JPH0681582B2 - Protein gel manufacturing method - Google Patents
Protein gel manufacturing methodInfo
- Publication number
- JPH0681582B2 JPH0681582B2 JP1087643A JP8764389A JPH0681582B2 JP H0681582 B2 JPH0681582 B2 JP H0681582B2 JP 1087643 A JP1087643 A JP 1087643A JP 8764389 A JP8764389 A JP 8764389A JP H0681582 B2 JPH0681582 B2 JP H0681582B2
- Authority
- JP
- Japan
- Prior art keywords
- protein
- transglutaminase
- gel
- protein gel
- paste
- 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
Links
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- Jellies, Jams, And Syrups (AREA)
Description
【発明の詳細な説明】 (産業上の利用分野) 本発明は蛋白ゲルの製造法に関する。TECHNICAL FIELD The present invention relates to a method for producing a protein gel.
(従来技術) 従来から大豆蛋白等の熱凝固性蛋白ペーストを低温処理
(坐り等)したり、高温処理したりして蛋白ゲルを製造
する方法が知られている。(Prior Art) Conventionally, a method for producing a protein gel by subjecting a heat-coagulable protein paste such as soybean protein to a low temperature treatment (such as sitting) or a high temperature treatment has been known.
一方、蛋白ゲル強度を強くする方法として、特開昭58-1
49645、特開昭59-59151、特開昭61-152247、特開昭64-1
0949、特開昭64-27471号等,には、トランスグルタミナ
ーゼを用いる方法が記載されている。On the other hand, as a method for increasing the strength of protein gel, Japanese Patent Laid-Open No. 58-1
49645, JP-A-59-59151, JP-A-61-152247, JP-A-64-1
0949, JP-A-64-27471 and the like describe a method using transglutaminase.
しかし、アミノ糖を併用することは知られていない。However, it is not known to use an amino sugar together.
(解決しようとする問題点) 本発明者等はゲル強度の強い蛋白ゲルを目的とした。(Problems to be Solved) The present inventors aimed at a protein gel having a high gel strength.
(問題を解決する為の手段) 本発明者等はトランスグルタミナーゼによる蛋白ゲルの
製造を研究する程度で、もっとゲル強度を上げることが
出来ないか鋭意研究の結果、グルコサミンを併用すれば
意外にもゲル強度が上昇する知見を得、更に研究の結果
グルコサミン等のアミノ糖による蛋白のゲル強度増強効
果を見出して本発明を完成するに到った。(Means for Solving the Problem) The present inventors have studied the production of protein gels using transglutaminase, and as a result of earnest research as to whether it is possible to further increase the gel strength, it was surprising that glucosamine was used in combination. The inventors obtained the finding that the gel strength increases, and as a result of further research, they found the effect of enhancing the gel strength of a protein by an amino sugar such as glucosamine, and completed the present invention.
即ち、本発明は、蛋白及びアミノ糖を含むペーストを
低温及び/又は高温処理することを特徴とする蛋白ゲル
の製造法、及び蛋白及びアミノ糖を含むペーストにス
トレプトバーティシリウム(Streptoverticillium)属
起源のトランスグルタミナーゼを作用させ低温及び/又
は高温処理することを特徴とする蛋白ゲルの製造法、で
ある。That is, the present invention provides a method for producing a protein gel, which comprises treating a paste containing a protein and an amino sugar at a low temperature and / or a high temperature, and the paste containing the protein and the amino sugar is derived from the genus Streptoverticillium. Is a method for producing a protein gel, which comprises treating with transglutaminase of (1) and performing low-temperature and / or high-temperature treatment.
先ずについて説明する。First, a description will be given.
本発明に用いる蛋白は、鳥獣魚介肉蛋白、大豆蛋白、そ
の他の熱凝固性蛋白もしくはこれらの混合物を用いるこ
とができる。As the protein used in the present invention, birds, meats and fishes meat protein, soybean protein, other thermocoagulable proteins, or a mixture thereof can be used.
鳥獣魚介肉蛋白は、牛、豚、鶏、馬、羊等の鳥獣肉、ス
ケソウダラ、グチ、ハモ、タチウオ、アジ、イワシ、エ
ソ、ホッケ、サメ、トビウオ等の魚肉の他エビ、イカ、
貝等の魚介類の肉、これらのする身等を用いることがで
きる。Birds and beef seafood proteins include poultry, poultry, chicken, horses, sheep and other birds and meats, pollock, guchi, duck, sea fish, horse mackerel, sardines, lizards, hooks, sharks, flying fish and other shrimp, squid,
Meat of seafood such as shellfish, and the body of these can be used.
大豆蛋白は脱脂大豆から水抽出して得られる豆乳粉末、
濃縮蛋白、分離蛋白等を用いることができ、これらと水
の混合ベースト或いはこれらと油脂及び水のエマルジョ
ン等も用いることができる。Soy protein is soy milk powder obtained by extracting water from defatted soybeans,
Concentrated proteins, separated proteins and the like can be used, and mixed bases of these with water or emulsions of these with oils and fats and water can also be used.
その他の熱凝固性蛋白として卵白等を用いることができ
る。Egg white or the like can be used as the other thermocoagulable protein.
本発明に用いるアミノ糖はグルコサミン、ガラクトサミ
ン、これらのポリマー(キトサン等)を用いることがで
きる。As the amino sugar used in the present invention, glucosamine, galactosamine and polymers thereof (such as chitosan) can be used.
ペーストは前記蛋白、アミノ糖及び水をサイレントカッ
ター等の均質機を用いてペースト状となしたものを用い
ることができる。ペーストにカルシウム等のアルカリ土
類金属塩、調味料、香辛料、着色料等を用いることは自
由である。As the paste, the above protein, amino sugar, and water can be used in the form of a paste using a homogenizer such as a silent cutter. It is free to use alkaline earth metal salts such as calcium, seasonings, spices, and coloring agents in the paste.
低温処理は通常坐り等に用いる1〜50℃の温度処理、高
温処理は通常70℃以上の煮る、蒸す、焼く、フライ等の
高温加熱を利用できる。The low temperature treatment may be a temperature treatment of 1 to 50 ° C. which is usually used for sitting, and the high temperature treatment may be a high temperature heating of 70 ° C. or higher such as boiling, steaming, baking and frying.
このようにして得られる蛋白ゲルはアミノ糖を用いない
蛋白ゲルよりゲル強度の強いものである。The protein gel thus obtained has stronger gel strength than the protein gel without amino sugar.
次にについて説明する。The following will be described.
本発明に用いる蛋白及びアミノ糖は前述の通りである。The protein and amino sugar used in the present invention are as described above.
本発明のトランスグルタミナーゼは、動物起源のものも
用いることができるが、高価でありカルシウム要求性な
ので微生物起源のものが好適である。例えば、Streptov
erticillium属biverti−cillatum、同pentacium,同hiro
shimense,同griseocarneum,同cinnamomeum,同griseo−v
erticillatum,同thioluteum,及び同ardum)の内より選
ばれた1種又は2種以上を培養して得ることができる。
好ましくはStreptoverticillium griseocarneum,同cinn
amoneum,同pentacium,同biverticillatum,hiroshimense
が適当である。その他Paramecium aurelia,Escherichia
coli等もトランスグルタミナーゼを生産するが細胞外
に分泌しなかったり、プロテアーゼも同時に生産するた
めトランスグルタミナーゼに混入し、トランスグルタミ
ナーゼにより重合したたん白の一部を切断する不都合が
ある。As the transglutaminase of the present invention, those of animal origin can be used, but those of microbial origin are preferable because they are expensive and require calcium. For example, Streptov
erticillium sp.biverti-cillatum, pentacium, hiro
shimense, griseocarneum, cinnamomeum, griseo−v
erticillatum, thioluteum, and ardum) can be obtained by culturing one or more selected from the group consisting of erticillatum, thioluteum, and ardum.
Preferably Streptoverticillium griseocarneum, cinn
amoneum, same pentacium, same biverticillatum, hiroshimense
Is appropriate. Others Paramecium aurelia, Escherichia
E. coli also produces transglutaminase but does not secrete it extracellularly, and since it also produces protease, it is contaminated with transglutaminase and cleaves a part of the protein polymerized by transglutaminase.
トランスグルタミナーゼはこれらの菌の培養液を粗製又
は精製して得ることができる。例えば、粗酵素として培
養液から菌体を除去したもの、更に限外濾過膜(例えば
分画分子量約1万以上)を用いて分画濃縮したもの、更
に乾燥(真空乾燥、凍結乾燥等)したもの等も用いるこ
とができる。Transglutaminase can be obtained by crude or purifying a culture solution of these bacteria. For example, a crude enzyme obtained by removing cells from the culture solution, further fractionated and concentrated by using an ultrafiltration membrane (for example, a cutoff molecular weight of about 10,000 or more), and further dried (vacuum drying, freeze drying, etc.) The thing etc. can also be used.
トランスグルタミナーゼを作用させる態様は、蛋白ペー
ストに対し、その粗蛋白1g当たり0.001単位以上、好ま
しくは0.01単位以上が適当である。A suitable mode of action of transglutaminase is 0.001 unit or more, preferably 0.01 unit or more per 1 g of the crude protein in the protein paste.
ただし、本発明において、トランスグルタミナーゼの酵
素活性即ち力価測定はN−カルボベンゾキシ−L−グル
タミニルグリシンとヒドロキシアミンを用いるJ,E,Folk
s等の方法〔Method in Enzymology,10.358,(1985)〕
によった。However, in the present invention, the enzymatic activity of transglutaminase, that is, titer determination, uses J, E, Folk using N-carbobenzoxy-L-glutaminylglycine and hydroxyamine.
s etc. [Method in Enzymology, 10.358, (1985)]
According to
又、トランスグルタミナーゼの蛋白ペーストに対する作
用時間、温度は必要とするゲル強度や酵素量にもよる
が、作用温度(例えば1〜50℃)で、約10分〜30時間が
適当である。例えば、魚肉練製品の高温座り(30〜50℃
×10分〜60分)や低温座り(2〜10℃×12〜20時間)を
反応に利用することが適当である。Although the action time and temperature of transglutaminase on the protein paste depend on the required gel strength and the amount of enzyme, about 10 minutes to 30 hours is suitable at the action temperature (for example, 1 to 50 ° C). For example, sitting at high temperature of fish meat products (30-50 ℃)
It is suitable to utilize low temperature sitting (2 to 10 ° C x 12 to 20 hours) for the reaction.
低温処理及び高温処理については前述の通りである。The low temperature treatment and the high temperature treatment are as described above.
以上のようにして得られる蛋白ゲルはアミノ糖を用いな
いものよりゲル強度の強いものである。The protein gel obtained as described above has a stronger gel strength than that without amino sugar.
以上本発明、によって得られる蛋白ゲルとしては、
例えば、蒲鉾、揚蒲、はんぺん、ちくわ、つみれ、魚そ
うめん、鳴門巻、魚肉ハム、魚肉ソーセージ、カニ脚様
蒲鉾、貝柱様食品等の魚肉練製品、畜肉ハム・ソーセー
ジ類等の肉加工食品、豆腐、揚げ、ガンモドキ等の伝統
的な食品と分離大豆蛋白を原料とするかかる伝統食品類
似食品等の大豆蛋白加工食品をあげることができる。As described above, the protein gel obtained by the present invention,
For example, kamaboko, fried fish, hanpen, chikuwa, tsumire, fish noodles, naruto rolls, fish ham, fish sausage, crab leg-like kamaboko, scallop-like food products, processed meat products such as meat ham and sausages, Examples thereof include traditional foods such as tofu, fried foods, and gems, and processed foods of soybean protein such as foods similar to such traditional foods using isolated soybean protein as a raw material.
尚、以下の実施例で表すゲル強度は「ネオカードメータ
M−302型」(飯尾電機株式会社)で測定した。The gel strength shown in the following examples was measured with "Neocard Meter M-302 type" (Iio Electric Co., Ltd.).
又、蛋白含量は大豆蛋白、鳥獣魚介肉蛋白の場合、予め
ケルダール法で測定した粗蛋白(全窒素×6.25)とし
た。In the case of soybean protein and poultry fish meat protein, the protein content was crude protein (total nitrogen x 6.25) measured in advance by the Kjeldahl method.
(実施例) 以下実施例により本発明の実施態様を説明する。(Examples) The embodiments of the present invention will be described with reference to the following examples.
実施例1 ポリペフトン2.0%、可溶性澱粉2.0%、酵母エキス0.2
%、燐酸塩0.2%、硫酸マグネシウム0.1%を含有する液
体培地(pH6.0)を殺菌・冷却後、Streptoverticillium
griseocarneum(IFO 12776)の菌糸懸濁液を注加し、3
0℃で3日間、通気攪拌培養した。得られた培養液を遠
心分離し、菌糸を除き、培養濾液を得た。更に、この培
養濾液を限外濾過(分画分子量1万)で濃縮し、真空乾
燥して部分精製酸素粉末を得た。酵素力価は2.0単位/g
であった。Example 1 Polypefton 2.0%, soluble starch 2.0%, yeast extract 0.2
%, Phosphate 0.2%, magnesium sulfate 0.1% liquid medium (pH 6.0) is sterilized and cooled, then Streptoverticillium
Add the mycelial suspension of griseocarneum (IFO 12776) and
The culture was carried out with aeration and stirring at 0 ° C. for 3 days. The obtained culture broth was centrifuged to remove mycelium, and a culture filtrate was obtained. Further, this culture filtrate was concentrated by ultrafiltration (molecular weight cut-off of 10,000) and vacuum dried to obtain partially purified oxygen powder. Enzyme titer is 2.0 units / g
Met.
実施例2 実施例1と同様の液体培地にStreptoverti-cillium cin
namoneum(IFO 12852)を培養し、培養液を実施例1と
同様に処理して、酵素力価10.8単位/gの部分精製酵素を
得た。Example 2 Streptoverti-cillium cin was added to the same liquid medium as in Example 1.
namoneum (IFO 12852) was cultured, and the culture solution was treated in the same manner as in Example 1 to obtain a partially purified enzyme having an enzyme titer of 10.8 units / g.
実施例3 分離大豆蛋白(不二製油(株)製「ニューフジプロ−
R」)の12%溶液にアミノ糖であるグルコサミン塩酸塩
(和光純薬工業(株)製)を0.08%/大豆蛋白g加えた
ものと、対照区としてグルコサミンを加えないものとを
調製し、各々に対し表―1及び表―2に示す酵素量を加
えて37℃で3時間反応させた。更にこの後80℃で30分加
熱した。ゲル強度を測定した結果を同表―1及び表―2
に示す。Example 3 Isolated soybean protein (“New Fuji Pro-” manufactured by Fuji Oil Co., Ltd.)
R ") of which 12% solution of glucosamine hydrochloride (manufactured by Wako Pure Chemical Industries, Ltd.), which is an amino sugar, was added at 0.08% / g of soybean protein and a control group to which glucosamine was not added, The amount of enzyme shown in Table-1 and Table-2 was added to each and the reaction was carried out at 37 ° C for 3 hours. After this, heating was further performed at 80 ° C. for 30 minutes. The results of gel strength measurement are shown in Table-1 and Table-2.
Shown in.
以上より、グルコサミン添加画分は対照区に比ベゲル強
度が高いことがわかった。又、グルコサミン添加及びト
ランスグルタミナーゼ作用により高くなった。 From the above, it was found that the fraction added with glucosamine had higher Begel strength than the control group. Moreover, it was increased by the addition of glucosamine and the action of transglutaminase.
(効果) 以上説明したように、本発明により、蛋白のゲル強度を
強くすることが可能になったものであり、種々のゲル化
食品等に応用できるものである。(Effect) As described above, the present invention makes it possible to increase the gel strength of a protein, and can be applied to various gelled foods and the like.
Claims (2)
プトバーティシリウム(Streptoverticillium)属起源
のトランスグルタミナーゼを作用させ低温及び/又は高
温処理することを特徴とする蛋白ゲルの製造法。1. A method for producing a protein gel, which comprises subjecting a paste containing a protein and an amino acid to a transglutaminase originating from the genus Streptoverticillium and treating the paste at low temperature and / or high temperature.
ン、これらのポリマーから選ばれた1種又は2種以上で
ある請求項1の製造法。2. The method according to claim 1, wherein the amino acid is one or more selected from glucosamine, galactosamine and polymers thereof.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1087643A JPH0681582B2 (en) | 1989-04-05 | 1989-04-05 | Protein gel manufacturing method |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP1087643A JPH0681582B2 (en) | 1989-04-05 | 1989-04-05 | Protein gel manufacturing method |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH02265440A JPH02265440A (en) | 1990-10-30 |
| JPH0681582B2 true JPH0681582B2 (en) | 1994-10-19 |
Family
ID=13920665
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP1087643A Expired - Fee Related JPH0681582B2 (en) | 1989-04-05 | 1989-04-05 | Protein gel manufacturing method |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0681582B2 (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP4427950B2 (en) * | 2001-02-28 | 2010-03-10 | 不二製油株式会社 | Soy protein, its production method and acidic protein food using the same |
-
1989
- 1989-04-05 JP JP1087643A patent/JPH0681582B2/en not_active Expired - Fee Related
Non-Patent Citations (1)
| Title |
|---|
| 別冊フードケミカル「キチン/キトサンの科学」(昭62.8.21)食品化学新聞社P.1〜P.4 |
Also Published As
| Publication number | Publication date |
|---|---|
| JPH02265440A (en) | 1990-10-30 |
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|---|---|---|---|
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