JP3894809B2

JP3894809B2 - Mirin and its manufacturing method

Info

Publication number: JP3894809B2
Application number: JP2002050707A
Authority: JP
Inventors: 裕 ▲高▼倉; 義雄 ▲吉▼浜; 彰二垂水
Original assignee: 宝ホールディングス株式会社
Priority date: 2001-03-22
Filing date: 2002-02-27
Publication date: 2007-03-22
Anticipated expiration: 2022-02-27
Also published as: JP2002345449A

Description

【０００１】
【発明の属する技術分野】
本発明は、みりん類の製造方法、及びこれにより得られるみりん類に関する。
【０００２】
【従来の技術】
みりん類の製造において、熟成醪は上槽した後、おり下げ工程、活性炭処理工程、火入れ殺菌工程、及び製品充てん工程を経て、製品として販売されている。このようにして得られたみりん類はグルコースを主成分とする糖質及びアミノ酸、オリゴペプチドといった可溶性窒素成分に富んでおり、これらの成分がさまざまな化学反応により保存中の変化をもたらしている。このような化学反応の一つであるアミノカルボニル反応は、製品みりん類の保存中における着色の増加及び色調の暗色化の原因となっている。これらはみりん類に含有される低分子の糖質、アミノ酸、及びオリゴペプチドによるものと考えられており、みりん類の品質劣化をもたらしている。
【０００３】
みりん類の着色増加及び色調の暗色化を防止する方法として、活性炭処理がある。しかし、この着色防止効果は、活性炭処理工程を行うまでに生じた着色物質を吸着除去しているのみであり、みりん類の保存中の着色の増加が抑制されているのではない。
【０００４】
活性炭処理以外に、みりん類の保存中の着色の進行を遅らせる手段として、柿渋を投入して８８℃以上で火入れを行い凝集物を沈殿清澄化する方法（特公昭５２−４６３８号）、及び乳酸菌を添加した水に糯米を浸漬する方法（特開平１１−１１３５５５号）が提案されている。しかし、柿渋を投入する方法では、着色防止効果は不十分である。また、乳酸菌を添加した水に糯米を浸漬する方法は乳酸菌を別途培養、集菌、及び洗浄する操作が必要であり、製造規模が大きくなるとその設備投資に要する金額も多大なものになる。このため、簡単な方法により製品として市販されているみりん類の着色の増加をさらに遅らせることができる方法の開発が望まれていた。
【０００５】
【発明が解決しようとする課題】
本発明は、このような状況をかんがみてなされたものであり、みりん類の保存中に起こる着色の増加及び色調の暗色化を抑制する方法を提供することを目的とする。
【０００６】
【課題を解決するための手段】
本発明を概説すると、第１の発明はみりん類の製造においており下げ工程を終了し、その後製品充てん工程までの間にプロテアーゼを作用させた後、製品みりん類中に該酵素活性を残存させないための失活又は除去処理を行うことを特徴とする、みりん類の保存中における着色の増加及び色調の暗色化が抑制された、品質劣化の少ないみりん類の製造方法に関し、第２の発明は第１の発明により得られるみりん類に関する。
【０００７】
本発明者らは、みりん類の製造方法及び得られたみりん類について鋭意検討を行った。その結果、みりん類の製造において、おり下げ工程を終了し、その後製品充てん工程までの間にのみりん類に酵素を作用させることにより、みりん類の保存中における着色の増加及び色調の暗色化が抑制されることを見出し、本発明の完成に至った。
【０００８】
【発明の実施の形態】
以下、本発明について具体的に説明する。
本発明におけるみりん類とは、みりん、アルコール含有発酵調味料、及び本直しのことを言う。本発明に使用する酵素は、プロテアーゼであることが好ましい。更に好ましくは、中性〜弱酸性付近で低分子ペプチド分解活性を有するプロテアーゼが好ましい。これらのプロテアーゼとしては、例えば、ヌクレイシン〔阪急共栄物産(株)製〕、オリエンターゼ２２ＢＦ〔阪急共栄物産(株)製〕、オリエンターゼＯＮＳ〔阪急共栄物産(株)製〕、ニュートラーゼ０．８Ｌ〔ノボザイムズジャパン(株)製〕、及びアルカラーゼ２．４Ｌ〔ノボザイムズジャパン（株）製〕を例示することができる。これらの酵素は単独又は組合せて使用することができ、好ましい例として、ヌクレイシンとアルカラーゼとの組合せを挙げることができる。
【０００９】
本発明の酵素はみりん類の製造工程中において、おり下げ工程を終了後、製品充てん工程までの任意の時期に使用するのが好ましい。おり下げ工程を行っていない段階で酵素を作用させると、蛋白質等の生体高分子が酵素作用を妨害するので、本発明の効果が十分発揮されない。おり下げ工程の方法については、蛋白質等の生体高分子を不溶化、沈殿させる方法であれば特に限定はない。なお、みりん類の製造において、おり下げ工程後、あるいはおり下げ工程と同時に活性炭処理工程が一般的に行われているが、本発明における酵素の添加は、おり下げ工程終了後であれば、活性炭処理の有無に関わらず有効である。また、酵素を作用させた後に活性炭処理を行ってもよい。
【００１０】
おり下げ工程を行ったみりん類に酵素を作用させる方法は特に限定はなく、例としては、みりん類に酵素を添加してかくはん溶解させる方法、担体に固定化した酵素を充填したカラム中にみりん類を通過させる方法、等を挙げることができる。本発明において使用する酵素の添加量は、みりん類の着色の増加及び色調の暗色化に対する抑制効果を発揮できる量であれば特に制限はないが、一般的には、酵素の最適条件下、３０℃で１分間に１μｍｏｌの基質を変換させる酵素量を１単位としたとき、みりん類１００ｍｌ当り２７．６単位以上あればよい。しかしながら、酵素の種類により、酵素単位の表示及び測定方法が異なる場合があるので、使用する酵素に適した方法を採用すればよい。例えば、酵素がプロテアーゼの場合、乳製カゼインを基質として、ｐＨ７．０及び３０℃で１分間に１μｇのチロシンに相当するＴＣＡ可溶性のフォリン試薬呈色物質を生成する酵素量を１単位（Ｕ）とし、みりん類１００ｍｌ当り５,０００単位以上であればよい。みりん類に酵素を作用させる温度は、該酵素が失活しない温度であればよく、その時間は長時間の加熱による著しい着色増加が生じない程度であれば特に限定はない。作用させる温度及び時間の一例として、それぞれ５５℃及び５時間を挙げることができる。
【００１１】
酵素を作用させた後は、製品みりん類中に該酵素活性を残存させないための失活又は除去処理を行う。作用させた酵素を失活又は除去する方法は特に限定はないが、例えばみりん類に酵素を直接添加、かくはん溶解して作用させた場合には、加熱失活させる方法を用いることができる。この場合の加熱温度は、該酵素が失活する温度であれば問題はない。担体に固定化した酵素を充填したカラム中にみりん類を通過させて作用させた場合は、当然のことながら酵素の失活又は除去処理は不要である。また、製品充てん前に火入れ殺菌工程を行う場合は、この工程で酵素を失活させることもできる。
【００１２】
本発明における着色抑制の有無は例えば、下記の方法により判定することができる。すなわち、前述の方法に基づいて酵素を作用させたみりん類及び酵素無添加のみりん類（対照）について５５℃で保存試験を行い、経日的に４３０ｎｍにおける吸光度（ＯＤ₄₃₀）を測定する。そして、対照との吸光度の差（ΔＯＤ＝［対照みりん類のＯＤ₄₃₀］−［酵素添加みりん類のＯＤ₄₃₀］）、及び吸光度の比（ΔＯＤ´＝［酵素添加みりん類のＯＤ₄₃₀］／［対照みりん類のＯＤ₄₃₀］）を求める。その結果、ΔＯＤが経日的に増加し、且つΔＯＤ´＜１．０００により着色抑制の有無を評価し、ΔＯＤ及びΔＯＤ´の大小により着色抑制の程度を評価することができる。
【００１３】
また、みりん類の色調を示す指標として、ＯＤ₄₃₀の常用対数（ｌｏｇＯＤ₄₃₀）と５３０ｎｍにおける吸光度（ＯＤ₅₃₀）の常用対数（ｌｏｇＯＤ₅₃₀）との差〔ΔＡ＝ｌｏｇＯＤ₄₃₀−ｌｏｇＯＤ₅₃₀〕を求める。その結果、この値が大きい程、みりん類の色調が明るいと評価できる。
【００１４】
かくして本発明により、保存中の着色増加及び色調の暗色化が抑制された、品質劣化の少ないみりん類が提供される。
【００１５】
【実施例】
以下、本発明を実施例によって更に具体的に説明するが、本発明はこれらの実施例に限定されるものではない。
【００１６】
実施例１
おり下げ前後における酵素添加の影響
市販の酵素製剤としてヌクレイシン〔阪急共栄物産(株)、５０，０００Ｕ／ｇ〕を用い、みりん製造工程の各段階に酵素を作用させ、製品化後のみりんの着色増加に及ぼす影響を調べた。すなわち、表１の仕込配合でみりん醪を調製し、表２に示す３段階でそれぞれヌクレイシンを０．１ｗ／ｖ％添加して５５℃で５時間反応させた。対照として、酵素製剤を添加せずに同様に加温した。
【００１７】
【表１】

【００１８】
【表２】

【００１９】
酵素との反応後、比較例１では常法により上槽し、おり下げ工程、活性炭処理工程、及び火入れ殺菌工程を行って製品みりんを得、保存試験に供した。比較例２では、酵素との反応後おり下げ工程以降比較例１と同じ処理を行い、保存試験に供した。実施例１では、酵素との反応後火入れ殺菌工程を行い、保存試験に供した。保存試験は、５５℃で１１日間行い、０日から経日的に４３０ｎｍの吸光度（ＯＤ₄₃₀）を測定し、ΔＯＤ及びΔＯＤ´を求めた。ΔＯＤ及びΔＯＤ´の変化を表３に示す。酵素添加を行ったみりん、及び酵素反応を行わずに同様に上槽後の工程を経た無処理みりんの一般分析値〔ｐＨ、アミノ窒素（Ｆ−Ｎ）、全窒素（Ｔ−Ｎ）、還元糖（ＤＳ）、及び全糖（ＴＳ）〕を表４に示す。なお、一般分析値は第四回改正国税庁所定分析法注解に基づいて行った。
【００２０】
【表３】

【００２１】
【表４】

【００２２】
表３より、比較例１ではΔＯＤは経日的に減少し、且つΔＯＤ´＞１．０００であり、酵素添加の有無に関わらず変化が見られなかった。一方、比較例２及び実施例１では、ΔＯＤは経日的に上昇したが、その程度は実施例１の方が顕著であった。また、ΔＯＤ´＜１．０００であったが、実施例１の方が低値であった。したがって、みりんに酵素を作用させるのは、おり下げ工程後が適切であることが明らかとなった。表４より火入れ殺菌工程後のみりんの一般分析値に差は見られず、これらの官能評価においても有意差は見られなかった。また、保存試験中におりの発生はいずれの場合においても見られなかった。
【００２３】
実施例２
酵素添加量の影響
市販の酵素製剤としてヌクレイシン〔阪急共栄物産(株)製、５０，０００Ｕ／ｇ〕を用い、おり下げ工程後に異なる酵素濃度で作用させ、製品化後のみりんの着色増加に及ぼす影響を調べた。すなわち、表５の仕込配合に従ってみりん醪を調製して３０℃で３０日間熟成後常法により上槽し、おり下げ工程、活性炭処理工程を行った。これにヌクレイシンを０．１、及び１．０ｗ／ｖ％添加し、５５℃で５時間反応を行った。反応後、火入れ殺菌工程を行い製品化し、保存試験に供した。保存試験は、５５℃で１８日間行い、実施例１と同様にΔＯＤ、ΔＯＤ´を求めた。ΔＯＤ及びΔＯＤ´の変化を表６に示す。
【００２４】
【表５】

【００２５】
【表６】

【００２６】
表６より、ΔＯＤは酵素添加量が０．１及び１．０ｗ／ｖ％のどちらも経日的に増加しており、後者の方が高い増加傾向を示したが、大差ではなかった。ΔＯＤ´は酵素添加量が０．１及び１．０ｗ／ｖ％のどちらもΔＯＤ´＜１．０００であり、後者の方が低値であったが、大差ではなかった。したがって、ヌクレイシンの添加量は０．１ｗ／ｖ％、すなわちみりん１００ｍｌ当り５，０００Ｕで十分であることが明らかとなった。火入れ殺菌工程後のみりんの一般分析値及び官能評価においては有意差が見られなかった。また、保存試験中におりの発生はいずれの場合においても見られなかった。
【００２７】
実施例３
酵素の種類の影響
市販の酵素製剤としてヌクレイシン〔阪急共栄物産(株)製、５０，０００Ｕ／ｇ〕、オリエンターゼ２２ＢＦ〔阪急共栄物産(株)製、２２０，０００Ｕ／ｇ〕、及びオリエンターゼＯＮＳ〔阪急共栄物産(株)製、１００，０００Ｕ／ｇ〕を用い、製品化後のみりんの着色増加に及ぼす影響を調べた。表５の仕込配合に従ってみりん醪を調製して３０℃で３０日間熟成後、常法により上槽し、おり下げ工程、及び活性炭処理工程を行った。これに各酵素製剤を０．１ｗ／ｖ％添加し、５５℃で５時間反応を行った。反応後、火入れ殺菌工程を行い製品化し、保存試験に供した。保存試験は、５５℃で１４日間行い、実施例１と同様にΔＯＤ及びΔＯＤ´を求めた。ΔＯＤ及びΔＯＤ´の変化を表７に示す。
【００２８】
【表７】

【００２９】
表８より、ΔＯＤは用いた酵素剤の種類に関係なく経日的に増加しており、またΔＯＤ´＜１．０００であった。したがって、みりんに該酵素を添加することにより着色抑制効果が見られることが明らかになった。火入れ殺菌工程後のみりんの一般分析値及び官能評価においては有意差が見られなかった。また、保存試験中におりの発生はいずれの場合においても見られなかった。
【００３０】
実施例４
酵素の添加による着色増加及び色調への影響
市販の酵素製剤としてニュートラーゼ０．８Ｌ〔ノボザイムズジャパン(株)製、８５，０００Ｕ／ｍｌ〕を用い、製品化後のみりんの着色増加及び色調に及ぼす影響を調べた。表５の仕込配合に従ってみりん醪を調製して３０℃で３０日間熟成後、常法により上槽し、おり下げ工程、及び活性炭処理工程を行った。これに酵素製剤を０．１ｖ／ｖ％添加し、５５℃で５時間反応を行った。反応後、火入れ殺菌工程を行い製品化し、保存試験に供した。保存試験は５５℃で行い、実施例１と同様にΔＯＤ及びΔＯＤ´、並びに色調として、ΔＡを経日的に求めた。対照として、酵素剤を添加せずに反応、火入れ殺菌、及び製品化を行った。その結果、ΔＯＤが経日的に増加し、ΔＯＤ´＜１．０００であったので、酵素剤の添加による着色増加の抑制が認められた。ΔＡの変化は図１に示すように、保存７日目以降には酵素剤を添加したみりんの方がΔＡが大きくなった。更に、これ以降、酵素剤の添加の有無によるみりんの保存中におけるΔＡの差は経日的に増大し、保存２８日目以降はその差が一定になった。したがって、おり下げ処理工程後のみりんに酵素剤を添加することにより、製品化みりんの保存中における着色の増加及び色調の暗色化への抑制効果が見られることが明らかになった。火入れ殺菌工程後のみりんの一般分析値及び官能評価においては有意差が見られなかった。また、保存試験中におりの発生はいずれの場合においても見られなかった。
【００３１】
実施例５
酵素の添加による色調への影響（２）
市販の酵素製剤としてヌクレイシン〔阪急共栄物産(株)製、５０，０００Ｕ／ｇ〕、及びアルカラーゼ２．４Ｌ〔ノボザイムズジャパン（株）製、９１，０００Ｕ／ｍｌ〕を用い、製品化後のみりんの着色増加及び色調に及ぼす影響を調べた。表５の仕込配合に従ってみりん醪を調製して３０℃で３０日間熟成後、常法により上槽し、おり下げ工程、及び活性炭処理工程を行った。これにヌクレイシインを０．１ｗ／ｖ％又はアルカラーゼ２．４Ｌを０．１ｖ／ｖ％添加し、５５℃で５時間反応を行った。反応後、火入れ殺菌工程を行い製品化し、保存試験に供した。保存試験は５５℃で行い、実施例１と同様にΔＯＤ及びΔＯＤ´、並びに色調としてΔＡを求めた。対照として、酵素剤を添加せずに反応、火入れ殺菌、及び製品化を行った。その結果、酵素剤の種類に関係なく、ΔＯＤは経日的に増加し、ΔＯＤ´＜１．０００であった。保存中におけるΔＡの経日的な変化は、実施例４と同様に酵素剤を添加したみりんの方が大きく、その差は保存日数の経過と共に増大し、保存２８日目以降は一定になった。保存４２日目の各みりんのΔＡを図２に示すが、このように各みりんのΔＡは酵素剤を添加したみりんの方が大きかった。したがって、おり下げ処理工程後のみりんに酵素剤を添加することにより、保存中における着色の増加及び色調の暗色化への抑制効果が見られることが明らかになった。火入れ殺菌工程後のみりんの一般分析値及び官能評価においては有意差が見られなかった。また、保存試験中におりの発生はいずれの場合においても見られなかった。
【００３２】
実施例６
酵素の作用温度による着色及び色調への影響
市販の酵素製剤としてヌクレイシン〔阪急共栄物産(株)製、５０，０００Ｕ／ｇ〕を用い、酵素の作用温度による製品化後のみりんの着色増加及び色調に及ぼす影響を調べた。表５の仕込配合に従って新たにみりん醪を調製して３０℃で３０日間熟成後、常法により上槽し、おり下げ工程、及び活性炭処理工程を行った。これに酵素製剤を０．１ｗ／ｖ％添加し、４０、５０、又は６０℃で５時間反応を行った。反応後、火入れ殺菌工程を行い製品化し、保存試験に供した。保存試験は５５℃で行い、実施例１と同様にΔＯＤ及びΔＯＤ´、並びに色調としてΔＡを求めた。対照として、酵素剤を添加せずに各温度で反応、火入れ殺菌、及び製品化を行った。その結果、ΔＯＤは経日的に増加し、ΔＯＤ´＜１．０００であった。特に、酵素を作用させる温度が５０℃及び６０℃の方が、ΔＯＤの増加傾向は大きく、ΔＯＤ´はこれらの温度で作用させた方が、小さい値であった。保存中におけるΔＡの経日的な変化は、酵素剤の作用温度に関係なく、実施例４と同様に酵素剤を添加したみりんの方が大きく、その差は保存日数の経過と共に増大し、保存２８日目以降は一定になった。保存２８日目の各みりんのΔＡを図３に示すが、このように各みりんのΔＡは酵素剤を添加したみりんの方が大きく、酵素の有無によるその差は５０℃の時が最も大きく、次いで６０℃、４０℃の順であった。したがって、おり下げ処理工程後のみりんに酵素を４０〜６０℃で作用させることにより、着色の抑制効果及び色調の暗色化への抑制効果が見られることが明らかになり、特に５０〜６０℃で酵素を作用させることが効果的であることが明らかになった。火入れ殺菌工程後のみりんの一般分析値及び官能検査においては有意差が見られなかった。また、保存試験中におりの発生はいずれの場合においても見られなかった。
【００３３】
【発明の効果】
本発明によれば、みりん類の製造において、おり下げ処理工程を終了し、その後製品充てん工程までの間にプロテアーゼを作用させた後、製品みりん類中に該酵素活性を残存させないための失活又は除去処理を行うことにより、従来のみりん類よりも保存中における着色の増加及び色調の暗色化が抑制された、品質劣化の少ないみりん類を得ることができる。
【図面の簡単な説明】
【図１】酵素剤としてニュートラーゼ０．８Ｌを０．１ｖ／ｖ％添加したみりんの５５℃で保存中におけるΔＡ（色調）の変化を示す図である。
【図２】酵素剤としてヌクレイシンを０．１ｗ／ｖ又はアルカラーゼ２．４Ｌを０．１ｖ／ｖ％添加したみりんの５５℃で４２日保存におけるΔＡ（色調）を示す図である。
【図３】酵素剤としてヌクレイシンを０．１ｗ／ｖ％添加したみりんの４０、５０、又は６０℃で反応後の５５℃で２８日保存におけるΔＡ（色調）を示す図である。[0001]
BACKGROUND OF THE INVENTION
The present invention relates to a method for producing mirin and mirin obtained thereby.
[0002]
[Prior art]
In the production of mirin, ripened rice cake is sold as a product after going through the upper tank, through the lowering process, the activated carbon treatment process, the fire sterilization process, and the product filling process. Mirins thus obtained are rich in soluble nitrogen components such as carbohydrates and amino acids and oligopeptides mainly composed of glucose, and these components cause changes during storage by various chemical reactions. The aminocarbonyl reaction, which is one of such chemical reactions, causes an increase in coloration and darkening of the color tone during storage of product mirins. These are thought to be due to low molecular weight sugars, amino acids, and oligopeptides contained in mirins, which leads to quality degradation of mirins.
[0003]
As a method for preventing an increase in coloring of mirins and darkening of the color tone, there is an activated carbon treatment. However, this anti-coloring effect only adsorbs and removes the colored substances produced up to the activated carbon treatment step, and does not suppress an increase in coloring during storage of mirins.
[0004]
In addition to the activated carbon treatment, as a means of delaying the progress of coloring during storage of mirins, a method of throwing astringent astringents and firing at 88 ° C. or higher to precipitate and clarify aggregates (Japanese Patent Publication No. 52-4638), and lactic acid bacteria There has been proposed a method (Japanese Patent Laid-Open No. 11-113555) for immersing rice bran in water to which is added. However, the coloring prevention effect is not sufficient in the method of throwing the astringency. Moreover, the method of immersing glutinous rice in water to which lactic acid bacteria have been added requires operations for separately culturing, collecting and washing the lactic acid bacteria, and as the production scale increases, the amount of capital investment required increases. Therefore, it has been desired to develop a method capable of further delaying the increase in coloring of mirins marketed as a product by a simple method.
[0005]
[Problems to be solved by the invention]
This invention is made | formed in view of such a condition, and it aims at providing the method of suppressing the increase in coloring and darkening of a color tone which occur during the preservation | save of mirin.
[0006]
[Means for Solving the Problems]
Outline of the present invention is that the first invention does not leave the enzyme activity in the product mirins after the lowering process is finished in the production of mirins and the protease is allowed to act after the product filling process. and performing deactivation or removal treatment, darkening of the color and increased color during storage of mirin compound is suppressed, relates to a process for the production of small mirin such quality deterioration, the second invention is the The present invention relates to mirin obtained by the invention of 1.
[0007]
The present inventors diligently studied a method for producing mirins and the obtained mirins. As a result, in the production of mirins, by causing the enzyme to act on the phosphorous only during the period between the lowering process and the subsequent product filling process, there is an increase in coloration and darkening of the color tone during the preservation of mirins. It was found that it was suppressed, and the present invention was completed.
[0008]
DETAILED DESCRIPTION OF THE INVENTION
Hereinafter, the present invention will be specifically described.
The mirins in the present invention refer to mirin, alcohol-containing fermented seasonings, and rework. The enzyme used in the present invention is preferably a protease. More preferably, a protease having a low molecular weight peptide-degrading activity near neutral to weakly acidic is preferred. Examples of these proteases include, for example, Nucleicin (manufactured by Hankyu Kyoei Bussan Co., Ltd.), Orientase 22BF (manufactured by Hankyu Kyoei Bussan Co., Ltd.), Orientase ONS (manufactured by Hankyu Kyoei Bussan Co., Ltd.), Neutase 0.8L [Novozymes Japan K.K.] and Alcalase 2.4L [Novozymes Japan K.K.] can be exemplified. These enzymes can be used alone or in combination, and preferred examples include a combination of nucleicin and alcalase.
[0009]
The enzyme of the present invention is preferably used at any time from the end of the lowering step to the product filling step in the manufacturing process of mirin. If the enzyme is allowed to act at a stage where the lowering process is not performed, biopolymers such as proteins interfere with the enzyme action, so that the effects of the present invention are not sufficiently exhibited. The method of the lowering step is not particularly limited as long as it is a method for insolubilizing and precipitating biopolymers such as proteins. In the production of mirins, an activated carbon treatment process is generally performed after the lowering process or simultaneously with the lowering process. It is effective regardless of the presence or absence of processing. Moreover, you may perform activated carbon treatment after making an enzyme act.
[0010]
There is no particular limitation on the method of allowing the enzyme to act on mirins subjected to the lowering process. Examples of the method include adding an enzyme to mirin and stirring and dissolving, mirin in a column packed with an enzyme immobilized on a carrier. And the like, and the like. The amount of the enzyme used in the present invention is not particularly limited as long as it can exert an inhibitory effect on the increase in coloring of mirins and the darkening of the color tone. Assuming that the amount of enzyme that converts 1 μmol of substrate per minute at 1 ° C. is 1 unit, it may be 27.6 units or more per 100 ml of mirins. However, since the enzyme unit display and measurement method may vary depending on the type of enzyme, a method suitable for the enzyme used may be employed. For example, when the enzyme is a protease, the amount of enzyme that produces a TCA-soluble forin reagent colorant corresponding to 1 μg of tyrosine per minute at pH 7.0 and 30 ° C. using dairy casein as a substrate is 1 unit (U) And 5,000 units or more per 100 ml of mirin. The temperature at which the enzyme is allowed to act on mirins is not particularly limited as long as the enzyme does not deactivate, and the time is such that no significant increase in coloration due to prolonged heating occurs. As an example of the temperature and time to act, 55 degreeC and 5 hours can be mentioned, respectively.
[0011]
After the enzyme is allowed to act, a deactivation or removal treatment is performed to prevent the enzyme activity from remaining in the product mirin. The method for inactivating or removing the acted enzyme is not particularly limited. For example, when the enzyme is directly added to mirins and stirred and dissolved to act, a method for inactivating by heating can be used. The heating temperature in this case is not a problem as long as the enzyme is deactivated. When mirins are allowed to act through a column packed with an enzyme immobilized on a carrier, it is of course unnecessary to deactivate or remove the enzyme. Moreover, when performing a flame sterilization process before product filling, an enzyme can also be deactivated by this process.
[0012]
The presence or absence of color suppression in the present invention can be determined, for example, by the following method. That is, a storage test is carried out at 55 ° C. for mirins subjected to the enzyme action and mirins with no enzyme added (control) based on the method described above, and the absorbance (OD ₄₃₀ ) at ₄₃₀ nm is measured over time. The difference in absorbance between the control (.DELTA.OD = [control mirin acids OD _430] - [OD ₄₃₀ of enzyme addition mirin acids]), and the ratio of absorbance (ΔOD' = [OD ₄₃₀ of enzyme addition mirin acids] / [ Determine the OD ₄₃₀ ]) of the control mirin. As a result, ΔOD increases with time, and the presence / absence of coloring suppression can be evaluated by ΔOD ′ <1.000, and the degree of coloring suppression can be evaluated by the magnitude of ΔOD and ΔOD ′.
[0013]
Further, as an index indicating the color tone of mirin acids determines the difference [ΔA = logOD ₄₃₀ -logOD _530] the common logarithm of common logarithm of the OD _₄₃₀ (logOD ₄₃₀₎ and the absorbance at _{_{530nm (OD 530) (logOD 530}} ). As a result, it can be evaluated that the larger the value, the brighter the color of mirins.
[0014]
Thus, according to the present invention, there are provided mirins with reduced quality deterioration in which increase in coloring during storage and darkening of color tone are suppressed.
[0015]
【Example】
EXAMPLES Hereinafter, the present invention will be described more specifically with reference to examples, but the present invention is not limited to these examples.
[0016]
Example 1
Effect of enzyme addition before and after lowering: Nucleicin (Hankyu Kyoei Bussan Co., Ltd., 50,000 U / g) is used as a commercially available enzyme preparation. Enzyme is allowed to act on each stage of the mirin production process, and coloring of phosphorus only after commercialization. The effect on the increase was investigated. That is, mirin koji was prepared with the charging composition shown in Table 1, and 0.1 w / v% of nucleicin was added in each of the three stages shown in Table 2 and reacted at 55 ° C. for 5 hours. As a control, warming was similarly performed without adding the enzyme preparation.
[0017]
[Table 1]

[0018]
[Table 2]

[0019]
After the reaction with the enzyme, in Comparative Example 1, an upper tank was prepared by a conventional method, and a product mirin was obtained by performing a lowering process, an activated carbon treatment process, and a fired sterilization process, and subjected to a storage test. In Comparative Example 2, the same treatment as Comparative Example 1 was performed after the lowering step after the reaction with the enzyme and subjected to a storage test. In Example 1, after the reaction with the enzyme, a flame sterilization step was performed and subjected to a storage test. The storage test was carried out at 55 ° C. for 11 days, and absorbance at 430 nm (OD ₄₃₀ ) was measured daily from day 0 to obtain ΔOD and ΔOD ′. Table 3 shows changes in ΔOD and ΔOD ′. General analysis values of mirin with added enzyme and untreated mirin without the enzymatic reaction and after the upper tank [pH, amino nitrogen (FN), total nitrogen (TN), reduction Sugars (DS) and total sugars (TS)] are shown in Table 4. The general analysis values were based on the fourth revision of the NTA-specified analysis method.
[0020]
[Table 3]

[0021]
[Table 4]

[0022]
From Table 3, in Comparative Example 1, ΔOD decreased with time and ΔOD ′> 1.000, and no change was observed regardless of the presence or absence of enzyme addition. On the other hand, in Comparative Example 2 and Example 1, ΔOD increased with time, but the degree was more remarkable in Example 1. Further, ΔOD ′ <1.000, but the value in Example 1 was lower. Therefore, it became clear that the enzyme was allowed to act on mirin after the lowering step. From Table 4, no difference was found in the general analysis value of phosphorus only after the flame sterilization process, and no significant difference was found in these sensory evaluations. In addition, no occurrence of defects during the storage test was observed in any case.
[0023]
Example 2
Effect of enzyme addition amount Nucleicin (manufactured by Hankyu Kyoei Bussan Co., Ltd., 50,000 U / g) is used as a commercially available enzyme preparation, and it is allowed to act at different enzyme concentrations after the lowering process, affecting the increase in coloring of phosphorus only after commercialization. The effect was investigated. That is, mirin koji was prepared according to the charging composition shown in Table 5 and aged for 30 days at 30 ° C. and then placed in a conventional manner, followed by a lowering process and an activated carbon treatment process. 0.1 and 1.0 w / v% of nucleicin were added thereto, and the reaction was performed at 55 ° C. for 5 hours. After the reaction, a fire sterilization process was performed to produce a product, which was subjected to a storage test. The storage test was conducted at 55 ° C. for 18 days, and ΔOD and ΔOD ′ were determined in the same manner as in Example 1. Table 6 shows changes in ΔOD and ΔOD ′.
[0024]
[Table 5]

[0025]
[Table 6]

[0026]
From Table 6, ΔOD increased with time for both 0.1 and 1.0 w / v% of enzyme addition, and the latter showed a higher tendency of increase, but it was not a large difference. ΔOD ′ was ΔOD ′ <1.000 in both cases where the enzyme addition amount was 0.1 and 1.0 w / v%, and the latter was lower, but was not significantly different. Therefore, it was revealed that the amount of nucleicin added was 0.1 w / v%, that is, 5,000 U per 100 ml of mirin. There was no significant difference in the general analytical value and sensory evaluation of phosphorus only after the flame sterilization process. In addition, no occurrence of defects during the storage test was observed in any case.
[0027]
Example 3
Effect of enzyme type As commercially available enzyme preparations, Nuclein [Hankyu Kyoei Bussan Co., Ltd., 50,000 U / g], Orientase 22BF [Hankyu Kyoei Bussan Co., Ltd., 220,000 U / g], and Orientase ONS [Hankyu Kyoei Bussan Co., Ltd., 100,000 U / g] was used to examine the effect on phosphorus coloring increase only after commercialization. According to the charging composition shown in Table 5, mirin koji was prepared and aged at 30 ° C. for 30 days, and then an upper tank was prepared by a conventional method, followed by a lowering process and an activated carbon treatment process. 0.1 w / v% of each enzyme preparation was added thereto, and the reaction was performed at 55 ° C. for 5 hours. After the reaction, a fire sterilization process was performed to produce a product, which was subjected to a storage test. The storage test was conducted at 55 ° C. for 14 days, and ΔOD and ΔOD ′ were determined in the same manner as in Example 1. Changes in ΔOD and ΔOD ′ are shown in Table 7.
[0028]
[Table 7]

[0029]
From Table 8, ΔOD increased with time regardless of the type of enzyme used, and ΔOD ′ <1.000. Therefore, it became clear that the coloring suppression effect was seen by adding this enzyme to mirin. There was no significant difference in the general analytical value and sensory evaluation of phosphorus only after the flame sterilization process. In addition, no occurrence of defects during the storage test was observed in any case.
[0030]
Example 4
Effect of color increase and color tone by addition of enzyme Neutase 0.8L (Novozymes Japan Co., Ltd., 85,000 U / ml) is used as a commercially available enzyme preparation. The effect was investigated. According to the charging composition shown in Table 5, mirin koji was prepared and aged at 30 ° C. for 30 days, and then an upper tank was prepared by a conventional method, followed by a lowering process and an activated carbon treatment process. To this was added 0.1 v / v% of the enzyme preparation and reacted at 55 ° C. for 5 hours. After the reaction, a fire sterilization process was performed to produce a product, which was subjected to a storage test. The storage test was performed at 55 ° C., and ΔA and ΔOD ′ and color tone were obtained over time as in Example 1. As a control, reaction, flame sterilization, and commercialization were performed without adding the enzyme agent. As a result, ΔOD increased with time and ΔOD ′ <1.000. Therefore, suppression of increase in coloration due to the addition of the enzyme agent was recognized. As shown in FIG. 1, the change in ΔA was larger in mirin with the enzyme added after the seventh day of storage. Furthermore, after that, the difference in ΔA during storage of mirin with and without the addition of the enzyme agent increased with time, and the difference became constant after 28 days of storage. Therefore, it was clarified that by adding an enzyme agent to phosphorus only after the lowering treatment step, an effect of increasing coloring during storage of commercialized mirin and suppressing darkening of the color tone can be seen. There was no significant difference in the general analytical value and sensory evaluation of phosphorus only after the flame sterilization process. In addition, no occurrence of defects during the storage test was observed in any case.
[0031]
Example 5
Influence on color tone by addition of enzyme (2)
As commercial enzyme preparations, Nucleicin (Hankyu Kyoei Bussan Co., Ltd., 50,000 U / g) and Alcalase 2.4 L (Novozymes Japan Co., Ltd., 91,000 U / ml) were used. The effect on color increase and color tone was investigated. According to the charging composition shown in Table 5, mirin koji was prepared and aged at 30 ° C. for 30 days, and then an upper tank was prepared by a conventional method, followed by a lowering process and an activated carbon treatment process. To this was added 0.1 w / v% of nucleicin or 0.1 v / v% of alcalase 2.4 L, and the reaction was carried out at 55 ° C. for 5 hours. After the reaction, a fire sterilization process was performed to produce a product, which was subjected to a storage test. The storage test was performed at 55 ° C., and ΔOD and ΔOD ′ were obtained in the same manner as in Example 1, and ΔA was obtained as the color tone. As a control, reaction, flame sterilization, and commercialization were performed without adding the enzyme agent. As a result, regardless of the type of enzyme agent, ΔOD increased with time, and ΔOD ′ <1.000. The change over time in ΔA during storage was greater for mirin to which the enzyme agent was added as in Example 4, and the difference increased with the passage of storage days, and became constant after the 28th day of storage. . The ΔA of each mirin on the 42nd day of storage is shown in FIG. 2. Thus, the ΔA of each mirin was larger for mirin with the addition of an enzyme agent. Therefore, it has been clarified that by adding an enzyme agent to phosphorus only after the lowering treatment step, an increase in coloring during storage and a suppression effect on darkening of the color tone can be seen. There was no significant difference in the general analytical value and sensory evaluation of phosphorus only after the flame sterilization process. In addition, no occurrence of defects during the storage test was observed in any case.
[0032]
Example 6
Effect of enzyme working temperature on coloring and color tone Nucleicin (manufactured by Hankyu Kyoei Bussan Co., Ltd., 50,000 U / g) was used as a commercially available enzyme preparation. The effects on the A freshly prepared mirin koji was prepared according to the charging composition shown in Table 5, and after aging at 30 ° C. for 30 days, it was placed in an upper tank by a conventional method, followed by a lowering process and an activated carbon treatment process. To this, 0.1 w / v% of the enzyme preparation was added and reacted at 40, 50, or 60 ° C. for 5 hours. After the reaction, a fire sterilization process was performed to produce a product, which was subjected to a storage test. The storage test was performed at 55 ° C., and ΔOD and ΔOD ′ were obtained in the same manner as in Example 1, and ΔA was obtained as the color tone. As a control, reaction, flame sterilization, and commercialization were performed at each temperature without adding the enzyme agent. As a result, ΔOD increased with time, and ΔOD ′ <1.000. In particular, when the temperature at which the enzyme is allowed to act is 50 ° C. and 60 ° C., the increase tendency of ΔOD is large, and ΔOD ′ is a small value when acting at these temperatures. The change of ΔA over time during storage is greater for mirin to which the enzyme agent is added, as in Example 4, regardless of the working temperature of the enzyme agent, and the difference increases with the passage of storage days. It became constant after the 28th day. The ΔA of each mirin on the 28th day of storage is shown in FIG. 3. Thus, the ΔA of each mirin is larger in mirin with the addition of an enzyme agent, and the difference depending on the presence or absence of the enzyme is greatest at 50 ° C. Next, the order was 60 ° C. and 40 ° C. Therefore, it becomes clear that the effect of suppressing the coloring and the darkening of the color tone can be seen by allowing the enzyme to act on phosphorus at 40-60 ° C. only after the lowering treatment step, particularly at 50-60 ° C. It became clear that it was effective to make an enzyme act. There was no significant difference in the general analytical value and sensory test of phosphorus only after the flame sterilization process. In addition, no occurrence of defects during the storage test was observed in any case.
[0033]
【The invention's effect】
According to the present invention, in the production of mirins, after the lowering process is completed and the protease is allowed to act until the product filling process , the deactivation is performed so that the enzyme activity does not remain in the mirins. Alternatively, by performing the removal treatment, it is possible to obtain mirins with less deterioration in quality, in which an increase in coloring during storage and darkening of the color tone are suppressed as compared with conventional phosphorous compounds.
[Brief description of the drawings]
FIG. 1 is a graph showing changes in ΔA (color tone) during storage at 55 ° C. of mirin added with 0.1 v / v% of neutase 0.8 L as an enzyme agent.
FIG. 2 is a graph showing ΔA (color tone) of mirin added with 0.1 w / v of nuclasin or 0.1 v / v% of alcalase as an enzyme agent at 42 ° C. for 42 days.
FIG. 3 is a diagram showing ΔA (color tone) of mirin added with 0.1 w / v% of nucleicin as an enzyme agent after storage at 40, 50, or 60 ° C. and stored at 55 ° C. for 28 days.

Claims

In the production of mirins, after the lowering process is completed and the protease is allowed to act until the product filling process , the inactivation or removal process is performed so that the enzyme activity does not remain in the mirins. A process for producing mirin with little deterioration in quality, in which an increase in coloring during storage of mirin and darkening of color tone is suppressed .

A mirin obtained by the method according to claim 1 .