JPH04197156A - Softener for edible meat - Google Patents
Softener for edible meatInfo
- Publication number
- JPH04197156A JPH04197156A JP2326542A JP32654290A JPH04197156A JP H04197156 A JPH04197156 A JP H04197156A JP 2326542 A JP2326542 A JP 2326542A JP 32654290 A JP32654290 A JP 32654290A JP H04197156 A JPH04197156 A JP H04197156A
- Authority
- JP
- Japan
- Prior art keywords
- meat
- softener
- elastase
- hard
- enzymes
- 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
- 235000013372 meat Nutrition 0.000 title abstract description 18
- 102000016387 Pancreatic elastase Human genes 0.000 claims abstract description 11
- 108010067372 Pancreatic elastase Proteins 0.000 claims abstract description 11
- 108010091431 meat tenderizer Proteins 0.000 claims description 2
- 235000015278 beef Nutrition 0.000 abstract description 4
- 235000019658 bitter taste Nutrition 0.000 abstract description 4
- 241000287828 Gallus gallus Species 0.000 abstract description 3
- 235000013330 chicken meat Nutrition 0.000 abstract description 3
- 235000015277 pork Nutrition 0.000 abstract 1
- 102000004190 Enzymes Human genes 0.000 description 10
- 108090000790 Enzymes Proteins 0.000 description 10
- 229940088598 enzyme Drugs 0.000 description 10
- 235000018102 proteins Nutrition 0.000 description 10
- 102000004169 proteins and genes Human genes 0.000 description 10
- 108090000623 proteins and genes Proteins 0.000 description 10
- 241001465754 Metazoa Species 0.000 description 7
- 239000004365 Protease Substances 0.000 description 4
- 241000283690 Bos taurus Species 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 210000003205 muscle Anatomy 0.000 description 3
- 102000008186 Collagen Human genes 0.000 description 2
- 108010035532 Collagen Proteins 0.000 description 2
- 102000016942 Elastin Human genes 0.000 description 2
- 108010014258 Elastin Proteins 0.000 description 2
- 108090000526 Papain Proteins 0.000 description 2
- 102000004142 Trypsin Human genes 0.000 description 2
- 108090000631 Trypsin Proteins 0.000 description 2
- 230000032683 aging Effects 0.000 description 2
- 229920001436 collagen Polymers 0.000 description 2
- 229920002549 elastin Polymers 0.000 description 2
- 102000034240 fibrous proteins Human genes 0.000 description 2
- 108091005899 fibrous proteins Proteins 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 210000000663 muscle cell Anatomy 0.000 description 2
- 229940055729 papain Drugs 0.000 description 2
- 235000019834 papain Nutrition 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 108010043137 Actomyosin Proteins 0.000 description 1
- 102000011632 Caseins Human genes 0.000 description 1
- 108010076119 Caseins Proteins 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 102000009123 Fibrin Human genes 0.000 description 1
- 108010073385 Fibrin Proteins 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- 108090000270 Ficain Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 239000004902 Softening Agent Substances 0.000 description 1
- 241000282898 Sus scrofa Species 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 235000009508 confectionery Nutrition 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000010411 cooking Methods 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 235000019836 ficin Nutrition 0.000 description 1
- POTUGHMKJGOKRI-UHFFFAOYSA-N ficin Chemical compound FI=CI=N POTUGHMKJGOKRI-UHFFFAOYSA-N 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 210000004379 membrane Anatomy 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 230000000956 myotropic effect Effects 0.000 description 1
- 230000017448 oviposition Effects 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 210000004303 peritoneum Anatomy 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 235000020995 raw meat Nutrition 0.000 description 1
- 230000000384 rearing effect Effects 0.000 description 1
- 230000009967 tasteless effect Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
Abstract
Description
【発明の詳細な説明】 [産業上の利用分野] 本発明は、食用肉の軟化剤に関する。[Detailed description of the invention] [Industrial application field] The present invention relates to a tenderizer for edible meat.
[従来の技術]
動物例えばウシ、ニワトリなどの肉を食用に供するとき
、その肉が余りに硬いと食感を損なうことになる。その
ため、肉を軟らかくするのに、種々の方策が考えられる
。その一つとして、酵素を用・いる方法がある。酵素は
、調理中にその活性を失うため、好ましい方法と考えら
れる。[Prior Art] When meat from animals such as cows and chickens is eaten, if the meat is too hard, the texture will be impaired. Therefore, various methods can be considered to make meat tender. One method is to use enzymes. Enzymes are considered the preferred method since they lose their activity during cooking.
肉の硬さを決めているのは、筋細胞内の筋原線維蛋白質
例えばアクトミオシンによる構造の状態と、筋細胞外の
例えば結合組織線維蛋白質例えばコラーゲン、エラスチ
ンなどによる構造(筋向膜、筋周膜なと)の状態である
。前者の構造は、熟成により変化をうける。What determines the firmness of meat is the structural state of myofibrillar proteins such as actomyosin within the muscle cells, and the structure of connective tissue fibrous proteins such as collagen and elastin outside the muscle cells (myotropic membrane, muscle It is in a state of peritoneum. The structure of the former undergoes changes with aging.
一方、細胞外の硬蛋白質の構造による肉の硬さは、動物
の年令、飼育条件、筋肉の部位に依存する。特に、採卵
廃鶏、乳用庚午のような老齢の動物では、硬蛋白質含量
が高く、筋肉が硬い、この硬蛋白質は、熟成により変化
をうけない、内在性エンドペブチターゼが、これら硬蛋
白質に殆ど作用できないことがその原因の一つである。On the other hand, the firmness of meat due to the structure of extracellular hard proteins depends on the age of the animal, rearing conditions, and muscle location. In particular, in old animals such as egg-laying hens and dairy cows, the hard protein content is high and the muscles are hard.This hard protein does not change with aging. One of the reasons for this is that it has little effect on
そのため、外在性のプロテアーゼを添加して硬蛋白質を
分解することが試みられている。Therefore, attempts have been made to add exogenous proteases to degrade hard proteins.
微生物由来の酵素は、筋原線維蛋白質に作用できるが、
硬蛋白質に殆ど作用しない、一方、植物由来の酵素例え
ばパパイン、フィシンは、筋原線維蛋白質にも、硬蛋白
質にもよく作用する。又、従来用いられている動物由来
の酵素例えばトリプシンは、植物由来の酵素に似ている
が、硬蛋白質に対する作用はやや弱い。Enzymes derived from microorganisms can act on myofibrillar proteins, but
On the other hand, plant-derived enzymes such as papain and ficin act well on both myofibrillar proteins and scleroproteins. Furthermore, conventionally used animal-derived enzymes, such as trypsin, are similar to plant-derived enzymes, but their effect on hard proteins is somewhat weak.
従って、硬蛋白質の分解には、植物由来及び動物由来の
酵素が利用できることが考えられるが、従来用いられて
いる酵素例えばパパイン、トリブシンでは、容易に筋原
線維構造が分解され、肉特有の好ましいテクスチャーが
失われる。又、これら酵素を使用すると、得られた製品
に、食感を害する苦みが生ずる。Therefore, enzymes derived from plants and animals can be used to decompose hard proteins, but conventionally used enzymes such as papain and tribucin easily decompose myofibrillar structures, which are preferable and unique to meat. Texture is lost. Furthermore, when these enzymes are used, the resulting product has a bitter taste that impairs its texture.
[発明の概要]
本発明は、エラスターゼを含有する食用肉の軟化剤に関
する。[Summary of the Invention] The present invention relates to an edible meat tenderizer containing elastase.
本発明の軟化剤に用いられるエラスターゼは、動物の種
々の組織特にブタの膵臓から得られ、カゼイン、エラス
チン、フィブリン、変性コラーゲンを分解する、灰色〜
淡褐色の粉末で、味は殆どない、毒性(LD、。)は、
経口で〉15万工ラスターゼ単位/kg(ラット及びマ
ウス)であり、殆どない0本発明では、精製したもので
も、精製しないものでもよい。Elastase used in the softening agent of the present invention is obtained from various animal tissues, particularly pig pancreas, and degrades casein, elastin, fibrin, and denatured collagen.
Light brown powder, almost tasteless, toxic (LD,.)
Orally > 150,000 Lastase units/kg (rats and mice), almost negligible 0 In the present invention, purified or unpurified products may be used.
本発明の軟化剤は、生肉の加工前、好ましくは加工直前
に、肉に均一に添加する。対象とする肉は、食用に供す
るものであればどんな肉でもよく、例えばウシ、ニワト
リ、ブタ、ウマなどが挙げられる。 添加された肉を、
一定時間室温又はそれよりやや高い温度に置いて加工例
えば焼いたり、煮たりする。添加量は、対象となる肉に
よりやや異なるが、肉100gに対し10〜5000エ
ラスターゼ単位、好ましくは100〜3000 エ
ラスターゼ単位、最も好ましくは300〜1000エラ
スターゼ単位である。The tenderizer of the present invention is uniformly added to raw meat before processing, preferably immediately before processing. The target meat may be any meat that is edible, such as cow, chicken, pig, horse, etc. Added meat,
It is left at room temperature or a slightly higher temperature for a certain period of time and then processed, such as by baking or boiling. The amount added varies slightly depending on the target meat, but is 10 to 5,000 elastase units, preferably 100 to 3,000 elastase units, and most preferably 300 to 1,000 elastase units per 100 g of meat.
本発明の軟化剤は、従来用いられている植物由来及び動
物由来の酵素に比べて、得られた製品に苦みが全くなく
、又そのテキスチャーも肉特有のものが失われることな
く、保持されている。The tenderizer of the present invention has no bitterness in the resulting product compared to conventionally used plant-derived and animal-derived enzymes, and its texture retains its characteristic meat properties. There is.
[実施例コ
実施例 1
硬蛋白質の多い牛肉500gを細切りし、これに、エラ
スターゼを5000エラスターゼ単位加え、均一になる
ようによく混和した。室温で、1時間放置した後、常法
に従って焼いた。得られた焼肉は、柔らかく、甘味があ
って、硬蛋白質の少ない牛肉を焼いたのと殆ど変わらな
かった。[Example 1] 500 g of beef containing a large amount of hard protein was cut into thin pieces, and 5,000 elastase units of elastase were added thereto, and the mixture was thoroughly mixed until the mixture was homogeneous. After being left at room temperature for 1 hour, it was baked in a conventional manner. The resulting yakiniku was tender and sweet, almost the same as grilled beef with less hard protein.
一方、同じ牛肉でエラスターゼ処理をしないものでは、
硬く、甘味も殆どなかった。又、トリプシン処理をした
ものでは、肉′特有のテクスチャーが失われ、しかも苦
みが生じ、食用に適さなかった。On the other hand, the same beef that is not treated with elastase,
It was hard and had almost no sweetness. In addition, when trypsin-treated meat loses its characteristic texture and has a bitter taste, it is not suitable for consumption.
Claims (1)
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2326542A JPH04197156A (en) | 1990-11-28 | 1990-11-28 | Softener for edible meat |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP2326542A JPH04197156A (en) | 1990-11-28 | 1990-11-28 | Softener for edible meat |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH04197156A true JPH04197156A (en) | 1992-07-16 |
Family
ID=18188996
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2326542A Pending JPH04197156A (en) | 1990-11-28 | 1990-11-28 | Softener for edible meat |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPH04197156A (en) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2008301779A (en) * | 2007-06-08 | 2008-12-18 | Iris Ohyama Inc | Pet food |
-
1990
- 1990-11-28 JP JP2326542A patent/JPH04197156A/en active Pending
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JP2008301779A (en) * | 2007-06-08 | 2008-12-18 | Iris Ohyama Inc | Pet food |
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