JP2001061445A - Protease decomposition product - Google Patents

Protease decomposition product

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Publication number
JP2001061445A
JP2001061445A JP24426999A JP24426999A JP2001061445A JP 2001061445 A JP2001061445 A JP 2001061445A JP 24426999 A JP24426999 A JP 24426999A JP 24426999 A JP24426999 A JP 24426999A JP 2001061445 A JP2001061445 A JP 2001061445A
Authority
JP
Japan
Prior art keywords
protein
protease
amino acid
enzyme
action
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
JP24426999A
Other languages
Japanese (ja)
Other versions
JP4334698B2 (en
Inventor
Motonori Koide
元紀 小出
Kazuhiko Hirano
和彦 平野
Takeshi Uchida
武 打田
Keiichi Kubota
啓一 久保田
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.)
Taiyo Kagaku KK
Original Assignee
Taiyo Kagaku KK
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Filing date
Publication date
Application filed by Taiyo Kagaku KK filed Critical Taiyo Kagaku KK
Priority to JP24426999A priority Critical patent/JP4334698B2/en
Publication of JP2001061445A publication Critical patent/JP2001061445A/en
Application granted granted Critical
Publication of JP4334698B2 publication Critical patent/JP4334698B2/en
Anticipated expiration legal-status Critical
Expired - Lifetime legal-status Critical Current

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Abstract

PROBLEM TO BE SOLVED: To provide a protease decomposition product free from salt, producible at a low cost and having the advantages of a protease decomposition product having high amino acid conversion comprising the physiological functions such as hypotensive action, antioxidation action, lipid metabolism promoting action, immunopotentiation action, blood cholesterol reducing action, alcohol absorption inhibiting action and iron and calcium absorption promoting action and the lowering of allergenic effect and attracting attention, owing to the above functions, as a material usable in the fields of foods, cosmetics, pharmaceuticals, etc. SOLUTION: A protease decomposition product having an amino acid conversion of >=65% and thick taste can be produced by treating a chicken egg protein having high amino acid score with a protease under alkaline condition and hydrolyzing the product with rice malt.

Description

【発明の詳細な説明】DETAILED DESCRIPTION OF THE INVENTION

【0001】[0001]

【発明の属する技術分野】本発明は、アルカリ条件下で
鶏卵蛋白質に蛋白分解酵素を処理した後に麹を作用させ
ることにより得られる蛋白酵素分解物及び該蛋白酵素分
解物を含有する食品、栄養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 protein enzyme digest obtained by treating a chicken egg protein with a protease under alkaline conditions and then allowing the koji to act thereon, and a food or nutrient containing the protein enzyme digest. It is about.

【0002】[0002]

【従来の技術】従来、蛋白酵素分解物は蛋白分解酵素も
しくは塩酸分解等による加水分解で得られ、原料蛋白質
の供給源としては植物由来、動物由来の蛋白質が用いら
れる。植物由来の蛋白質としては、大豆、小麦、トウモ
ロコシ等があり、動物由来の蛋白質としては、魚肉、畜
肉、牛乳、鶏卵等がある。
2. Description of the Related Art Conventionally, a proteolytic product is obtained by hydrolysis using a proteolytic enzyme or hydrochloric acid, and plant and animal-derived proteins are used as a source of raw material proteins. Plant-derived proteins include soybeans, wheat, corn, and the like, and animal-derived proteins include fish meat, animal meat, milk, chicken eggs, and the like.

【0003】蛋白質を分解する方法は塩酸分解等で加水
分解した後、中和する方法や、蛋白質分解酵素によっ
て、ペプチドまで分解する方法。さらに、高温域で分解
する方法などがある。
[0003] Methods for decomposing proteins include a method of hydrolyzing with hydrochloric acid or the like, followed by neutralization, or a method of decomposing to peptides with a protease. Further, there is a method of decomposing in a high temperature range.

【0004】しかしながら通常、蛋白分解酵素による蛋
白質の分解では、蛋白分解物において独特の苦みを生
じ、風味的にも嫌みが感じられ、その使用はかぎられた
ものとなっており、蛋白質を塩酸で加水分解した場合、
加水分解中に変異原物質が副生されることが確認され、
その安全性が問題となりつつある。
[0004] However, usually, when a protein is degraded by a protease, the proteolysate produces a unique bitterness, and the taste is disliked, and its use is limited. When hydrolyzed,
It was confirmed that mutagen was produced as a by-product during hydrolysis,
Its safety is becoming an issue.

【0005】また、原料となる蛋白質はその種類により
栄養価が異なり例えば、母乳の必須アミノ酸を基準にし
た構成必須アミノ酸の百分比(アミノ酸スコア)は、牛
肉(76)、米(50)、小麦(36)、とうもろこし
(40)、魚(69)、大麦(43)となっており、ア
ミノ酸バランスにおいてこれら原料の蛋白質が決して理
想的な蛋白質とは言えないものである。また、従来の鶏
卵蛋白酵素分解物のアミノ酸化率は、最も高いもので5
0〜55%であり、高度に分解されたものは存在しなか
った。
[0005] Further, the protein as a raw material has a different nutritional value depending on the type thereof. For example, the percentage of the essential amino acids (amino acid score) based on the essential amino acids of breast milk is as follows: beef (76), rice (50), wheat ( 36), corn (40), fish (69) and barley (43), and these amino acids are not ideal proteins in terms of amino acid balance. In addition, the amino acid conversion rate of the conventional enzyme digest of egg protein is 5% at the highest.
0-55%, none highly degraded.

【0006】[0006]

【発明が解決しようとする課題】このような背景におい
て、本発明は苦みのない、なおかつ味に厚味を持った蛋
白酵素分解物を提供することを目的とするものである。
SUMMARY OF THE INVENTION Under such a background, an object of the present invention is to provide a protein enzyme hydrolyzate having no bitterness and having a thick taste.

【0007】[0007]

【課題を解決するための手段】本発明者らは、上記課題
の解決に鋭意工夫を重ねた結果、鶏卵蛋白質をアルカリ
条件下で蛋白分解酵素処理した後に、麹を作用させるこ
とにより、卵本来の風味が消去され、味の厚みが増大さ
れ、しかもアミノ酸化率の高い、鶏卵蛋白酵素分解物が
得られるということを見出し本発明を完成した。
Means for Solving the Problems The inventors of the present invention have devoted themselves to solving the above-mentioned problems, and as a result, after treating the egg protein with a protease under alkaline conditions, and then allowing the koji to act, the original egg is obtained. It has been found that the flavor of E. coli is eliminated, the thickness of the taste is increased, and a protein degradation product of a chicken egg protein having a high amino acid conversion rate can be obtained.

【0008】すなわち、本発明は鶏卵蛋白質蛋にアルカ
リ条件下で蛋白分解酵素を処理した後に麹を作用させる
ことを特徴とする蛋白酵素分解物、または該蛋白酵素分
解物のアミノ酸化率が65%以上である蛋白酵素分解物
である。以下本発明を詳述する。
[0008] That is, the present invention is characterized by treating a chicken egg protein protein with a protease under alkaline conditions and then allowing the koji to act, or the amino acid conversion rate of the protein enzyme degradation product is 65%. The above is a protein enzymatic degradation product. Hereinafter, the present invention will be described in detail.

【0009】[0009]

【発明の実施の形態】本発明において使用される鶏卵蛋
白質としては、通常以下に述べる蛋白質が用いられる。
すなわち、鶏卵液または鶏卵粉末を原料として有機溶剤
抽出法もしくは超臨界抽出法にて脂質部分を取り除いた
鶏卵蛋白質であり、液体、粉体の形態は問わない。ま
た、卵黄蛋白、卵白蛋白の割合は任意の割合で使用可能
であり、特に限定されるものではない。
BEST MODE FOR CARRYING OUT THE INVENTION As the chicken egg protein used in the present invention, the following proteins are usually used.
That is, it is a chicken egg protein obtained by removing a lipid portion from a chicken egg solution or a chicken egg powder as a raw material by an organic solvent extraction method or a supercritical extraction method, and may be in any form of liquid or powder. The ratio of egg yolk protein and egg white protein can be used in any ratio, and is not particularly limited.

【0010】本発明の蛋白分解酵素とは、蛋白を加水分
解するプロテアーゼ、ペプチダーゼの酵素であり、通常
Rhizopus属、Aspergillus属、Mu
cor属、Bacillus属、Pseudomona
s属、Streptococcus属、Escheri
chia属等の微生物由来、レンニン、パンクレアチン
等の動物由来、パパイン、ブロメライン、フィシン等の
植物に由来する酵素が用いられ、好ましくはRhizo
pus属、Aspergillus属、Bacillu
s属由来の酵素が望ましく、その精製品や粗製品が単独
もしくは2種以上を併用して利用できるものであり、複
数の組み合わせによる使用でも何ら問題はない。
[0010] The proteolytic enzyme of the present invention is a protease or peptidase enzyme that hydrolyzes proteins, and is usually of the genus Rhizopus, Aspergillus or Mu.
genus cor, genus Bacillus, Pseudomona
genus Streptococcus, Escheri
Enzymes derived from microorganisms such as genus chia, animals such as rennin and pancreatin, and plants derived from plants such as papain, bromelain and ficin are used, and preferably Rhizo.
genus pus, Aspergillus, Bacillu
An enzyme derived from the s genus is desirable, and its purified or crude product can be used alone or in combination of two or more, and there is no problem even when used in a plurality of combinations.

【0011】また本発明に使用する麹としては特に限定
するものではないが麹菌の液体培養液(液体麹)、小麦
ふすま等を培地とした固体培地に蛋白分解酵素を生産す
る麹菌を接種して得られる固体麹等があげられる。
The koji used in the present invention is not particularly limited, but is inoculated with a koji mold producing proteinase into a solid medium containing a liquid culture of koji mold (liquid koji) or wheat bran. And the resulting solid koji.

【0012】蛋白分解酵素は至適pHによってアルカリ
性、中性、酸性に大きく分けられ、さらに基質を分解す
る部位によりエンド型とエキソ型に分けられるが、本発
明ではこれら蛋白分解酵素をアルカリ条件下で使用する
ことが好ましい。これら蛋白分解酵素の使用量は、用い
る蛋白分解酵素の種類や組み合わせによって適宜決めら
れるものであり、特に限定されるものではないが、通常
基質である蛋白質1g当たりに対する蛋白分解酵素の活
性単位で表され、通常10〜50,000単位、好まし
くは1,00〜30,000単位、さらに好ましくは
1,000〜10,000単位の範囲から任意に選ばれ
るものである。
[0012] Protease is roughly classified into alkaline, neutral and acidic depending on the optimum pH, and further divided into endo-type and exo-type depending on the site for decomposing the substrate. It is preferable to use them. The amount of these proteases used is appropriately determined depending on the type and combination of the proteases used, and is not particularly limited, but is usually expressed in terms of the activity units of the proteases per gram of the substrate protein. It is usually arbitrarily selected from the range of 10 to 50,000 units, preferably 1,000 to 30,000 units, and more preferably 1,000 to 10,000 units.

【0013】尚、上記活性単位の測定法として一例をあ
げれば、カゼインに蛋白分解酵素が作用するときにペプ
チド結合の切断に伴って増加する酸可溶性分解物(TC
A可溶性分解物)の量を測定する方法があり、蛋白分解
酵素がカゼインに30℃で作用するとき、反応初期の1
分間に1マイクログラム(μg)のチロシンに相当する
非蛋白性のフォリン試液呈色物質の増加をもたらす酵素
量を1単位とするものである。
As an example of a method for measuring the above activity unit, an acid-soluble degradation product (TC) which increases with the cleavage of a peptide bond when a protease acts on casein.
A) There is a method of measuring the amount of the soluble decomposed product (A soluble decomposed product).
The amount of the enzyme that causes an increase in the color substance of the non-protein folin test solution corresponding to 1 microgram (μg) of tyrosine per minute is defined as one unit.

【0014】測定法の詳細は、カゼイン溶液(注1)5
mlを正確に量り、試験管に入れ、30±0.5℃で1
0分間加温した後、試料溶液(注2)1mlを正確に量
って加え、直ちに振り混ぜ、30±0.5℃で正確に1
0分間放置し、トリクロル酢酸溶液5mlを加えてよく
振り混ぜ、再び30±0.5℃で30分間放置した後、
濾紙で濾過する。その濾液2mlを正確に量り、炭酸ナ
トリウム溶液5ml及び薄めたフォリン試液1mlを加
えてよく振り混ぜ、30±0.5℃で30分間放置した
後、この液について波長660nmにおける吸光度AT
を測定する。別に試料溶液1mlにトリクロル酢酸溶液
5mlを加え、次に、カゼイン溶液5mlを加えて振り
混ぜ、30±0.5℃で30分間放置し、以下同様の操
作にて吸光度AB測定する。
For details of the measurement method, refer to Casein solution (Note 1) 5
weigh accurately, place in a test tube, and
After heating for 0 minutes, accurately weigh 1 ml of the sample solution (Note 2), shake immediately, and mix accurately at 30 ± 0.5 ° C.
Leave for 0 minutes, add 5 ml of trichloroacetic acid solution, shake well, leave again at 30 ± 0.5 ° C for 30 minutes,
Filter through filter paper. 2 ml of the filtrate was accurately measured, 5 ml of sodium carbonate solution and 1 ml of diluted folin reagent were added, and the mixture was shaken well and allowed to stand at 30 ± 0.5 ° C. for 30 minutes.
Is measured. Separately, 5 ml of a trichloroacetic acid solution is added to 1 ml of the sample solution, then 5 ml of a casein solution is added, and the mixture is shaken, left at 30 ± 0.5 ° C. for 30 minutes, and the absorbance AB is measured by the same operation.

【0015】 F:吸光度差が1.000に相当するチロシン量を検量
線より求めた値(μg) W:試料溶液1ml中の試料の量(g)
[0015] F: value obtained from the calibration curve for the amount of tyrosine corresponding to an absorbance difference of 1.000 (μg) W: amount of sample in 1 ml of sample solution (g)

【0016】(注1) 1)酸性プロテアーゼの場合:カゼイン1.20g(無
水物換算)を量り、0.05N乳酸100mlを加えて
加温溶解し、0.5N水酸化ナトリウムを加えてpH
3.0に調整し、Mcllvaine緩衝液40ml及
び水を加えて200mlとする。 2)中性及びアルカリ性プロテアーゼの場合:カゼイン
1.20g(無水物換算)を量り、0.05Nリン酸二
ナトリウム溶液160mlを加えて加温溶解し、0.5
N塩酸を加えてpH7.0に調整し、水を加えて200
mlとする。
(Note 1) 1) In the case of an acidic protease: 1.20 g (in terms of anhydrous) of casein was weighed, dissolved in 100 ml of 0.05N lactic acid under heating, and added with 0.5N sodium hydroxide to adjust the pH.
Adjust to 3.0 and add 40 ml of McIllvaine buffer and water to 200 ml. 2) In the case of neutral and alkaline proteases: 1.20 g (in terms of anhydrous) of casein was weighed, and 160 ml of a 0.05N disodium phosphate solution was added thereto, followed by heating and dissolving.
N hydrochloric acid was added to adjust the pH to 7.0, and water was added to add 200
ml.

【0017】(注2) 1)酸性プロテアーゼの場合:試料1.000gを正確
に量り、水を加えて溶かし100mlとする。必要なら
ば遠心分離する。次いで蛋白分解力が25〜40単位/
mlの範囲に入るように水を用いて希釈し、試料溶液と
する。 2)中性及びアルカリ性プロテアーゼの場合:試料1.
000gを正確に量り、酢酸カルシウム・塩化ナトリウ
ム混液を加えて溶かし、100mlとする。必要ならば
遠心分離する。次いで蛋白分解力が中性プロテアーゼの
場合は30〜40単位/ml、アルカリ性プロテアーゼ
の場合は15〜20単位/mlの範囲に入るように酢酸
カルシウム・塩化ナトリウム混液を用いて希釈して試料
溶液とする。
(Note 2) 1) In the case of an acidic protease: 1.000 g of a sample is accurately measured and dissolved by adding water to make 100 ml. Centrifuge if necessary. Next, the proteolytic power is 25-40 units /
Dilute with water so as to fall within the range of ml to obtain a sample solution. 2) For neutral and alkaline proteases: Sample 1.
Accurately weigh 000 g, add calcium acetate / sodium chloride mixed solution and dissolve to make 100 ml. Centrifuge if necessary. Then, the mixture is diluted with a mixed solution of calcium acetate and sodium chloride so that the proteolytic activity falls within the range of 30 to 40 units / ml in the case of neutral protease and 15 to 20 units / ml in the case of alkaline protease. I do.

【0018】<試薬・試液の調製> 1)トリクロル酢酸溶液 酸性プロテアーゼの場合:トリクロル酢酸71.7gに
水を加えて溶かし、1000mlとする。 中性及びアルカリ性プロテアーゼの場合:トリクロル酢
酸18g及び酢酸ナトリウム(無水)18gに6N酢酸
55ml及び水を加えて溶かし1000mlとする。 2)炭酸ナトリウム(0.55M) 炭酸ナトリウム(無水)58.3gに水を加えて溶か
し、1000mlとする。 3)フォリン試液 市販品のフェノール試薬10mlに水を加えて30ml
とする。 4)Mcllvaine緩衝液 0.2Mリン酸ナトリウム溶液に0.1Mクエン酸溶液
を加えてpH3.0に調整する。 0.2Mリン酸ナトリウム溶液:リン酸ナトリウム(1
2水塩)71.6gを水に溶かし、1000mlとす
る。 0.1Mクエン酸溶液:クエン酸21.0gに水を加え
て溶かし、1000mlとする。 5)酢酸カルシウム・塩化ナトリウム混液 酢酸カルシウム0.35g及び塩化ナトリウム0.58
gを量り、水を加えて溶かした後、1N塩酸又は1N水
酸化ナトリウム溶液を加えてpH6.0に調整し、水を
加えて1000mlとする。
<Preparation of Reagents and Reagents> 1) Trichloroacetic acid solution For acidic protease: Add water to 71.7 g of trichloroacetic acid to make 1000 ml. Neutral and alkaline proteases: 6N acetic acid (55 ml) and water are added to 18 g of trichloroacetic acid and 18 g of sodium acetate (anhydrous) to make 1000 ml. 2) Sodium carbonate (0.55M) Dissolve 58.3 g of sodium carbonate (anhydrous) by adding water to make 1000 ml. 3) Folin TS: Add 30 ml of water to 10 ml of commercially available phenol reagent
And 4) Mcllvaine buffer solution A 0.1 M citric acid solution is added to a 0.2 M sodium phosphate solution to adjust the pH to 3.0. 0.2 M sodium phosphate solution: sodium phosphate (1
Dissolve 71.6 g in water to make 1000 ml. 0.1 M citric acid solution: Dissolve 21.0 g of citric acid by adding water to make 1000 ml. 5) Calcium acetate / sodium chloride mixed solution 0.35 g of calcium acetate and 0.58 of sodium chloride
g of the solution, water is added to dissolve the mixture, and the mixture is adjusted to pH 6.0 with 1N hydrochloric acid or 1N sodium hydroxide solution, and then made up to 1000 ml with water.

【0019】<チロシン検量線の作成>市販のチロシン
標準品を105℃で3時間乾燥し、その0.500gを
正確に量り、0.2N塩酸を加えて溶かし、正確に50
0mlとする。この液1ml、2ml、3ml及び4m
lを正確に量り、それぞれに0.2N塩酸を加えて正確
に100mlとする。それぞれの液2ml中にはチロシ
ンが20μg、40μg、60μg及び80μg含まれ
る。それぞれの液2mlを正確に量り、炭酸ナトリウム
溶液5ml及び薄めたフォリン試液1mlを加え、30
±0.5℃で30分間放置した後、この液につき660
nmにおける吸光度A1、A2、A3及びA4を測定す
る。別に0.2N塩酸2mlを用いて同様に操作して吸
光度A0を測定する。これより縦軸に吸光度差(A1−
A0、A2−A0、A3−A0及びA4−A0)を、横
軸にそれぞれの液2ml中のチロシン量(μg)をとり
検量線とする。
<Preparation of Tyrosine Calibration Curve> A commercially available tyrosine standard was dried at 105 ° C. for 3 hours, 0.500 g of the tyrosine standard was accurately weighed, and 0.2N hydrochloric acid was added to dissolve it.
Make it 0 ml. 1ml, 2ml, 3ml and 4m of this liquid
Measure exactly 1 and add 0.2 N hydrochloric acid to each to make exactly 100 ml. 2 ml of each solution contains 20 μg, 40 μg, 60 μg and 80 μg of tyrosine. Measure exactly 2 ml of each solution, add 5 ml of sodium carbonate solution and 1 ml of diluted Folin TS, add 30 ml
After standing at ± 0.5 ° C for 30 minutes, 660
The absorbances A1, A2, A3 and A4 in nm are measured. Separately, the absorbance A0 is measured in the same manner using 2 ml of 0.2N hydrochloric acid. From this, the absorbance difference (A1-
A0, A2-A0, A3-A0, and A4-A0) are plotted with the tyrosine amount (μg) in 2 ml of each liquid on the horizontal axis, and used as a calibration curve.

【0020】以上の操作より、吸光度差1.000に対
するチロシン量(Fμg)を求めるものである。
From the above operation, the amount of tyrosine (Fμg) with respect to the absorbance difference of 1.000 is determined.

【0021】本発明においては、まず鶏卵蛋白質の混合
液を調整することから始まる。蛋白質の純度にもよる
が、通常、粗蛋白値として1〜30%、好ましくは1〜
20%、さらに好ましくは1〜10%に調整後、pHを
9〜13の範囲に調整する。
In the present invention, the procedure starts with preparing a mixture of chicken egg proteins. Although it depends on the purity of the protein, it is usually 1 to 30% as a crude protein value, preferably 1 to 30%.
After adjusting to 20%, more preferably 1 to 10%, the pH is adjusted to the range of 9 to 13.

【0022】鶏卵蛋白質をアルカリ条件にすることによ
り、後の加水分解が加速的に向上し、アミノ酸化率65
%以上の蛋白酵素分解物が容易に得られるものである。
By setting the egg protein under alkaline conditions, the subsequent hydrolysis is accelerated and the amino acid conversion rate is reduced to 65%.
% Or more of the enzymatically degraded protein is easily obtained.

【0023】次に、pH調整した鶏卵蛋白質の混合液
に、蛋白分解酵素を作用させ、さらに麹を作用させるこ
とにより、加水分解するものである。蛋白分解酵素の添
加量としては前述の、基質蛋白質1g当たりに対する蛋
白分解酵素の活性単位で表され、通常10〜50,00
0単位、好ましくは1,00〜30,000単位、さら
に好ましくは1,000〜10,000単位の範囲から
任意に選ばれるものである。
Next, a mixture of pH-adjusted chicken egg protein is hydrolyzed by the action of a protease and the action of koji. The amount of the protease added is represented by the activity unit of the protease per 1 g of the substrate protein as described above, and is usually from 10 to 50,000.
It is arbitrarily selected from the range of 0 units, preferably from 1,000 to 30,000 units, and more preferably from 1,000 to 10,000 units.

【0024】その他加水分解の条件として、以下に限定
されるものではないが、一例をあげると、一次反応で蛋
白分解酵素を働かせる温度は蛋白分解酵素が働く温度域
で有れば如何なる温度帯でも加水分解可能であるが、本
発明の蛋白酵素分解物を得るためには、通常−5〜60
℃の範囲で良く、好ましくは0〜40℃、さらに好まし
くは10〜30℃が良い。−5℃以下では完全に凍結し
てしまい蛋白質の効果的な分解が出来なくなるためであ
り、60℃以上では蛋白分解酵素の酵素活性が低下して
しまい効率的な分解が出来なくなるためである。次に、
加水分解の時間は、1時間〜10日、さらに好ましくは
1日〜5日であれば十分である。
Other conditions for the hydrolysis are not limited to the following, but as an example, the temperature at which the protease is activated in the primary reaction may be in any temperature range as long as the temperature is within the temperature range in which the protease is activated. Although it can be hydrolyzed, it is usually -5 to 60 in order to obtain the enzyme degradation product of the present invention.
C., preferably 0 to 40 C., and more preferably 10 to 30 C. If the temperature is lower than -5 ° C, the protein is completely frozen and the protein cannot be effectively decomposed. If the temperature is higher than 60 ° C, the enzyme activity of the proteolytic enzyme is reduced and the protein cannot be decomposed efficiently. next,
The time for the hydrolysis is 1 hour to 10 days, more preferably 1 day to 5 days.

【0025】また、二次反応として麹を働かせる温度
は、麹が働く温度域で有れば如何なる温度帯でも、加水
分解可能であるが、本発明の蛋白分解物を得るために
は、通常−5〜60℃の範囲で良く好ましくは、0〜4
0℃さらに好ましくは、0〜30℃が良い。次に、加水
分解の時間は、アミノ酸化率65%を得るに足る時間だ
け分解すれば良く、基質の蛋白質の量、蛋白質分解酵素
の量、加水分解の温度によって適宜決定されるが、通
常、加水分解の温度が−5〜10℃であれば1時間〜1
20日、10〜20℃であれば1時間〜90日、20〜
30℃であれば1時間〜70日で十分である。
The temperature at which the koji works as a secondary reaction can be hydrolyzed in any temperature range as long as it is within the temperature range in which the koji works. The temperature is preferably in the range of 5 to 60 ° C, preferably 0 to 4 ° C.
0 ° C, more preferably 0 to 30 ° C. Next, the hydrolysis time may be degraded for a time sufficient to obtain an amino acid conversion rate of 65%, and is appropriately determined depending on the amount of the substrate protein, the amount of the protease, and the hydrolysis temperature. If the hydrolysis temperature is -5 to 10 ° C, 1 hour to 1
20 days, 10 to 20 ° C, 1 hour to 90 days, 20 to 20 ° C
At 30 ° C., 1 hour to 70 days is sufficient.

【0026】アルカリ条件下蛋白分解酵素を作用させた
後、麹を加える時期については特に限定されるものでな
いが、好ましくは反応後のpHが9以下、さらに好まし
くは8以下となった時点で加えることが望ましい。
The timing of adding the koji after the protease is allowed to act under alkaline conditions is not particularly limited, but it is preferably added when the pH after the reaction becomes 9 or less, more preferably 8 or less. It is desirable.

【0027】本発明は、アルカリ条件下で、鶏卵蛋白混
合液に蛋白分解酵素を作用させた後に、麹を作用させ、
加水分解することを特徴としており、鶏卵蛋白以外の蛋
白原料では、アミノ酸化率65%以上のものは得られな
い。
According to the present invention, a koji is allowed to act on a chicken egg protein mixed solution under alkaline conditions, after the protease is allowed to act on the mixed solution.
It is characterized by being hydrolyzed, and no protein raw material other than chicken egg protein can have an amino acid conversion rate of 65% or more.

【0028】ここで、アミノ酸化率については、既知の
種々の方法により測定可能であり、NaSO−TN
BS法やHPLC法等により測定するものであり、一例
としてNaSO−TNBS法によるアミノ酸化率の
測定は、通常下記の方法により行われる。
Here, the amino acid conversion rate can be measured by various known methods, and Na 2 SO 3 -TN
The measurement is performed by the BS method, the HPLC method, or the like. For example, the measurement of the amino acid conversion rate by the Na 2 SO 3 -TNBS method is usually performed by the following method.

【0029】<方法>NaSO−TNBS法は蛋白
質のTNP化に基づいたアミノ基の定量方法で、TNB
S(2,4,6−トリニトロベンゼンスルホン酸ナトリ
ウム塩−2HO)がアミノ基を持つ化合物と混合し、
適度のアルカリ性にすると反応が始まり、橙色を呈する
ときの吸光度(420nm)を測定するものである。ア
ミノ酸化率としては、TNBS法にて測定した値を用い
下式にて算出するものである。
<Method> The Na 2 SO 3 -TNBS method is a method for quantifying an amino group based on TNP conversion of a protein.
S (2,4,6-trinitrobenzene sulfonate sodium salt-2H 2 O) were mixed with a compound having an amino group,
The reaction starts when the alkalinity is moderate, and the absorbance (420 nm) when the orange color is exhibited is measured. The amino acid conversion rate is calculated by the following formula using the value measured by the TNBS method.

【0030】TNBS測定用試料(ホウ酸buffer
で希釈した試料)0.5mlに呈色用緩衝液2.0m
l、0.01M亜硫酸溶液0.5ml、TNBS溶液
0.5mlを加えて、37℃×60分反応させた後、吸
光度 420nmで測定する。
TNBS measurement sample (borate buffer)
Sample diluted in 0.5) Color buffer 2.0m in 0.5ml
1, 0.5 ml of a 0.01 M sulfurous acid solution and 0.5 ml of a TNBS solution are added and reacted at 37 ° C. for 60 minutes, and the absorbance is measured at 420 nm.

【0031】<試薬>TNBS溶液:2,4,6−トリ
ニトロベンゼンスルホン酸ナトリウム塩−2HO、1
00mgをとり、100ml の蒸留水に溶解する
(0.00284M)。尚、この試薬を0.5mlを用
いた場合、1.42μmoleのTNBSが含まれてい
るので、0.5μmole程度までのアミノ酸の定量に
は支障はない。 呈色用緩衝液:0.15Mホウ酸ナトリウム緩衝液(ホ
ウ砂3.81gを100mlの温水に溶かす)あるいは
4M−ホウ酸カリウム緩衝液(ホウ酸24.7gに水酸
化カリウムを入れ、溶解しながらpH9.2に調整を行
う、後に蒸留水で100mlとする)を使用する。
<Reagent> TNBS solution: 2,4,6-trinitrobenzenesulfonic acid sodium salt-2H 2 O,
Take 00 mg and dissolve in 100 ml of distilled water (0.00284M). When 0.5 ml of this reagent is used, 1.42 μmole of TNBS is contained, so that there is no problem in quantifying amino acids up to about 0.5 μmole. Coloring buffer: 0.15 M sodium borate buffer (dissolve 3.81 g of borax in 100 ml of warm water) or 4 M-potassium borate buffer (24.7 g of boric acid is charged with potassium hydroxide and dissolved) While adjusting the pH to 9.2, and then make up to 100 ml with distilled water).

【0032】また、本発明で用いるアミノ酸化率の測定
方法として以下の計算式でも算出可能である。尚、遊離
のアミノ酸の測定は公知の測定方法であるフォルモール
滴定により測定され、総アミノ酸量についてはケルダー
ル法により測定するものである。 このようにして製造した蛋白酵素分解物は、そのままで
使用することも可能であるが、適宣、活性炭やイオン交
換樹脂による処理によって、着色物質や焦げ臭などの原
因となる香気成分を除去して使用することもできる。ま
た、得られた蛋白酵素分解物は、素材として単品使用さ
れる他、天然エキスまたはその代替物、基本だし素材や
風味調味料等に配合使用することができる。
Further, the amino acid conversion rate used in the present invention can be calculated by the following formula. The free amino acid is measured by formol titration, which is a known measuring method, and the total amount of amino acids is measured by the Kjeldahl method. The protein enzyme hydrolyzate produced in this way can be used as it is, but it is possible to remove odor components that cause coloring substances and burnt smell by appropriately treating with activated carbon or ion exchange resin. Can also be used. In addition, the obtained protein enzyme hydrolyzate can be used alone as a raw material, or can be blended and used with a natural extract or its substitute, a basic stock material, a flavor seasoning, and the like.

【0033】さらに、以上の工程で得られる蛋白酵素分
解物は加水分解工程中に塩が加えられていないので、脱
塩工程は必要なく、産業上、塩が存在していないことは
有益である。
Furthermore, since the protein-enzyme hydrolyzate obtained in the above step has no salt added during the hydrolysis step, a desalting step is not required, and it is advantageous in industry that no salt is present. .

【0034】かくして得られる本発明の蛋白酵素分解物
は、アミノ酸単体・ジペプチド、トリペプチドで構成さ
れ、構成ペプチドを例示すれば、Asp−Glu、Gl
u−Ser、Ser−Gly、Val−Leu等のジペ
プチド、Asp−Glu−Ser、Glu−Leu−S
er等のトリペプチド等があげられる。本発明の蛋白酵
素分解物は、食品分野、化粧品分野、医薬品分野などの
素材として利用可能であるとともに、必要に応じて、味
や栄養価、保存性等を向上させる目的で核酸系調味料、
化学調味料、旨味調味料、味噌、醤油、塩、食塩、油脂
等の素材と混合し使用することができる。以下実施例を
あげて本発明を具体的に説明するが、本発明はこれによ
って限定されるものではない。
The thus obtained protein hydrolyzate of the present invention is composed of simple amino acids / dipeptides and tripeptides. Examples of the constituent peptides include Asp-Glu and Gl.
Dipeptides such as u-Ser, Ser-Gly, Val-Leu, Asp-Glu-Ser, Glu-Leu-S
er and the like. The protein enzyme hydrolyzate of the present invention can be used as a material in the food field, cosmetics field, pharmaceutical field, and the like, and, if necessary, a nucleic acid seasoning for the purpose of improving taste, nutritional value, storage stability, etc.
It can be used by mixing with materials such as chemical seasoning, umami seasoning, miso, soy sauce, salt, salt, oil and fat. Hereinafter, the present invention will be described specifically with reference to Examples, but the present invention is not limited thereto.

【0035】[0035]

【実施例】実施例1 脱脂卵黄粉末(蛋白質含有量82%)0.827kgに
水10.72とエタノール2.68kgを加えて混合液
を調製し、さらに苛性ソーダを加え、pH11に調整
後、加水分解するために蛋白分解酵素として細菌アルカ
リプロテアーゼ(Bacillus subtilis
起源:活性単位220,000単位/g)を対蛋白質1
g当たり6,000単位を混合し、12℃、1週間処理
した後に麹を0.34kg加え、これを12℃、8週間
かけて分解した。その後85℃で30分間加熱して酵素
を失活させ、蛋白酵素分解物を得た。得られた蛋白酵素
分解物をNo.2濾紙(ADOVANTEC TOYO
製)を用いて濾過して、濾液9.7kgを得た。このも
ののアミノ酸化率を測定したところ、総アミノ態チッソ
量(T.N)1.29、遊離アミノ態チッソ量(F.
N)0.924、アミノ酸化率71.6%、その食塩含
有量(モール法)は0%であった。
Example 1 A mixture was prepared by adding 10.72 kg of water and 2.68 kg of ethanol to 0.827 kg of defatted egg yolk powder (protein content 82%), and further adding caustic soda to adjust the pH to 11, followed by adding water. Bacterial alkaline protease (Bacillus subtilis) as a proteolytic enzyme for degradation
Origin: 220,000 units of activity / g) per protein 1
After mixing at 6,000 units per g and treating at 12 ° C. for one week, 0.34 kg of koji was added and decomposed at 12 ° C. for eight weeks. Thereafter, the mixture was heated at 85 ° C. for 30 minutes to inactivate the enzyme, thereby obtaining a protein enzyme degradation product. The obtained protein enzyme hydrolyzate was 2 filter paper (ADOVANTEC TOYO
Was used to obtain 9.7 kg of a filtrate. When the amino acid conversion of this product was measured, the total amount of amino nitrogen (TN) was 1.29 and the amount of free amino nitrogen (F.N.
N) was 0.924, the amino acid conversion ratio was 71.6%, and the salt content (Mor method) was 0%.

【0036】比較例1 一方、小麦グルテン(蛋白質含有量76.6%)0.8
85kgに水10.72とエタノール2.68kgを加
えて混合液を調製し、さらに苛性ソーダを加え、pH1
1に調整後、加水分解するために蛋白分解酵素として細
菌アルカリプロテアーゼ(Bacillus subt
ilis起源:活性単位220,000単位/g)を対
蛋白質1g当たり6,000単位を混合し、12℃、1
週間処理した後に麹を0.34kg加え、これを12
℃、8週間かけて分解した。その後85℃で30分間加
熱して酵素を失活させ、低分子ペプチド液を得た。得ら
れた低分子ペプチド液をNo.2濾紙(ADOVANT
EC TOYO製)を用いて濾過して、濾液9.9kg
を得た。このもののアミノ化率を測定したところ、総ア
ミノ態チッソ量(T.N)1.31、遊離アミノ態チッ
ソ量(F.N)0.65、アミノ酸化率49.0%、そ
の食塩含有量(モール法)は0%であった。
Comparative Example 1 On the other hand, wheat gluten (protein content: 76.6%) 0.8
A mixture is prepared by adding 10.72 kg of water and 2.68 kg of ethanol to 85 kg, and further adding caustic soda,
After being adjusted to 1, a bacterial alkaline protease (Bacillus subt) was used as a proteolytic enzyme for hydrolysis.
iris origin: 220,000 units of activity / g), 6,000 units per gram of protein, 12 ° C, 1
After weekly treatment, add 0.34 kg of koji and add 12
Decomposed for 8 weeks at ℃. Thereafter, the enzyme was inactivated by heating at 85 ° C. for 30 minutes to obtain a low-molecular peptide solution. The obtained low-molecular peptide solution was designated as No. 2 filter paper (ADOVANT
9.9 kg of the filtrate.
I got When the amination ratio of this product was measured, the total amount of amino nitrogen (TN) was 1.31, the amount of free amino nitrogen (FN) was 0.65, the amino acid conversion was 49.0%, and the salt content thereof was (Mole method) was 0%.

【0037】実施例1と比較例1で得られた蛋白酵素分
解物を市販めんつゆに添加し、官能評価した。配合比
は、市販めんつゆ100mlに本発明の蛋白酵素分解物
0.5gを添加した。
The protein enzyme-decomposed products obtained in Example 1 and Comparative Example 1 were added to commercially available noodle soup and subjected to a sensory evaluation. The blending ratio was such that 0.5 g of the protein enzyme digest of the present invention was added to 100 ml of commercially available noodle soup.

【0038】対照として、無添加めんつゆを用意し、三
点比較法で味覚パネル30名による官能評価を実施し
た。結果を表1に示す。
As a control, non-added noodle soup was prepared, and a sensory evaluation was conducted by 30 taste panels using a three-point comparison method. Table 1 shows the results.

【0039】[0039]

【表1】 [Table 1]

【0040】実施例1と比較例1の結果より、アルカリ
条件下で鶏卵蛋白質に、蛋白分解酵素を作用させた後
に、麹を作用させ加水分解することにより、味に厚味を
持ったアミノ酸化率65%以上の優れた品質の蛋白酵素
分解物が得られたことは明らかである。
From the results of Example 1 and Comparative Example 1, it was found that a proteinase was allowed to act on chicken egg protein under alkaline conditions, and then koji was allowed to act on the protein to hydrolyze it. It is clear that an excellent quality enzyme degradation product having a rate of 65% or more was obtained.

【0041】実施例2 おから(蛋白質含有量4.0%)3.3kgと脱脂全卵
粉末(蛋白質含量84.3%)0.65kgに水10.
72Kgを加えて混合液を調製し、さらに苛性ソーダを
加え、pH12に調整後、ブタノール2.68Kgを加
え、加水分解するために蛋白分解酵素として細菌アルカ
リプロテアーゼ(Bacillus subtilis
起源:活性単位220,000単位/g)を対蛋白質1
g当たり8,000単位を混合し、15℃、5日間処理
した後に麹を0.5kg加え、これを15℃、10週間
かけて分解した。その後85℃で30分間加熱して酵素
を失活させ、蛋白分解液を得た。得られた蛋白分解液を
No.2濾紙(ADOVANTEC TOYO製)を用
いて濾過して、濾液6.4kgを得、このもののアミノ
酸化率を測定したところ、総アミノ態チッソ量(T.
N)0.92、遊離アミノ態チッソ量(F.N)0.6
86、アミノ酸化率74.6%、その食塩含有量(モー
ル法)は0%であった。
Example 2 3.3 kg of okara (protein content 4.0%) and 0.65 kg of defatted whole egg powder (protein content 84.3%) and water 10.
72 Kg was added to prepare a mixture, and caustic soda was further added to adjust the pH to 12. Then, 2.68 kg of butanol was added, and a bacterial alkaline protease (Bacillus subtilis) was used as a protease for hydrolysis.
Origin: 220,000 units of activity / g) per protein 1
After mixing at 8,000 units per g and treating at 15 ° C. for 5 days, 0.5 kg of koji was added and decomposed at 15 ° C. for 10 weeks. Thereafter, the enzyme was inactivated by heating at 85 ° C. for 30 minutes to obtain a proteolytic solution. The obtained protein hydrolyzate was 2 using a filter paper (manufactured by ADOVANTEC TOYO) to obtain 6.4 kg of a filtrate. The amino acid conversion of the filtrate was measured.
N) 0.92, free amino nitrogen (F.N) 0.6
86, the amino acid conversion ratio was 74.6%, and the salt content (Mor method) was 0%.

【0042】比較例2 おから(蛋白質含有量4.0%)3.3kgと小麦グル
テン(蛋白質含量85.2%)0.65kgに水11.
4Kgを加えて混合液を調製し、さらに苛性ソーダを加
え、pH12に調整後、加水分解するために蛋白分解酵
素として細菌中性プロテアーゼ(Asperugill
us oryzae起源:活性単位3000000単位
/g)を対蛋白質1g当たり8000単位を混合し、1
5℃、5日間処理した後に麹を0.5kg加え、これを
15℃、10週間かけて分解した。その後85℃で30
分間加熱して酵素を失活させ、蛋白分解液を得た。得ら
れた蛋白分解液をNo.2濾紙(ADOVANTEC
TOYO製)を用いて濾過して、このもののアミノ酸化
率を測定したところ、総アミノ態チッソ量(T.N)
0.95、遊離アミノ態チッソ量(F.N)0.53
6、アミノ酸化率56.4%、その食塩含有量(モール
法)は0%であった。
Comparative Example 2 3.3 kg of okara (protein content: 4.0%) and 0.65 kg of wheat gluten (protein content: 85.2%) were added to 11.1 of water.
4 Kg was added to prepare a mixed solution, caustic soda was further added to adjust the pH to 12, and then a neutral protease (Asperugill) was used as a protease for hydrolysis.
us oryzae origin: 3,000,000 units of activity / g), and 8000 units per gram of protein.
After treatment at 5 ° C. for 5 days, 0.5 kg of koji was added, and this was decomposed at 15 ° C. for 10 weeks. Then at 85 ° C for 30
The enzyme was inactivated by heating for one minute to obtain a proteolytic solution. The obtained protein hydrolyzate was 2 filter paper (ADOVANTEC
The product was filtered using TOYO (manufactured by TOYO) and the amino acid conversion of the product was measured.
0.95, free amino nitrogen (FN) 0.53
6. The degree of amino acid conversion was 56.4%, and the salt content (Mor method) was 0%.

【0043】実施例2と比較例2の結果より、アルカリ
条件下で鶏卵蛋白質に蛋白分解酵素を作用させた後に、
麹を作用させることによりアミノ酸化率65%以上の優
れた品質の蛋白酵素分解物が得られたことは明らかであ
る。
From the results of Example 2 and Comparative Example 2, after the protease was allowed to act on the egg protein under alkaline conditions,
It is clear that the use of the koji yielded an excellent quality protein hydrolyzate with an amino acid conversion of 65% or more.

【0044】実施例3 脱脂卵黄粉末(蛋白質含有量83.3%)0.365k
gと脱脂大豆(蛋白質含量82.0%)0.44kgに
水10.72kgとエタノーノル2.50kgを加えて
混合液を調製し、さらに苛性ソーダを加え、pH10に
調整後、加水分解するために蛋白分解酵素として細菌ア
ルカリプロテアーゼ(Bacillussubtili
s起源:活性単位220,000単位/g)を対蛋白質
1g当たり6,000単位を混合し、12℃、10日間
処理した後に麹を0.2kg加え、12℃で11週間か
けて分解した。その後85℃で30分間加熱して酵素を
失活させ、蛋白分解液を得た。得られた蛋白分解液をN
o.2濾紙(ADOVANTEC TOYO製)を用い
て濾過して、このもののアミノ酸化率を測定したとこ
ろ、総アミノ態チッソ量(T.N)1.28、遊離アミ
ノ態チッソ量(F.N)0.914、アミノ酸化率7
1.4%、その食塩含有量(モール法)は0%であっ
た。
Example 3 Skim egg yolk powder (protein content: 83.3%) 0.365 k
g and 0.44 kg of defatted soybean (protein content: 82.0%), add 10.72 kg of water and 2.50 kg of ethanol to prepare a mixed solution, further add caustic soda, adjust the pH to 10, and hydrolyze the protein. Bacterial alkaline protease (Bacillus subtili) as a degrading enzyme
(s origin: 220,000 units / g of active unit) was mixed with 6,000 units per gram of protein, treated at 12 ° C for 10 days, added with 0.2 kg of koji, and decomposed at 12 ° C for 11 weeks. Thereafter, the enzyme was inactivated by heating at 85 ° C. for 30 minutes to obtain a proteolytic solution. The obtained protein hydrolyzate is
o. 2 was filtered using filter paper (manufactured by ADOVANTEC TOYO), and the amino acid conversion of the product was measured. The total amino nitrogen content (TN) 1.28 and the free amino nitrogen content (FN) 0. 914, amino acid conversion rate 7
1.4%, and its salt content (Moll method) was 0%.

【0045】比較例3 一方、小麦グルテン(蛋白質含有量76.6%)0.5
38kgと脱脂大豆(蛋白質含量82.0%)0.32
5kgに水10.72kgとエタノーノル2.50kg
を加えて混合液を調整し、さらに苛性ソーダを加え、p
H10に調整後、加水分解するために蛋白分解酵素とし
て細菌アルカリプロテアーゼ(Bacillus su
btilis起源:活性単位220,000単位/g)
を対蛋白質1g当たり6,000単位を混合し、12
℃、10日間処理した後に麹を0.2kg加え、12℃
で11週間かけて分解した。その後85℃で30分間加
熱して酵素を失活させ、蛋白分解液を得た。得られた蛋
白分解液をNo.2濾紙(ADOVANTEC TOY
O製)を用いて濾過して、このもののアミノ酸化率を測
定したところ、総アミノ態チッソ量(T.N)1.3
0、遊離アミノ態チッソ量(F.N)0.656、アミ
ノ酸化率50.5%、その食塩含有量(モール法)は0
%であった。
Comparative Example 3 On the other hand, wheat gluten (protein content: 76.6%) 0.5
38 kg and defatted soybean (protein content 82.0%) 0.32
5kg, 10.72kg of water and 2.50kg of ethanol
To adjust the mixture, and further add caustic soda, p
After adjusting to H10, a bacterial alkaline protease (Bacillus su) was used as a proteolytic enzyme for hydrolysis.
btilis origin: 220,000 active units / g)
Is mixed with 6,000 units per gram of protein,
After treatment at 10 ° C for 10 days, 0.2 kg of koji was added,
For 11 weeks. Thereafter, the enzyme was inactivated by heating at 85 ° C. for 30 minutes to obtain a proteolytic solution. The obtained protein hydrolyzate was 2 filter paper (ADOVANTEC TOY
O), and the amino acid conversion of the product was measured, and the total amino nitrogen content (TN) was 1.3.
0, free amino type nitrogen (FN) 0.656, amino acid conversion rate 50.5%, salt content (Moll method) is 0
%Met.

【0046】実施例3と比較例3の結果より、アルカリ
条件下で蛋白分解酵素を作用させた後に、麹を作用させ
ることにより、アミノ酸化率65%以上の優れた品質の
蛋白酵素分解物が得られたことは明らかである。
From the results of Example 3 and Comparative Example 3, it was found that a high-quality protein enzyme hydrolyzate having an amino acid conversion rate of 65% or more was obtained by allowing koji to act after the action of the protease under alkaline conditions. It is clear that it has been obtained.

【0047】実施例3と比較例3で得られた蛋白酵素分
解物を市販めんつゆに添加し、官能評価を実施した。配
合比は、市販めんつゆ100mlに本発明の蛋白酵素分
解物0.5gを添加した。
The protein hydrolyzate obtained in Example 3 and Comparative Example 3 was added to commercially available noodle soup, and the sensory evaluation was performed. The blending ratio was such that 0.5 g of the protein enzyme digest of the present invention was added to 100 ml of commercially available noodle soup.

【0048】対照として、無添加めんつゆを用意し、三
点比較法で味覚パネル30名による官能評価を実施し
た。結果を表2に示す。
As a control, noodle soup without additives was prepared, and a sensory evaluation was conducted by 30 taste panels using a three-point comparison method. Table 2 shows the results.

【0049】[0049]

【表2】 [Table 2]

【0050】実施例3と比較例3の結果より、アルカリ
条件下で鶏卵蛋白質に、蛋白分解酵素を作用させた後
に、麹を作用させることにより、味に厚味を持ったアミ
ノ酸化率65%以上の優れた品質の蛋白酵素分解物が得
られたことは明らかである。
According to the results of Example 3 and Comparative Example 3, the egg protein was allowed to act on the egg protein under alkaline conditions, and then the koji was allowed to act on the egg protein. It is clear that the above-mentioned high-quality degraded protein enzyme was obtained.

【0051】本発明の実施態様をあげれば、以下のとお
りである。 (1)鶏卵蛋白質にアルカリ条件下で蛋白分解酵素を作
用させた後に、麹を作用させることにより、味に厚味を
持ったアミノ酸化率65%以上の蛋白酵素分解物に関す
るものである。 (2)前記(1)の蛋白酵素分解物を含む食品、飼料、
肥料、栄養剤、化粧品、医薬品。
The embodiments of the present invention are as follows. (1) The present invention relates to a protein enzyme hydrolyzate having a thick taste and an amino acid conversion rate of 65% or more, which is obtained by treating a chicken egg protein with a protease under alkaline conditions and then reacting with koji. (2) a food or feed containing the protein / enzyme hydrolyzate of the above (1);
Fertilizers, nutrients, cosmetics, pharmaceuticals.

【0052】(3)鶏卵蛋白質が、鶏卵液または鶏卵粉
末を原料として有機溶剤抽出法もしくは超臨界抽出法に
て脂質部分を取り除いた鶏卵蛋白質であり、液体、粉体
の形態は問わず、卵黄蛋白質、卵白蛋白質の割合につい
て特に限定なしに、任意の割合で使用する前記(1)〜
(2)いずれか記載の蛋白酵素分解物。 (4)アルカリが、水酸化ナトリウム、水酸化カリウム
などのアルカリ金属の水酸化物であり、これらの精製品
や粗製品を使用する前記(1)〜(2)いずれか記載の
蛋白酵素分解物。
(3) The chicken egg protein is a chicken egg protein obtained by removing a lipid portion from a chicken egg solution or a chicken egg powder as a raw material by an organic solvent extraction method or a supercritical extraction method. The above-mentioned (1) to (10) are used in any ratio, without any particular limitation on the ratio of protein and egg white protein.
(2) The enzyme-decomposed product of any one of the above. (4) The protein enzyme-decomposed product according to any of (1) to (2), wherein the alkali is a hydroxide of an alkali metal such as sodium hydroxide or potassium hydroxide, and a purified or crude product thereof is used. .

【0053】(5)蛋白分解酵素が、プロテアーゼ、ペ
プチダーゼで、Rhizopus属、Aspergil
lus属、Mucor属、Bacillus属、Pse
udomonas属、Streptococcus属、
Escherichia属等の微生物由来、レンニン、
パンクレアチン等の動物由来、パパイン、ブロメライ
ン、フィシン等の植物に由来する酵素であり、好ましく
はRhizopus属、Aspergillus属、B
acillus属由来の酵素で、その精製品や粗製品を
単独もしくは2種以上併用して利用する前記(1)〜
(2)いずれか記載の蛋白酵素分解物。 (6)粗蛋白質の含量が1〜30%、好ましくは1〜2
0%、さらに好ましくは1〜10%の混液に調整する前
記(1)〜(2)いずれか記載の蛋白酵素分解物。
(5) Proteolytic enzymes are proteases and peptidases, Rhizopus genus, Aspergil
lus, Mucor, Bacillus, Pse
genus udomonas, Streptococcus,
Microbial origin such as Escherichia, rennin,
Enzymes derived from animals such as pancreatin and plants derived from papain, bromelain, ficin, etc., preferably Rhizopus, Aspergillus, B
(1)-an enzyme derived from the genus acillus, wherein the purified or crude product is used alone or in combination of two or more.
(2) The enzyme-decomposed product of any one of the above. (6) The content of the crude protein is 1 to 30%, preferably 1 to 2
The protein enzyme digest according to any one of the above (1) and (2), which is adjusted to a mixture of 0%, more preferably 1 to 10%.

【0054】(7)蛋白分解酵素の添加量が、通常基質
である蛋白質1g当たりに対する蛋白分解酵素の活性単
位で表され、通常10〜50,000単位、好ましくは
1,00〜30,000単位、さらに好ましくは1,0
00〜10,000単位の範囲から任意に選ばれるもの
である前記(1)〜(2)いずれか記載の蛋白酵素分解
物。 (8)加水分解の温度が、通常−5〜50℃の範囲で良
く、好ましくは0〜40℃、さらに好ましくは0〜30
℃である前記(1)〜(2)いずれか記載の蛋白酵素分
解物。 (9)加水分解時間が、加水分解の温度が−5〜10℃
であれば1時間〜100日、10〜20℃であれば1時
間〜70日、20〜30℃であれば1時間〜30日で十
分である前記(1)〜(2)いずれか記載の蛋白酵素分
解物。
(7) The amount of proteolytic enzyme added is usually expressed in terms of the activity unit of proteolytic enzyme per 1 g of the substrate protein, and is usually from 10 to 50,000 units, preferably from 1,000 to 30,000 units. , More preferably 1,0
The proteolytic product according to any one of the above (1) and (2), which is arbitrarily selected from the range of 00 to 10,000 units. (8) The hydrolysis temperature is usually in the range of -5 to 50C, preferably 0 to 40C, more preferably 0 to 30C.
The protein enzyme-decomposed product according to any one of the above (1) and (2), which is at ° C. (9) The hydrolysis time is such that the hydrolysis temperature is -5 to 10C.
1 hour to 100 days, 10 hours to 20 degrees Celsius, 1 hour to 70 days, and 20 hours to 30 degrees Celsius, 1 hour to 30 days are sufficient. Degradation products of protein enzymes.

【0055】[0055]

【発明の効果】本発明の蛋白酵素分解物は、味に厚味を
持ち、アミノ酸スコアが良好であり、食品、飼料、肥
料、栄養剤、化粧品、医薬品等あらゆる分野に、アミノ
酸源として広く利用可能な蛋白酵素分解物を提供するも
のである。
EFFECTS OF THE INVENTION The enzyme-decomposed product of the present invention has a thick taste and a good amino acid score, and is widely used as an amino acid source in all fields such as foods, feeds, fertilizers, nutrients, cosmetics and pharmaceuticals. It is intended to provide a possible protein enzyme degradation product.

───────────────────────────────────────────────────── フロントページの続き (72)発明者 久保田 啓一 三重県四日市市赤堀新町9番5号 太陽化 学株式会社内 Fターム(参考) 4B018 LB09 MD22 MD72 MD80 MD90 ────────────────────────────────────────────────── ─── Continuing on the front page (72) Inventor Keiichi Kubota 9-5 Akabori Shinmachi, Yokkaichi-shi, Mie Taiyo Kagaku Co., Ltd. F-term (reference) 4B018 LB09 MD22 MD72 MD80 MD90

Claims (4)

【特許請求の範囲】[Claims] 【請求項1】 鶏卵蛋白質をアルカリ条件下で、蛋白分
解酵素を用い処理した後に麹を作用させることを特徴と
する蛋白酵素分解物。
1. A protein-enzymatic degradation product obtained by treating a chicken egg protein with a protease under alkaline conditions and then allowing koji to act.
【請求項2】 アミノ酸化率が65%以上である請求項
1記載の蛋白酵素分解物。
2. The protein enzyme-decomposed product according to claim 1, wherein the amino acid conversion rate is 65% or more.
【請求項3】 請求項1または2記載の蛋白酵素分解物
を含有する食品。
3. A food containing the enzyme-decomposed product of claim 1 or 2.
【請求項4】 請求項1または2記載の蛋白酵素分解物
を含有する栄養剤。
4. A nutrient containing the enzyme-decomposed product of claim 1 or 2.
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