JPS63219348A - Fermentation product compounded with protease - Google Patents
Fermentation product compounded with proteaseInfo
- Publication number
- JPS63219348A JPS63219348A JP62053878A JP5387887A JPS63219348A JP S63219348 A JPS63219348 A JP S63219348A JP 62053878 A JP62053878 A JP 62053878A JP 5387887 A JP5387887 A JP 5387887A JP S63219348 A JPS63219348 A JP S63219348A
- Authority
- JP
- Japan
- Prior art keywords
- low
- protease
- temperature
- krill
- activity
- 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.)
- Pending
Links
- 108091005804 Peptidases Proteins 0.000 title claims abstract description 42
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 title claims abstract description 39
- 239000004365 Protease Substances 0.000 title claims abstract description 38
- 238000000855 fermentation Methods 0.000 title claims abstract description 5
- 230000004151 fermentation Effects 0.000 title claims abstract description 5
- 230000000694 effects Effects 0.000 claims abstract description 23
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims abstract description 16
- 241000239366 Euphausiacea Species 0.000 claims abstract description 13
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims abstract description 11
- 239000011780 sodium chloride Substances 0.000 claims abstract description 5
- 101710118538 Protease Proteins 0.000 claims abstract description 4
- 102000018389 Exopeptidases Human genes 0.000 claims abstract description 3
- 108010091443 Exopeptidases Proteins 0.000 claims abstract description 3
- 102000035195 Peptidases Human genes 0.000 claims abstract description 3
- 239000002994 raw material Substances 0.000 abstract description 6
- 150000003839 salts Chemical class 0.000 abstract description 5
- 235000010469 Glycine max Nutrition 0.000 abstract description 4
- 244000294411 Mirabilis expansa Species 0.000 abstract description 4
- 235000015429 Mirabilis expansa Nutrition 0.000 abstract description 4
- 235000013536 miso Nutrition 0.000 abstract description 4
- 230000003247 decreasing effect Effects 0.000 abstract description 3
- 235000019992 sake Nutrition 0.000 abstract description 3
- 235000013405 beer Nutrition 0.000 abstract description 2
- 238000002360 preparation method Methods 0.000 abstract description 2
- 235000010627 Phaseolus vulgaris Nutrition 0.000 abstract 1
- 244000046052 Phaseolus vulgaris Species 0.000 abstract 1
- 238000013329 compounding Methods 0.000 abstract 1
- 102000004190 Enzymes Human genes 0.000 description 11
- 108090000790 Enzymes Proteins 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 239000000243 solution Substances 0.000 description 6
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 5
- 229940098773 bovine serum albumin Drugs 0.000 description 5
- 238000000034 method Methods 0.000 description 5
- 102000004142 Trypsin Human genes 0.000 description 4
- 108090000631 Trypsin Proteins 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- 239000012588 trypsin Substances 0.000 description 4
- 239000004475 Arginine Substances 0.000 description 3
- 244000068988 Glycine max Species 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 235000021329 brown rice Nutrition 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 210000002808 connective tissue Anatomy 0.000 description 2
- 238000000354 decomposition reaction Methods 0.000 description 2
- 230000000593 degrading effect Effects 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 240000006439 Aspergillus oryzae Species 0.000 description 1
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 1
- 239000004278 EU approved seasoning Substances 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 241000862632 Soja Species 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 235000009754 Vitis X bourquina Nutrition 0.000 description 1
- 235000012333 Vitis X labruscana Nutrition 0.000 description 1
- 240000006365 Vitis vinifera Species 0.000 description 1
- 235000014787 Vitis vinifera Nutrition 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 235000013334 alcoholic beverage Nutrition 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000012888 bovine serum Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000008034 disappearance Effects 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 239000000796 flavoring agent Substances 0.000 description 1
- 235000019634 flavors Nutrition 0.000 description 1
- 235000011194 food seasoning agent Nutrition 0.000 description 1
- 210000002196 fr. b Anatomy 0.000 description 1
- 210000003918 fraction a Anatomy 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000035784 germination Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 235000013555 soy sauce Nutrition 0.000 description 1
- 238000010025 steaming Methods 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 235000021419 vinegar Nutrition 0.000 description 1
- 239000000052 vinegar Substances 0.000 description 1
Landscapes
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Soy Sauces And Products Related Thereto (AREA)
Abstract
Description
【発明の詳細な説明】 （産業上の利用分野） 本発明はプロテアーゼ配合醗酵製品に関する。[Detailed description of the invention] (Industrial application field) The present invention relates to protease-containing fermentation products.
（従来の技術）
本発明者らはオキアミが捕獲後、常温（南氷洋気温）に
放置すると急速に自己消化し、蛋白質溶解を生ずること
に着目し、オキアミ中にプロテアーゼ、キチナーゼ等の
溶解酵素が存在することを予想し、オキアミから酵素を
単離することに成功し、該酵素が低温領域に至適温度領
域を有する低温プロテアーゼであることを見い出した。(Prior art) The present inventors focused on the fact that krill rapidly self-digests when left at room temperature (Southern Ocean temperature) after capture, resulting in protein dissolution. We predicted that this would happen, and succeeded in isolating the enzyme from krill, and found that the enzyme is a low-temperature protease with an optimum temperature range in the low-temperature region.
そこで種々研究を行ったところ、例えば上記プロテアー
ゼを醗酵製品の製造時に原料中に配合する場合には、低
温で蛋白質の分解を行うことができ、その結果、低温、
減塩条件下でＷＡ＃することが可能であることを見い出
した。更に上記オキアミから得られる低温プロテアーゼ
にエタノールを添加すると、その酵素活性が一層高めら
れることを見い出した。We conducted various studies and found that, for example, when the protease mentioned above is added to raw materials during the production of fermented products, it is possible to decompose proteins at low temperatures;
It has been found that WA# is possible under low salt conditions. Furthermore, we have found that when ethanol is added to the low-temperature protease obtained from krill, the enzymatic activity is further enhanced.
（発明が解決しようとする問題点）
本発明は低温、減塩条件下でも効率良く醗酵し、従って
必要に応じ減塩することも可能な醗酵製品を提供するこ
とにある。(Problems to be Solved by the Invention) The object of the present invention is to provide a fermented product that can be efficiently fermented even at low temperatures and under low-salt conditions, and can therefore be reduced in salt if necessary.
（問題点を解決するための手段）
本発明はオキアミより抽出された低温プロテアーゼを配
合してなる醗酵製品に係る。(Means for Solving the Problems) The present invention relates to a fermented product containing low-temperature protease extracted from krill.
本発明で用いられる低温プロテアーゼは分子量約５万及
び約３．３万のエキソプロテアーゼ及びエンドプロテア
ーゼ活性を有する２種類のプロテアーゼを含み、約５〜
２０℃の低温領域に至適温度領域を有し、ＮａＣｌ耐性
を有する低温プロテアーゼである。The low-temperature protease used in the present invention includes two types of proteases having exoprotease and endoprotease activities with a molecular weight of about 50,000 and about 33,000, and has a molecular weight of about 50,000 to 33,000.
It is a low-temperature protease that has an optimum temperature range in the low-temperature range of 20°C and is resistant to NaCl.
本発明において用いられる上記プロテアーゼは、例えば
オキアミを原料として、これに適量の生理リン酸緩衝液
を加え、ホモデナイズし、粗を過により結合組織を除去
後、遠心分離し、その上澄液をデルシ戸遇して濃縮する
ことにより得られる。The above-mentioned protease used in the present invention is made from krill, for example, by adding an appropriate amount of physiological phosphate buffer to it, homodenizing it, removing the connective tissue by filtration, centrifuging it, and discarding the supernatant. It can be obtained by concentrating it on a personal basis.
即ち上記プロテアーゼは具体的には例えば次の様にして
得られる。Specifically, the above protease can be obtained, for example, as follows.
未加熱（生鮮状態）のまま、捕獲後急速凍結されたオキ
アミを凍結のまま細切して、２〜５倍量の生理リン酸緩
衝液（Ｐ Ｂ Ｓ ）を加えてワーリングブレングーを
用いてホモデナイズし、四重ガーゼでＬ過して結合組織
を除去後、１０，０００ｘｇで１０〜３０分遠心分離し
て上澄液を採り、この上澄液をＳ ｅｐｌ＋ａｃｒｙｌ
Ｓ ４００ （スウェーデン、サルマシャ社ｇ１）
を用いて、ゲルシ濾過分離を行うことにより、プロテア
ーゼ活性１０倍以上に濃縮された低温プロテアーゼ酵素
液が得られる。Unheated (fresh) krill that was caught and quickly frozen was cut into small pieces while still frozen, and 2 to 5 times the volume of physiological phosphate buffer (PBS) was added to the krill using a Waring Brengu. After homogenizing and passing through quadruple gauze to remove connective tissue, centrifuge at 10,000xg for 10 to 30 minutes to collect the supernatant.
S 400 (Sweden, Salmasha g1)
By performing Gelsi filtration separation using the following method, a low-temperature protease enzyme solution with a concentration of 10 times or more of the protease activity can be obtained.
得られたプロテアーゼの特性は次の通りである。The properties of the obtained protease are as follows.
（１）酵素活性の検出
濃縮プロテアーゼ標品（ＰＢＳ溶液）を牛血清アルブミ
ンを基質として反応させ、トリクロル酢酸（Ｔ ＣＡ
）沈澱を行い、上清の酸可溶性画分の増加によりプロテ
アーゼ活性の検出を試みたが、本性では酵素活性は認め
られず、ポリアクリルアミドデル電気泳動（Ｐ Ａ Ｇ
Ｅ ）にかけ牛血清アルブミンのバンドの消失により
酵素活性を調べた。その結果牛血清フルプミンバンドが
完全に消失し、低分子領域に複数のバンドが出現したこ
とから、オキアミ酵素液中にプロテアーゼ活性が確認さ
れた。(1) Detection of enzyme activity A concentrated protease preparation (PBS solution) was reacted with bovine serum albumin as a substrate, and trichloroacetic acid (T CA
) precipitation, and an attempt was made to detect protease activity by increasing the acid-soluble fraction of the supernatant, but no enzymatic activity was observed, and polyacrylamide delta electrophoresis (PAG) was performed.
E) The enzyme activity was examined by the disappearance of the bovine serum albumin band. As a result, the bovine serum Fulpmin band completely disappeared and multiple bands appeared in the low molecular weight region, confirming protease activity in the krill enzyme solution.
本プロテアーゼは切断部位特異性が比較的高いエンドプ
ロテアーゼであり、アミノ酸１０個以上のペプチド断片
を与えることを示している。このために、先のＴＣＡ法
では本酵素の活性が見出されなかった原因である。This protease is an endoprotease with relatively high cleavage site specificity, and has been shown to yield peptide fragments of 10 or more amino acids. This is the reason why the activity of this enzyme was not found in the previous TCA method.
（２）デルＩ過による酵素の精製
オキアミホモジネートを５ｅｐｌ＋ａｅｒｙｌ Ｓ −
２００゜Ｓ −３００，Ｓ−４００でＰＢＳｔｒ：ｌＬ
衝液として用いて分画した結果、Ｓ−４００が最適であ
り、１回のゲルｌ過分離で９０％以上の活性分画を果た
すことが出来ており、この活性分画には２つの分画区が
得られ、両分Ａ区よりは分子量約５万、画分Ｂからは分
子量約３．３万のものが得られた。(2) Purification of enzyme by Del I filtration 5 epl + aeryl S -
PBStr: 1L at 200°S-300, S-400
As a result of fractionation using S-400 as a buffer solution, it was found that S-400 was the most suitable, and more than 90% of the active fractions were achieved in one gel separation, and this active fraction included two fractions. Fraction A had a molecular weight of about 50,000, and fraction B had a molecular weight of about 33,000.
（３）酵素の基質特異性
本酵素はアルギニンに最も高い基質特異性を示し、リジ
ン及びロイシンに対しても活性を示したが、チロシン及
びフェニルアラニンに対しては活性を示さなかった。こ
の基質特異性はトリプシンと類似しており、Ａ、Ｂ両画
分はトリプシンと同様アルギニンに対して最も高い活性
を示した。リジンに対してはトリプシンは分解初期速度
はアルギニンの５０％以上であったのに対し、Ａ、Ｂ両
画分ともかなり低い分解速度を与えた。またトリプシン
はロイシンに対して分解活性を示さなかったが、Ａ、Ｂ
両画分ともに弱いロイシン分解活性を示した。(3) Substrate specificity of the enzyme This enzyme showed the highest substrate specificity for arginine, and also showed activity for lysine and leucine, but did not show activity for tyrosine and phenylalanine. This substrate specificity is similar to that of trypsin, and both fractions A and B showed the highest activity toward arginine, similar to trypsin. For lysine, the initial decomposition rate of trypsin was more than 50% that of arginine, whereas both fractions A and B gave a considerably lower decomposition rate. Also, trypsin did not show degrading activity for leucine, but
Both fractions showed weak leucine degrading activity.
（４）至適ｐＨ
種々のｐＨのリンｐＨｕＬ衝液中でＢ画分を牛血清アル
ブミン（ＢＳＡ）と反応させ、ＰＡＧＥ法で活性を測定
すると、ｐＨ６，５〜８．０では高い活性を示した。(4) Optimal pH When the B fraction was reacted with bovine serum albumin (BSA) in phosphorus pH HuL buffer solutions at various pHs and the activity was measured by PAGE method, high activity was shown at pH 6.5 to 8.0. .
（５）至適温度
本発明のプロテアーゼは、種々の温度で牛血清アルブミ
ンと反応させ分析した結果、Ａ、Ｂ両画分共に５℃及１
／１０℃でも活性を示し、２０℃で最大活性を示した。(5) Optimal temperature The protease of the present invention was analyzed by reacting with bovine serum albumin at various temperatures.
It showed activity even at /10°C and showed maximum activity at 20°C.
しかも３７℃以上のより高い温度で活性が低下したこと
より、低温プロテアーゼであり、他に例のない特異的な
プロテアーゼであることが明らかである。Furthermore, since the activity decreased at higher temperatures of 37° C. or higher, it is clear that it is a low temperature protease and is a unique and unique protease.
即ち本プロテアーゼは、低温領域特に５〜２０℃にかけ
て特異的に至適温度領域を有することを特徴とする低温
プロテアーゼである。That is, the present protease is a low-temperature protease characterized by having an optimal temperature range specifically in the low-temperature range, particularly from 5 to 20°C.
（６）熱安定性
本発明のプロテアーゼはＡ、Ｂ両画分ともに５０〜７０
℃で処理すると酵素活性の部分的低下が起こリ、ｓｏ’
ｃ以上では完全に失活した。(6) Thermal stability of the protease of the present invention is 50-70 for both fractions A and B.
Treatment at ℃ may cause a partial decrease in enzyme activity, so'
At temperatures above c, the activity was completely inactivated.
（７）ＮａＣ１酎性
本発明のプロテアーゼは１０％ＮａＣｌ存在下でも酵素
活性の低下は認められなかった。(7) NaCl-induced decrease in enzyme activity of the protease of the present invention was not observed even in the presence of 10% NaCl.
本発明では上記のような特性を有するプロテアーゼを醗
酵製品の製造時に原料中に配合する。醗酵製品としては
任意のものを例示でき、例えば味噌、醤油、食酢、ブド
ツ酒、ビール、清酒等の酒類、調味料、その他を例示で
き、これらに限定されるものではない。本発明ではこれ
らの醗酵製品の原料の１つとして上記低温プロテアーゼ
を使用することを特徴とする。In the present invention, a protease having the above-mentioned characteristics is blended into raw materials during the production of fermented products. Examples of fermented products include, but are not limited to, alcoholic beverages such as miso, soy sauce, vinegar, grape sake, beer, and sake, seasonings, and others. The present invention is characterized in that the above-mentioned low-temperature protease is used as one of the raw materials for these fermented products.
本発明において上記低温プロテアーゼの使用量は目的と
する製品に応じ適宜選択することができ、限定的なもの
ではない。本発明の醗酵製品は上記低温プロテアーゼを
原料の一成分とする以外は公知の方法により製造するこ
とができる。In the present invention, the amount of the low-temperature protease used can be appropriately selected depending on the intended product, and is not limited. The fermented product of the present invention can be produced by a known method except for using the above-mentioned low-temperature protease as one of the raw materials.
更にエタノールは上記低温プロテアーゼの酵素活性を一
層高めることが見い出された。従って上記低温プロテア
ーゼ及びエタ／−ルの配合された醸酵製品は一層優れた
特性を有する。エタノールの添加量は広い範囲から選択
できるが、通常は醗＃製品の原料中に約０．１〜５重景
重量好ましくは約１〜２重量％とするのが良い、添加は
公知の方法に従って行うことができる。Furthermore, it has been found that ethanol further increases the enzymatic activity of the above-mentioned low-temperature protease. Therefore, the fermented product containing the low-temperature protease and ethanol has better properties. The amount of ethanol added can be selected from a wide range, but it is usually about 0.1 to 5% by weight, preferably about 1 to 2% by weight, in the raw material of the ethanol product.Addition is carried out according to known methods. It can be carried out.
（実 施 例） 以下に参考例及び実施例を挙げて説明する。(Example) Reference examples and examples will be described below.
参考例１
未加熱（生鮮状！！りのまま、捕獲後急速凍結されたオ
キアミを凍結のまま細切して、３倍量の生理リン酸緩衝
ａ（Ｐ Ｂ Ｓ ）を加えてワーリングブレングーを用
いてホモデナイズし、四重が一ゼでｔ過して結合ＩＩＬ
總を除去後、１０，０００ｘｇで１０〜３０分遠心分離
して上澄液を採り、この上澄液をＳ ｅｐｌ＋ａｃｒｙ
ｌＳ−４００を用いて、デルシ濾過分離を行うことによ
り、プロテアーゼ活性１０倍以上に濃縮された低温プロ
テアーゼ酵素液を得た。Reference Example 1 Unheated (fresh!!) krill that was captured and quickly frozen was cut into small pieces while still frozen, and 3 times the amount of physiological phosphate buffer a (P B S ) was added to Waring Brengu. Homogenize with
After removing the filtrate, centrifuge at 10,000xg for 10 to 30 minutes to collect the supernatant.
By performing Delsi filtration separation using IS-400, a low-temperature protease enzyme solution with a protease activity concentrated 10 times or more was obtained.
実施例１
玄米３．０に、をよく水洗いし水切後、沸騰水中で５〜
１０分間煮沸し３０〜６０分水切りを行い、しかるのち
、加圧蒸煮缶に入れ圧力０．６ｋｇ／ ｃｍ２で３０分
程度蒸煮する。徘圧後蒸し玄米をとり出し３０〜３３℃
まで冷却ののち、アスペルギルス・オリーゼの菌株を接
種し、常法通９床ねせ（発芽を待つ）盛り込み一番手入
、二番手入を経て出麹とする。Example 1 Brown rice 3.0 was thoroughly washed with water, drained, and then soaked in boiling water for 5 to 50 minutes.
Boil for 10 minutes, drain for 30 to 60 minutes, then put in a pressure steamer and steam for about 30 minutes at a pressure of 0.6 kg/cm2. After steaming, take out the steamed brown rice and heat it to 30-33℃.
After cooling to a temperature of 100 mL, inoculate with Aspergillus oryzae strain, rest for 9 times as usual (wait for germination), and use the first and second steps to make koji.
この出麹に食塩０．８ｋｇ及び上記低温プロテアーゼ酵
素液１００ｇをまぜ合せておき、一方大豆を３．７６ｋ
ｇ蒸煮し、上記塩切り麹とをまぜ合せ・味噌。の仕込を
行って２０℃以下で発酵させた６発酵状態は良好であり
、熟成後の低温味噌は味、香典すぐれたものが得られた
。Mix 0.8 kg of salt and 100 g of the above-mentioned low-temperature protease enzyme solution with this de-koji, and on the other hand, add 3.76 kg of soybeans.
g Steam and mix with the above salt-cut koji and miso. The fermentation conditions of 6, which were prepared and fermented at 20°C or lower, were good, and the low-temperature miso after aging had excellent taste and flavor.
実施例２
脱脂大豆に撒水後飽和水蒸気で６．Ｏｋｇ／ｃａ２Ｇで
、３０秒問加熱加圧したのち急激に大気圧下に放出して
得た蒸煮脱脂大豆のうち８． Ｏｋｇを採取し、このも
のに７スペルギルス・ソーヤの種麹を１０．および炒熱
割砕小麦を３．１ｋｇ加え、これを製麹室へ盛込み２８
〜３５℃、６５時間！１１！シた。Example 2 After watering defatted soybeans, 6. 8. Steamed and defatted soybeans obtained by heating and pressurizing at Okg/ca2G for 30 seconds and then rapidly releasing them to atmospheric pressure. Collect Okg and add 7.0 kg of Supergillus soja seed koji to 10.0 kg. Add 3.1 kg of fried cracked wheat and add this to the koji making room 28
~35℃, 65 hours! 11! Shita.
得られた麹に１０％食塩水１２１１上記低温プロテア一
ゼ酵素液１２０ｇ及びエタノール３０ｇを加え２０１ボ
ツトに仕込み２０℃コントロールで熟成させ、島とは常
法により圧搾、製戊することにより低温すが得られた。To the obtained koji, add 120g of 10% saline solution, 120g of the above-mentioned low-temperature protease enzyme solution, and 30g of ethanol. Obtained.
（以 上） 出 願 人 林兼産業株式会社 代 理 人 弁理士 １）村 巖 手続補正書 昭和６２年９月１０日(that's all) Applicant Hayashikane Sangyo Co., Ltd. Representative Patent Attorney 1) Iwao Mura Procedural amendment September 10, 1986
Claims (3)
してなる醗酵製品。(1) A fermented product containing low-temperature protease extracted from krill.
子量約５万及び約３．３万のエキソプロテアーゼ及びエ
ンドプロテアーゼ活性を有する２種類のプロテアーゼを
含み、約５〜２０℃の低温領域に至適温度領域を有し、
ＮａＣｌ耐性を有する低温プロテアーゼである特許請求
の範囲第１項記載の醗酵製品。(2) Low-temperature protease extracted from krill contains two types of proteases with molecular weights of approximately 50,000 and 33,000, having exoprotease and endoprotease activities, and has an optimal temperature in the low temperature range of approximately 5 to 20 degrees Celsius. has an area,
The fermentation product according to claim 1, which is a low temperature protease having NaCl tolerance.
の醗酵製品。(3) The fermented product according to claim 1, which contains ethanol.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP62053878A JPS63219348A (en) | 1987-03-09 | 1987-03-09 | Fermentation product compounded with protease |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP62053878A JPS63219348A (en) | 1987-03-09 | 1987-03-09 | Fermentation product compounded with protease |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPS63219348A true JPS63219348A (en) | 1988-09-13 |
Family
ID=12955006
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP62053878A Pending JPS63219348A (en) | 1987-03-09 | 1987-03-09 | Fermentation product compounded with protease |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS63219348A (en) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1997029179A1 (en) * | 1996-02-12 | 1997-08-14 | Gist-Brocades B.V. | Process for producing fermentable wort |
| JP2003511093A (en) * | 1999-10-20 | 2003-03-25 | ノルデュール・イーエイチエフ | Protein hydrolyzate produced using marine protease |
| WO2007133093A2 (en) * | 2006-05-16 | 2007-11-22 | Biozymatic Sus | Method for decomposing organic waste |
| CN104605299A (en) * | 2015-01-29 | 2015-05-13 | 臧晋 | Pleurotus eryngii pickle fermented product and preparation method of pleurotus eryngii pickle fermented product |
-
1987
- 1987-03-09 JP JP62053878A patent/JPS63219348A/en active Pending
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1997029179A1 (en) * | 1996-02-12 | 1997-08-14 | Gist-Brocades B.V. | Process for producing fermentable wort |
| JP2003511093A (en) * | 1999-10-20 | 2003-03-25 | ノルデュール・イーエイチエフ | Protein hydrolyzate produced using marine protease |
| WO2007133093A2 (en) * | 2006-05-16 | 2007-11-22 | Biozymatic Sus | Method for decomposing organic waste |
| WO2007133093A3 (en) * | 2006-05-16 | 2008-04-10 | Biozymatic Sus | Method for decomposing organic waste |
| CN104605299A (en) * | 2015-01-29 | 2015-05-13 | 臧晋 | Pleurotus eryngii pickle fermented product and preparation method of pleurotus eryngii pickle fermented product |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5180597A (en) | Process for the production of hydrolyzed vegetable proteins using gaseous hydrochloric acid and the product therefrom | |
| EP0065663A1 (en) | Method for the preparation of a protein hydrolyzate from whey protein | |
| CN1543507A (en) | Method of deamidation of milk protein and method of denaturation of milk protein | |
| JPS63219348A (en) | Fermentation product compounded with protease | |
| JP2619298B2 (en) | Production method of salt-free concentrated powder seasoning | |
| KR20050090041A (en) | Method for extracting effective ingredients from hartshorn or antler | |
| JPH0353850A (en) | Making of hydrolyzed vegetable protein and product obtained therefrom | |
| JPH0391445A (en) | Enzyme-denatured protein and its process | |
| JPS60164496A (en) | Preparation of low-molecular peptide | |
| JP2799352B2 (en) | Process for producing corn gluten meal hydrolyzate | |
| JPH09262064A (en) | Soybean processed food | |
| JPH05209000A (en) | Peptide composition having decreased allergenicity | |
| KR20040048650A (en) | process for preparing hydrolysates as seasoning agents from the egg white and hydrolysates obtained by said process | |
| DK146630B (en) | PROCEDURE FOR GELATINE PREPARATION BY PROCESSING COLLAGENIC MATERIAL WITH PROTEOLYTIC ENZYMES | |
| SU1237154A1 (en) | Method of obtaining protein hydrolysate from bone | |
| JPH08252075A (en) | Enzymatic decomposition type seasoning | |
| KR100407764B1 (en) | Method for Production of Silk Peptides | |
| JPS5814813B2 (en) | Foaming agent and its manufacturing method | |
| JPH04121161A (en) | Seasoning and production thereof | |
| JP4548339B2 (en) | High glutamine / glutamic acid-containing polypeptide mixture and process for producing the same | |
| JPS59118063A (en) | Preparation of torn cuttlefish | |
| JPH0254061B2 (en) | ||
| JPS63219377A (en) | Low-temperature protease and isolation thereof | |
| JPH0662793A (en) | Production of solid malted rice | |
| JPH0425780B2 (en) |