JPS6237950B2 - - Google Patents
Info
- Publication number
- JPS6237950B2 JPS6237950B2 JP54144307A JP14430779A JPS6237950B2 JP S6237950 B2 JPS6237950 B2 JP S6237950B2 JP 54144307 A JP54144307 A JP 54144307A JP 14430779 A JP14430779 A JP 14430779A JP S6237950 B2 JPS6237950 B2 JP S6237950B2
- Authority
- JP
- Japan
- Prior art keywords
- myojelly
- water retention
- salt
- muscle
- meat
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired
Links
- 108090000623 proteins and genes Proteins 0.000 claims description 20
- 102000004169 proteins and genes Human genes 0.000 claims description 20
- 206010016807 Fluid retention Diseases 0.000 claims description 17
- 235000013372 meat Nutrition 0.000 claims description 11
- 210000003205 muscle Anatomy 0.000 claims description 11
- 238000000034 method Methods 0.000 claims description 10
- 235000002639 sodium chloride Nutrition 0.000 claims description 7
- 241000251468 Actinopterygii Species 0.000 claims description 6
- 210000001087 myotubule Anatomy 0.000 claims description 5
- 239000002244 precipitate Substances 0.000 claims description 5
- 241001465754 Metazoa Species 0.000 claims description 3
- 239000007791 liquid phase Substances 0.000 claims description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 2
- 239000011780 sodium chloride Substances 0.000 claims description 2
- 230000002195 synergetic effect Effects 0.000 claims description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 2
- 238000007598 dipping method Methods 0.000 claims 1
- 241000894007 species Species 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 19
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 6
- 238000004925 denaturation Methods 0.000 description 5
- 230000036425 denaturation Effects 0.000 description 5
- 235000013305 food Nutrition 0.000 description 5
- 230000008014 freezing Effects 0.000 description 5
- 238000007710 freezing Methods 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 230000007423 decrease Effects 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 235000019465 surimi Nutrition 0.000 description 4
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 3
- 238000000605 extraction Methods 0.000 description 3
- 241000238424 Crustacea Species 0.000 description 2
- 241001121816 Metapenaeus joyneri Species 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 238000005336 cracking Methods 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 239000004744 fabric Substances 0.000 description 2
- 238000007654 immersion Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 238000002791 soaking Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 238000010257 thawing Methods 0.000 description 2
- 108010043137 Actomyosin Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000011632 Caseins Human genes 0.000 description 1
- 108010076119 Caseins Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 108010082495 Dietary Plant Proteins Proteins 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 108010068370 Glutens Proteins 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 235000021120 animal protein Nutrition 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
- 238000005119 centrifugation Methods 0.000 description 1
- 230000002925 chemical effect Effects 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 238000010411 cooking Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 235000021312 gluten Nutrition 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 235000015110 jellies Nutrition 0.000 description 1
- 239000008274 jelly Substances 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 238000010298 pulverizing process Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000004381 surface treatment Methods 0.000 description 1
- 230000002522 swelling effect Effects 0.000 description 1
Landscapes
- Meat, Egg Or Seafood Products (AREA)
Description
【発明の詳細な説明】
本発明は動物筋肉を液相中で微細に粉砕し、遠
心分離した沈澱物である蛋白質(ミオゼリー)
〔特公昭58−23053号公報参照〕を筋肉繊維と接触
させることによつて筋肉繊維の保水性を向上させ
る方法に関するものである。[Detailed description of the invention] The present invention produces protein (myojelly), which is a precipitate obtained by finely pulverizing animal muscle in a liquid phase and centrifuging it.
[Refer to Japanese Patent Publication No. 58-23053] The present invention relates to a method for improving the water retention capacity of muscle fibers by contacting the same with muscle fibers.
一般に蓄肉、魚肉、甲殻類の肉などは鮮度の低
下に伴なつてその筋肉繊維の保水性が低下し、筋
肉繊維の身割れなどを起こし品質が低下すると共
に、特に保蔵のための凍結によつてドリツプの流
出等保水力が低下したり身割れによる品質低下な
どが起こる。また蓄肉ハムなどの場合には製品保
管中に離水などの現象が発生し商品価値を著しく
低下させている。そのために従来異種蛋白質のイ
ンジエクシヨン、タンブリング、食塩浸漬による
表面処理、燐酸系添加剤による保水性の改良など
の方法が実施されている。 In general, as the freshness of stored meat, fish meat, and crustacean meat decreases, the water retention capacity of the muscle fibers decreases, resulting in cracking of the muscle fibers, resulting in a decrease in quality. Water retention capacity decreases due to leakage of drips, and quality deteriorates due to cracking. Furthermore, in the case of stored meat ham, phenomena such as syneresis occur during product storage, significantly reducing the product value. To this end, methods such as in-die extraction of foreign proteins, tumbling, surface treatment by immersion in common salt, and improvement of water retention using phosphoric acid additives have been carried out.
しかし之等の方法は何れも本質的な保水性の改
良にはならず、特に燐酸系添加剤の多用は種々問
題が提起されており好ましくない。 However, none of these methods substantially improves water retention, and in particular, extensive use of phosphoric acid additives poses various problems and is therefore undesirable.
本発明者等は新しく開発調製したミオゼリーの
性質とその利用法に関し種々研究検討を加えた結
果、ミオゼリーが従来から使用されているスリ身
などの蛋白素材と異なり、保水性の改良に対して
顕著な効果を発揮せしめることを見出すと共に、
ミオゼリーが冷凍耐性に優れており、併せて生鮮
食肉と同様の柔軟性と可逆性のある構造を有して
いることを確認し、特に瞬間変性から長時間未変
性までの広い範囲の性質を目的に合わせて任意に
選択出来ることとにより本発明を完成した。 The present inventors conducted various research studies on the properties of the newly developed and prepared myojelly and its usage, and found that myojelly, unlike the conventionally used protein materials such as surimi, has a remarkable ability to improve water retention. In addition to discovering the effects that can be achieved,
It was confirmed that myojelly has excellent freezing resistance, as well as a flexible and reversible structure similar to that of fresh meat, with the aim of achieving a wide range of properties, from instant denaturation to long-term non-denaturation. The present invention has been completed by allowing arbitrary selection according to the requirements.
ミオゼリーの性質を要約すると次ぎの通りであ
る。 The properties of myojelly can be summarized as follows.
ミオゼリーの性質
保水力に富んでいること、
接着性を有すること、
ゲル形成能が強いこと、
色を白くすることによつて見栄えを良くする
こと、
臭いが良くなること、
味が良くなること、
著しく冷凍変性した蓄肉、魚肉、甲殻類肉など
は何れも
(1) 筋肉の切断面が雑布状に身割れする
(2) 保水力が低下する
(3) 解凍時のドリツプが大量に発生する
(4) 加熱ドリツプも多い
(5) 食感が劣化する
(6) 酸化による食品としての価値が著しく低下す
る
(7) 中には食品として用い得ないものさえある
之等の問題点を解決するため蓄肉では従来、異
種蛋白質、例えばグルテン、大豆分離蛋白などの
植物蛋白、カゼイン、アルブミン、スリ身などの
動物蛋白などをインジエクシヨン、タンブリン
グ、浸漬などの方法によつて、また魚肉・蓄肉で
は薄い食塩水への浸漬や燐酸系、アミノ酸系物質
の添加による保水性改良法が実施されているが、
現在までに食感上満足出来るものは未だ存在して
いない。Properties of Myojelly: High water retention capacity, adhesive properties, strong gel-forming ability, white color for better appearance, better smell, better taste, Any meat, fish, or crustacean meat that has been severely frozen-denatured will (1) have the cut surface of the muscle crack like a rag, (2) have a reduced water-holding capacity, and (3) produce a large amount of drips when thawed. (4) There are many heated drips (5) The texture deteriorates (6) The value as a food is significantly reduced due to oxidation (7) Some products cannot even be used as food. Conventionally, in the production of meat, foreign proteins such as gluten, vegetable proteins such as soybean isolate protein, animal proteins such as casein, albumin, and surimi are added by methods such as injecting, tumbling, and soaking, and in the case of fish and farmed meat, dilute salt is used. Water retention improvement methods have been implemented, such as immersion in water and the addition of phosphoric acid-based or amino acid-based substances.
To date, there has not yet been anything satisfying in terms of texture.
即ち食品としての筋肉は保水性に寄与するアク
トミオシンを主とする塩溶性蛋白質と、それ自体
は保水性力に欠けてはいるが熱凝固して固くなる
水溶性蛋白質、更には硬蛋白質と言われているコ
ラーゲン系蛋白質のゼラチンへの変性などの相乗
的作用によつて食品としての潤沢なテクスチユア
ーを形成するものであり、特に塩溶性蛋白質は保
水性、食感に対して重要な因子である。しかるに
鮮度低下あるいは冷凍変性した筋肉は、その重要
な塩溶性蛋白質が酵素的性質を有している水溶性
蛋白質の影響、或いは氷結による物理的化学的影
響により食品として最も重要な保水性、構造性を
消失して了うのである。そのため劣化した当量相
当の塩溶性蛋白質を補充すれば、その性質が回復
する筈であるとの考えのもとに実際にスリ身など
の良質を塩溶性蛋白質を主成分とする蛋白質をイ
ンジエクシヨンしてみた筋肉組織内部にまで乏等
の蛋白質が浸透しづらくカマボコ的弾力が出るだ
けで、特に冷凍耐性に弱く、また保水力の点でも
加熱離水などの点でも満足出来ない。 In other words, muscle as a food consists of salt-soluble proteins, mainly actomyosin, which contribute to water retention, water-soluble proteins, which themselves lack water-retention ability but harden through heat coagulation, and hard proteins. The rich texture of food is formed through synergistic effects such as the denaturation of collagen-based proteins into gelatin, and salt-soluble proteins are particularly important factors for water retention and texture. . However, muscle that has lost its freshness or has been freeze-denatured loses water retention and structure, which are most important for food, due to the influence of water-soluble proteins whose important salt-soluble proteins have enzymatic properties, or the physical and chemical effects of freezing. It ends when it disappears. Therefore, based on the idea that if you replenish the equivalent amount of salt-soluble protein that has deteriorated, its properties should be restored, we actually injected high-quality surimi, such as surimi, into a protein whose main component is salt-soluble protein. It is difficult for the poor protein to penetrate into the muscle tissue, resulting in a hollow-like elasticity, which makes it particularly weak against freezing, and is unsatisfactory in terms of water retention and heat syneresis.
之等に対し本発明法によるミオゼリーを鮮度の
低下した筋肉、或いは冷凍変性した筋肉に添加後
に調理するか、または凍結前にミオゼリーを添加
しておいて解凍後に調理するか、何れの場合にお
いても筋肉組織細部にまで良質の塩溶性蛋白質が
よく浸透し従来に得られなかつた程度に筋肉が改
良され殆んど生鮮品と変わらないまでに改良され
た。 For this purpose, myojelly according to the method of the present invention can be added to muscle whose freshness has decreased or muscle that has been frozen and denatured and then cooked, or the myojelly can be added before freezing and then cooked after thawing, in either case. The high-quality salt-soluble protein penetrates into the details of the muscle tissue, improving the muscle to a degree that has never been achieved before, and improving it to the point where it is almost as good as a fresh product.
上記の如き格段の効果は液相中での充分粉砕さ
れているため蛋白質の変質が少なく、且つ遠心分
離で得られた沈澱物であるのでその形状が微細で
あることによるものではないかと推測される。 It is speculated that the above-mentioned remarkable effect is due to the fact that the protein is sufficiently pulverized in the liquid phase, so there is little denaturation of the protein, and since it is a precipitate obtained by centrifugation, its shape is fine. Ru.
以下に実施例により更に本発明を説明する。 The present invention will be further explained below with reference to Examples.
実施例 1
助宗ダラ落し身1000grを水溶液に懸濁せしめ、
ホモジナイザーで1分間摩砕し、未粉砕部分を
布にて除き、遠心機にて遠心効果1000G以上を与
え上澄液を除き、沈澱物(ミオゼリー)1100grを
得た。Example 1 Suspend 1000g of Sukemune Dara Ochimi in an aqueous solution,
The mixture was ground with a homogenizer for 1 minute, the unground portion was removed with a cloth, and the supernatant liquid was removed using a centrifuge with a centrifugal effect of 1000 G or more to obtain 1100 gr of precipitate (myojelly).
該ミオゼリーを5、10、20、30、50倍希釈し、
1年間冷凍保蔵してスポンジ化した助宗ダラフイ
レーにインジエクシヨン、タンブリング、浸漬法
にて前記ミオゼリーを夫々添加後、調理加工した
ものと、冷凍後1ケ月間保蔵し解凍したものとの
対比を行なつた処、無添加区は解凍ドリツプが15
〜20%にて調理加工時に更に20〜25%の加熱ドリ
ツプが出たが、ミオゼリー添加区は添加法又は添
加量の差によるテクスチユアーの差は認められる
が、加熱ドリツプは2〜3%以下で完全な保水性
を示し、原魚当りの最終歩留は総べて100%を越
えインジエクシヨンとタンブリングとを併用した
場合には最大160%を示した。 The myojelly was diluted 5, 10, 20, 30, and 50 times,
A comparison was made between Sukemune Dara fillet, which had been frozen and stored for one year and made into a sponge, and which was cooked and processed after adding the above-mentioned myojelly by in-die extraction, tumbling, and soaking methods, and that which had been frozen, stored for one month, and then thawed. The additive-free area has a thawed drip of 15
At ~20%, an additional 20-25% of heated drips were generated during cooking processing, but in the myojelly-added group, there were differences in texture due to differences in the addition method or amount, but heated drips were below 2-3%. It exhibited perfect water retention, and the final yield per raw fish exceeded 100% in all cases, and reached a maximum of 160% when injection and tumbling were used together.
希釈倍率による差は5〜10倍量ではインジエク
シヨンはノズルの関係で容易ではないが、10倍以
上30倍で良好であり、50倍を超えると保水性の改
良には効果はあるが、食感の改良には不満足であ
つた。 The difference in dilution ratio is that when the amount is 5 to 10 times, in-die extraction is not easy due to the nozzle, but when it is 10 times to 30 times, it is good, and when it exceeds 50 times, it is effective in improving water retention, but it does not improve texture. was not satisfied with the improvement.
添加する時にミオゼリー希釈液に0.1〜5%の
食塩を添加した場合(ブレミツクス法と言う)は
食塩添加量の多い程ゲル弾力性が強くなり、調理
加工時に食塩と接触させる法(ポストミツクス法
と言う)より加熱ゲル形成力、即ち構造性、テク
スチユアーに優れている結果が得られた。 When 0.1 to 5% salt is added to the diluted myojelly solution (called the blemix method), the more salt added, the stronger the gel elasticity becomes. Results were obtained that showed superior thermal gel-forming ability, that is, superior structure and texture.
実施例 2
シバエビのムキ身1000grを水溶液に懸濁せし
め、ホモジナイザーにて90秒摩砕し、未粉砕部分
を布にて除き、遠心機にて遠心効果1000G以上
を与え上澄液を除き沈澱物(ミオゼリー)1050gr
を得た。Example 2 Suspend 1000g of Shiba shrimp muki in an aqueous solution, grind it for 90 seconds with a homogenizer, remove the unground part with a cloth, apply a centrifugal effect of 1000G or more with a centrifuge, remove the supernatant liquid, and precipitate. (Myo jelly) 1050gr
I got it.
該ミオゼリーを使つて、実施例1の冷凍助宗ダ
ラと同様に実施した。シバエビの場合はミオゼリ
ーの膨潤性のために希釈率は5〜20倍が好まし
く、実施例1と同様完全な保水性を示し、冷凍解
凍の操作を繰り返しても同等であつた。また食塩
の添加はプレミツクスの時は添加後、常温で1時
間以内に生ミオゲルが形成し、魚肉のミオゼリー
の変性に比べ著しく速いことが判つた。 The myojelly was used in the same manner as for the frozen Sukemune cod in Example 1. In the case of Shiba shrimp, the dilution rate is preferably 5 to 20 times due to the swelling properties of myojelly, and as in Example 1, it exhibited perfect water retention and remained the same even after repeated freezing and thawing operations. It was also found that raw myogel was formed within one hour at room temperature after addition of salt in the case of premixed salt, which was significantly faster than the denaturation of myojelly from fish meat.
Claims (1)
を水中若しくは液相中で微細に粉砕、遠心分離し
沈澱として得られた蛋白質(以下、ミオゼリーと
言う)から成る新規な魚肉食肉用品質改良剤をイ
ンジエクシヨン、タンブリング、浸漬若しくは塗
布し食塩との相乗作用による筋肉繊維の保水性改
良法。1. A novel quality improver for fish meat, which is made of protein obtained as a precipitate by finely crushing and centrifuging animal muscles of the same or different species in water or in a liquid phase (hereinafter referred to as myojelly), is applied to animal muscles. A method for improving water retention of muscle fibers by injecting, tumbling, dipping or applying synergistic action with common salt.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP14430779A JPS5668357A (en) | 1979-11-09 | 1979-11-09 | Improvement of water retention of muscular fiber |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP14430779A JPS5668357A (en) | 1979-11-09 | 1979-11-09 | Improvement of water retention of muscular fiber |
Publications (2)
Publication Number | Publication Date |
---|---|
JPS5668357A JPS5668357A (en) | 1981-06-09 |
JPS6237950B2 true JPS6237950B2 (en) | 1987-08-14 |
Family
ID=15359030
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP14430779A Granted JPS5668357A (en) | 1979-11-09 | 1979-11-09 | Improvement of water retention of muscular fiber |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPS5668357A (en) |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2004001800A2 (en) | 2002-06-19 | 2003-12-31 | Foster-Miller, Inc. | Chip package sealing method |
US11407202B2 (en) | 2018-08-06 | 2022-08-09 | Toyo Kohan Co., Ltd. | Roll-bonded laminate, method for producing the same, and heat radiation reinforcement member for electronic equipment |
Families Citing this family (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7160567B2 (en) * | 2002-09-24 | 2007-01-09 | Proteus Industries, Inc. | Process for retaining moisture in cooked food with a peptide |
EP1542551B1 (en) * | 2002-09-24 | 2011-06-15 | Proteus Industries, Inc. | Process for retaining moisture in cooked food |
JP6509285B2 (en) * | 2017-07-28 | 2019-05-08 | 健太郎 手塚 | Meat mass processing method |
-
1979
- 1979-11-09 JP JP14430779A patent/JPS5668357A/en active Granted
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2004001800A2 (en) | 2002-06-19 | 2003-12-31 | Foster-Miller, Inc. | Chip package sealing method |
US11407202B2 (en) | 2018-08-06 | 2022-08-09 | Toyo Kohan Co., Ltd. | Roll-bonded laminate, method for producing the same, and heat radiation reinforcement member for electronic equipment |
Also Published As
Publication number | Publication date |
---|---|
JPS5668357A (en) | 1981-06-09 |
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