. Separated. In addition, 0.22M of the reaction solution of the first step reaction
The TCA solubility was 24%. The precipitated fraction was adjusted to pH 2.0 and solid content 7% by weight with water and hydrochloric acid, 100 mg of pepsin was added to 1 L of this solution, and the mixture was stirred at 60 ° C for 2 hours.
Hydrolysis was performed again for 0 minutes (second step reaction). The solubility of 0.22 M TCA in the reaction solution was 44%. The second-step reaction solution was mixed with the supernatant fraction of the first-step reaction, 3% by weight of Ca hydroxide was added to the solid content of the mixed solution, and NaOH was added.
The solution was adjusted to pH 6.5, subjected to heat treatment at 120 ° C. for 7 seconds in a continuous direct heat sterilizer, and then cooled to room temperature. After cooling, the insoluble component was removed by centrifugation at 5000 G for 10 minutes to obtain a supernatant fraction containing "both hydrolysates", which was spray-dried and the insoluble component was removed to remove the soy protein hydrolyzate (C -2) was prepared. The solubility of C-2 in 0.22M TCA was 73%, and the solid content recovery rate was 70%.

【0035】〔比較製造例3〕分離大豆蛋白カードに水
及びリン酸を加えてpH2.5、分離大豆蛋白濃度を1
0重量%に調製し、この溶液1Lに対して37℃、pH
2.5のままペプシン(日本バイオコン社製)400mg
を加え、1時間加水分解した(第一段分解)。反応液を
電気泳動で分析した結果、大豆蛋白中の11S成分のみ
選択的に加水分解され、11S成分に相当する移動度の
バンドは消失していた。その後、第一段反応液を分離す
ることなく、そのままのpHの状態で溶液温度のみ70
℃まで昇温させ、昇温過程中で未分解で残る7S成分を
酵素加水分解(第二段分解)し、「両加水分解物」調製
した。なお、第一段反応液の0.22M TCA可溶率は、3
1%であり、第ニ段反応液の0.22M TCA可溶率は、4
3%であった。
Comparative Production Example 3 Water and phosphoric acid were added to the isolated soybean protein curd to adjust the pH to 2.5 and the isolated soybean protein concentration to 1
Adjusted to 0% by weight, 1 liter of this solution at 37 ° C, pH
As it is 2.5, pepsin (manufactured by Nippon Biocon) 400 mg
Was added for hydrolysis for 1 hour (first stage decomposition). As a result of analyzing the reaction solution by electrophoresis, only the 11S component in soybean protein was selectively hydrolyzed, and the mobility band corresponding to the 11S component disappeared. Then, without separating the first-step reaction solution, the solution temperature is kept at 70 without changing the pH.
The temperature was raised to 0 ° C., and the 7S component that remained undecomposed during the temperature raising process was enzymatically hydrolyzed (second-stage decomposition) to prepare a “both hydrolyzate”. The solubility of 0.22M TCA in the first-stage reaction solution was 3
1% and the 0.22M TCA solubility of the second stage reaction solution was 4%.
It was 3%.

【0036】調製された蛋白加水分解物溶液は、NaOH溶
液を用いてpH6.5に調整した。この溶液を連続式直
接加熱殺菌装置にて120℃、7秒間加熱処理を行った
後、噴霧乾燥を行い、大豆蛋白加水分解物(C−3)を
調製した。なお、C−3の0.22M TCA可溶率は、46
%であった。
The prepared protein hydrolyzate solution was adjusted to pH 6.5 with a NaOH solution. This solution was heat-treated at 120 ° C. for 7 seconds with a continuous direct heat sterilizer, and then spray-dried to prepare a soybean protein hydrolyzate (C-3). The solubility of C-3 of 0.22M TCA was 46.
%Met.

【0037】〔比較製造例4〕分離大豆蛋白カードに水
及びリン酸を加えてpH2.5、分離大豆蛋白濃度を1
0重量%に調製し、この溶液1Lに対して60℃、pH
2.5のままペプシン(日本バイオコン社製)200mg
を加え、2時間加水分解した。反応液を電気泳動で分析
した結果、大豆蛋白中の11S成分、7S成分ともに加
水分解されていた。この反応液をNaOH溶液を用いてpH
6.5に調整、この溶液を連続式直接加熱殺菌装置にて
120℃、7秒間加熱処理を行った後、噴霧乾燥を行
い、大豆蛋白加水分解物(C−4)を調製した。なお、
C−4の0.22M TCA可溶率は、56%であった。
[Comparative Production Example 4] Water and phosphoric acid were added to the isolated soybean protein curd to adjust the pH to 2.5 and the isolated soybean protein concentration to 1
Adjusted to 0% by weight, 1 liter of this solution at 60 ° C, pH
200 mg as it is 200 mg of pepsin (manufactured by Nippon Biocon)
Was added and hydrolyzed for 2 hours. As a result of analyzing the reaction solution by electrophoresis, both the 11S component and the 7S component in soybean protein were hydrolyzed. PH of this reaction solution with NaOH solution
The solution was adjusted to 6.5, and this solution was heat-treated at 120 ° C. for 7 seconds by a continuous direct heat sterilizer, and then spray-dried to prepare a soybean protein hydrolyzate (C-4). In addition,
C-4 had a solubility of 0.22 M TCA of 56%.

【0038】製造例および比較製造例の試作条件を表−
1に纏めた。
The trial production conditions of the production example and the comparative production example are shown in the table.
Summarized in 1.

【表1】 [Table 1]

【0039】〔機能評価〕(各大豆蛋白加水分解物の起
泡力、乳化力評価) (起泡力の評価)本発明での評価は油系での起泡容量と
その安定性により評価する。本発明の製造例と比較製造
例との起泡力の差をより明らかにする目的で以下に述べ
る方法により泡品質(起泡安定性)を評価した。すなわ
ち、3重量%水溶液をpH4およびpH7に調整し、こ
の100mlに大豆油5mlを加えて、これをホモヂナイザ
ー(日本精機社製)により10,000rpmで1分間処
理、調製された泡をメスシリンダーに移してその泡容量
(ml)を測定した。安定性の評価は、起泡直後と1時間
放置後の泡容量(ml)の変化量から評価した。
[Functional Evaluation] (Evaluation of Foaming Power and Emulsifying Power of Each Soybean Protein Hydrolyzate) (Evaluation of Foaming Power) The evaluation in the present invention is based on the foaming capacity in an oil system and its stability. . The foam quality (foaming stability) was evaluated by the method described below for the purpose of clarifying the difference in foaming power between the production examples of the present invention and the comparative production examples. That is, a 3 wt% aqueous solution was adjusted to pH 4 and pH 7, 5 ml of soybean oil was added to 100 ml of this, and this was treated with a homogenizer (manufactured by Nippon Seiki Co., Ltd.) at 10,000 rpm for 1 minute. The foam volume (ml) was measured after transfer. The stability was evaluated from the amount of change in the foam volume (ml) immediately after foaming and after standing for 1 hour.

【0040】(乳化力の評価)本発明品の機能評価を、
乳化活性を測定することで評価した。乳化活性は、pH
4、5.5、およびpH7に調整した試料溶液(1重量
%)3mlに大豆油1mlを加え、超音波分散機で乳化物を
調製し、0.1%SDS溶液で1000倍に希釈して溶液
濁度(500nmの吸光度)を測定した。評価は、その濁
度値が高い程乳化力が高いと判断する。
(Evaluation of emulsifying power) Functional evaluation of the product of the present invention
It was evaluated by measuring the emulsifying activity. Emulsifying activity is pH
1 ml of soybean oil was added to 3 ml of the sample solution (1% by weight) adjusted to 4, 5.5, and pH 7 to prepare an emulsion with an ultrasonic disperser, which was diluted 1000 times with a 0.1% SDS solution. The solution turbidity (absorbance at 500 nm) was measured. In the evaluation, the higher the turbidity value, the higher the emulsifying power.

【0041】各製造例および比較製造例で調製した各大
豆蛋白加水分解物の起泡力評価結果を表−2に乳化力評
価結果を表−3に示した。
The foaming power evaluation results of each soybean protein hydrolyzate prepared in each Production Example and Comparative Production Example are shown in Table-2, and the emulsification power evaluation results are shown in Table-3.

【表2】 [Table 2]

【0042】[0042]

【表3】 [Table 3]

【0043】表−2および表3の結果のように本発明で
述べるところの「両加水分解物」をある特定の条件、即
ちpH4.3以下、100℃以上の酸性加熱処理を行っ
た場合(T群)に、起泡力の有効な改善効果が得られ、
乳化力においても弱酸性域(pH5.5)から酸性域
(pH4)の乳化力が改善されていることが分かる。ま
た、酸性加熱処理の前段階でフィターゼ処理やキトサン
添加、更にはこれらの両操作を施すことが一層の品質改
善に有効であることが分かる。これらT−1a〜2bの
起泡力、乳化力は、C−2と比較しても同等かそれ以上
の物性であり、本発明の製造法により製品歩留まりを犠
牲にすることなく優れた品質を付与させることが可能に
なった。
As shown in the results of Tables 2 and 3, the "both hydrolysates" described in the present invention were subjected to acidic heat treatment at a specific condition, that is, pH 4.3 or less and 100 ° C or more ( T group), an effective improvement effect of the foaming force is obtained,
Regarding the emulsifying power, it can be seen that the emulsifying power from the weakly acidic range (pH 5.5) to the acidic range (pH 4) is improved. Further, it can be seen that it is effective to further improve quality by performing phytase treatment, addition of chitosan, and both of these operations before the acidic heat treatment. The foaming power and emulsifying power of T-1a to 2b are equivalent to or higher than those of C-2, and the production method of the present invention provides excellent quality without sacrificing product yield. It has become possible to give it.

【0044】〔応用例1〕(マヨネーズ様ドレッシン
グ) 製造例1〜2および比較製造例1〜2で調製した各大豆
蛋白加水分解物を用いてマヨネーズ様ドレッシングの調
製を試み、更にその粒子径を測定することで評価を実施
した。ドレッシングの調製は、下記のサラダ油を除く配
合物を混合し溶解させた後、これにサラダ油を添加しな
がらホモヂナイザー(日本精機社製)を用いて乳化(7
000rpm)し、マヨネーズ様ドレッシングを調製し
た。各調製品の乳化粒子径をレーザー粒度分布計(島津
製作所社製SALD−2000A)を用いて測定した。
[Application Example 1] (Mayonnaise-Like Dressing) An attempt was made to prepare a mayonnaise-like dressing using each of the soybean protein hydrolysates prepared in Production Examples 1-2 and Comparative Production Examples 1-2, and the particle size was further determined. Evaluation was performed by measuring. The dressing was prepared by mixing and dissolving the following ingredients except salad oil, and then emulsifying with a homogenizer (manufactured by Nippon Seiki Co., Ltd.) while adding salad oil thereto (7
000 rpm) to prepare a mayonnaise-like dressing. The emulsified particle size of each preparation was measured using a laser particle size distribution meter (SALD-2000A manufactured by Shimadzu Corporation).

【0045】マヨネーズ様ドレッシングの配合は次の通
り(例示の部は重量基準)。サラダ油:74部、食酢:
13部、蛋白分解物試料:2部、調味料:2部、香辛
料:1部、水:8部。
The composition of the mayonnaise-like dressing is as follows (exemplified parts are by weight). Salad oil: 74 parts, vinegar:
13 parts, protein degradation product sample: 2 parts, seasoning: 2 parts, spice: 1 part, water: 8 parts.

【0046】[0046]

【表4】 [Table 4]

【0047】製造例および比較製造例の全ての調製品と
もマヨネーズ様組織の乳化物を調製できた。中でも本発
明の製造例T−1〜4は、比較製造例C−4にほぼ近似し
た乳化粒度状態で品質的にも優れたものであった。本結
果は、酸性条件での乳化力がより向上されていることを
示唆するものである。また、本発明の製造例T−1〜4
で得られるマヨネーズ様乳化物は、比較製造例C−4で
得られるマヨネーズ様乳化物よりも苦味が少なく風味的
にも向上していた。この理由は、C−4に比べてT−1〜
4の方が分解度が低い為、苦味を呈する低分子ペプチド
の含有量が少なくなっていることによるものと考えられ
る。よって本発明での製造法を用いれば、マヨネーズ様
ドレッシングの乳化剤として従来以上に大豆蛋白加水分
解物の品質を高めることが可能である。
Emulsions having a mayonnaise-like structure could be prepared from all the preparations of Production Examples and Comparative Production Examples. Above all, Production Examples T-1 to T-4 of the present invention were excellent in quality in an emulsified particle size state substantially similar to Comparative Production Example C-4. This result suggests that the emulsifying power under acidic conditions is further improved. In addition, Production Examples T-1 to 4 of the present invention
The mayonnaise-like emulsion obtained in Example 1 had less bitterness and improved flavor in comparison with the mayonnaise-like emulsion obtained in Comparative Production Example C-4. The reason for this is that T-1 ~
It is considered that this is because the content of the low-molecular-weight peptide exhibiting a bitterness is small because the decomposition degree of 4 is lower. Therefore, by using the production method of the present invention, it is possible to further improve the quality of a soybean protein hydrolyzate as an emulsifier for a mayonnaise-like dressing.

【0048】〔応用例2〕(スポンジケーキ) 製造例1〜2および比較製造例1〜2で調製した各大豆
蛋白加水分解物を起泡剤としてオールインミックス法で
のスポンジケーキを調製した。ケーキ生地の配合(例示
の部は重量基準)は次の通りである。薄力粉:100部、
砂糖:100部、全卵:200部、サラダ油:20部、ソルビト
ール:15部、食塩:1部、蛋白加水分解物試料:8部。
[Application Example 2] (Sponge cake) A sponge cake was prepared by the all-in-mix method using each of the soybean protein hydrolysates prepared in Production Examples 1-2 and Comparative Production Examples 1-2 as a foaming agent. The composition of the cake dough (the example part is based on the weight) is as follows. Soft flour: 100 parts,
Sugar: 100 parts, whole egg: 200 parts, salad oil: 20 parts, sorbitol: 15 parts, salt: 1 part, protein hydrolyzate sample: 8 parts.

【0049】スポンジケーキの調製は、サラダ油を除く
全ての原料をまず均一分散させ、そこにサラダ油を添
加、生地に馴染ませた後、品温を25℃に調整、これを
ホイッパー羽根を用いてケンウッドミキサー(愛工舎製
作所社製「プロKM−230」)にて目盛り6の設定で4
分間ホイップさせケーキ生地を調製した。、得られた生
地280gを160℃、30分間焼成し、室温まで放冷
させた後、スポンジケーキのボリューム、食感、風味を
評価した。ケーキの風味と食感は、良いものから順に◎
(非常に良い)、○(良好)、△(少し劣る)、×(劣
る)で示す。
To prepare the sponge cake, all the raw materials except the salad oil were first uniformly dispersed, and the salad oil was added to the dough to adjust it to the dough, and then the temperature of the product was adjusted to 25 ° C., using a whipper blade to make Kenwood. Use a mixer ("Pro KM-230" manufactured by Aikosha Seisakusho Co., Ltd.) to set the scale 6 to 4
It was whipped for a minute to prepare a cake dough. After 280 g of the obtained dough was baked at 160 ° C. for 30 minutes and allowed to cool to room temperature, the volume, texture and flavor of the sponge cake were evaluated. The flavor and texture of the cake are ◎
It is shown as (very good), ◯ (good), Δ (slightly inferior), and x (inferior).

【0050】[0050]

【表5】 [Table 5]

【0051】製造例2のT−3のみ起泡力やや低かった
が、他のT−1、T−2、T−4は本試作条件において
良好な起泡力を示し、オールインミックス法での起泡剤
として品質的に満足できるレベルにあった。中でも特に
T−2は、優れた起泡力があり、調製されたスポンジケ
ーキの食感も最も優れていた。また、比較製造例のC−
1〜3は、ホイップ時間を延長しても生地比重0.55
程度までしか低下しなかった。以上のように本発明の製
造方法を用いれば、従来品よりもスポンジケーキ用起泡
剤の機能を向上させた大豆蛋白加水分解物を調製でき
る。
Although only T-3 of Production Example 2 had a slightly low foaming power, the other T-1, T-2, and T-4 exhibited good foaming power under the conditions of this trial production, and the all-in-mix method was used. The foaming agent was of a quality-satisfactory level. Above all
T-2 had an excellent foaming power, and the texture of the prepared sponge cake was also the best. In addition, C- of Comparative Production Example
1-3, the specific gravity of the dough is 0.55 even if the whipping time is extended.
It fell only to a certain degree. As described above, by using the production method of the present invention, it is possible to prepare a soybean protein hydrolyzate in which the function of the foaming agent for sponge cake is improved as compared with the conventional product.

【0052】応用例3(フラワーペースト) 製造例1〜2および比較製造例1〜2で調製した各大豆
蛋白加水分解物を用いて酸性タイプでのフラワーペース
ト適性について評価した。配合は、以下に示した簡易モ
デル配合を設定し、試料濃度1%、油分30%配合のpH
4の酸性ペースト生地を調製。一晩放置後のペースト生
地5gを絞り袋を用いてろ紙上に絞り出し、これに水1g
をろ紙に含ませ、密閉容器に入れた後、200℃のオー
ブンで10分加熱処理し、加熱後のペースト生地の油分
離状態および保形性を評価することで酸性タイプのフラ
ワーペースト適性を評価した。ペーストの調製は、55
℃の温水で油以外の原料を溶解させたのち、油を添加し
て予備乳化し、溶液pHを4に調整して予備乳化を更に続
け、これを高圧ホモゲナイザー(100Kg/cm2)で乳
化し、この生地溶液300gをラボニーダー(特殊機化
工業社製「TK−03型」)を用いて生地温度85℃まで
撹拌加熱することでペースト生地を調製した。(撹拌回
転数:120rpm ジャケット温度:120℃)
Application Example 3 (Flower Paste) Using each of the soybean protein hydrolysates prepared in Production Examples 1 and 2 and Comparative Production Examples 1 and 2, the acid type was evaluated for suitability for flower paste. For the formulation, set the simple model formulation shown below, and the pH of the formulation with a sample concentration of 1% and oil content of 30%.
Prepare 4 acidic paste dough. After leaving overnight, squeeze 5 g of paste dough onto a filter paper using a squeezing bag and add 1 g of water to it.
Filter paper, put in a closed container, heat treated in an oven at 200 ° C for 10 minutes, and evaluate the oil separation state and shape retention of the paste dough after heating to evaluate acid type flower paste suitability. did. Paste preparation is 55
After dissolving raw materials other than oil with warm water at ℃, add oil to pre-emulsify, adjust the solution pH to 4 and continue pre-emulsification, emulsify this with a high pressure homogenizer (100 Kg / cm2), A paste dough was prepared by stirring and heating 300 g of this dough solution to a dough temperature of 85 ° C. using a lab kneader (“TK-03 type” manufactured by Tokushu Kika Kogyo Co., Ltd.). (Stirring speed: 120 rpm Jacket temperature: 120 ° C)

【0053】簡易モデル配合(例示の部は重量基準) 試料:1部、菜種油:30部、砂糖:10部、デキスト
リン:6部、加工澱粉:7部、水:46部 *pH4への調製にはクエン酸を用いて調製した。
Simple model formulation (examples are based on weight) Sample: 1 part, rapeseed oil: 30 parts, sugar: 10 parts, dextrin: 6 parts, modified starch: 7 parts, water: 46 parts * For pH 4 preparation Was prepared with citric acid.

【0054】[0054]

【表6】 [Table 6]

【0055】評価結果のように製造例のT−1a〜T2
bは、保形性およびオイルオフ評価とも良好な結果得ら
れ、酸性タイプのフラワーペースト向け乳化剤として好
適な素材になるものと判断された。一方の比較例C−1
a〜cの場合では、ペースト調製時の加熱撹拌中に油分
離が生じてペーストそのものが調製できなかったり(C
−1b,c)、ペーストの焼成耐性が低い(C−1a)
など酸性タイプのフラワーペースト向け乳化剤としての
機能は劣っていた。
As shown in the evaluation results, T-1a to T2 of the production example
b was obtained with good results in terms of shape retention and oil-off evaluation, and was judged to be a suitable material as an emulsifier for acidic type flower paste. One Comparative Example C-1
In cases a to c, oil separation occurs during heating and stirring during paste preparation, and the paste itself cannot be prepared (C
-1b, c), the firing resistance of the paste is low (C-1a)
The function as an emulsifier for acidic type flower paste was poor.

【0056】[0056]

【発明の効果】本発明により、大豆蛋白中の7S成分
(β−コングリシニン)及び11S成分(グリシニン)
由来の蛋白加水分解物(ポリペプチド)の製造に関し
て、分画操作を必要とすることなく分画操作処理品と同
等以上の優れた乳化力及び起泡力を持つ大豆蛋白加水分
解物を調製することが可能となり、歩留まりや生産性を
格段に改善できるようになった。
INDUSTRIAL APPLICABILITY According to the present invention, 7S component (β-conglycinin) and 11S component (glycinin) in soybean protein
Regarding the production of protein hydrolyzate (polypeptide) derived from soybean, a soybean protein hydrolyzate having excellent emulsifying power and foaming power equal to or higher than that of the fractionated product is prepared without the need for fractionation It has become possible to significantly improve yield and productivity.

───────────────────────────────────────────────────── フロントページの続き (72)発明者 岩岡 栄治 茨城県筑波郡谷和原村絹の台4丁目3番地 不二製油株式会社つくば研究開発センタ ー内   ─────────────────────────────────────────────────── ─── Continued front page    (72) Inventor Eiji Iwaoka             4-3 Kinindai, Taniwahara Village, Tsukuba-gun, Ibaraki Prefecture               Fuji Oil Co., Ltd. Tsukuba Research and Development Center             -In

Claims (9)

【特許請求の範囲】[Claims] 【請求項1】大豆蛋白の加水分解を行うにおいて、先ず
大豆蛋白中の7S成分(β−コングリシニン)または1
1S成分(グリシニン)のいずれかを選択的に加水分解
し、次いで未分解の画分を更に加水分解することで7S
成分および11S成分の両方の加水分解物を得、これを
pH4.3以下、100℃以上の条件で加熱処理を施すことを
特徴とする大豆蛋白加水分解物の製造方法。
1. When hydrolyzing soybean protein, first, the 7S component (β-conglycinin) or 1 in soybean protein is used.
By selectively hydrolyzing any of the 1S component (glycinin) and then further hydrolyzing the undegraded fraction, 7S
A method for producing a soybean protein hydrolyzate, characterized in that a hydrolyzate of both the ingredient and the 11S ingredient is obtained, and this is subjected to heat treatment under conditions of pH 4.3 or lower and 100 ° C or higher.
【請求項2】加水分解物の加熱処理前にフィターゼを用
いて大豆由来の混在するフィチン酸の低フィチン化を行
う、請求項1記載の大豆蛋白加水分解物の製造方法。
2. The method for producing a soybean protein hydrolyzate according to claim 1, wherein a phytase is used to reduce the phytic acid mixed with phytic acid derived from soybean before the heat treatment of the hydrolyzate.
【請求項3】加水分解物の加熱処理をする前に、加水分
解物の固形物重量に対してキトサンを0.1〜10重量%添
加した後、加熱処理を施す請求項1または2記載の大豆
蛋白加水分解物の製造方法。
3. The soybean protein according to claim 1 or 2, wherein before the heat treatment of the hydrolyzate, 0.1 to 10% by weight of chitosan is added to the solid weight of the hydrolyzate and then the heat treatment is performed. Method for producing hydrolyzate.
【請求項4】低変性大豆蛋白を原料とし、選択的加水分
解が、大豆蛋白中の11S成分の選択的加水分解である
請求項1から3のいずれかの製造方法。
4. The production method according to claim 1, wherein the low-denaturation soybean protein is used as a raw material, and the selective hydrolysis is selective hydrolysis of the 11S component in the soybean protein.
【請求項5】選択的加水分解が、反応時間4時間以内、
pH3.0以下、45℃以下で行われる請求項4の製造方
法。
5. The selective hydrolysis is carried out within a reaction time of 4 hours,
The method according to claim 4, which is carried out at pH 3.0 or lower and 45 ° C. or lower.
【請求項6】未分解の画分の加水分解が、45℃を超える
温度またはpH3.0よりも高いpHで実施される請求項
4〜5のいずれかの製造方法。
6. The process according to claim 4, wherein the hydrolysis of the undegraded fraction is carried out at a temperature above 45 ° C. or at a pH higher than pH 3.0.
【請求項7】 低変性大豆蛋白を原料とし、選択的加水
分解が、大豆蛋白中の7S成分の選択的加水分解である
請求項1から3のいずれかの製造方法。
7. The method according to claim 1, wherein the low-denaturation soybean protein is used as a raw material, and the selective hydrolysis is selective hydrolysis of the 7S component in the soybean protein.
【請求項8】選択的加水分解が、反応時間2時間以内、
pH3.0より高いpH、50℃以上で行われる請求項7の
製造方法。
8. The selective hydrolysis is carried out within a reaction time of 2 hours,
The method according to claim 7, which is carried out at a pH higher than pH 3.0 and at 50 ° C. or higher.
【請求項9】 未分解の画分の加水分解が、45℃以下の
温度、pH3.0以下で行われる請求項8の製造方法。
9. The method according to claim 8, wherein the hydrolysis of the undecomposed fraction is carried out at a temperature of 45 ° C. or lower and a pH of 3.0 or lower.
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Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2005063039A1 (en) * 2003-12-26 2005-07-14 Fuji Oil Company, Limited Creams, whipped products thereof, dry powders thereof and process for producing the same
WO2006038413A1 (en) * 2004-09-30 2006-04-13 Fuji Oil Company, Limited Egg food material or processed egg product
JP2006212346A (en) * 2005-02-07 2006-08-17 Tsugio Baba Extinguishing agent, extinguisher and fire retardant, flame retardant sheet, and flame retardant fiber
WO2015122424A1 (en) * 2014-02-12 2015-08-20 不二製油株式会社 Egg replacement for spongy food

Citations (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS63216437A (en) * 1987-03-06 1988-09-08 Japanese Res & Dev Assoc Bio Reactor Syst Food Ind Production of hydrolyzed gluten
JPS6430544A (en) * 1987-07-24 1989-02-01 Shichiro Niwano Preparation of expanded food
JP2001069920A (en) * 1998-07-29 2001-03-21 Fuji Oil Co Ltd Soybean protein hydrolyzate, its production and product using the same

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS63216437A (en) * 1987-03-06 1988-09-08 Japanese Res & Dev Assoc Bio Reactor Syst Food Ind Production of hydrolyzed gluten
JPH0679541B2 (en) * 1987-03-06 1994-10-12 日清製粉株式会社 Method for producing hydrolyzed gluten
JPS6430544A (en) * 1987-07-24 1989-02-01 Shichiro Niwano Preparation of expanded food
JP2001069920A (en) * 1998-07-29 2001-03-21 Fuji Oil Co Ltd Soybean protein hydrolyzate, its production and product using the same

Cited By (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO2005063039A1 (en) * 2003-12-26 2005-07-14 Fuji Oil Company, Limited Creams, whipped products thereof, dry powders thereof and process for producing the same
WO2006038413A1 (en) * 2004-09-30 2006-04-13 Fuji Oil Company, Limited Egg food material or processed egg product
JP2006212346A (en) * 2005-02-07 2006-08-17 Tsugio Baba Extinguishing agent, extinguisher and fire retardant, flame retardant sheet, and flame retardant fiber
JP4630682B2 (en) * 2005-02-07 2011-02-09 二夫 馬場 Fire extinguisher, fire extinguisher and flame retardant, flame proof sheet, flame retardant fiber
WO2015122424A1 (en) * 2014-02-12 2015-08-20 不二製油株式会社 Egg replacement for spongy food
JPWO2015122424A1 (en) * 2014-02-12 2017-03-30 不二製油株式会社 Sponge food egg substitute

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