JPH09299065A - Production of fish-paste product of fish meat and animal meat - Google Patents
Production of fish-paste product of fish meat and animal meatInfo
- Publication number
- JPH09299065A JPH09299065A JP8115900A JP11590096A JPH09299065A JP H09299065 A JPH09299065 A JP H09299065A JP 8115900 A JP8115900 A JP 8115900A JP 11590096 A JP11590096 A JP 11590096A JP H09299065 A JPH09299065 A JP H09299065A
- Authority
- JP
- Japan
- Prior art keywords
- meat
- fish
- transglutaminase
- elasticity
- product
- 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 claims abstract description 40
- 241000251468 Actinopterygii Species 0.000 title claims abstract description 31
- 229940023462 paste product Drugs 0.000 title claims abstract description 12
- 238000004519 manufacturing process Methods 0.000 title claims description 13
- 241001465754 Metazoa Species 0.000 title abstract description 5
- 108060008539 Transglutaminase Proteins 0.000 claims abstract description 41
- 102000003601 transglutaminase Human genes 0.000 claims abstract description 41
- 239000000137 peptide hydrolase inhibitor Substances 0.000 claims abstract description 26
- 238000006911 enzymatic reaction Methods 0.000 claims abstract description 23
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 claims abstract description 19
- 235000015220 hamburgers Nutrition 0.000 claims abstract description 10
- 239000002994 raw material Substances 0.000 claims abstract description 9
- 238000000034 method Methods 0.000 claims description 8
- 244000144972 livestock Species 0.000 claims description 7
- 235000004611 garlic Nutrition 0.000 claims description 5
- 244000245420 ail Species 0.000 claims 1
- 230000000694 effects Effects 0.000 abstract description 9
- 235000011194 food seasoning agent Nutrition 0.000 abstract description 7
- 229920002472 Starch Polymers 0.000 abstract description 6
- 150000003839 salts Chemical class 0.000 abstract description 6
- 235000019698 starch Nutrition 0.000 abstract description 6
- 239000008107 starch Substances 0.000 abstract description 6
- 238000011282 treatment Methods 0.000 abstract description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 abstract description 5
- 241001098054 Pollachius pollachius Species 0.000 abstract description 4
- 241000785681 Sander vitreus Species 0.000 abstract description 3
- 235000013305 food Nutrition 0.000 abstract description 3
- 239000000047 product Substances 0.000 description 33
- 235000019688 fish Nutrition 0.000 description 25
- 238000010438 heat treatment Methods 0.000 description 21
- 230000001953 sensory effect Effects 0.000 description 8
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 7
- 238000011156 evaluation Methods 0.000 description 7
- 239000000796 flavoring agent Substances 0.000 description 7
- 235000019634 flavors Nutrition 0.000 description 7
- 235000019465 surimi Nutrition 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 229940088598 enzyme Drugs 0.000 description 5
- 239000005457 ice water Substances 0.000 description 5
- 240000002234 Allium sativum Species 0.000 description 4
- 239000012467 final product Substances 0.000 description 4
- 235000013622 meat product Nutrition 0.000 description 4
- 230000035484 reaction time Effects 0.000 description 4
- 238000009938 salting Methods 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 3
- 241000555825 Clupeidae Species 0.000 description 3
- YBHQCJILTOVLHD-YVMONPNESA-N Mirin Chemical compound S1C(N)=NC(=O)\C1=C\C1=CC=C(O)C=C1 YBHQCJILTOVLHD-YVMONPNESA-N 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 125000002252 acyl group Chemical group 0.000 description 3
- 229910052791 calcium Inorganic materials 0.000 description 3
- 239000011575 calcium Substances 0.000 description 3
- 235000021189 garnishes Nutrition 0.000 description 3
- 235000020993 ground meat Nutrition 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 238000000465 moulding Methods 0.000 description 3
- 238000012545 processing Methods 0.000 description 3
- 108090000623 proteins and genes Proteins 0.000 description 3
- 235000019512 sardine Nutrition 0.000 description 3
- NEAQRZUHTPSBBM-UHFFFAOYSA-N 2-hydroxy-3,3-dimethyl-7-nitro-4h-isoquinolin-1-one Chemical compound C1=C([N+]([O-])=O)C=C2C(=O)N(O)C(C)(C)CC2=C1 NEAQRZUHTPSBBM-UHFFFAOYSA-N 0.000 description 2
- 108010000912 Egg Proteins Proteins 0.000 description 2
- 102000002322 Egg Proteins Human genes 0.000 description 2
- 108010064983 Ovomucin Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 230000009849 deactivation Effects 0.000 description 2
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 235000018102 proteins Nutrition 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 235000020995 raw meat Nutrition 0.000 description 2
- QCVGEOXPDFCNHA-UHFFFAOYSA-N 5,5-dimethyl-2,4-dioxo-1,3-oxazolidine-3-carboxamide Chemical compound CC1(C)OC(=O)N(C(N)=O)C1=O QCVGEOXPDFCNHA-UHFFFAOYSA-N 0.000 description 1
- 235000017166 Bambusa arundinacea Nutrition 0.000 description 1
- 235000017491 Bambusa tulda Nutrition 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 206010013911 Dysgeusia Diseases 0.000 description 1
- 108010071289 Factor XIII Proteins 0.000 description 1
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
- 108010070551 Meat Proteins Proteins 0.000 description 1
- 244000082204 Phyllostachys viridis Species 0.000 description 1
- 235000015334 Phyllostachys viridis Nutrition 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 241000269851 Sarda sarda Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108010073771 Soybean Proteins Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 229940098113 Transglutaminase inhibitor Drugs 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 108010046377 Whey Proteins Proteins 0.000 description 1
- 102000007544 Whey Proteins Human genes 0.000 description 1
- 244000273928 Zingiber officinale Species 0.000 description 1
- 235000006886 Zingiber officinale Nutrition 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 238000005054 agglomeration Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 239000011425 bamboo Substances 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000007598 dipping method Methods 0.000 description 1
- 235000014103 egg white Nutrition 0.000 description 1
- 210000000969 egg white Anatomy 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 229940012444 factor xiii Drugs 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 235000008397 ginger Nutrition 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 150000004698 iron complex Chemical class 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 235000015277 pork Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 235000013580 sausages Nutrition 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 229940001941 soy protein Drugs 0.000 description 1
- 238000005507 spraying Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 125000003396 thiol group Chemical class [H]S* 0.000 description 1
- 238000006276 transfer reaction 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
- 235000021119 whey protein Nutrition 0.000 description 1
Landscapes
- Fish Paste Products (AREA)
- Meat, Egg Or Seafood Products (AREA)
Abstract
Description
【0001】[0001]
【発明の属する技術分野】本発明は、魚肉又は畜肉を主
原料とし、この主原料にトランスグルタミナーゼ及びプ
ロテアーゼインヒビターを添加し、油中で当該酵素反応
を行うことを特徴とする魚肉、畜肉練り製品の製造法に
関する。TECHNICAL FIELD The present invention relates to a fish meat or a meat-paste product characterized by using fish meat or livestock meat as a main raw material, adding transglutaminase and protease inhibitor to the main raw material, and carrying out the enzyme reaction in oil. Regarding manufacturing method.
【0002】[0002]
【従来の技術】蒲鉾に代表される水産練り製品の一般的
な製造法には、原料魚肉の解砕、荒摺り、塩摺り、本摺
り、成形、加工等の工程が取られ、成形後坐り工程を取
ることが一般的である。水産練り製品の内でも、揚げ蒲
の場合は、この坐り工程がないために、製品としては弾
力に欠けるものが多く、その後の加工処理(例えば、お
でん、レトルト品)などすると、全く弾力を失い、本来
の食感とはまったく異なるものとなってしまうという大
きな問題がある。この欠点を解消する為に、それ自体が
ゲル化するような弾力付与素材(大豆蛋白、小麦蛋白、
卵白など)を使用する場合があるが、最終製品が風味が
悪かったり、又魚肉本来の食感からかけ離れたものとな
ってしまうなどの別の問題が生じる。2. Description of the Related Art A general method for manufacturing a fish paste product represented by Kamaboko includes the steps of crushing raw fish meat, rough shaving, salting, main shaving, molding, processing, etc. It is common to take Among the fish paste products, in the case of deep-fried garnish, there is no sitting process, so many products lack elasticity, and subsequent processing (e.g. oden, retort products) loses elasticity at all, There is a big problem that it will be completely different from the original texture. In order to eliminate this drawback, the elasticity imparting material (soy protein, wheat protein,
Egg white etc.) may be used, but another problem occurs such that the final product has a bad taste or becomes far from the original texture of fish meat.
【0003】一方、ハンバーグ、ミートボールなどの畜
肉練り製品の製造法は、原料畜肉のミンチ、塩摺り、本
摺り、成形、加熱等の工程がとられる。しかし、この場
合も揚げ蒲と同様、ハンバーグ、ミートボールなどでは
成形後時間をおかずに、そのままフライヤーや蒸し器に
入れられ加熱調理される。従って、このようなハンバー
グ、ミートボールなどに於いては、上述したような揚げ
蒲と同じような問題を抱えている。On the other hand, the method for producing a kneaded meat product such as hamburger steak and meatballs involves the steps of mincing raw meat, salting, main-slicing, molding, heating and the like. However, in this case as well, like fried garlic, hamburgers, meatballs, etc. are put in a fryer or steamer as they are and cooked without any time after molding. Therefore, such hamburgers, meatballs and the like have the same problems as the above-mentioned fried sardines.
【0004】一方、トランスグルタミナーゼを添加し
て、畜肉及び水産練り製品を製造する方法は以前から報
告されており(特開平2ー186961号、特開平3ー
175929号、特開平4ー267219号等参照)、
これにより従来にない弾力性に富み、加熱処理にも耐性
のある練り製品を製造することが可能となっていた。On the other hand, a method for producing livestock meat and fish paste products by adding transglutaminase has been previously reported (see JP-A-2-186961, JP-A-3-175929, JP-A-4-267219, etc.). ),
As a result, it has become possible to produce a kneaded product that is rich in elasticity and is resistant to heat treatment, which has never been achieved.
【0005】しかし、従来揚げ蒲、ハンバーグ、ミート
ボールのような酵素反応工程を充分取れない水産又は畜
肉練り製品へのトランスグルタミナーゼの利用は、酵素
反応時間が充分取れない為に、充分な効果が得られない
ことが多かった。もちろん、酵素(トランスグルタミナ
ーゼ)反応時間を充分取れるように製造プロセスを少し
変更できれば上記課題はある程度解決できる訳である
が、連続的な装置を使用する場合はラインが長くなり広
いスペースが必要となる、又、非連続式装置を使用する
場合でも加熱装置を新たに必要とする等の理由により、
製造プロセスの変更はなかなか困難であるのが現状であ
る。[0005] However, the use of transglutaminase in marine products or meat-paste products such as deep-fried garnish, hamburger steak and meatballs, which does not have a sufficient enzymatic reaction step, has a sufficient effect because the enzymatic reaction time cannot be sufficiently obtained. I couldn't do much. Of course, if the manufacturing process can be slightly changed so that the enzyme (transglutaminase) reaction time can be taken sufficiently, the above problems can be solved to some extent, but if a continuous device is used, the line becomes long and a wide space is required. Also, even when using a non-continuous type device, because of the need for a new heating device,
At present, it is difficult to change the manufacturing process.
【0006】[0006]
【本発明が解決しようとする課題】従って、本発明の目
的は揚げ蒲、ミートボール等のトランスグルタミナーゼ
反応時間を十分取れない水産、畜肉練り製品に、弾力性
を与え、更には、その後のレトルト処理に代表される過
激な加熱処理に対しても弾力性を失わない技術の提供で
ある。Therefore, the object of the present invention is to impart elasticity to marine products and meat-paste products such as deep-fried flesh and meatballs that do not have sufficient transglutaminase reaction time, and further to carry out the subsequent retort treatment. It is the provision of technology that does not lose elasticity even with the extreme heat treatment represented by.
【0007】[0007]
【課題を解決するための手段】本発明者等は上記課題を
解決する為に鋭意検討を重ねた結果、水産又は畜肉練り
製品の製造工程において主原料である魚肉又は畜肉にト
ランスグルタミナーゼ及びプロテアーゼインヒビターを
添加し、油中で酵素反応を行うことにより弾力を増強さ
せ、その後の加工処理にも耐性のある練り製品を得られ
ることを見い出し、本発明を完成するに至らしめた。Means for Solving the Problems As a result of intensive studies to solve the above-mentioned problems, the present inventors have found that transglutaminase and protease inhibitors are added to fish meat or livestock meat which is a main raw material in the production process of marine products or meat products. The inventors have found that a kneaded product which is added and undergoes an enzymatic reaction in oil to enhance elasticity, and which is resistant to the subsequent processing, can be obtained, and the present invention has been completed.
【0008】即ち、本発明は、主原料である魚肉又は畜
肉にトランスグルタミナーゼ及びプロテアーゼインヒビ
ターを添加し、油中で当該酵素反応を行うことを特徴と
する水産又は畜肉練り製品の製造法に関する。That is, the present invention relates to a method for producing a marine product or a meat paste product, which comprises adding transglutaminase and a protease inhibitor to fish or livestock meat which is a main raw material and carrying out the enzyme reaction in oil.
【0009】[0009]
【発明の実施の形態】以下に本発明を詳細に説明する。
本発明は揚げ蒲、竹輪、蒲鉾等の全ての水産練り製品及
びハンバーグ、ミートボール、ソーセージ等の全ての畜
肉練り製品に使用可能であるが、通常はトランスグルタ
ミナーゼ反応工程を充分取れない、揚げ蒲等の水産練り
製品 、ハンバーグ、ミートボール等の畜肉練り製品、
及びこれらのレトルト製品の製造に取り分け有効であ
る。DESCRIPTION OF THE PREFERRED EMBODIMENTS The present invention will be described below in detail.
The present invention can be used for all fish paste products such as fried bonito, bamboo rings, and kamaboko, and for all meat paste products such as hamburger steak, meatballs, sausages, etc. Fish paste products, live meat products such as hamburgers and meatballs,
And is particularly effective in the manufacture of these retort products.
【0010】本発明の特徴は水産又は畜肉練り製品の製
造工程に於いて主原料である魚肉又は畜肉にトランスグ
ルタミナーゼ及びプロテアーゼインヒビターを添加し、
油中で当該酵素反応を行わせることにある。A feature of the present invention is that transglutaminase and protease inhibitors are added to fish meat or livestock meat which is a main raw material in the production process of marine products or meat paste products,
The purpose is to carry out the enzyme reaction in oil.
【0011】さて、トランスグルタミナーゼの添加時期
は特に制限は無いが、通常、水産練り製品及び畜肉練り
製品とも塩摺り工程後に行えば良い。The timing of adding transglutaminase is not particularly limited, but usually, it may be carried out after the salting step for both the fish paste product and the meat paste product.
【0012】トランスグルタミナーゼの添加量は特に制
限は無いが、通常、原料魚肉又は畜肉摺り身1g当たり
0.05〜30ユニット、好ましくは0.1〜10ユニッ
トである。尚、0.05ユニット以下では該酵素を添加
した効果が発揮できず、又30ユニット以上では魚肉又
は畜肉蛋白が凝集化現象を示し、離水しやすくなり、最
終製品である揚げ蒲、ハンバーグ等の練り肉品から弾
力、しなやかさを奪うことになり好ましくない。The amount of transglutaminase added is not particularly limited, but is usually 0.05 to 30 units, preferably 0.1 to 10 units per gram of raw fish meat or ground meat. If the amount of the enzyme is less than 0.05 unit, the effect of adding the enzyme cannot be exhibited, and if it is more than 30 unit, the fish meat or animal meat protein shows an agglomeration phenomenon, which facilitates water separation, and the final product such as fried ginger and hamburger. It is not preferable because it will lose elasticity and suppleness from the meat product.
【0013】トランスグルタミナーゼを作用せしめる条
件、即ち坐りに相当する油中での加熱条件は、通常トラ
ンスグルタミナーゼ反応温度の範囲である約30〜約1
00℃で行えば良い。又、作用時間は温度によって異な
るが、通常約30秒〜約2時間程度である。尚、この条
件は一応の目安であり、これを厳守しなければならない
訳ではない。水中で加熱を行うことも可能であるが、水
中加熱を行った場合は、作用時間によっても異なるが水
溶性の調味成分の溶出がみられる。これに伴い、最終製
品として味覚的に薄味になったり、揚げ色が薄くなる。
従って油中加熱を行う方が好ましい。The conditions that allow transglutaminase to act, that is, the heating conditions in oil corresponding to sitting are usually about 30 to about 1 which is the range of the transglutaminase reaction temperature.
It may be carried out at 00 ° C. The working time is usually about 30 seconds to about 2 hours, although it depends on the temperature. It should be noted that this condition is a tentative standard, and it is not necessary to strictly observe it. Although it is possible to perform heating in water, when heating in water, elution of water-soluble seasoning components is observed, although it varies depending on the action time. Along with this, the final product has a lighter taste and a deeper fried color.
Therefore, heating in oil is preferable.
【0014】従って、油中に浸漬することにより加熱す
ることが最も酵素反応の効果を発揮させれる。しかし、
浸漬法以外にも加温された油を当該食品の表面にスプレ
ー、シャワーなどの方法による噴霧することによって
も、ある程度の効果を得ることもできる。Therefore, the most effective enzymatic reaction can be obtained by heating by immersing in oil. But,
In addition to the dipping method, the heated oil may be sprayed onto the surface of the food product by a method such as spraying or showering to obtain a certain effect.
【0015】また、プロテアーゼインヒビターの添加時
期は特に制限は無いが、通常、水産練り製品及び畜肉練
り製品とも塩摺り工程後に行えば良い。尚、プロテアー
ゼインヒビターはトランスグルタミナーゼと同時に添加
してもよく、又時間をづらして添加しても良い。The timing of addition of the protease inhibitor is not particularly limited, but normally, it may be carried out after the salting step for both the fish paste product and the meat paste product. The protease inhibitor may be added at the same time as transglutaminase, or may be added over a period of time.
【0016】また、プロテアーゼインヒビターの添加量
も特に制限は無いが、通常、原料魚肉又は畜肉摺り身1
g当たり、0.1mg〜20mgである。尚、プロテア
ーゼインヒビターの役割は、原料魚肉又は畜肉摺り身中
に存在するプロテアーゼが30℃〜100℃、特に60
℃付近で原料肉に働き、揚げ蒲又はミートボールなどの
製品の弾力を落とす現象(通常、水産業界では”戻り”
と言われる)を防止するために加えるのである。The amount of the protease inhibitor added is not particularly limited, but usually raw fish meat or live meat surimi 1
It is 0.1 mg to 20 mg per g. The role of the protease inhibitor is that protease present in raw fish meat or ground meat is 30 ° C to 100 ° C, especially 60 ° C.
Phenomenon that acts on raw meat near ℃ and reduces the elasticity of products such as fried garnish or meatballs (usually "return" in the fisheries industry)
Is said to be added).
【0017】本発明に於いて用いられるトランスグルタ
ミナーゼとしては、カルシウム非依存性のものとカルシ
ウム依存性のものとがある。前者の例としては、ストレ
プトベルチシリウム属などに属する微生物由来のもの
(例えば、特開平1−27471号参照)を挙げること
ができる。後者の例としては、モルモット肝臓由来のも
の(特公平1−50382号参照)、魚由来のもの(例
えば、関信夫、日本水産学会誌第5巻、第1号125ー
132頁、1990年参照)、血液中の存在するもの
(Factor XIIIとも称せられる)等をあげることができ
る。この他、遺伝子組換えにより製造されるもの(例え
ば、特開平1−300889号、特開平5ー19988
3号、特開平6−225775号参照)等も用いること
ができる。The transglutaminase used in the present invention includes calcium-independent ones and calcium-dependent ones. Examples of the former include those derived from microorganisms belonging to the genus Streptoverticillium (see, for example, JP-A-1-27471). Examples of the latter include those derived from guinea pig liver (see Japanese Patent Publication No. 1-50382) and those derived from fish (see, for example, Nobuo Seki, Journal of Japan Fisheries Society, Vol. 5, No. 1, pages 125-132, 1990). ), Those present in blood (also called Factor XIII), and the like. In addition to these, those produced by gene recombination (for example, Japanese Patent Laid-Open Nos. 1-300889 and 5-19988).
No. 3, JP-A-6-225775) and the like can also be used.
【0018】本発明において、これらいずれのトランス
グルタミナーゼでも用いることができ、起源および製法
に制限されるものではない。但し、機能性及び経済性の
点から、カルシウム非依存性のものが好ましい。例え
ば、上述の微生物由来のトランスグルタミナーゼ(前掲
特開平1−27471号参照)はいずれの条件も満足す
るものであり、現時点では最適と言えであろう。In the present invention, any of these transglutaminases can be used and is not limited to the origin and production method. However, from the viewpoint of functionality and economy, calcium-independent ones are preferable. For example, the above-mentioned microbial-derived transglutaminase (see Japanese Patent Laid-Open No. 1-27471 cited above) satisfies all the conditions, and can be said to be optimal at the present time.
【0019】プロテアーゼインヒビターとしては、セリ
ン系プロテアーゼ及びチオール系プロテアーゼなどのイ
ンヒビターが代表的である。本発明に用いるプロテアー
ゼインヒビターは、食品用として使用できるものであれ
ば特に種類を限定するものではない。また、純品なプロ
テアーゼインヒビター以外に、プロテアーゼインヒビタ
ーを多く含有するもの等も用いられる。本発明に於いて
用いられるプロテアーゼインヒビターとしては、例え
ば、卵白由来のオボムコイド、ホエー蛋白、プラズマ蛋
白等を用いることができる。Typical protease inhibitors are inhibitors such as serine-based proteases and thiol-based proteases. The protease inhibitor used in the present invention is not particularly limited as long as it can be used for food. In addition to pure protease inhibitors, those containing a large amount of protease inhibitors may also be used. As the protease inhibitor used in the present invention, for example, ovomucoid derived from egg white, whey protein, plasma protein and the like can be used.
【0020】さて、トランスグルタミナーゼ反応後、当
該トランスグルタミナーゼを加熱失活させる必要があ
る。この加熱による失活は通常、油中加熱、水中加熱、
フライパン上での直接加熱等により達成される。After the transglutaminase reaction, it is necessary to inactivate the transglutaminase by heating. Deactivation due to this heating is usually done in oil, underwater,
It is achieved by direct heating on a frying pan.
【0021】次に、トランスグルタミナーゼ及びプロテ
アーゼインヒビターを用いる本発明のスケトウダラを用
いた例で以下に簡単に説明することにする。Next, an example using the pollock of the present invention which uses a transglutaminase and a protease inhibitor will be briefly described below.
【0022】スケトウタラ等の冷凍摺り身(C級)を解
凍する。次に、例えばフードカッターに入れ、軽く1分
程度荒摺りをする。その後、摺り身に対して少量の食塩
及び氷水を約40〜100%加え、混合する。次いで、
トランスグルタミナーゼとプロテアーゼインヒビター、
必要に応じて澱粉、調味料等を加え混合する。これらの
混合処理は、最終製品の食感維持のためには常に15℃
以下、好ましくは10℃以下で行うのが好ましい。Thaw frozen surimi (class C) such as walleye pollack. Next, for example, it is put in a hood cutter and lightly rubbed for about 1 minute. Then, a small amount of salt and ice water are added to the surimi and the mixture is mixed at about 40 to 100%. Then
Transglutaminase and protease inhibitors,
Add starch, seasoning, etc., if necessary, and mix. These mixing treatments are always performed at 15 ° C to maintain the texture of the final product.
Hereafter, it is preferably carried out at 10 ° C. or lower.
【0023】この生地を目的に応じて成形加工する。得
られた生成物を油中に導入し、坐りを行う。この間にト
ランスグルタミナーゼを作用させる訳である。酵素反応
条件は上述したように、通常約30〜約100℃の範囲
で行えば良い。又、酵素反応を行わせる時間は温度によ
って異なるが、通常約30秒〜約2時間である。また、
連続式の揚げ機を用いる場合は、初温を上記温度範囲に
設定し、本加熱時に揚げ処理を行うような操作をすれば
よい。The dough is molded according to the purpose. The product obtained is introduced into oil and sitting is carried out. During this period, transglutaminase is allowed to act. As described above, the enzyme reaction condition may be usually in the range of about 30 to about 100 ° C. The time for carrying out the enzyme reaction varies depending on the temperature, but is usually about 30 seconds to about 2 hours. Also,
When a continuous frying machine is used, the initial temperature may be set in the above temperature range and the frying treatment may be performed during the main heating.
【0024】酵素反応工程後、トランスグルタミナーゼ
を失活させる為に加熱する。加熱処理条件は、揚げ蒲で
あればフライヤー中約160ー180℃で約1ー10分
程度等である。上記加熱処理条件は一つ目安であり、成
形品のサイズによって適宜定めればよい。いずれにして
もトランスグルタミナーゼが失活すれば足りるのであ
る。After the enzymatic reaction step, heating is performed to inactivate transglutaminase. As for the heat treatment condition, if it is deep fried, the temperature is about 160 to 180 ° C. for about 1 to 10 minutes in a fryer. The above heat treatment conditions are one guide and may be appropriately determined depending on the size of the molded product. In any case, deactivation of transglutaminase is sufficient.
【0025】念の為に申し述べるが、トランスグルタミ
ナーゼとはペプチド鎖内にあるグルタミン残基のγーカ
ルボキシアミド基のアシル移転反応を触媒する酵素であ
る。このトランスグルタミナーゼはアシル受容体として
タンパク質中のεーアミノ基が反応すると、タンパク質
分子内又は分子間に於いて、εー(γーGlu)ーLy
s架橋結合(以下、GーL結合と略する)が形成され
る。また、水がアシル受容体として機能するときは、グ
ルタミン残基が脱アミド化されてグルタミン酸残基にな
る反応を進行させる酵素である。As a reminder, transglutaminase is an enzyme that catalyzes the acyl transfer reaction of the γ-carboxamide group of the glutamine residue in the peptide chain. This transglutaminase acts as an acyl acceptor when the ε-amino group in the protein reacts with ε- (γ-Glu) -Ly within or between protein molecules.
An s-crosslinking bond (hereinafter abbreviated as GL bond) is formed. When water functions as an acyl acceptor, it is an enzyme that promotes a reaction in which a glutamine residue is deamidated to become a glutamic acid residue.
【0026】尚、本発明でいうトランスグルタミナーゼ
の活性単位は、次のようなハイドロキサメート法により
測定され、かつ定義される。即ち、ベンジルオキシカル
ボニル−L−グルタミルグリシンとヒドロキシルアミン
を基質として反応を行い、生成したヒドロキサム酸をト
リクロロ酢酸存在下で鉄錯体を形成させた後、525n
mの吸光度を測定し、ヒドロキサム酸の量を検量線より
求め、活性を算出する(前掲特開平1−27471公報
参照)。The activity unit of transglutaminase referred to in the present invention is measured and defined by the following hydroxamate method. That is, benzyloxycarbonyl-L-glutamylglycine is reacted with hydroxylamine as a substrate to form the hydroxamic acid produced in the presence of trichloroacetic acid to form an iron complex.
The absorbance of m is measured, the amount of hydroxamic acid is determined from a calibration curve, and the activity is calculated (see the above-mentioned JP-A-1-27471).
【0027】[0027]
【実施例】以下、本発明を実施例に従って説明する。本
発明の技術的範囲は、もちろん下記の実施例によって限
定されるものではない。なお、実施例中の部は特に拘ら
ない限り重量部の略記である。DESCRIPTION OF THE PREFERRED EMBODIMENTS The present invention will be described below with reference to embodiments. The technical scope of the present invention is of course not limited by the examples below. The parts in the examples are abbreviated to weight parts unless otherwise specified.
【0028】(実施例1)市販C級スケトウタラ冷凍摺
り身を500部解砕後、解凍した。これに氷水200
部、食塩3部、澱粉5部、みりん1部、調味料等2部、
トランスグルタミナーゼ0.5部(魚肉擂り身1g当た
り0.1ユニット添加したことになる)及びプロテアー
ゼインヒビター(協同乳業社製(商品名:P−WP
C))0.5部を添加、混合後、成形した。次に、60
℃で15分間油中で酵素反応工程をとった。その後、1
70℃で5分間加熱して揚げ蒲を調製した。この170
℃、5分間の加熱によりトランスグルタミナーゼは失活
した。尚、60℃、15分の酵素反応工程を取らない以
外は、全く同じ方法で調製したものをコントロールとし
た。Example 1 Commercially available C-class Alaska pollack frozen ground meat was crushed and then thawed. 200 ice water
Part, salt 3 parts, starch 5 parts, mirin 1 part, seasoning 2 parts,
0.5 parts of transglutaminase (which means that 0.1 unit was added per 1 g of fish meat) and protease inhibitor (manufactured by Kyodo Daigaku Co., Ltd. (trade name: P-WP
C)) 0.5 part was added, mixed and molded. Next, 60
The enzymatic reaction step was taken in oil for 15 minutes at ° C. Then 1
It was heated at 70 ° C. for 5 minutes to prepare fried garlic. This 170
The transglutaminase was inactivated by heating at 5 ° C for 5 minutes. A control was made by the same method except that the enzyme reaction step at 60 ° C. for 15 minutes was not performed.
【0029】本製品及びコントロールを訓練された10
名の専門パネルによる官能検査に供し、弾力性、しなや
かさ、風味の好ましさ、食感の好ましさを評価した。
尚、官能評価はそれぞれの項目を10点満点で評価し、
10人のパネルの平均点を表示した。0点はそれぞれ、
「弾力がない」、「しなやかでない」、「風味が好まし
くない」及び「食感が好ましくない」を示す。又、10
点は「弾力がある」、「しなやかである」、「風味が好
ましい」及び「食感が好ましい」を示す。5点は「ふつ
う」を意味する。10 trained in this product and controls
It was subjected to a sensory test by a specialist panel of the name, and evaluated for elasticity, suppleness, preference of flavor, and preference of texture.
In addition, sensory evaluation evaluates each item with a maximum of 10 points,
The average score of the panel of 10 people was displayed. 0 points are
"Not elastic", "not supple", "unfavorable flavor" and "unfavorable texture" are shown. Also, 10
The points indicate “elastic”, “supple”, “preferable flavor” and “preferable texture”. Five points means "normal".
【0030】また、本製品及びコントロールを冷却し、
品温25℃としてからレオメータを用いて破断強度(g
/cm2)及び凹み(mm)を測定した。破断強度の数
値が高い程弾力があり、凹みの数値が高い程しなやかと
言える。In addition, the product and the control are cooled,
Breaking strength (g
/ Cm 2 ) and the depression (mm) were measured. It can be said that the higher the value of the breaking strength is, the more the elasticity is, and the higher the value of the dent is, the more supple.
【0031】破断強度、凹み及び官能評価の測定結果は
表1に示した。尚、表1中「風味」とは「風味の好まし
さ」、「食感」とは「食感の好ましさ」のことである。The measurement results of breaking strength, dent and sensory evaluation are shown in Table 1. In Table 1, "flavor" means "flavor preference" and "texture" means "texture preference".
【0032】[0032]
【表1】 [Table 1]
【0033】(実施例2)市販C級スケトウタラ冷凍摺
り身を500部解砕後、解凍した。これに氷水200
部、食塩3部、澱粉5部、みりん1部、調味料等2部、
トランスグルタミナーゼ0.5部(魚肉擂り身1g当た
り0.1ユニット添加したことになる)及びプロテアー
ゼインヒビター(太陽化学社製(商品名:オボムコイ
ド))0.5部を添加、混合した。その後、成形し、次
に60℃、15分油中で酵素反応工程を取った。次に、
170℃で5分間加熱して揚げ蒲を調製した。この17
0℃、5分間の加熱によりトランスグルタミナーゼを失
活させた。尚、60℃、15分の酵素反応工程を取る以
外は、全く同じ方法で調製したものをコントロールとし
た。Example 2 500 parts of a commercially available C-class walleye pollack frozen surimi was crushed and then thawed. 200 ice water
Part, salt 3 parts, starch 5 parts, mirin 1 part, seasoning 2 parts,
0.5 parts of transglutaminase (which means that 0.1 unit was added per 1 g of grated fish meat) and 0.5 parts of protease inhibitor (Taiyo Kagaku Co., Ltd. (trade name: ovomucoid)) were added and mixed. After that, it was molded and then subjected to an enzymatic reaction step in oil at 60 ° C. for 15 minutes. next,
It was heated at 170 ° C. for 5 minutes to prepare fried kamabushi. This 17
The transglutaminase was inactivated by heating at 0 ° C. for 5 minutes. A control was made by the same method except that the enzyme reaction step was performed at 60 ° C. for 15 minutes.
【0034】実施例1と同じように、本製品及びコント
ロールを訓練された10名の専門パネルによる官能検査
に供し、弾力性、しなやかさ、風味の好ましさ、食感の
好ましさを評価した。また、実施例1と同様に破断強度
及び凹みを測定した。尚、官能評価、破断強度及び凹み
の測定結果を表2に示した。評価基準は実施例1と同様
である。In the same manner as in Example 1, the product and the control were subjected to a sensory test by 10 trained specialized panels to evaluate the elasticity, suppleness, taste preference, and mouthfeel preference. did. Further, the breaking strength and the depression were measured in the same manner as in Example 1. Table 2 shows the results of sensory evaluation, breaking strength and dent measurement. The evaluation criteria are the same as in Example 1.
【0035】[0035]
【表2】 [Table 2]
【0036】(実施例3)市販豚もも肉を500部解砕
後、氷水200部、食塩3部、澱粉5部、調味料等2
部、トランスグルタミナーゼ0.5部(畜肉摺り身1g
当たり0.1ユニット添加したことになる)及びプロテ
アーゼインヒビターとして牛血漿粉末((太陽化学社
製:商品名フィッシュアップB))0.2部を添加、混
合した。その後、成形し、次に40℃で15分油中で酵
素反応工程を取った。反応終了後、フライパンで加熱し
ハンバーグを調製した。この加熱によりトランスグルタ
ミナーゼを失活させた。尚、40℃で30分の酵素反応
工程を取る以外は、全く同じ方法で調製したものをコン
トロールとした。(Example 3) After crushing 500 parts of commercially available pork leg meat, 200 parts of ice water, 3 parts of salt, 5 parts of starch, seasoning, etc. 2
Part, transglutaminase 0.5 part (meat surimi 1g
0.1 unit per 1 unit) and 0.2 part of bovine plasma powder (Taiyo Kagaku Co., Ltd .: trade name Fish Up B) as a protease inhibitor were added and mixed. Then, it was molded and then subjected to an enzymatic reaction step in oil at 40 ° C. for 15 minutes. After completion of the reaction, hamburger was prepared by heating in a frying pan. This heating deactivated the transglutaminase. A control was made by the same method except that the enzyme reaction step was performed at 40 ° C. for 30 minutes.
【0037】実施例1と同じように、本製品及びコント
ロールを訓練された10名の専門パネルによる官能検査
に供し、弾力性、ジューシー感、風味の好ましさ、食感
の好ましさを評価した。また、実施例1と同様に破断強
度及び凹みを測定した。官能評価、破断強度及び凹みの
測定結果を表3に示した。評価基準は実施例1と同様で
ある。In the same manner as in Example 1, the product and the control were subjected to a sensory test by 10 trained specialized panels, and the elasticity, juiciness, taste preference, and texture preference were evaluated. did. Further, the breaking strength and the depression were measured in the same manner as in Example 1. Table 3 shows the results of sensory evaluation, breaking strength and dent measurement. The evaluation criteria are the same as in Example 1.
【0038】[0038]
【表3】 [Table 3]
【0039】更に、本発明品をレトルト処理に供して
も、弾力性、ジューシー感は維持され、又風味及び食感
の好ましさも維持されていた。Further, even when the product of the present invention was subjected to the retort treatment, the elasticity and juiciness were maintained, and the flavor and texture were also favorably maintained.
【0040】(参考例)市販SA級ミナミタラ冷凍摺り
身を500部解砕後、解凍した。これに氷水100部、
食塩3部、澱粉5部、みりん1部、調味料等2部、トラ
ンスグルタミナーゼ0.5部(これは魚肉擂り身1g当
たり 0.1ユニット添加したことになる)及びプロテ
アーゼインヒビター(協同乳業社製(商品名:P−WP
C))0.5部を添加し、混合後、成形し50℃で10
分間油中で酵素反応工程を行った。その後、170℃で
5分間加熱して揚げ蒲を調製した。この170℃、5分
間加熱によりトランスグルタミナーゼは失活した。これ
を本発明品とした。Reference Example: Commercially available SA grade Minami Tara frozen surimi was crushed for 500 parts and then thawed. 100 parts of ice water,
3 parts of salt, 5 parts of starch, 1 part of mirin, 2 parts of seasoning, etc., 0.5 parts of transglutaminase (this means that 0.1 unit was added per 1 g of fish paste) and a protease inhibitor (manufactured by Kyodo Dairy Co., Ltd.). (Product name: P-WP
C)) 0.5 part was added, mixed, and molded to obtain 10 at 50 ° C.
The enzymatic reaction step was performed in oil for minutes. Then, it was heated at 170 ° C. for 5 minutes to prepare fried garlic. The transglutaminase was inactivated by heating at 170 ° C. for 5 minutes. This was designated as the product of the present invention.
【0041】一方、プロテアーゼインヒビターを添加し
ない以外、全く同様に調製した揚げ蒲をコントロール1
とした。また、プロテアーゼインヒビターを添加せず、
かつ酵素反応工程を取らない以外は全く同様に調製した
揚げ蒲をコントロール2とした。更に、トランスグルタ
ミナーゼを添加しない以外は全く同様に調製した揚げ蒲
をコントロール3とした。On the other hand, the fried sardines prepared in the same manner except that no protease inhibitor was added were used as control 1
And Also, without adding protease inhibitors,
In addition, the fried garlic prepared in exactly the same manner as the control 2 except that the enzyme reaction step was not taken. Further, fried sardines prepared in exactly the same manner as above except that transglutaminase was not added was used as Control 3.
【0042】本発明品及びコントロール1、2、3をそ
れぞれ10名の専門パネルによる官能検査に供し、弾
力、しなやかさ、風味の好ましさ、食感の好ましさを評
価した。その結果を表4に示した。尚、評価基準は 実
施例1と同様である。The product of the present invention and Controls 1, 2 and 3 were each subjected to a sensory test by a panel of 10 persons, and the elasticity, suppleness, taste preference, and texture preference were evaluated. The results are shown in Table 4. The evaluation criteria are the same as in Example 1.
【0043】[0043]
【表4】 [Table 4]
【0044】表4の結果から、分かるように本発明品が
最も好まれた。また、プロテアーゼインヒビターを添加
しなくとも充分酵素反応(トランスグルタミナーゼ反
応)時間を取ったもの(コントロール1)は本発明品の
次に好まれた。更に、トランスグルタミナーゼを添加し
たが充分反応時間を取らなかったもの(コントロール
2)は、効果が認められるが充分では無かった。As can be seen from the results in Table 4, the product of the present invention was most preferred. Also, a product (Control 1), which took sufficient time for enzymatic reaction (transglutaminase reaction) without adding a protease inhibitor, was preferred next to the product of the present invention. Further, the one in which transglutaminase was added but the reaction time was not sufficient (control 2) showed the effect, but it was not sufficient.
【0045】[0045]
【発明の効果】主原料である魚肉又は畜肉にトランスグ
ルタミナーゼ及びプロテアーゼインヒビターを添加し
て、油中で当該酵素反応を行うことにより得られる水産
又は畜肉練り製品は、従来品に比べて弾力性、しなやか
さ、ジューシー感、風味、食感とも極めて良好であっ
た。また、その後にレトルト処理を行っても弾力、しな
やかさ等の効果は全く低減しないものであった。EFFECT OF THE INVENTION A fish or meat paste product obtained by adding a transglutaminase and a protease inhibitor to fish or livestock meat which is a main raw material and carrying out the enzyme reaction in oil is more elastic and supple than conventional products. The juiciness, flavor and texture were extremely good. Further, even if the retort treatment is performed thereafter, the effects such as elasticity and suppleness are not reduced at all.
Claims (3)
ルタミナーゼ及びプロテアーゼインヒビターを添加し、
油中で当該酵素反応を行うことを特徴とする水産又は畜
肉練り製品の製造法。1. A transglutaminase and a protease inhibitor are added to fish or livestock meat which is a main raw material,
A method for producing a fish or meat paste product, which comprises carrying out the enzyme reaction in oil.
る請求項1記載の製造法。2. The method according to claim 1, wherein the temperature in the oil is about 30 ° C. to about 100 ° C.
ーグ、ミートボール又はそれらのレトルト処理品である
請求項1記載の製造法。3. The method according to claim 1, wherein the fish or meat paste product is a fried garlic, a hamburger, a meatball or a retort processed product thereof.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP8115900A JPH09299065A (en) | 1996-05-10 | 1996-05-10 | Production of fish-paste product of fish meat and animal meat |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP8115900A JPH09299065A (en) | 1996-05-10 | 1996-05-10 | Production of fish-paste product of fish meat and animal meat |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH09299065A true JPH09299065A (en) | 1997-11-25 |
Family
ID=14673992
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP8115900A Pending JPH09299065A (en) | 1996-05-10 | 1996-05-10 | Production of fish-paste product of fish meat and animal meat |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH09299065A (en) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1084621A3 (en) * | 1999-09-17 | 2001-04-25 | Ajinomoto Co., Inc. | Salting agent for food processing |
| WO2001062888A3 (en) * | 2000-02-23 | 2002-01-31 | Lever Hindustan Ltd | Improved composition of marine product |
| WO2007026922A1 (en) * | 2005-08-30 | 2007-03-08 | Ajinomoto Co., Inc. | Method for preparation of transglutaminase-containing matter having reduced protease activity |
| WO2007026921A1 (en) * | 2005-08-30 | 2007-03-08 | Ajinomoto Co., Inc. | Method for determination of protease activity in transglutaminase-containing matter and adhesive transglutaminase preparation |
| CN110754623A (en) * | 2019-11-07 | 2020-02-07 | 肖鸿章 | Mutton balls and preparation method thereof |
-
1996
- 1996-05-10 JP JP8115900A patent/JPH09299065A/en active Pending
Cited By (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1084621A3 (en) * | 1999-09-17 | 2001-04-25 | Ajinomoto Co., Inc. | Salting agent for food processing |
| US6770310B1 (en) | 1999-09-17 | 2004-08-03 | Ajinomoto Co., Inc. | Pickle solution including transglutaminese, method of making and method of using |
| WO2001062888A3 (en) * | 2000-02-23 | 2002-01-31 | Lever Hindustan Ltd | Improved composition of marine product |
| WO2007026922A1 (en) * | 2005-08-30 | 2007-03-08 | Ajinomoto Co., Inc. | Method for preparation of transglutaminase-containing matter having reduced protease activity |
| WO2007026921A1 (en) * | 2005-08-30 | 2007-03-08 | Ajinomoto Co., Inc. | Method for determination of protease activity in transglutaminase-containing matter and adhesive transglutaminase preparation |
| JP4905351B2 (en) * | 2005-08-30 | 2012-03-28 | 味の素株式会社 | Method for producing transglutaminase-containing product with reduced protease activity |
| JP4973496B2 (en) * | 2005-08-30 | 2012-07-11 | 味の素株式会社 | Method for measuring protease activity of transglutaminase-containing substance and transglutaminase preparation for adhesion |
| CN110754623A (en) * | 2019-11-07 | 2020-02-07 | 肖鸿章 | Mutton balls and preparation method thereof |
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