JP3432260B2 - Food physical property improver containing fractionated concentrate of water soluble protein of fish meat as main component - Google Patents

Food physical property improver containing fractionated concentrate of water soluble protein of fish meat as main component

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Publication number
JP3432260B2
JP3432260B2 JP31099293A JP31099293A JP3432260B2 JP 3432260 B2 JP3432260 B2 JP 3432260B2 JP 31099293 A JP31099293 A JP 31099293A JP 31099293 A JP31099293 A JP 31099293A JP 3432260 B2 JP3432260 B2 JP 3432260B2
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JP
Japan
Prior art keywords
gel
protein
food
water
fish meat
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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JP31099293A
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Japanese (ja)
Other versions
JPH07123925A (en
Inventor
宏樹 山本
郁夫 木村
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.)
Nippon Suisan KK
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Nippon Suisan KK
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Priority to JP31099293A priority Critical patent/JP3432260B2/en
Publication of JPH07123925A publication Critical patent/JPH07123925A/en
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Anticipated expiration legal-status Critical
Expired - Fee Related legal-status Critical Current

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Description

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

【0001】[0001]

【産業上の利用分野】本発明は、魚肉水溶性タンパク質
の分画濃縮物を主要成分とする食品物性改良剤に関する
ものである。さらに詳しくは、本発明はすりみ水晒し液
あるいは魚肉水抽出物からの魚肉水溶性タンパク質分画
濃縮物を主要成分とするタンパク質ゲル状食品の物性改
良剤、すりみ練り製品用ゲル増強剤などのタンパク質食
品物性改良剤に関するものである。
BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a food property improving agent containing a fish meat water-soluble protein fractionated concentrate as a main component. More specifically, the present invention relates to a physical property improver for protein gel-like foods containing a fish meat water-soluble protein fraction concentrate from a ground water bleaching solution or a fish meat water extract as a main component, a gel enhancer for a ground product, etc. The present invention relates to a protein food property improving agent.

【0002】[0002]

【従来の技術】魚類は、一般に、一時期に大量に漁獲さ
れることが多く、しかも鮮度低下が速いことから、品質
を保ちながら加工することが求められている。加工処理
法としては、急速冷凍、塩蔵、乾燥、缶詰、すりみ加工
等がある。この中でもすりみ加工法は、タンパク質の機
能を保持した状態で保存することを可能にした点で画期
的であると言える。すなわち、従来の技術では、鮮度低
下が速くミールなどにしか加工しきれなかった栄養豊富
な魚から、すりみ加工技術を使うことによってカマボコ
ゲル形成性を保持した機能性タンパク質として応用でき
るようになった訳である。
2. Description of the Related Art In general, fish are often caught in large quantities at one time, and their freshness is rapidly deteriorated. Therefore, it is required to process fish while maintaining their quality. Examples of processing methods include quick freezing, salting, drying, canning, and grinding processing. Among them, the surimi processing method is epoch-making in that it enables preservation while retaining the protein function. In other words, with the conventional technology, it became possible to apply from nutritious fish that could not be processed only to meal etc. because the freshness declined quickly and to use it as a functional protein that retained the kamaboko gel forming property by using the surimi processing technology. It is a translation.

【0003】現在、日本で約50万トンのすりみが消費
されている。すりみ加工法の特徴は、魚肉中の水溶性画
分を水晒しにより除き、これに糖などの冷凍変性防止剤
を混合し、急速凍結することである。魚肉中の水溶性画
分は、蒲鉾ゲル物性を低減させ、また、冷凍保存性を低
下させるために、除去されている。一方、水溶性タンパ
ク質は、魚肉中のタンパク質の約20%にあたり、資源
の有効利用から考えて、水晒しで排出される水溶性タン
パク質の利用法の開発が望まれている。
At present, about 500,000 tons of surimi is consumed in Japan. A characteristic of the surimi processing method is that the water-soluble fraction in fish meat is removed by exposure to water, and a freezing denaturation inhibitor such as sugar is mixed with this to rapidly freeze. The water-soluble fraction in fish meat has been removed in order to reduce the physical properties of kamaboko gel and to reduce the frozen storage stability. On the other hand, water-soluble proteins account for about 20% of proteins in fish meat, and in view of effective utilization of resources, it is desired to develop a method of utilizing water-soluble proteins discharged by exposure to water.

【0004】水晒しすると筋形質タンパク質や脂質など
網状構造形成に寄与しない成分が除かれて、筋原繊維が
濃縮されるため極めて細かく足の強い製品ができるので
あるが、特開平3−27271号公報には、魚肉を処理
加工して魚肉すりみ又は魚肉練製品を製造するに際し
て、魚肉又は魚肉処理排液から抽出される筋漿タンパク
質画分とカルシウム塩を用いることを特徴とする魚肉の
処理加工法が記載されており、、すりみの水晒し工程で
除かれる水溶性タンパク質の中にカマボコゲルのゲル強
度を増大させる成分を含むことが示され、水晒しで除去
される水溶性タンパク質の全てが、必ずしもゲル形成阻
害因子でないことが確認された。
When exposed to water, components that do not contribute to the formation of a network structure, such as myoplasmic proteins and lipids, are removed, and myofibrils are concentrated, so that an extremely fine and strong product can be produced. JP-A-3-27271 The publication discloses that when a fish meat is processed to produce a fish meat paste or a fish meat paste product, a muscle protein fraction extracted from a fish meat or a fish meat treatment effluent and a calcium salt treatment are used. The processing method is described, it is shown that the water-soluble protein removed in the water exposure step of surimi contains a component that increases the gel strength of kamaboko gel, and all the water-soluble proteins removed by water exposure Was confirmed to be not necessarily a gel formation inhibitor.

【0005】[0005]

【発明が解決しようとする課題】本発明は、水晒し等で
排出される水溶性タンパク質を食品物性改良剤として有
効利用することを目的とする。本発明は、すりみ水晒し
液あるいは魚肉水抽出物から、本来水晒し等で取り除く
べき水溶性タンパク質、すなわち熱変性時にアクトミオ
シンに凝集する性質のある水溶性タンパク質(以下、
「ゲル形成阻害因子」と称することもある。)を分離
し、そほかの本来水晒し等で取り除くべきでない有効な
水溶性タンパク質(以下、「ゲル形成促進因子」と称す
ることもある。)を濃縮して食品物性改良剤として食品
原料に戻して利用しようとするものである。さらに本発
明は、ゲル形成促進因子を濃縮しゲル形成阻害因子を少
なくして原料に戻す際、そのゲル形成促進作用を強め、
必要によりゲル形成阻害作用を弱めて食品物性改良剤と
して食品原料に戻そうとするものである。
SUMMARY OF THE INVENTION It is an object of the present invention to effectively use a water-soluble protein discharged by exposure to water as a food property improving agent. The present invention is a water-soluble protein that should be removed by water exposure or the like, that is, a water-soluble protein having the property of aggregating to actomyosin during heat denaturation (hereinafter,
It may also be referred to as "gel formation inhibitor". ) Is separated, and effective water-soluble proteins that should not be removed by other means such as exposure to water (hereinafter also referred to as "gel formation promoting factor") are concentrated and returned to food materials as food property improving agents. Is intended to be used. Furthermore, the present invention enhances the gel formation promoting action when the gel formation promoting factor is concentrated and the gel formation inhibiting factor is reduced and returned to the raw material,
If necessary, the gel formation inhibitory effect is weakened to return to a food material as a food property improving agent.

【0006】本発明は、魚肉から抽出される水溶性タン
パク質、および、すりみの水晒し工程で排出される水溶
性タンパク質からタンパクゲル食品の物性改良作用を示
す有用タンパク質を分画し濃縮した、ゲル形成阻害作用
を示すタンパク質を実質的に含有せず、ゲル形成促進作
用を示す有用タンパク質を高濃度で含有する魚肉水溶性
タンパク質分画濃縮物を主要成分とする食品物性改良剤
並びにそのゲル形成促進作用に関する物性を改良した食
品物性改良剤の提供を目的とする。
[0006] The present invention fractionates and concentrates a useful protein having an action of improving physical properties of a protein gel food from a water-soluble protein extracted from fish meat and a water-soluble protein discharged in the step of exposing ground bean to water, An agent for improving physical properties of foods, which mainly contains a fish meat water-soluble protein fraction concentrate containing a high concentration of a useful protein exhibiting a gel formation-promoting action and substantially free of a protein exhibiting a gel formation-inhibiting action, and its gel formation It is an object of the present invention to provide a food physical property improving agent having improved physical properties relating to a promoting action.

【0007】[0007]

【課題を解決するための手段】タンパク質の濃縮方法に
は、イオン交換法、ゲル濾過法、硫安分画法など種々の
方法があるが、すりみ水晒しは本来ゲル形成阻害因子を
取り除く処理であることからも明らかであるが、すりみ
水晒し液あるいは、魚肉水抽出物に含有される水溶性タ
ンパク質の中にはゲル形成阻害因子が多く含有されてお
り、すりみ水晒し液等に存在する魚肉水溶性タンパク質
を資源的に有効利用しようとすることは無意味であると
考えられ、したがって、魚肉水溶性タンパク質の資源の
有効利用の観点からこれらのタンパク質の濃縮方法をす
りみ水晒し液あるいは、魚肉水抽出物に適用することは
これまで考えすらされなかった。すなわち、すりみ水晒
し液あるいは、魚肉水抽出物からゲル形成阻害因子を選
択的に除去し、ゲル形成促進因子を選択的に濃縮しよう
とすることについてはこれまで課題すらなかった。
[Means for Solving the Problems] There are various methods such as an ion exchange method, a gel filtration method, and an ammonium sulfate fractionation method for protein concentration. As is clear from the fact that the water-soluble protein contained in the water-extracted surimi or the water extract of fish meat contains many gel-formation-inhibitory factors, it is present in the water-exposed liquid etc. It is considered meaningless to try to effectively utilize the fish meat water-soluble protein as a resource. Therefore, from the viewpoint of effective utilization of the fish meat water-soluble protein resource, a method for concentrating these proteins is used as a water-exposing solution. Alternatively, its application to fish meat water extracts has never even been considered. That is, there has been no problem up to now in order to selectively remove the gel formation inhibiting factor and selectively concentrate the gel formation promoting factor from the ground water exposure solution or the fish meat water extract.

【0008】したがって、すりみ水晒し液あるいは、魚
肉水抽出物からゲル形成促進因子を選択的に濃縮し、ゲ
ル形成阻害因子を選択的に除去する食品科学的な製造方
法は知られていない。本発明においてすりみ水晒し液か
らエタノール分画法、酸性pH沈殿法によりタンパクゲ
ル形成阻害因子の一部が除去され、ゲル形成促進因子が
濃縮されること、また、カルシウム塩の共存下でゲル形
成促進効果が増大すること、さらに、プロテアーゼイン
ヒビターを含む食品を添加することにより分画濃縮物に
除去されずに含まれるゲル形成阻害因子の作用を抑制
し、ゲル形成促進効果が増大することを見いだし、本発
明を完成するに至った。
[0008] Therefore, there is no known food-scientific production method for selectively concentrating the gel formation promoting factor and selectively removing the gel formation inhibiting factor from the ground water exposure solution or the fish meat water extract. In the present invention, a part of the protein gel formation-inhibiting factor is removed from the squeezed water soaked solution by the ethanol fractionation method and the acidic pH precipitation method to concentrate the gel formation promoting factor, and the gel is coexisted in the presence of calcium salt. The formation-promoting effect is increased, and further, the addition of a food containing a protease inhibitor suppresses the action of the gel-formation-inhibitory factor contained in the fraction concentrate without being removed, thereby increasing the gel-formation-promoting effect. They have found the present invention and completed the present invention.

【0009】本発明において、すりみ水晒し液、また
は、魚肉水抽出物からのゲル形成促進因子が濃縮される
エタノール濃度としては、50%エタノール飽和濃度ま
で認められるが、好ましくは、30%飽和濃度付近で高
活性沈殿物として回収される。
In the present invention, as the ethanol concentration at which the gel formation promoting factor from the ground water exposure solution or fish meat water extract is concentrated, 50% ethanol saturation concentration is recognized, but preferably 30% saturation. It is recovered as a highly active precipitate near the concentration.

【0010】また、酸性pH処理法では、食品製造上使
用可能な酢酸、クエン酸、りん酸、塩酸などの酸を用い
て、魚肉水抽出物、すりみ水晒し液のpHを酸性とし、
ゲル形成促進因子を沈殿させて高活性で濃縮することが
出来る。pHが、6.5〜5.0にかけてゲル形成促進
因子が沈殿として回収されるが、好ましくはpH5.5
〜5.2にかけて高濃度で回収される。pH4.5以下
では、ゲル形成促進因子の失活が認められ好ましくな
い。
In the acidic pH treatment method, acids such as acetic acid, citric acid, phosphoric acid and hydrochloric acid which can be used in food production are used to make the pH of the fish meat water extract and the ground water exposure solution acidic.
The gel formation promoting factor can be precipitated and concentrated with high activity. Although the gel formation promoting factor is recovered as a precipitate when the pH is 6.5 to 5.0, it is preferably pH 5.5.
It is recovered in a high concentration from ˜5.2. At a pH of 4.5 or less, inactivation of the gel formation promoting factor is observed, which is not preferable.

【0011】さらに、始めに酸性pHでゲル形成因子を
沈殿として回収した後、回収された沈殿物中の夾雑タン
パク質を除くために、再溶解し、これに適量のエタノー
ルを添加して再精製を行っても、さらに高活性のゲル促
進物質が回収できる。
Furthermore, first, the gel-forming factor is recovered as a precipitate at an acidic pH, and then it is redissolved in order to remove contaminating proteins in the recovered precipitate, and an appropriate amount of ethanol is added thereto for repurification. Even if it goes, a gel stimulant having higher activity can be recovered.

【0012】回収されたゲル形成促進因子の作用を増大
させるために、乳酸カルシウム、塩化カルシウム、硫酸
カルシウムなどの各種のカルシウム塩を0.01〜0.
2%程度、好ましくは、0.1%程度添加すると効果が
みられる。
In order to enhance the action of the recovered gel formation promoting factor, various calcium salts such as calcium lactate, calcium chloride and calcium sulfate are added in an amount of 0.01 to 0.
The effect can be seen by adding about 2%, preferably about 0.1%.

【0013】さらに、食品中にプロテアーゼインヒビタ
ーを含む食品、例えば、卵白、乳清タンパク質、血漿タ
ンパク質、大豆抽出物、ジャガイモ抽出物、各種植物の
葉抽出物などを回収されたゲル形成促進因子に混合する
ことによってもゲル形成促進効果の増大が認められる。
これらのプロテアーゼインヒビターを含む食品を単独、
あるいは混合して使用してもかまわない。また、ここに
示したプロテアーゼインヒビターを含む食品だけに、限
定するものではない。
Further, food containing a protease inhibitor in the food, for example, egg white, whey protein, plasma protein, soybean extract, potato extract, leaf extract of various plants, etc. is mixed with the recovered gel formation promoting factor. By doing so, the gel formation promoting effect is also increased.
Foods containing these protease inhibitors alone,
Alternatively, they may be mixed and used. Further, the present invention is not limited to the food containing the protease inhibitor.

【0014】本発明で得られるゲル形成促進因子(物
質)を含むものは、各種のたん白食品の物性改良剤とし
ての応用が可能である。例えば、各種の魚肉すりみ、オ
キアミタンパク質などを主成分にした蒲鉾などの各種練
り製品、畜肉ハム、ソーセージ、乳タンパク質を主成分
にしたヨーグルト、チーズなどの乳製品、大豆たん白、
小麦たん白などを主成分とした麺、団子などが挙げられ
る。本発明でゲル形成促進物の抽出に使用される魚肉と
しては、スケトウダラ、グチ、ホキ、ミナミダラ、マイ
ワシ、イトヨリ、キンメ、マアジ、コイなどであるが、
この限りではない。
The substance containing the gel formation promoting factor (substance) obtained in the present invention can be applied as a physical property improving agent for various protein foods. For example, various ground fish meat, various kneaded products such as kamaboko whose main component is krill protein, meat ham, sausage, yogurt whose main component is milk protein, dairy products such as cheese, soy protein,
Examples include noodles and dumplings containing wheat protein as a main component. Examples of the fish meat used for extracting the gel formation promoter in the present invention include walleye pollock, crocodile, hoki, minamidara, sardine, sardine, quince, horse mackerel, carp, and the like.
Not limited to this.

【0015】本発明で得られるゲル形成促進物質のSD
S−ポリアクリルアミド電気泳動分析を行うと、まだ多
数のバンドが認められ、タンパク質として完全に精製さ
れてはいないが、分離されたタンパク質の比率、ゲル形
成促進活性の増大から食品のゲル物性改良剤として応用
可能である。
SD of the gel formation promoting substance obtained in the present invention
When S-polyacrylamide electrophoresis analysis was carried out, many bands were still observed, and although it was not completely purified as a protein, the ratio of separated proteins and the increase in gel formation promoting activity resulted in an improvement in the gel physical property of foods. Can be applied as.

【0016】したがって、本発明で得られるゲル形成促
進物質をタンパク質の一成分として特定は出来ないが、
例えば、魚肉に含まれる酵素として、各タンパク質を結
合させる作用のあるトランスグルタミナーゼ(以下、
「TGase」と略することもある。)もゲル形成促進
作用を示すので、ゲル形成促進物質の中の促進作用を示
す成分群の一成分として含まれると考えることも出来
る。
Therefore, although the gel formation promoting substance obtained in the present invention cannot be specified as one component of protein,
For example, as an enzyme contained in fish meat, transglutaminase (hereinafter,
It may be abbreviated as "TGase". ) Also has a gel formation promoting action, it can be considered to be included as one component of the component group showing a promoting action in the gel formation promoting substance.

【0017】本発明では、ゲル形成促進物質の性状の測
定にTGase活性を一部指標として利用しているが、
ゲル形成促進物質がTGase酵素であると限定してい
るわけではない。
In the present invention, the TGase activity is used as a part of the index for measuring the properties of the gel formation promoting substance.
The gel formation promoter is not limited to the TGase enzyme.

【0018】ゲル形成促進活性の測定法 魚肉から抽出した塩溶性タンパク質のアクトミオシンの
ゲル化を指標とした試験管倒置法により測定した。アク
トミオシンのゲル化の程度を判定するゲル形成試験の一
般的な反応組成は、7〜10mg/mlスケトウダラア
クトミオシン、0.3M NaCl、25mM Tri
s−HCl(pH7.5)、8%ソルビトールとし、こ
れに適当量のゲル形成促進物質を添加して行った。反応
は、30℃で2時間行い、ゲル化の程度は、試験管を倒
置したときのゲルの状態から判定し、次のように表し
た。 (−) :倒置するとすぐ流れだしゲル化していない
状態 (−+) :倒置しても形を保っているが、弱い振動を
加えると崩れてしまうゲル化の程度が弱い状態 (+) :倒置しても形を保っているが、強い振動を
加えるとやや形が崩れるゲル化の程度の強い状態 (++) :倒置しても形を保っていて、強い振動を加
えても形が崩れないゲル化の程度の非常に強い状態 (+++):(++)よりも強いゲル化状態を示すもの
Method for measuring gel formation accelerating activity It was measured by a test tube inversion method using the gelation of actomyosin, a salt-soluble protein extracted from fish meat, as an index. The general reaction composition of the gel formation test to determine the degree of gelation of actomyosin is 7 to 10 mg / ml walleye pollack actomyosin, 0.3M NaCl, 25 mM Tri.
s-HCl (pH 7.5) and 8% sorbitol were used, and an appropriate amount of a gel formation promoting substance was added thereto. The reaction was carried out at 30 ° C. for 2 hours, and the degree of gelation was judged from the state of the gel when the test tube was inverted, and expressed as follows. (-): Immediately when inverted, it starts to flow and does not gel (-+): It retains its shape even when inverted, but collapses when weak vibration is applied. The degree of gelation is weak (+): Inversion Even if it keeps its shape, it loses its shape a little when strong vibration is applied. Strong state of gelation (++): It keeps its shape even when it is placed upside down, and does not lose its shape even when strong vibration is applied. Very strong gelation state (++): A gelation state stronger than (++)

【0019】トランスグルタミナーゼ活性測定法 TAKAGIらの方法(Analytical Bio
chem.135,295−298(1986))に準
じて、TGaseの作用により、アセチル化カゼインに
モノダンシルカダベリンが取り混まれると蛍光強度が増
大するので、この変化を測定することによりTGase
活性を求めた。一般的な、反応組成は、終濃度6.6m
M CaCl,50mM Tris−HCL(pH
7.5),4.5mM DTT,2mg/mlアセチル
化カゼイン、10μMモノダンシルカダベリン及び適当
量のゲル形成促進物質で活性測定を行った。反応は、モ
ノダンシルカダベリンを添加して開始し、30℃で1時
間または2時間反応を行い、最後にEDTAを添加して
反応を停止した。濁りのある場合は、遠心あるいは、濾
過をして除いた。反応液の蛍光強度は、Ex.350n
m,Em.480nmにて測定した。活性は、相対強度
△FIで表した。
Method for measuring transglutaminase activity TAKAGI et al. (Analytical Bio)
chem. 135,295-298 (1986)), the fluorescence intensity increases when monodansyl cadaverine is mixed into acetylated casein by the action of TGase. Therefore, by measuring this change, TGase
The activity was sought. The general reaction composition is 6.6 m final concentration.
M CaCl 2 , 50 mM Tris-HCL (pH
7.5), 4.5 mM DTT, 2 mg / ml acetylated casein, 10 μM monodansyl cadaverine and an appropriate amount of gel formation promoting substance were used for activity measurement. The reaction was started by adding monodansyl cadaverine, followed by reaction at 30 ° C. for 1 hour or 2 hours, and finally by adding EDTA to stop the reaction. If it was turbid, it was removed by centrifugation or filtration. The fluorescence intensity of the reaction solution is Ex. 350n
m, Em. It was measured at 480 nm. The activity was represented by relative intensity ΔFI.

【0020】[0020]

【実施例】本発明を実施例で詳しく説明する。本発明
は、実施例によって何ら限定されない。
EXAMPLES The present invention will be described in detail with reference to Examples. The present invention is in no way limited by the examples.

【0021】参考例1 魚肉水溶性タンパク質の分画濃縮物の製造 −50℃で凍結保存したクログチの筋肉を細切後、2倍
量の水を加えてホモジナイズをした。これを7000x
G,20分間遠心分離後、上清をガーゼ、脱脂綿濾過を
行い、濾過液(10.4kg)を、水抽出物として得
た。クログチ筋肉水抽出物の性状を表1に示した。
Reference Example 1 Production of Fraction Concentrate of Water-Soluble Protein of Fish Meat The muscle of crocodile frozen and stored at -50 ° C was shredded, and homogenized by adding twice the amount of water. 7000x this
After centrifugation at G for 20 minutes, the supernatant was filtered with gauze and absorbent cotton to obtain a filtrate (10.4 kg) as a water extract. The properties of the crocodile muscle water extract are shown in Table 1.

【0022】[0022]

【表1】 [Table 1]

【0023】上記クログチ筋肉水抽出物に10〜50%
飽和濃度になるように冷エタノールを添加し、一定時間
氷冷中に保持した後、遠心分離をして上清と沈殿に分
け、沈殿画分の量、アクトミオシンのゲル化能、TGa
se活性を測定した。その結果、アクトミオシンのゲル
化を促進する因子は、約10%〜40%エタノール濃度
内で、沈殿し、ゲル化能は++〜+++を示し、TGa
se活性は、水抽出物の3〜4倍に向上した。沈殿物量
は、10〜30%画分で水抽出物重量の約18%が回収
された。
10 to 50% of the above-mentioned crocodile muscle water extract
Cold ethanol was added to a saturated concentration, and the mixture was kept in ice-cooling for a certain period of time, and then centrifuged to separate into a supernatant and a precipitate. The amount of the precipitated fraction, the gelling ability of actomyosin, and TGa
The se activity was measured. As a result, the factor that promotes the gelation of actomyosin was precipitated in the ethanol concentration of about 10% to 40%, and the gelling ability showed ++ to ++, and TGa
The se activity was 3 to 4 times higher than that of the water extract. The amount of precipitate was 10 to 30%, and about 18% of the weight of the water extract was recovered.

【0024】実施例1 参考例1の方法に準じて、クログチ筋肉水抽出物約4リ
ットルに30%のエタノールを加え、沈殿物を回収し
た。この沈殿物は、アクトミオシンゲル化能+++、T
Gase活性△FI=132と高い値を示した。この沈
殿物をスケトウダラすりみに対して重量比7.5%添加
し、これに3%食塩、30%加水を行い、擂潰後、ポリ
塩化ビニリデンンチューブに充填し、90℃40分、あ
るいは、30℃1時間坐り処理後、90℃40分間ボイ
ルしたものを、カマボコゲルとして試作した。なお、対
照として、エタノール沈殿物の替わりに水を添加したも
のを用いた。この時、何れのカマボコにも0.1%の乳
酸カルシウムを添加した。坐り処理をしないで直接90
℃40分間ボイルしたものをコントロールゲル(Cゲ
ル)、坐り処理をしたものを(Sゲル)としてゲル強度
を表2に示した。クログチ筋肉水抽出物のエタノール沈
殿物を添加した蒲鉾のゲル強度は、対照としたものよ
り、Cゲルで150,Sゲルで400も高い値を示し
た。
Example 1 According to the method of Reference Example 1, 30% ethanol was added to about 4 liters of crocodile muscle water extract, and the precipitate was recovered. This precipitate has an actomyosin gelation ability +++, T
Gase activity ΔFI = 132, which was a high value. To the walleye pollack surimi, 7.5% by weight of this precipitate was added, 3% sodium chloride and 30% water were added thereto, and after crushing, filled in a polyvinylidene chloride tube, 90 ° C. for 40 minutes, or After sitting at 30 ° C. for 1 hour and boiled at 90 ° C. for 40 minutes, it was prototyped as a kamaboko gel. As a control, water was added instead of the ethanol precipitate. At this time, 0.1% calcium lactate was added to each of the scorpions. 90 without sitting
The gel strength is shown in Table 2 with the control gel (C gel) as boiled at 40 ° C for 40 minutes and the (S gel) as seated. The gel strength of the kamaboko, to which the ethanol precipitate of the crocodile muscle water extract was added, was 150 and 400 gels, respectively, higher than those of the control.

【0025】[0025]

【表2】 [Table 2]

【0026】参考例2 魚肉水溶性タンパク質の分画濃縮物製造例 シログチすりみ水晒し排液を遠心分離し、夾雑する筋原
繊維タンパク質を除去した上清液に、pH調製剤として
酢酸を氷冷下で滴下し、pHを6.5から4.0に調整
した。その時に沈殿として回収される区分のアクトミオ
シンゲル化促進能とTGase活性を測定した結果を表
3に示した。pH5.5付近でゲル形成促進因子が沈殿
濃縮されることが認められる。また、pH5よりも低い
pH下では、ゲル形成促進物質の失活が推察される。
Reference Example 2 Production Example of Fraction Concentrate of Fish Meat Water-Soluble Protein Silogchi Surimi Exposed to water, the drainage was centrifuged to remove contaminating myofibrillar protein, and acetic acid as a pH adjuster was added to the supernatant. The mixture was added dropwise under cold conditions, and the pH was adjusted to 6.5 to 4.0. Table 3 shows the results of measuring the actomyosin gelation-promoting ability and TGase activity of the section collected as a precipitate at that time. It is observed that the gel formation promoting factor is concentrated in the vicinity of pH 5.5. Further, at a pH lower than pH 5, deactivation of the gel formation promoting substance is presumed.

【0027】[0027]

【表3】 [Table 3]

【0028】実施例2 シログチすりみ水晒し排液を遠心分離し、夾雑する筋原
繊維タンパク質を除去した上清液に、pH調整剤として
酢酸を氷冷下で滴下し、pHを5.5に調整した後、遠
心分離して沈殿物を回収した。この沈殿物はアクトミオ
シンゲル化能+++、TGase活性△FI=115と
高い値を示した。この沈殿物をスケトウダラすりみに対
して重量比2.5%添加し、これに3%食塩、30%加
水を行い、擂潰後、ポリ塩化ビニリデンチューブに充填
し、90℃で40分、あるいは30℃1時間坐り処理
後、90℃40分間ボイルしたものを、カマボコゲルと
して試作した。なお、対照として、pH5.5沈殿物の
替わりに水を添加したものを用いた。この時、何れのカ
マボコにも0.1%の乳酸カルシウムを添加した。坐り
処理をしないで直接90℃40分間ボイルしたものをコ
ントロールゲル(Cゲル)、坐り処理をしたものを(S
ゲル)としてゲル強度を表4に示した。シログチすりみ
水晒し排液のpH5.5沈殿物を添加した蒲鉾のゲル強
度は、対照としたものよりも、Cゲルで62、Sゲルで
は286も高い値を示した。
Example 2 Acetic acid as a pH adjusting agent was added dropwise under ice cooling to the supernatant liquid obtained by removing the contaminating myofibrillar protein by centrifuging the drainage solution that had been exposed to shirochi ground water, and the pH was adjusted to 5.5. After adjusting to, the mixture was centrifuged to collect the precipitate. This precipitate showed high values of actomyosin gelation ability +++ and TGase activity ΔFI = 115. 2.5% of the weight ratio of this precipitate with respect to walleye pollack is added, 3% sodium chloride and 30% water are added to this, and after crushing, filled into a polyvinylidene chloride tube, 40 minutes at 90 ° C., or After sitting at 30 ° C. for 1 hour and boiled at 90 ° C. for 40 minutes, a trial product was prepared as a kamaboko gel. As a control, a solution to which water was added instead of the pH 5.5 precipitate was used. At this time, 0.1% calcium lactate was added to each of the scorpions. The control gel (C gel) was boiled directly at 90 ° C for 40 minutes without sitting, and the sitting gel was used (S
The gel strength as a gel is shown in Table 4. The gel strength of the Kamaboko to which the pH 5.5 precipitate of the wastewater exposed to water of Shiroguchi ground bean was added was 62 in the C gel and 286 in the S gel, which were higher than those in the control.

【0029】[0029]

【表4】 [Table 4]

【0030】参考例3 魚肉水溶性タンパク質の分画濃縮物製造例 スケトウダラすりみ水晒し排液に含まれる筋原繊維タン
パク質を遠心分離で除去後、得られる上清液に、適当量
の酢酸を滴下し、形成する沈殿画分を遠心分離法で回収
した。沈殿物のアクトミオシンゲル化促進能とTGas
e活性を表5に示した。グチ筋肉よりTGase活性が
低いのにもかかわらずpH沈殿法で沈殿する画分にアク
トミオシンのゲル化促進作用が確認できた。
Reference Example 3 Production Example of Fraction Concentrate of Fish Meat Water-Soluble Protein After removing the myofibrillar protein contained in the effluent exposed to Alaska pollack groundwater by centrifugation, an appropriate amount of acetic acid was added to the resulting supernatant. The resulting precipitate fraction was added dropwise and collected by centrifugation. Actomyosin gelation promoting ability of precipitates and TGas
The e activity is shown in Table 5. Although the TGase activity was lower than that of the goat muscle, the gelation promoting action of actomyosin was confirmed in the fraction precipitated by the pH precipitation method.

【0031】[0031]

【表5】 [Table 5]

【0032】実施例3 シログチすりみ水晒し排液を遠心分離し、夾雑する筋原
繊維タンパク質を除去した上清液に、30%飽和濃度に
なるように冷エタノールを添加し、一定時間氷冷中で保
持した後、遠心分離して沈殿物を回収した。この沈殿物
は、アクトミオシンゲル化能+++、TGase活性△
FI=118と高い値を示した。この沈殿物と、沈殿物
に対して、乳酸カルシウムを重量比2%、プロテアーゼ
インヒビターである血漿タンパク加水分解物を重量比4
%で混合し、魚肉水溶性タンパク質分画濃縮物とカルシ
ウム塩、プロテアーゼインヒビターの混合物を得た。こ
の混合物を、スケトウダラすりみに対して重量比5.0
%添加し、これに3%食塩、30%加水を行い、擂潰
後、ポリ塩化ビニリデンチューブに充填し、90℃40
分、あるいは、30℃1時間坐り処理後、90℃40分
間ボイルしたものを、カマボコゲルとして試作した。な
お、対照として、この混合物の替わりに水を添加したも
のを用いた。坐り処理をしないで直接90℃40分間ボ
イルしたものをコントロールゲル(Cゲル)、坐り処理
をしたものを坐りゲル(Sゲル)としてゲル強度を表6
に示した。シログチすりみ水晒し排液のエタノール沈殿
物と、カルシウム塩およびプロテアーゼインヒビターの
混合物を添加した蒲鉾のゲル強度は、対照としたものよ
り、Cゲルで60、Sゲルで390も高い値を示した。
Example 3 Shiroguchi ground water exposure Exudate after exposure to water was centrifuged, and contaminated myofibrillar protein was removed. To the supernatant, cold ethanol was added to a saturated concentration of 30% and ice-cooled for a certain period of time. After holding in, it was centrifuged to collect the precipitate. This precipitate has actomyosin gelation ability +++ and TGase activity Δ
FI = 118, which was a high value. 2% by weight of calcium lactate and 4% by weight of plasma protein hydrolyzate, which is a protease inhibitor, with respect to this precipitate.
% To obtain a mixture of the fish meat water-soluble protein fraction concentrate, calcium salt, and protease inhibitor. A weight ratio of this mixture to Alaska pollack ground is 5.0.
%, Add 3% sodium chloride and 30% water to this, crush and fill a polyvinylidene chloride tube at 90 ° C 40
Minutes, or sitting at 30 ° C. for 1 hour and boiled at 90 ° C. for 40 minutes to make a trial product as a kama-kogo gel. As a control, water was added instead of this mixture. The gel strength was determined by using the control gel (C gel) that was boiled directly at 90 ° C. for 40 minutes without sitting treatment, and the sitting gel (S gel) that was subjected to sitting treatment.
It was shown to. The gel strength of the ethanol precipitate of the bleached groundwater exposure effluent and the kamaboko added with the mixture of the calcium salt and the protease inhibitor was 60 in the C gel and 390 in the S gel, which were higher than those in the control. .

【0033】[0033]

【表6】 [Table 6]

【0034】[0034]

【発明の効果】従来利用されずに排出されていたすりみ
水晒し排液や魚肉水抽出物中に含まれるゲル形成促進作
用を示す有用タンパク質を食品物性改良剤として有効に
利用することができる。すりみ水晒し排液や魚肉水抽出
物から分離、濃縮して得られた有用タンパク質高濃度含
有液の食品物性改良剤、そのゲル形成促進作用を強め、
必要によりゲル形成阻害作用を弱めた食品物性改良剤を
提供することができる。
EFFECTS OF THE INVENTION Useful proteins, which have not been conventionally used but are exposed to ground water and exposed to ground water, and which have a gel formation promoting action, can be effectively used as a food property improving agent. . Food physical property improving agent of liquid containing high concentration of useful protein obtained by separating and concentrating from wastewater bleaching effluent or fish meat water extract, enhancing its gel formation promoting action,
It is possible to provide a food property-improving agent having a weakened gel formation-inhibiting effect if necessary.

Claims (6)

(57)【特許請求の範囲】(57) [Claims] 【請求項1】 すり身水晒し液あるいは魚肉水抽出物を
pH6.5〜5.0の酸性処理による、あるいは、10
0%エタノール濃度の水−エタノールによる抽出に
よる濃縮処理により、ゲル形成阻害作用を示すタンパク
質の含量が少なく、ゲル形成促進作用を示す有用タンパ
ク質を高濃度で含有する魚肉水溶性タンパク質分画濃縮
物を主要成分とすることを特徴とする食品のゲル形成促
進作用に関する物性の改良剤。
1. A ground water bleaching solution or a fish meat water extract
by acid treatment at pH 6.5 to 5.0, or 10
~ For extraction with water-ethanol at 40 % ethanol concentration
A food product characterized by having a low content of a protein exhibiting a gel formation-inhibiting effect by the concentration treatment by a concentration process and containing a fish meat water-soluble protein fraction concentrate containing a high concentration of a useful protein exhibiting a gel-forming promoting activity as a main component. Of the physical properties of the gel formation promoting action of
【請求項2】 主要成分としてカルシウム塩を併用する
請求項1記載の食品のゲル形成促進作用に関する物性の
改良剤。
2. An agent for improving physical properties of a food according to claim 1, which further comprises a calcium salt as a main component .
【請求項3】 主要成分としてさらに卵白、乳清タンパ
ク質、血漿タンパク質、大豆抽出物、ジャガイモ抽出物
または各種植物の葉抽出物からなるプロテアーゼインヒ
ビターを含む食品成分を併用する請求項2記載の食品の
ゲル形成促進作用に関する物性の改良剤。
3. Egg white and whey tampa as main components
Protein, plasma protein, soybean extract, potato extract
Alternatively, the protease inhibitor consisting of leaf extract of various plants
The agent for improving physical properties of a food according to claim 2, which is used in combination with a food component containing bitter .
【請求項4】 上記の食品がタンパク質食品である請求
項1、請求項2または請求項3記載の食品のゲル形成促
進作用に関する物性の改良剤。
4. The agent for improving physical properties of the food according to claim 1, 2 or 3 wherein the food is a protein food .
【請求項5】 上記のタンパク質食品がタンパク質ゲル
状食品である請求項4記載の食品のゲル形成促進作用に
関する物性の改良剤。
5. The above protein food is a protein gel
The physical property-improving agent for promoting gel formation of the food according to claim 4, which is a food product.
【請求項6】 上記のタンパク質ゲル状食品が練り製品
であり、上記の改良剤がすりみ練り製品用ゲル増強剤で
ある請求項5記載の食品のゲル形成促進作用に関する物
性の改良剤。
6. The above-mentioned protein gel-like food is a paste product.
And the above improver is a gel enhancer for ground paste products.
An agent for improving physical properties of a food according to claim 5, which has an effect of promoting gel formation.
JP31099293A 1993-11-07 1993-11-07 Food physical property improver containing fractionated concentrate of water soluble protein of fish meat as main component Expired - Fee Related JP3432260B2 (en)

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JP3432260B2 true JP3432260B2 (en) 2003-08-04

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EP0958833A1 (en) * 1998-05-20 1999-11-24 Erasmus Universiteit Rotterdam Methods and means for preventing or treating inflammation
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