JP3543419B2 - Soy protein for retort food and retort food - Google Patents

Soy protein for retort food and retort food Download PDF

Info

Publication number
JP3543419B2
JP3543419B2 JP13974195A JP13974195A JP3543419B2 JP 3543419 B2 JP3543419 B2 JP 3543419B2 JP 13974195 A JP13974195 A JP 13974195A JP 13974195 A JP13974195 A JP 13974195A JP 3543419 B2 JP3543419 B2 JP 3543419B2
Authority
JP
Japan
Prior art keywords
protein
retort
glycinin
kda
soybean
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
Application number
JP13974195A
Other languages
Japanese (ja)
Other versions
JPH08332029A (en
Inventor
将彦 佐本
武志 赤坂
千晶 宮崎
弘之 森
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
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Fuji Oil Co Ltd filed Critical Fuji Oil Co Ltd
Priority to JP13974195A priority Critical patent/JP3543419B2/en
Publication of JPH08332029A publication Critical patent/JPH08332029A/en
Application granted granted Critical
Publication of JP3543419B2 publication Critical patent/JP3543419B2/en
Anticipated expiration legal-status Critical
Expired - Fee Related legal-status Critical Current

Links

Landscapes

  • Beans For Foods Or Fodder (AREA)
  • Food Preservation Except Freezing, Refrigeration, And Drying (AREA)

Description

【0001】
【産業上の利用分野】
この発明はレトルト食品用大豆蛋白質及びレトルト食品に関するものであり、とりわけ、レトルト処理をしても色・風味の悪化が抑制された大豆蛋白質及びこれを原料とするレトルト食品に関するものである。
【0002】
【従来の技術】
レトルト食品は一般に、100℃以上の湿熱加熱を受けて商業的無菌性を付与された容器包装詰加圧加熱殺菌食品であり、細菌胞子の死滅する条件、即ち例えば120℃4分以上の高温、高圧で処理することにより、保存性が優れている。
【0003】
分離大豆蛋白質は、種々の大豆蛋白の中でも最も精製されて蛋白質含量が約90%以上に高められている素材で、乳化,蛋白質強化,ゲル形成等の機能があるが、レトルト処理すると分離大豆蛋白質の色や風味が悪化するのでレトルト食品の蛋白性原料として用いることには困難があり、大豆蛋白質又はその加水分解物の機能を役立てることに制約があった。
【0004】
【発明が解決しようとする課題】
本発明者らは、レトルト処理しても色・風味の悪化が起こらない大豆蛋白質が得られないかを種々検討する中で、大豆蛋白質を分画してレトルト処理した状態を比較したところ、脂質と相互作用している34kDa付近の蛋白質を含む画分がレトルト処理で非常に色・風味の悪化を起こす部分であること、及び、この蛋白質の画分を除去乃至低減させた大豆蛋白はレトルト処理しても色、風味の悪化がおこりにくく、レトルト食品用に好適に使用できる等の知見を得た。この発明はこのような知見によって完成された。
【0005】
【課題を解決するための手段】
即ちこの発明の一つは、グリシニン以外の28〜35kDaの蛋白質が実質的に低減されたレトルト食品用大豆蛋白質であり、好ましくは、グリシニン以外の28〜35kDaの蛋白質が、β−コングリシニン(以下において「7S蛋白質」ということがある)及びグリシニン(以下において「11S蛋白質」ということがある)の総和量に対して8%以下であるレトルト食品用大豆蛋白質であるが、グリシニン以外の28〜35kDaの蛋白質を特に低減していない通常の大豆蛋白質であるとグリシニン以外の28〜35kDaの蛋白質をコングリシニン及びグリシニンの総和量に対して9%程度を含む。
【0006】
グリシニン以外の28〜35kDaの蛋白質が除去されているか、どの程度除去されているかは、加水分解があまり起こっていないものについて、SDS−ポリアクリルアミドゲル電気泳動法で容易に確認できる。例えば、Laemmli,U.K.,Nature,227,680−685(1970)に記載のようにSDS−ポリアクリルアミドゲル電気泳動を利用して次のように行う。分析サンプル中には大豆蛋白質にして20〜30μg(蛋白態窒素として3.2〜4.8μg)を12%のポリアクリルアミドゲル(厚さ1mm,幅5mm)にアプライし、泳動させ泳動後クーマシー・ブリリアント・ブルーを染色剤として泳動後の蛋白質を染色する。この染色された各蛋白質のスポットの吸光量をデンシトメトリーで440nmの吸光度をリファレンスとし、590nmの吸光度を測定したスキャニングパターンのピーク面積として求めると、この面積は蛋白質量と相関する。この明細書における、グリシニン以外の28〜35kDaの蛋白質のβ−コングリシニン及びグリシニンの総和量に対する量比は、グリシニン以外の28〜35kDaの蛋白質の吸光量のβ−コングリシニン及びグリシニンの吸光量の総和量に対する割合で求めた。
【0007】
この発明において、グリシニン以外の28〜35kDaの蛋白質が実質的に低減されたレトルト食品用大豆蛋白質は、その調製方法がどのようなものであるかは特に問わないが、塩類が溶解した水溶液若しくは硫酸イオン等の多価アニオンの存在する水溶液を用いて原料大豆蛋白質を酸性下に処理することにより、グリシニン以外の28〜35kDaの蛋白質の画分を選択的に沈降性画分に濃縮させ、上清画分を採取することができる。
【0008】
この好ましい調製方法によれば、7S画分と11S画分に分取する必要がないので、原料大豆中の両画分の比、例えば使用する米国産の一般的な大豆である場合、製品蛋白質中にも原料のβ─コングリシニンとグリシニンの重量比をそのまま保って、通常1:2〜4:5の範囲で含んでいる。また得られるレトルト食品用大豆蛋白質は、大豆の主要な貯蔵蛋白質であるβ─コングリシニンとグリシニンとを殆ど失わず、レトルト食品用大豆蛋白質(の全蛋白態窒素100重量%)中にそれらを通常70重量%以上含んでおり、最も通常には75〜90%含んでいる。
【0009】
上記調製法における原料大豆蛋白質は、大豆または脱脂大豆から抽出した豆乳、またはこれを等電点pHに調節して沈澱分離した酸沈澱大豆蛋白、それを中和した所謂分離蛋白などが例示できるが、脱脂された、それも熱披瀝の少ない低変性の蛋白質が、最終目的蛋白質を収率よく得るのに役立ち、また収穫後ひねていない大豆の蛋白質である方が安定的に良好な収率に管理し易い。
【0010】
原料大豆蛋白質を酸性下に処理する態様は、大豆蛋白質の水性抽出液から沈降性画分を生じさせるものであっても、酸沈澱大豆蛋白から溶解性画分を抽出するものであってもよく、また酸性下のpHは5.0以下の範囲を採用するのがよい。塩類を使用する場合はその種類とpH領域に応じた塩濃度を適宜選択する。即ち、酸性下のpHが3.5〜5.0であれば、処理時の塩濃度が、酢酸塩若しくは多価の酸根を有する塩の濃度で90mM以上、または塩化物の濃度で1200mM以上であるのがよく、より好ましくは前者で150mM以上後者で2000mM以上である。酸性下のpHが2.0〜4.0であれば、処理時の塩濃度が、酢酸塩若しくは多価の酸根を有する塩で3mM以上、または塩化物の濃度で600mM以上であるのがよく、より好ましくは前者で20mM以上後者で900mM以上である。
【0011】
塩類は、そのカウンターイオンの所謂ホーフマイスター系列(Hofmeister's series) の順と似て、クエン酸塩, 酒石酸塩, 硫酸塩といった2価以上の多価の酸根をもつ塩、次いで酢酸塩, 次いで塩化物が、この順にグリシニン以外の28〜35kDaの蛋白質の沈降性を強める選択性が優れているので、塩化物だと多量の使用量が必要であるのに対し、2価以上の多価の酸根をもつ塩や酢酸塩は、少量使用で足る。また塩類は、ナトリウムまたはカリウムといったアルカリ金属の塩が適している。アルカリ土類金属の塩だと主要な貯蔵蛋白質と結合を起こしやすいので、塩濃度が高い範囲では収率よく大豆蛋白質を得るという目的の達成に劣るが、塩濃度が低い場合、例えば100mM程度以下であればそのような問題は殆どなく、カルシウムやマグネシウム等のアルカリ土類金属の塩も使用できる。ただし用いる塩類の濃度は、高くなるにつれて、低減させようとする蛋白質画分の選択的沈降性が増すが、ある程度以上の濃度になると主要貯蔵蛋白質の沈降性も増して来て選択性が低下するから、塩類の濃度はイオン強度で5以下好ましくは4以下の範囲で実施されるのがよい。
【0012】
また上清画分を採取する以前の工程において、大豆蛋白質が、還元剤または電気的還元下で処理されてもよく、採取した上清画分は必要に応じて、中和、脱塩、脱ホエー、加熱殺菌もしくは乾燥することができる。
【0013】
この発明の他の一つは、上記のようにして得た蛋白質、即ちグリシニン以外の28〜35kDaの蛋白質が実質的に低減された大豆蛋白質またはその加水分解物を、蛋白性原料の一部または全部として含有するレトルト食品である。
【0014】
加水分解を行う場合は、レトルト食品用大豆蛋白質を水溶液でプロテアーゼを含む酵素的方法によって行うのが、強酸や強アルカリを用いて加水分解する方法よりも一般に風味及び色調的によい。加水分解の程度は酵素の種類と目的に応じて行えばよく、例えば市販の枯草菌由来のプロテアーゼを用いて行う場合は、0.4Mのトリクロル酢酸溶液に可溶の蛋白質の割合(全窒素に対する可溶性蛋白質の窒素の量)が概ね20%以上になるまで加水分解するとゲル形成力をなくすことができ、また概ね80%以下に保つとアミノ酸までに分解してしまわないオリゴペプチドの領域に保つことができる。酵素による加水分解は80℃以上に加熱することにより反応を停止することができる。
【0015】
レトルト食品は、例えば経腸栄養食,蛋白強化飲料,乳コーヒー,缶コーヒー,スープ等の飲料、魚肉練製品,畜肉練製品等の練製品、または豆腐類製品であることができ、従ってまた液状、クリーム状、ゲル状、またはそれらの共存状態のいずれであってもよい。
【0016】
蛋白性原料は目的により、上記特定の大豆蛋白質若しくはその加水分解物の単独、またはカゼイン、乳蛋白、肉蛋白など他の蛋白性原料と併用して、所望量用いられ、目的とする加工食品の種類に応じた配合、プロセスを経て、容器中に充填され、レトルト加熱される。
【0017】
例えば、乳コーヒーや缶コーヒー飲料中には、カゼインや乳蛋白と併用して用いることができ、またコレステロール低下を目的とする栄養食品には大豆蛋白質単独の蛋白原料を用いることができる。
【0018】
また例えば目的製品が練製品である場合には、レトルト食品用大豆蛋白質若しくはその加水分解物は単独の水性ペーストまたは魚肉、畜肉、等のペースト中に混和され、成型してヒートセット(加熱凝固)され、これが他のたれや汁物と併せて容器詰めされレトルト加熱されてもよいし、或いは上記ペーストをレトルト容器中に充填してレトルト加熱とヒートセットを兼ねて行ってもよい。
【0019】
この発明のレトルト食品は、いわゆるレトルトパウチ食品と称される「プラスチックフィルムもしくは金属箔又はこれらを多層に合わせたものを袋状その他の形状に成型した容器に調整した食品を詰め、熱溶融により密封し、加圧加熱殺菌したもの」に限らず、広く「気密性のある容器包装に食品を入れ、密封した後、加圧加熱殺菌したもの」をいい、缶詰食品、びん詰め食品を含む容器包装詰食品全体をいう。
【0020】
加熱レベルの条件は、食品に生育する微生物の種類及び食品の物理化学的要因によって異なるが一般に100℃を越える温度、例えば通常の非酸性食品だと中心部の温度が120℃4分以上加熱されるような条件が選択される。
【0021】
このようにしてグリシニン以外の28〜35kDaの蛋白質が除去された大豆蛋白質は例えば、レトルトパックのマーボー豆腐の素材として使用された場合のように白い色がレトルト処理をしても鮮やかで味が落ちない等の利点が期待できる。いずれにせよ、この発明において大豆蛋白質またはその加水分解物を製品中3%以上の濃度で用いても、従来の大豆蛋白に由来した色、風味の悪化はレトルト食品であってもよく抑制されるのである。
【0022】
【実施例】
以下にこの発明の実施例を示す。
【0023】
実施例1及び比較例
低変性脱脂大豆100gに水1000mlの水を加え、ホモミキサーで攪拌し、1NのNaOHの添加によってpH7.5に調整し、室温で30分抽出し、攪拌スラリーを布で絞っておからを除去し、さらに不溶物を3000g,10分の遠心分離で除去した。おからと不溶物に水1000mlの水を加え、上記と同じ操作でさらに可溶性蛋白質を抽出し、1回目と2回目の抽出物を混合して脱脂豆乳とした。この脱脂豆乳に10mMになるように亜硫酸水素ナトリウムを加え、5分放置後、1N HClでpH4.5に調整した。沈澱蛋白質を遠心分離(3000g,10分)で採取し、これを酸沈蛋白質とした。酸沈蛋白質に500mlの水を加え、1Mになるように硫酸ナトリウムを加え、攪拌し、溶解する蛋白質を抽出し、これを2回繰り返した。この抽出蛋白質をグリシニン以外の28〜34kDa蛋白質を含まない蛋白質画分とした。SDS−ポリアクリルアミドゲル電気泳動の結果から、この画分はグリシニン以外の28〜34kDa蛋白質は7S,11S蛋白質量に対して2.2%に低減されていた。
【0024】
この蛋白質画分溶液を100倍の水に対して透析を行ない、イオン強度が低下することで沈殿した大豆蛋白質を遠心分離で採取し、中和して凍結乾燥した分離蛋白質を調製した。
【0025】
実施例2
実施例1と同様に調製した豆乳に10mM、5mM、又は3mMの濃度になるように硫酸ナトリウムを加え、攪拌し、HClでpHを2.8に調整し、遠心(10000g,10分)を行って、不溶物を除去し、上清を苛性ソーダでpH4.5に調整して沈澱画分を遠心(3000g,10分)で採取し、この沈澱物を中和して凍結乾燥した分離蛋白質を調製した。この蛋白質のグリシニン以外の28〜34kDa蛋白質は7S,11S蛋白質量に対して低減されていた。
【0026】
比較例1
実施例1と同様に調製した豆乳を塩酸でpH4.5に調整し、沈澱した蛋白質を遠心分離(3000g,10分)で採取し、NaOHで中和して分離大豆蛋白質を調整した。この蛋白質のグリシニン以外の28〜34kDa蛋白質は7S,11S蛋白質量に対して9.0%であった。
【0027】
実施例1,2及び比較例1で得られた各分離蛋白質が3%含まれる水溶液を各々調製し、缶につめ、121℃,30分の加熱を行ない、冷却後の風味・色の変化を、官能的に評価した。色(明るい/10点から暗い/1点),及び風味(無味/10点 から 悪い/1点)の2項目について20人のパネラーによって品質の官能評価を行ない、その平均値を示した。色、風味の評価は、グリシニン以外の28〜34kDaの少ない方が、レトルト処理前に優れているだけでなく、レトルト処理をすることによっても、悪化しにくいこと即ちレトルト食品用大豆蛋白質として好適であることが認められた。即ちグリシニン以外の28〜35kDaの蛋白質のβ−コングリシニン及びグリシニンの総和量に対して8%以下、好ましくは7%以下、より好ましくは5.5%以下である大豆蛋白質が、レトルト食品用に良い結果を示した。
【0028】

Figure 0003543419
*本文中に記載のように、SDS−ポリアクリルアミドゲル電気泳動分析により泳動後、蛋白質染色、デンシトメトリーで測定した7S、11S蛋白質吸光量に対するグリシニン以外の28〜34kDa蛋白質の吸光量の割合(%)
【0029】
実施例3
実施例1で調製したレトルト食品用大豆蛋白質を水に溶解して5%溶液を調製し、これにトリプシンを作用させて、0.4Mのトリクロル酢酸溶液に可溶の蛋白質が30%になるまで加水分解し、95℃で15分間加熱することによって、反応を止めた。この加水分解した溶液を缶に詰めて、121℃30分の加熱を行い、冷却後の風味・色の変化を官能により評価した。
【0030】
比較は比較例1で調製した分離大豆蛋白質を、レトルト食品用大豆蛋白質に代えて使用する他は、本例と同様に加水分解、レトルト加熱、冷却したものであるが、本例のレトルト品の方が比較より顕著に色及び風味において優れていた。
【0031】
実施例4
実施例1または比較例1で得た分離蛋白質5重量部(以下部は重量部)を、菜種油30部、蔗糖5部、水60部と混合して、ホモゲナイズ(80kg/cm2)した乳化飲料とし、缶に詰めて、121℃,30分のレトルト処理を行ない、その色・風味の変化を実施例と比較例1と同様の官能評価方法で確認した。
【0032】
Figure 0003543419
【0033】
上記の結果の様に、乳化飲料においてもグリシニン以外の28〜35kDaの蛋白質を含まない画分ではレトルト処理による色や風味の劣化が顕著に防止されることが認められた。
【0034】
実施例5
実施例1または比較例1で得た分離蛋白質6部を、魚肉すり身30部、菜種油29部、味剤5部、水30部と配合して、ケーシングチューブに詰め、121℃,30分のレトルト処理を行ない、レトルトソーセージを得た。レトルト後の製品の色や風味の評価を行ったところ、実施例1の分離大豆蛋白質を用いたレトルトソーセージの方が比較例の分離大豆蛋白質を用いたレトルトソーセージよりも明らかに優れていた。
【0035】
実施例6
実施例1と比較例1で使用した2つの分離蛋白質を使用して、次表の配合で生地を調製し成形し(10cm×5cm×1cm)蒸し加熱を行い「豆腐ステーキ」を作製した。この「豆腐ステーキ」とたれ(市販調味料、砂糖、濃口醤油、味醂、酒、澱粉及び水からなる)を1:1の配合でレトルト袋に充填し、脱気シールした後、120℃,30分のレトルト処理を行ない、その色・風味の変化を実施例1等と同様の官能評価方法で確認した結果、分離大豆蛋白質から調製した大豆蛋白食品のレトルト加熱品においてもグリシニン以外の28〜34kDaの蛋白質を除去した画分ではレトルト処理による色や風味の劣化が少なく品質が良好であることが認められた。
【0036】
Figure 0003543419
【0037】
【発明の効果】
以上のように、グリシニン以外の28〜35kDaの蛋白質が実質的に低減された大豆蛋白質、またはその加水分解物は、これを蛋白性成分の一部または全部として用いて、レトルト処理をしても色・風味の悪化が抑制されたレトルト食品を得ることができ、従って、大豆蛋白質の用途を拡大するとともに、レトルト食品の食品に乳化、蛋白強化、ゲル化力等の大豆蛋白質の有する機能を役立たせることができる。[0001]
[Industrial applications]
The present invention relates to a soybean protein for a retort food and a retort food, and more particularly to a soybean protein whose color and flavor are suppressed from being deteriorated even after retort treatment, and a retort food using the same as a raw material.
[0002]
[Prior art]
The retort food is generally a pressurized and heat-sterilized food packaged in a container and package that has been provided with commercial sterility by being subjected to moist heat heating of 100 ° C. or more, and is capable of killing bacterial spores, for example, a high temperature of 120 ° C. for 4 minutes or more. By processing at high pressure, storage stability is excellent.
[0003]
Isolated soy protein is the most purified material among various soy proteins and has a protein content of about 90% or more, and has functions such as emulsification, protein enhancement, and gel formation. It is difficult to use it as a proteinaceous raw material for retort foods because the color and flavor of the soybeans deteriorate, and there is a limitation in using the function of soybean protein or its hydrolyzate.
[0004]
[Problems to be solved by the invention]
The present inventors, while variously examining whether or not a soybean protein that does not cause deterioration in color and flavor even after retort treatment is obtained, compared the state of retort treatment after fractionating soybean protein, and The fraction containing a protein of around 34 kDa interacting with the soybean protein is a part that causes a significant deterioration in color and flavor by retort treatment, and the soybean protein from which this protein fraction has been removed or reduced is treated with retort treatment. However, it was found that the color and flavor hardly deteriorated, and that it could be suitably used for retort foods. The present invention has been completed based on such findings.
[0005]
[Means for Solving the Problems]
That is, one aspect of the present invention is a soybean protein for retort foods in which 28-35 kDa protein other than glycinin is substantially reduced, and preferably, 28-35 kDa protein other than glycinin is β-conglycinin (hereinafter referred to as “β-conglycinin”). It is a soy protein for retort foods that is 8% or less based on the total amount of “7S protein” and glycinin (hereinafter sometimes referred to as “11S protein”), but is 28-35 kDa other than glycinin. A normal soybean protein whose protein is not particularly reduced contains a protein of 28 to 35 kDa other than glycinin in an amount of about 9% based on the total amount of conglycinin and glycinin.
[0006]
Whether or not the protein of 28 to 35 kDa other than glycinin has been removed can be easily confirmed by SDS-polyacrylamide gel electrophoresis for a substance that has not undergone much hydrolysis. See, for example, Laemmli, U.S.A. K. , Nature, 227, 680-685 (1970) using SDS-polyacrylamide gel electrophoresis as follows. In the analysis sample, 20 to 30 μg of soybean protein (3.2 to 4.8 μg as protein nitrogen) was applied to a 12% polyacrylamide gel (1 mm in thickness and 5 mm in width). The protein after electrophoresis is stained using Brilliant Blue as a staining agent. When the absorbance of each stained protein spot is determined by densitometry using the absorbance at 440 nm as a reference and the absorbance at 590 nm is determined as the peak area of the scanning pattern, this area correlates with the protein mass. In this specification, the ratio of the amount of 28-35 kDa protein other than glycinin to the total amount of β-conglycinin and glycinin is the total amount of the absorbance of β-conglycinin and glycinin of the 28-35 kDa protein other than glycinin. Was calculated as a percentage.
[0007]
In the present invention, the retort food soybean protein in which 28-35 kDa protein other than glycinin has been substantially reduced is not particularly limited as to its preparation method, but an aqueous solution in which salts are dissolved or sulfuric acid is used. By treating the raw soybean protein under acidic conditions using an aqueous solution containing a polyvalent anion such as an ion, the fraction of the 28-35 kDa protein other than glycinin is selectively concentrated into a sedimentable fraction, and the supernatant Fractions can be collected.
[0008]
According to this preferred preparation method, there is no need to fractionate into 7S and 11S fractions, so that the ratio of both fractions in the raw soybean, for example, if the general soybean used in the United States is used, the product protein The weight ratio of β-conglycinin to glycinin as a raw material is maintained as it is, and it is usually contained in the range of 1: 2 to 4: 5. The obtained soy protein for retort foods hardly loses β-conglycinin and glycinin, which are the main storage proteins of soybeans, and usually contains 70% in soy protein for retort foods (100% by weight of total protein nitrogen). % Or more, most usually 75 to 90%.
[0009]
Examples of the raw soybean protein in the above-mentioned preparation method include soymilk extracted from soybean or defatted soybean, or acid-precipitated soybean protein obtained by adjusting the isoelectric point pH of the soybean milk, and a so-called separated protein obtained by neutralizing the soybean milk. Low-denatured, defatted, low heat protein protein helps to obtain the final target protein in good yield, and soybean protein, which is not twisted after harvesting, provides a stable and good yield. Easy to manage.
[0010]
The mode of treating the raw soybean protein under acidic conditions may be one that produces a sedimentable fraction from an aqueous extract of soybean protein, or one that extracts a soluble fraction from acid precipitated soybean protein. The pH under acidic conditions is preferably in the range of 5.0 or less. When salts are used, the salt concentration is appropriately selected according to the type and the pH range. That is, when the pH under acidic conditions is 3.5 to 5.0, the salt concentration at the time of treatment is 90 mM or more in the concentration of acetate or a salt having a polyvalent acid radical, or 1200 mM or more in the concentration of chloride. More preferably, it is 150 mM or more for the former and 2,000 mM or more for the latter. When the pH under acidic conditions is 2.0 to 4.0, the salt concentration during the treatment is preferably 3 mM or more for acetate or a salt having a polyvalent acid radical, or 600 mM or more for chloride concentration. More preferably, the former is 20 mM or more, and the latter is 900 mM or more.
[0011]
Salts are similar to the so-called Hofmeister's series of counter ions, which are salts with polyvalent or higher valent acid salts such as citrate, tartrate, and sulfate, then acetate, and then chloride. In this order, chloride is required to be used in a large amount, whereas divalent or higher polyvalent acid radicals are required because chlorides require a large amount to be used in order to enhance the sedimentation of proteins of 28 to 35 kDa other than glycinin. Salts and acetates having a small amount are sufficient to use. As the salts, salts of alkali metals such as sodium and potassium are suitable. Alkaline earth metal salts are likely to bind to the main storage protein, so it is inferior to achieving the purpose of obtaining soybean protein in good yields in the high salt concentration range, but low in salt concentration, for example, about 100 mM or less If so, there is almost no such problem, and salts of alkaline earth metals such as calcium and magnesium can also be used. However, as the concentration of salts used increases, the selective sedimentation of the protein fraction to be reduced increases, but when the concentration exceeds a certain level, the sedimentation of the main storage protein also increases and the selectivity decreases. Therefore, it is preferable that the concentration of the salts is in the range of 5 or less, preferably 4 or less in ionic strength.
[0012]
Further, in the step before collecting the supernatant fraction, the soybean protein may be treated under a reducing agent or electric reduction, and the collected supernatant fraction may be neutralized, desalted, or desalted as necessary. It can be whey, heat sterilized or dried.
[0013]
Another aspect of the present invention is to provide a protein obtained as described above, that is, a soybean protein or a hydrolyzate thereof in which 28-35 kDa protein other than glycinin has been substantially reduced, as a part of a proteinaceous material or It is a retort food contained as a whole.
[0014]
When the hydrolysis is carried out, the retort food-grade soybean protein is enzymatically treated with an aqueous solution using a protease, which is generally better in flavor and color tone than the method in which the hydrolysis is carried out using a strong acid or a strong alkali. The degree of hydrolysis may be determined according to the type and purpose of the enzyme. For example, when a commercially available protease derived from Bacillus subtilis is used, the ratio of the protein soluble in a 0.4 M trichloroacetic acid solution (based on the total nitrogen) Hydrolysis until the amount of soluble protein (nitrogen) reaches approximately 20% or more can eliminate gel-forming power, and if it is approximately 80% or less, it should be kept in the region of oligopeptides that will not be decomposed into amino acids. Can be. Enzymatic hydrolysis can be stopped by heating to 80 ° C. or higher.
[0015]
The retort food can be, for example, an enteral nutritional diet, a protein-enriched beverage, a beverage such as milk coffee, canned coffee, soup, a paste product such as a fish meat paste product, a livestock meat paste product, or a tofu product, and thus also a liquid product. , Cream, gel or coexistence thereof.
[0016]
Depending on the purpose, the proteinaceous raw material is used in a desired amount in the above-mentioned specific soybean protein or a hydrolyzate thereof alone or in combination with other proteinaceous raw materials such as casein, milk protein and meat protein. After being compounded and processed according to the type, it is filled in a container and heated by retort.
[0017]
For example, milk coffee or canned coffee beverages can be used in combination with casein or milk protein, and soy protein alone protein material can be used for nutritional foods aimed at lowering cholesterol.
[0018]
Further, for example, when the target product is a kneaded product, the soybean protein for retort food or its hydrolyzate is mixed into a single aqueous paste or a paste of fish meat, animal meat, etc., molded and heat-set (heat coagulation). Then, this may be packed in a container together with other sauces and soups and heated by retort, or the paste may be filled in a retort container to perform both retort heating and heat setting.
[0019]
The retort food of the present invention is a so-called retort pouch food called "a plastic film or a metal foil or a multilayered combination of these films packed with a prepared food in a bag-shaped or other shape, and sealed by heat melting. Not only food and pasteurized foods, but also widely refers to foods that are put into airtight containers and packaging, sealed, and then heat and sterilized under pressure. Containers and packaging including canned foods and bottled foods Refers to the whole stuffed food.
[0020]
The heating level depends on the type of microorganisms growing on the food and the physicochemical factors of the food, but is generally higher than 100 ° C. For example, in the case of ordinary non-acid food, the temperature at the center is heated to 120 ° C for 4 minutes or more. Is selected.
[0021]
The soy protein from which the 28-35 kDa protein other than glycinin has been removed in this way is, for example, a white color that is vivid and tasteless even after retort treatment, such as when used as a material for Marbo tofu in retort packs. There are advantages such as not. In any case, even if the soybean protein or its hydrolyzate is used in the present invention at a concentration of 3% or more in the product, the deterioration of the color and flavor derived from the conventional soybean protein can be suppressed even in a retort food. It is.
[0022]
【Example】
Hereinafter, examples of the present invention will be described.
[0023]
Example 1 and Comparative Example To 100 g of low-denatured defatted soybeans, add 1000 ml of water to 100 g of water, stir with a homomixer, adjust to pH 7.5 by adding 1N NaOH, extract at room temperature for 30 minutes, and stir the slurry with a cloth. The squeezed okara was removed, and the insolubles were further removed by centrifugation at 3000 g for 10 minutes. 1000 ml of water was added to the okara and the insoluble matter, and the soluble protein was further extracted by the same operation as described above, and the first and second extracts were mixed to obtain defatted soymilk. Sodium bisulfite was added to the defatted soy milk to a concentration of 10 mM, and the mixture was allowed to stand for 5 minutes, and then adjusted to pH 4.5 with 1N HCl. The precipitated protein was collected by centrifugation (3000 g, 10 minutes) and used as acid precipitated protein. 500 ml of water was added to the acid precipitated protein, sodium sulfate was added to 1 M, and the mixture was stirred to extract the soluble protein, and this was repeated twice. This extracted protein was used as a protein fraction containing no 28 to 34 kDa protein other than glycinin. From the result of SDS-polyacrylamide gel electrophoresis, in this fraction, the 28-34 kDa protein other than glycinin was reduced to 2.2% based on the 7S and 11S protein mass.
[0024]
This protein fraction solution was dialyzed against 100 times water, and soy protein precipitated due to a decrease in ionic strength was collected by centrifugation, neutralized, and lyophilized to prepare a separated protein.
[0025]
Example 2
Sodium sulfate was added to soymilk prepared in the same manner as in Example 1 to a concentration of 10 mM, 5 mM, or 3 mM, stirred, adjusted to pH 2.8 with HCl, and centrifuged (10000 g, 10 minutes). The supernatant was adjusted to pH 4.5 with caustic soda, and the precipitate fraction was collected by centrifugation (3000 g, 10 minutes), and the precipitate was neutralized to prepare a lyophilized separated protein. did. The 28-34 kDa protein other than glycinin of this protein was reduced relative to the 7S, 11S protein.
[0026]
Comparative Example 1
Soymilk prepared in the same manner as in Example 1 was adjusted to pH 4.5 with hydrochloric acid, and the precipitated protein was collected by centrifugation (3000 g, 10 minutes) and neutralized with NaOH to prepare a separated soybean protein. The amount of the 28-34 kDa protein other than glycinin in this protein was 9.0% based on the 7S and 11S proteins.
[0027]
Aqueous solutions each containing 3% of each separated protein obtained in Examples 1 and 2 and Comparative Example 1 were prepared, filled in cans, heated at 121 ° C. for 30 minutes, and the changes in flavor and color after cooling were measured. Sensually evaluated. Sensory evaluation of quality was performed by 20 panelists for two items of color (bright / 10 points to dark / 1 point) and flavor (no taste / 10 points to bad / 1 point), and the average value was shown. The evaluation of the color and flavor is that the smaller of 28 to 34 kDa other than glycinin is not only superior before the retort treatment, but also hardly deteriorated by the retort treatment, that is, it is suitable as a soy protein for retort foods. It was recognized that there was. That is, the soybean protein having a content of 28 to 35 kDa other than glycinin, which is 8% or less, preferably 7% or less, more preferably 5.5% or less based on the total amount of β-conglycinin and glycinin, is good for retort foods. The results are shown.
[0028]
Figure 0003543419
* As described in the text, after electrophoresis by SDS-polyacrylamide gel electrophoresis analysis, the ratio of the absorbance of 28-34 kDa protein other than glycinin to the absorbance of 7S and 11S proteins measured by protein staining and densitometry ( %)
[0029]
Example 3
The soy protein for retort foods prepared in Example 1 was dissolved in water to prepare a 5% solution, and trypsin was allowed to act on the solution, until the protein soluble in a 0.4 M trichloroacetic acid solution became 30%. The reaction was stopped by hydrolysis and heating at 95 ° C. for 15 minutes. The hydrolyzed solution was packed in a can, heated at 121 ° C. for 30 minutes, and the change in flavor and color after cooling was evaluated organoleptically.
[0030]
The comparison was the same as in this example except that the isolated soybean protein prepared in Comparative Example 1 was used in place of the soybean protein for retort foods. One was significantly better in color and flavor than the comparison.
[0031]
Example 4
5 parts by weight of the separated protein obtained in Example 1 or Comparative Example 1 (the following parts are parts by weight) were mixed with 30 parts of rapeseed oil, 5 parts of sucrose, and 60 parts of water, and homogenized (80 kg / cm 2 ) emulsified beverage After filling in a can and performing a retort treatment at 121 ° C. for 30 minutes, the change in color and flavor was confirmed by the same sensory evaluation method as in Example and Comparative Example 1.
[0032]
Figure 0003543419
[0033]
As shown in the above results, it was recognized that in the emulsified beverage, in the fraction containing no protein of 28 to 35 kDa other than glycinin, deterioration in color and flavor due to the retort treatment was remarkably prevented.
[0034]
Example 5
6 parts of the isolated protein obtained in Example 1 or Comparative Example 1 was mixed with 30 parts of fish meat surimi, 29 parts of rapeseed oil, 5 parts of flavoring agent, and 30 parts of water, and the mixture was packed in a casing tube and retorted at 121 ° C. for 30 minutes. Processing was performed to obtain retort sausage. When the color and flavor of the product after the retort were evaluated, the retort sausage using the isolated soybean protein of Example 1 was clearly superior to the retort sausage using the isolated soybean protein of the comparative example.
[0035]
Example 6
Using the two separated proteins used in Example 1 and Comparative Example 1, dough was prepared according to the composition shown in the following table, molded (10 cm × 5 cm × 1 cm), steamed and heated to produce “tofu steak”. This “tofu steak” and sauce (composed of commercially available seasonings, sugar, concentrated soy sauce, mirin, sake, starch and water) are filled in a 1: 1 mixture into a retort bag, degassed and sealed. And the change in color and flavor was confirmed by the same sensory evaluation method as in Example 1 and the like. As a result, the retort-heated soybean protein food prepared from the isolated soybean protein also contained 28 to 34 kDa other than glycinin. It was confirmed that the fraction from which the protein was removed had little deterioration in color and flavor due to the retort treatment and had good quality.
[0036]
Figure 0003543419
[0037]
【The invention's effect】
As described above, the soybean protein in which the protein of 28 to 35 kDa other than glycinin has been substantially reduced, or the hydrolyzate thereof, can be used as part or all of the proteinaceous component and subjected to retort treatment. It is possible to obtain a retort food in which the deterioration of color and flavor is suppressed, and therefore, the use of soy protein is expanded, and the functions of the soy protein such as emulsification, protein fortification, and gelling power in the food of the retort food are useful. Can be made.

Claims (3)

グリシニン以外の28〜35kDaの蛋白質がβ−コングリシニン及びグリシニンの総和量に対して8%以下であるレトルト食品用大豆蛋白質。A soy protein for retort foods, wherein the protein of 28 to 35 kDa other than glycinin is 8% or less based on the total amount of β-conglycinin and glycinin . グリシニン以外の28〜35kDaの蛋白質がβ−コングリシニン及びグリシニンの総和量に対して8%以下である大豆蛋白質またはその加水分解物を、蛋白性原料の一部または全部として含有するレトルト食品。A retort food containing soybean protein or a hydrolyzate of soybean protein in which 28-35 kDa protein other than glycinin is 8% or less based on the total amount of β-conglycinin and glycinin, as a part or all of a proteinaceous raw material. レトルト食品が、飲料、練製品、または豆腐類製品である請求項記載のレトルト食品。The retort food according to claim 2 , wherein the retort food is a beverage, a pasty product, or a tofu product.
JP13974195A 1995-06-06 1995-06-06 Soy protein for retort food and retort food Expired - Fee Related JP3543419B2 (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP13974195A JP3543419B2 (en) 1995-06-06 1995-06-06 Soy protein for retort food and retort food

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP13974195A JP3543419B2 (en) 1995-06-06 1995-06-06 Soy protein for retort food and retort food

Publications (2)

Publication Number Publication Date
JPH08332029A JPH08332029A (en) 1996-12-17
JP3543419B2 true JP3543419B2 (en) 2004-07-14

Family

ID=15252304

Family Applications (1)

Application Number Title Priority Date Filing Date
JP13974195A Expired - Fee Related JP3543419B2 (en) 1995-06-06 1995-06-06 Soy protein for retort food and retort food

Country Status (1)

Country Link
JP (1) JP3543419B2 (en)

Families Citing this family (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP1860959A2 (en) * 2005-03-22 2007-12-05 Solae, LLC A stable soy protein beverage composition

Also Published As

Publication number Publication date
JPH08332029A (en) 1996-12-17

Similar Documents

Publication Publication Date Title
US7465470B2 (en) Process for producing a soybean protein usable in acidic foods
Nishinari et al. Soy as a food ingredient
US3944676A (en) Process for the manufacture of soybean protein products
US5597607A (en) Process for preparing fractionated soybean proteins and foods using the same
JP6191822B2 (en) Concentrated soy protein material
EP1459635A1 (en) Transglutaminase cross-linked soy protein composition, fish and meat products and analogues thereof
JP2765489B2 (en) Soy protein and its manufacturing method
US5674548A (en) Defatted soybean milk, soybean protein and soybean protein material and process for preparing them
US4426395A (en) Retort salad and its production process
JP2008237127A (en) Soybean protein hydrolysate and its production method
JP3543419B2 (en) Soy protein for retort food and retort food
EP0752212A2 (en) Process for preparing fractionated soybean proteins and foods using the same
JP4479592B2 (en) Retort food
JP3824082B2 (en) Method for producing soy milk card
JP3484428B2 (en) Method for producing yeast extract
JPH0581219B2 (en)
JPH06209716A (en) Production of mixed protein crosslinked with soybean casein
JPWO2006038413A1 (en) Egg food material or processed egg product
JPH0365745B2 (en)
JP7450397B2 (en) Protein coagulant, protein-containing food and drink, physical property improving agent for protein-containing food and drink, and method for improving the physical properties of protein-containing food and drink
JP2645989B2 (en) Modified tofu and its manufacturing method
JPH0975007A (en) Soybean protein and gelled food
JPH09313111A (en) Soybean protein hydrolyzate and its production
JPH07227217A (en) Highly water-soluble soybean protein
KR20230104458A (en) Preparation method of sauce using enzyme treated egg yolk

Legal Events

Date Code Title Description
TRDD Decision of grant or rejection written
A01 Written decision to grant a patent or to grant a registration (utility model)

Free format text: JAPANESE INTERMEDIATE CODE: A01

Effective date: 20040316

A61 First payment of annual fees (during grant procedure)

Free format text: JAPANESE INTERMEDIATE CODE: A61

Effective date: 20040329

R150 Certificate of patent or registration of utility model

Free format text: JAPANESE INTERMEDIATE CODE: R150

FPAY Renewal fee payment (event date is renewal date of database)

Free format text: PAYMENT UNTIL: 20080416

Year of fee payment: 4

FPAY Renewal fee payment (event date is renewal date of database)

Free format text: PAYMENT UNTIL: 20090416

Year of fee payment: 5

FPAY Renewal fee payment (event date is renewal date of database)

Free format text: PAYMENT UNTIL: 20100416

Year of fee payment: 6

FPAY Renewal fee payment (event date is renewal date of database)

Free format text: PAYMENT UNTIL: 20110416

Year of fee payment: 7

FPAY Renewal fee payment (event date is renewal date of database)

Free format text: PAYMENT UNTIL: 20110416

Year of fee payment: 7

FPAY Renewal fee payment (event date is renewal date of database)

Free format text: PAYMENT UNTIL: 20120416

Year of fee payment: 8

LAPS Cancellation because of no payment of annual fees