JPH0646799A - Decomposed protein and pickle solution containing it - Google Patents
Decomposed protein and pickle solution containing itInfo
- Publication number
- JPH0646799A JPH0646799A JP4199802A JP19980292A JPH0646799A JP H0646799 A JPH0646799 A JP H0646799A JP 4199802 A JP4199802 A JP 4199802A JP 19980292 A JP19980292 A JP 19980292A JP H0646799 A JPH0646799 A JP H0646799A
- Authority
- JP
- Japan
- Prior art keywords
- soybean protein
- protein
- solution
- elastase
- soybean
- 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
Landscapes
- Meat, Egg Or Seafood Products (AREA)
Abstract
Description
【0001】[0001]
【産業上の利用分野】本発明はピックル液用蛋白分解物
及び蛋白分解物を含有するピックル液に関する。BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a protein degradation product for pickling liquid and a pickling liquid containing the protein degradation product.
【0002】[0002]
【従来技術】大豆蛋白は、従来からその結着性、保水性
等の機能特性や製造コストの低減の為にハム、ソーセー
ジ等の畜肉製品、蒲鉾等の水産練り製品およびその他の
惣菜などに幅広く使用されている。これらの中で、畜肉
製品、特にハム製造の際に大豆蛋白に求められる特性と
しては、最終製品中での結着性、保水性等の物性はもち
ろんのこと、高塩溶性、溶液状態での低粘性である。何
故なら、ハムの製造法は、大豆蛋白を調味液(ピックル
液)の中に加え、このピックル液を原料肉にインジェク
ションする方法が一般的であるからである。この場合通
常の大豆蛋白ではピックル液の粘性が極めて高くなる。
その為、インジェクターに負担がかかることや、高い粘
性の為に生じるピックル液中の泡が肉中に残存し、最終
製品中に空洞が生ずる等の操作性に問題があった。2. Description of the Related Art Soybean protein has been widely used for livestock products such as ham and sausage, fish paste products such as kamaboko, and other prepared foods in order to reduce functional costs such as binding property and water retention and reduction of manufacturing cost. Has been done. Among these, the properties required for soybean protein in the production of meat products, particularly ham, are not only the physical properties such as binding property in the final product, water retention property, but also high salt solubility and solution state. It has low viscosity. This is because the ham is generally produced by adding soybean protein to a seasoning liquid (pickle liquid) and injecting the pickle liquid into raw meat. In this case, the viscosity of the pickle solution becomes extremely high with ordinary soybean protein.
Therefore, there is a problem in operability such as a burden on the injector and bubbles in the pickled liquid caused by the high viscosity remaining in the meat, resulting in voids in the final product.
【0003】そこで、操作性の向上をはかるためにプロ
テアーゼ処理を施し、溶液粘度を低下した大豆蛋白の蛋
白分解物が最近開発されるようになった。しかし、酵素
処理大豆蛋白物は粘度の低下による作業性の向上という
メリットを有するが、大豆蛋白固有のゲル特性の低下、
特に異種蛋白との複合系における物性、保水性の低下と
それに伴う最終製品の歩留まり低下というデメリットを
生じる。Therefore, a proteolytic product of soybean protein has been recently developed which has been treated with a protease in order to improve the operability to reduce the solution viscosity. However, the enzyme-treated soybean protein has the merit of improving workability due to the decrease in viscosity, but the gel characteristic peculiar to soybean protein is deteriorated,
In particular, in the complex system with a heterologous protein, there are disadvantages that the physical properties and water retention are lowered and the yield of the final product is reduced accordingly.
【0004】過去、大豆蛋白の酵素分解に関する研究は
多くなされている。例えば、特開昭51−51552には低変
性脱脂大豆より得た豆乳を90〜150℃で10分〜1秒間加熱
処理し、微生物叉は酵素を作用させ、再度90〜150℃で1
0分〜1秒間加熱処理する方法、特開昭59−166040には、
大豆蛋白質溶液を加熱処理した後、ブロメライン又はパ
パインを作用させて凝乳状とし、乾燥、粉末化する方
法、特開昭62−14796には、植物性蛋白をペニシリウム
属由来の中性及び/又はアルカリ性プロテアーゼを用い
て酵素分解する方法がそれぞれ記載されている。しか
し、これらの目的とするところは、大豆臭の低減や酵素
処理による苦みの低減であり、溶液状態において粘度が
低く、さらには畜肉等の異種蛋白との複合系において優
れた物性を有する大豆蛋白分解物の提供を目指したもの
ではない。[0004] In the past, much research has been done on the enzymatic degradation of soybean proteins. For example, in JP-A-51-51552, soy milk obtained from low-denaturation defatted soybean is heat-treated at 90 to 150 ° C. for 10 minutes to 1 second, and microorganisms or enzymes are allowed to act on the soy milk again at 90 to 150 ° C.
Method of heat treatment for 0 minutes to 1 second, JP-A-59-166040,
After heat treatment of a soybean protein solution, bromelain or papain is allowed to act to form a coagulated state, followed by drying and pulverization. JP-A-62-14796 discloses a vegetable protein derived from Penicillium genus neutral and / or alkaline. Each method of enzymatically degrading with a protease is described. However, the purpose of these is to reduce soybean odor and bitterness due to enzyme treatment, has low viscosity in a solution state, and further has excellent physical properties in a complex system with a heterologous protein such as livestock meat. It is not intended to provide decomposed products.
【0005】[0005]
【発明が解決しようとする課題】通常、酵素処理を施し
た大豆蛋白の蛋白分解物は、溶液状態での粘度は低下す
る。また、これらのゲル物性も低下し、それとともに大
豆蛋白を使用した畜肉製品等の物性低下及び離水増加も
起こる。そこで、本発明者らは塩溶性に優れ、溶液状態
での粘度が低く、かつ畜肉製品等に混入してもその物性
を損なわない大豆蛋白分解物の提供を目的とする。[Problems to be Solved by the Invention] Generally, the proteolytic product of soybean protein treated with an enzyme has a reduced viscosity in a solution state. Further, the physical properties of these gels are also deteriorated, and along with that, the physical properties of livestock products and the like using soybean protein are deteriorated and water separation is increased. Therefore, the present inventors have an object to provide a soybean protein hydrolyzate which is excellent in salt solubility, has a low viscosity in a solution state, and does not impair the physical properties even when mixed in a meat product or the like.
【0006】[0006]
【問題を解決するための手段】本発明者らは、前記課題
を解決すべく使用酵素の選定、反応条件等の検討を種々
行ってきた。しかし、これら検討の中で使用酵素として
市販のパパイン等のプロテアーゼによる処理では前記課
題を解決するには至らなかった。そこで、使用酵素の更
なる選定、検討を行うことにより、ある種の酵素を用い
て大豆蛋白質を処理すれば、溶液状態での粘度が低く、
かつ大豆蛋白分解物のみではゲル物性は低いが、肉との
混合状態でのゲル物性は高く、保水性も良好な大豆蛋白
分解物を調製でき本発明を完成するに至らしめた。即
ち、本発明は大豆蛋白含有溶液をエラスターゼにより分
解して得られるピックル液用蛋白分解物及び大豆蛋白含
有溶液をエラスターゼにより分解して得られる分解物を
有するピックル液である。[Means for Solving the Problems] The inventors of the present invention have made various studies on selection of enzymes to be used and reaction conditions in order to solve the above problems. However, in these studies, treatment with a commercially available protease such as papain as the enzyme to be used did not solve the above-mentioned problems. Therefore, by further selecting and examining the enzyme to be used, if the soybean protein is treated with a certain enzyme, the viscosity in a solution state will be low,
The soybean protein hydrolyzate alone has low gel properties, but the soybean protein hydrolyzate having high gel property in a mixed state with meat and good water retention has been completed, thus completing the present invention. That is, the present invention is a pickle solution having a protein hydrolyzate for a pickle solution obtained by decomposing a soybean protein-containing solution with elastase and a degradable product obtained by decomposing a soybean protein-containing solution with elastase.
【0007】以下に、本発明を詳細に説明する。本発明
に於て大豆蛋白含有溶液とは大豆タンパク質を含んだ溶
液のことであり、大豆若しくは脱脂大豆から抽出した豆
乳や豆乳を酸沈澱させて得た酸沈澱大豆タンパク質を水
に再溶解させたもの、市販の大豆蛋白粉末を水に溶解し
たもの等を挙げることができ、いずれを用いても良い。
更に、大豆蛋白含有溶液には大豆蛋白以外の他の蛋白、
例えばカゼイン、小麦蛋白、トウモロコシ蛋白等の植物
性蛋白、またゼラチン、カゼイン等の動物性蛋白を含有
させても良い。The present invention will be described in detail below. In the present invention, the soybean protein-containing solution is a solution containing soybean protein, and soybean milk extracted from soybean or defatted soybean or acid-precipitated soybean protein obtained by acid-precipitating soybean milk was redissolved in water. Examples thereof include commercially available soybean protein powder dissolved in water, and any of these may be used.
Furthermore, the soy protein-containing solution contains other proteins other than soy protein,
For example, casein, wheat protein, corn protein, and other vegetable proteins, and gelatin, casein, and other animal proteins may be contained.
【0008】さて、本発明で用いるエラスターゼは、Mo
rihara,K. et al.(1965) J. Biol.Chem. 240, 3295-330
4; Mandl,I. et al.(1960) Arch. Biochem. Biophys. 9
1,47-53; Ozaki,H. et al.(1975) J. Biochem. 77, 171
-180; Morihara,K. et al.(1967) Areh. Biochem. Biop
hys. 120, 68-78; Mandl,I. et al.(1962) Proc. Soc.
Exp. Bio. Med. 109, 923-925,に報告されているように
動物の膵臓をはじめ植物、カビ、放線菌、細菌から分離
されているものを用いれば良い。従って、その起源は特
にとらわれない。しかし、多くのエラスタ−ゼの内、ア
ルカリ性バチルス属細菌由来のエラスターゼを用いるの
が最も好ましい。また、アルカリ性バチルス属細菌の一
例としてalklophilic Bacillus sp.Ya-B株(AJ 12619、F
ERM P-12261)を挙げることが出来る。The elastase used in the present invention is Mo.
rihara, K. et al. (1965) J. Biol. Chem. 240 , 3295-330
4; Mandl, I. et al. (1960) Arch. Biochem. Biophys. 9
1 , 47-53; Ozaki, H. et al. (1975) J. Biochem. 77 , 171
-180; Morihara, K. et al. (1967) Areh. Biochem. Biop
hys. 120 , 68-78; Mandl, I. et al. (1962) Proc. Soc.
As described in Exp. Bio. Med. 109 , 923-925, those isolated from the pancreas of animals, plants, molds, actinomycetes, and bacteria may be used. Therefore, its origin is not particularly limited. However, of the many elastases, it is most preferable to use elastase derived from an alkaline Bacillus bacterium. In addition, as an example of an alkaline Bacillus bacterium, an alklophilic Bacillus sp.Ya-B strain (AJ 12619, F
ERM P-12261) can be mentioned.
【0009】さて、アルカリ性バチルス属細菌由来のエ
ラスターゼは山崎らがアルカリ性バチルス属細菌(alklo
philic Bacillus sp.)Ya-B株(AJ 12619、FERM P-12261)
の培養ろ液より見いだした(Tsai,Y.C. et al.,Biochem.
Int.,7,577-583(1983))ものである。アルカリ性バチル
ス属細菌由来のエラスターゼを用いて食肉を軟化させる
試みは既になされている(特開平2−298477)。
また、これ以外にもアルカリ性バチルス属細菌由来のエ
ラスターゼの利用については種々の報告がなされている
(特願平3−228135等)。しかし、アルカリ性バ
チルス属細菌由来のエラスターゼを用いて得た分解物の
ピックル液への利用についての報告はない。As for elastase derived from an alkaline Bacillus bacterium, Yamazaki et al.
(philic Bacillus sp.) Ya-B strain (AJ 12619, FERM P-12261)
Was found in the culture filtrate of Tsai, YC et al., Biochem.
Int., 7 , 577-583 (1983)). Attempts to soften meat using elastase derived from an alkaline Bacillus bacterium have already been made (JP-A-2-298477).
In addition to this, various reports have been made on the use of elastase derived from an alkaline Bacillus bacterium (Japanese Patent Application No. 3-228135, etc.). However, there is no report on the use of a degradation product obtained by using an elastase derived from an alkaline Bacillus bacterium in a pickle solution.
【0010】次に、アルカリ性バチルス属由来のエラス
ターゼは通常の培養法に従って生産すれば良い。以下に
製造法の一例を示す。エラスチン含有寒天培地(グルコ
ース1%、酵母エキス0.5%、リン酸水素二カリウム0.1
%、硫酸マグネシウム0.02%、炭酸ナトリウム1%、エ
ラスチン0.5%、寒天1.5%)で生育させたアルカリ性バ
チルス属細菌(alkalophilic Bacillussp.)Ya-B株(AJ 12
619、FERM P-12261)をエラスターゼ生産培地(例えば、
グルコース1%、豆濃4%、酵母エキス0.5%、リン酸水
素二カリウム0.1%、硫酸マグネシウム0.02%、炭酸ナ
トリウム1%)に接種至、坂口フラスコで37℃、24時間の
培養を行い、その後本培養液を20リットルの同エラスタ
ーゼ含有培地で培養すれば良い。繰り返し述べるが、上
記方法は単なる一例であり、他の培養条件、培養スケー
ルで生産させてもかまわない。Next, the elastase derived from the genus Bacillus may be produced by an ordinary culture method. An example of the manufacturing method is shown below. Elastin-containing agar medium (glucose 1%, yeast extract 0.5%, dipotassium hydrogen phosphate 0.1
%, Magnesium sulfate 0.02%, sodium carbonate 1%, elastin 0.5%, agar 1.5%), and an alkaline bacillus bacterium (alkalophilic Bacillus sp.) Ya-B strain (AJ 12
619, FERM P-12261) with elastase production medium (for example,
Glucose 1%, soybean concentrate 4%, yeast extract 0.5%, dipotassium hydrogen phosphate 0.1%, magnesium sulfate 0.02%, sodium carbonate 1%) were inoculated, followed by cultivation at 37 ° C for 24 hours in a Sakaguchi flask. The main culture solution may be cultured in 20 liters of the same elastase-containing medium. To reiterate, the above method is merely an example, and it may be produced under other culture conditions and culture scales.
【0011】本発明で用いるエラスターゼとしては培養
後、遠心分離により菌体を除去し、培養液上清液を単に
集めて得た極めて精製度の低いものから、種々の精製操
作により完全に精製したものまで、いずれを用いても良
い。As the elastase used in the present invention, after culturing, cells are removed by centrifugation and the supernatant of the culture broth is simply collected to obtain an extremely low degree of purification, which is completely purified by various purification procedures. Any of these may be used.
【0012】エラスターゼの活性測定法については多く
の方法が報告されているが、本発明においてはelastin-
orceinを基質とした比色法(Sachar,L.A. et al.(1955)
Proc. Soc. Exp. Biol. Med. 90 323-326)を用いた。
スクリューキャップの付いたミニ試験管に20mgのelasti
n-orcein(E1500,Sigma)を取り、2mlの50mM NaHCO3-Na
2CO3緩衝液(pH 10.5)と適量の酵素溶液を添加して37
℃で振動しながら反応させ1時間後、1mlの反応停止液
(0.7M リン酸緩衝液、pH 6.0)を添加、遠心分離によ
り基質を除去して上清の590nmでの吸光度を測定する。
活性の測定は全elastin-orceinの半分を分解できる酵素
の量を10ユニットとして用いた。Many methods have been reported for measuring the activity of elastase, but in the present invention, elastin-
Colorimetric method using orcein as substrate (Sachar, LA et al. (1955)
Proc. Soc. Exp. Biol. Med. 90 323-326) was used.
20 mg elasti in mini test tube with screw cap
Take n-orcein (E1500, Sigma) and add 2 ml of 50 mM NaHCO 3 -Na
Add 2 CO 3 buffer (pH 10.5) and appropriate amount of enzyme solution.
After reacting for 1 hour while shaking at ℃, add 1 ml of reaction stop solution (0.7M phosphate buffer, pH 6.0), remove the substrate by centrifugation, and measure the absorbance of the supernatant at 590 nm.
For the measurement of activity, the amount of enzyme capable of degrading half of all elastin-orcein was used as 10 units.
【0013】本発明において、大豆蛋白含有物をエラス
ターゼにより酵素分解する条件は特に限定するものでは
ないが、通常蛋白濃度として約5〜20重量%、酵素量は
タンパク質1gあたりエラスターゼ活性として50〜1000
U、pHは中性及至アルカリ域付近(約pH5〜11)、温度は
約20〜55℃とし、反応時間は後述するように分解率によ
り決定される。本発明に於いては蛋白をアミノ酸まで完
全分解するのではなく、分解率は5〜20%、好ましくは
約7〜15%となるように分解するのが肝要である。ここ
で述べる分解率とは、プロテアーゼによる蛋白の分解の
程度の目安として用いているものであり、蛋白溶液中の
全窒素に対する終濃度0.2M TCA(トリクロル酢酸)可溶
性窒素の割合(百分率)のことをいう。次に、このエラ
スターゼによる分解後、係る分解液を粉末、乾燥化すれ
ば良い。In the present invention, the conditions for enzymatically decomposing the soybean protein-containing material with elastase are not particularly limited, but usually the protein concentration is about 5 to 20% by weight, and the enzyme amount is 50 to 1000 as the elastase activity per 1 g of protein.
U and pH are near neutral to alkaline range (about pH 5 to 11), temperature is about 20 to 55 ° C, and reaction time is determined by decomposition rate as described later. In the present invention, it is important that the protein is not completely decomposed into amino acids but is decomposed so that the decomposition rate is 5 to 20%, preferably about 7 to 15%. The degradation rate described here is used as a measure of the degree of protein degradation by proteases, and is the ratio (percentage) of the final concentration of 0.2 M TCA (trichloroacetic acid) soluble nitrogen to the total nitrogen in the protein solution. Say. Next, after the decomposition with elastase, the decomposition liquid may be powdered and dried.
【0014】通常のプロテア−ゼを用いて上記の分解率
程度に分解すると、蛋白溶液の粘度は低下するが、それ
に伴って異種蛋白との複合系におけるゲル物性や保水性
の低下がみられる。しかし、本発明のようにエラスター
ゼを用いて大豆蛋白質等の蛋白を酵素分解することによ
り、複合系におけるゲル物性や保水性の低下は防ぐこと
ができるばかりか、酵素分解を行っていない大豆蛋白等
を用いるよりも優れた複合系ゲルの調製が可能になる。
また、溶液状態での粘度が低下することにより、大豆蛋
白溶液特有の泡末安定性が抑えられ、蛋白溶液の泡切れ
も向上する。When the protein is decomposed to a level of the above-mentioned decomposition rate using an ordinary protease, the viscosity of the protein solution is reduced, but the gel properties and water retention in the complex system with the heterologous protein are also reduced accordingly. However, by enzymatically decomposing proteins such as soybean protein using elastase as in the present invention, not only can the deterioration of gel properties and water retention in the complex system be prevented, but soybean protein that has not been enzymatically degraded, etc. It is possible to prepare a composite gel superior to that using
Further, since the viscosity in the solution state is reduced, the foam powder stability peculiar to the soybean protein solution is suppressed, and the foam breakage of the protein solution is also improved.
【0015】本発明は大豆蛋白のエラスタ−ゼ分解物の
ピックル液への利用について記載したが、ゼラチン、カ
ゼイン等の動物性蛋白、小麦蛋白、トウモロコシ蛋白と
の植物性蛋白等にも適用可能である。Although the present invention has been described with respect to the use of a soybean protein elastase degradation product in a pickle solution, it is also applicable to animal proteins such as gelatin and casein, wheat proteins, and vegetable proteins such as corn proteins. is there.
【0016】[0016]
【実施例】以下、実施例により本発明を説明する。念の
為に申し述べるが、本発明は実施例に限定される訳では
ない。EXAMPLES The present invention will be described below with reference to examples. As a reminder, the invention is not limited to the examples.
【0017】実施例1 (大豆蛋白溶液の調製)脱脂大豆500gに対して9倍量の
水を加え攪拌抽出後、遠心分離によりオカラを除去し豆
乳を得る。豆乳を硫酸でpH4.5に調製し、等電点沈澱し
た大豆タンパク質を遠心分離により回収する。この大豆
タンパク質を苛性ソーダで中和し、10%濃度の大豆蛋白
溶液を調製した。Example 1 (Preparation of Soybean Protein Solution) 9 g of water was added to 500 g of defatted soybean, the mixture was extracted with stirring, and the okara was removed by centrifugation to obtain soybean milk. Soy milk is adjusted to pH 4.5 with sulfuric acid, and isoelectrically precipitated soy protein is recovered by centrifugation. The soybean protein was neutralized with caustic soda to prepare a 10% soybean protein solution.
【0018】(エラスターゼの調製)上述した方法によ
り培養したアルカリ性バチルス属細菌(alkalophilic B
acillus sp.)Ya-B株(FERM P-12261)より回収した粗酵
素液、つまり培養液を遠心分離した培養上清液をそのま
ま用いた。本粗酵素液のエラスターゼ活性は、4160 U/m
lであった。(Preparation of Elastase) The alkaline bacterium belonging to the genus Bacillus (alkalophilic B ) cultured by the above-mentioned method.
The crude enzyme solution recovered from the strain Accillus sp.) Ya-B (FERM P-12261), that is, the culture supernatant obtained by centrifuging the culture solution was used as it was. The elastase activity of this crude enzyme solution is 4160 U / m.
It was l.
【0019】(分解及び酵素処理大豆蛋白粉末の調製)
大豆蛋白10%液に対して表1に記載の所定のエラスター
ゼ粗酵素液を添加、35℃1時間酵素分解し120℃2分間加
熱失活後、凍結乾燥により酵素分解大豆タンパク質粉末
を得た。尚、酵素分解大豆蛋白粉末の対照としては、酵
素分解を施さず上記の方法で調製した大豆蛋白粉末を、
酵素間の差を観察するために表1に示すように市販酵素
(プロレザー(商品名)、天野製薬(株)製)で酵素分
解した大豆蛋白粉末を用いた。プロレザーによる分解は
50℃20分間行った。(Preparation of Soybean Protein Powder Degraded and Enzyme Treated)
A predetermined elastase crude enzyme solution shown in Table 1 was added to a 10% soybean protein solution, enzymatically decomposed at 35 ° C for 1 hour, heat-inactivated at 120 ° C for 2 minutes, and freeze-dried to obtain an enzymatically decomposed soybean protein powder. As a control of the enzyme-decomposed soybean protein powder, the soybean protein powder prepared by the above method without enzymatic decomposition,
In order to observe the difference between the enzymes, soybean protein powder enzymatically decomposed with a commercially available enzyme (Proleather (trade name), manufactured by Amano Pharmaceutical Co., Ltd.) was used as shown in Table 1. Disassembly by professional leather
It was carried out at 50 ° C for 20 minutes.
【0020】[0020]
【表1】 1)エラスターゼ活性 2)プロテアーゼ活性[Table 1] 1) Elastase activity 2) Protease activity
【0021】(評価)酵素分解した大豆蛋白粉末の塩溶
性測定は、10%食塩水100mlに2.5g大豆蛋白粉末を添
加、5℃にて1.5時間振とう後3000r.p.m.10分間遠心して
得た上清の蛋白量の全蛋白量に対する割合(百分率)で
示した。又、分解率は0.2Mトリクロル酢酸可溶性窒素の
全窒素に対する百分率で表した。大豆蛋白ゲルは大豆蛋
白粉末1重量部に対して3.5重量部の水を加え、真空らい
潰機で10分間らい潰した後70℃50分間加熱、調製した。
大豆蛋白ゲルの破断強度は不動工業社製のレオメーター
にて測定した。結果は表2に示す。(Evaluation) The salt solubility of the enzymatically decomposed soybean protein powder was obtained by adding 2.5 g of soybean protein powder to 100 ml of 10% saline, shaking at 5 ° C. for 1.5 hours, and then centrifuging at 3000 rpm for 10 minutes. The ratio of the protein content of Qing to the total protein content (percentage) is shown. The decomposition rate was expressed as a percentage of 0.2 M trichloroacetic acid-soluble nitrogen with respect to total nitrogen. Soybean protein gel was prepared by adding 3.5 parts by weight of water to 1 part by weight of soybean protein powder, crushing with a vacuum crushing machine for 10 minutes, and then heating at 70 ° C. for 50 minutes.
The breaking strength of the soybean protein gel was measured with a rheometer manufactured by Fudo Kogyo Co., Ltd. The results are shown in Table 2.
【0022】[0022]
【表2】 [Table 2]
【0023】結果は表2に示すようにB、Cは高い塩溶
性を示した。又、酵素量が少なく、分解率が多少低くて
も塩溶性の向上に効果があった。尚、分解率が上昇する
と大豆蛋白ゲルの破断強度は減少した。As shown in Table 2, B and C showed high salt solubility. Further, even if the amount of enzyme was small and the decomposition rate was somewhat low, it was effective in improving the salt solubility. The breaking strength of the soy protein gel decreased as the decomposition rate increased.
【0024】実施例2 実施例1と同様にして得た酵素処理した大豆蛋白粉末を
用いて表3に表した組成でピックル液を調製し、一夜冷
蔵後B型粘度計で粘度を測定した。Example 2 A pickle solution having the composition shown in Table 3 was prepared using the enzyme-treated soybean protein powder obtained in the same manner as in Example 1, and the viscosity was measured with a B-type viscometer after refrigeration overnight.
【0025】[0025]
【表3】 [Table 3]
【0026】このピックル液を用いてモデルハムを調製
した。モデルハムは豚赤身もも肉10重量部にピックル液
7重量部を混合後、カッティングし70℃50分間加熱して
調製した。モデルハムのゲル強度の測定は実施例1と同
様の方法で行った。尚、保水性は直径30mm、高さ5mmの
円柱形のサンプルに7kg、4分間加重したときに離水して
くる量のサンプル重量に対する割合(百分率)で、離水
率として表した。結果は表4に表わした。A model ham was prepared using this pickle solution. Model ham is pickled in 10 parts by weight of red pork leg meat
After mixing 7 parts by weight, the mixture was cut and heated at 70 ° C. for 50 minutes to prepare. The gel strength of model ham was measured by the same method as in Example 1. The water retention was expressed as a water separation rate, which is the ratio (percentage) of the amount of water released when a cylindrical sample having a diameter of 30 mm and a height of 5 mm was loaded with 7 kg for 4 minutes to the sample weight. The results are shown in Table 4.
【0027】[0027]
【表4】 [Table 4]
【0028】また、このモデルハムを官能評価に供し
た。官能評価は熟練した10名のパネラーにより行った。
酵素未処理品(サンプルA)を3点とし、5点満点で評価
を行い、その平均点を表した。結果は表5に示した。The model ham was also subjected to sensory evaluation. The sensory evaluation was performed by 10 skilled panelists.
The enzyme-untreated product (Sample A) was set to 3 points, and evaluation was performed on a scale of 5 points, and the average thereof was shown. The results are shown in Table 5.
【0029】[0029]
【表5】 [Table 5]
【0030】表4に示したようにサンプルB、C、Dは
ピックル液粘度が大幅に改善され、それとともに消泡性
が向上した。また、B、Cで調製したモデルハムはAに
比べて破断強度が向上し、圧出離水率が低く、保水性が
高いことが示された。また、表5に示すように官能評価
においてもAと比較して優れた値を示した。一方、Dで
調製したモデルハムはAに比べて破断強度が低下し、官
能評価においても劣った。As shown in Table 4, in Samples B, C and D, the pickle solution viscosity was significantly improved, and the defoaming property was also improved. Further, it was shown that the model hams prepared in B and C had higher breaking strength, lower squeezing water separation rate and higher water retention than those in A. Further, as shown in Table 5, the sensory evaluation also showed an excellent value as compared with A. On the other hand, the model ham prepared in D had a lower breaking strength than that in A and was also inferior in sensory evaluation.
【0031】実施例3 実施例2と同様にして調製したピックル液1重量部を豚
腕肉ブロック1重量部に対しインジェクターにて注入、
一晩低温下にてタンブリングの後スモーク加熱し、ハム
を調製した。官能評価は実施例2と同様にAを3点とし、
5点満点で評価を行い、平均点で表した。結果は表6に
示した。Example 3 1 part by weight of the pickle solution prepared in the same manner as in Example 2 was injected into 1 part by weight of the pork arm block with an injector,
Hams were prepared by tumbling overnight at low temperature and then heating with smoke. The sensory evaluation was performed by setting A to 3 as in Example 2,
Evaluation was made on a scale of 5 points and expressed as an average point. The results are shown in Table 6.
【0032】[0032]
【表6】 [Table 6]
【0033】表6の官能評価の結果でも、官能評価にお
いてもAと比較して優れた値を示した。一方、Dで調製
したモデルハムはAに比べて官能評価において劣った。The sensory evaluation results shown in Table 6 and the sensory evaluation also showed excellent values as compared with A. On the other hand, the model ham prepared in D was inferior to A in sensory evaluation.
【0034】[0034]
【発明の効果】以上詳述したように、エラスターゼで大
豆蛋白含有溶液を処理することにより、(1)塩溶性に
優れ、かつ(2)溶液状態で低粘度、更に(3)異種蛋
白との複合系において優れた物性を付加するピックル液
用大豆蛋白分解物を提供できる。また、係る分解物を含
有するピックル液を用いて調製したハム等の畜肉加工品
は食感等の優れたものである。As described in detail above, by treating a soybean protein-containing solution with elastase, (1) excellent salt solubility, (2) low viscosity in solution state, and (3) different protein It is possible to provide a soybean protein hydrolyzate for pickle liquid which adds excellent physical properties in a complex system. In addition, processed meat products such as ham prepared using a pickle solution containing the decomposed product have excellent texture and the like.
───────────────────────────────────────────────────── フロントページの続き (72)発明者 高木 博史 神奈川県川崎市川崎区鈴木町1−1 味の 素株式会社中央研究所内 (72)発明者 鳥羽 茂 神奈川県川崎市川崎区鈴木町1−1 味の 素株式会社食品総合研究所内 (72)発明者 土屋 俊浩 神奈川県川崎市川崎区鈴木町1−1 味の 素株式会社食品総合研究所内 ─────────────────────────────────────────────────── ─── Continuation of the front page (72) Inventor Hiroshi Takagi 1-1 Suzuki-cho, Kawasaki-ku, Kawasaki-shi, Kanagawa Ajinomoto Co., Inc. Central Research Laboratory (72) Inventor Shigeru Toba 1-cho Suzuki-cho, Kawasaki-ku, Kawasaki-shi, Kanagawa 1 Ajinomoto Co., Inc. Food Research Institute (72) Inventor Toshihiro Tsuchiya 1-1, Suzuki-cho, Kawasaki-ku, Kawasaki-shi, Kanagawa Ajinomoto Co., Inc. Food Research Institute
Claims (2)
分解して得られるピックル液用蛋白分解物。1. A protein degradation product for pickle liquid obtained by degrading a soybean protein-containing solution with elastase.
分解して得られる分解物を有するピックル液。2. A pickle solution having a decomposition product obtained by decomposing a soybean protein-containing solution with elastase.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP4199802A JPH0646799A (en) | 1992-07-27 | 1992-07-27 | Decomposed protein and pickle solution containing it |
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP4199802A JPH0646799A (en) | 1992-07-27 | 1992-07-27 | Decomposed protein and pickle solution containing it |
Publications (1)
Publication Number | Publication Date |
---|---|
JPH0646799A true JPH0646799A (en) | 1994-02-22 |
Family
ID=16413877
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP4199802A Pending JPH0646799A (en) | 1992-07-27 | 1992-07-27 | Decomposed protein and pickle solution containing it |
Country Status (1)
Country | Link |
---|---|
JP (1) | JPH0646799A (en) |
Cited By (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1996018311A1 (en) * | 1994-12-12 | 1996-06-20 | Fuji Oil Company, Limited | Process for producing soybean protein material |
EP0797927A1 (en) * | 1996-03-28 | 1997-10-01 | Fuji Oil Co., Ltd. | Soybean protein hydrolysate, process for producing the same, and meat products and drinks using the same |
-
1992
- 1992-07-27 JP JP4199802A patent/JPH0646799A/en active Pending
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO1996018311A1 (en) * | 1994-12-12 | 1996-06-20 | Fuji Oil Company, Limited | Process for producing soybean protein material |
EP0797927A1 (en) * | 1996-03-28 | 1997-10-01 | Fuji Oil Co., Ltd. | Soybean protein hydrolysate, process for producing the same, and meat products and drinks using the same |
US6126973A (en) * | 1996-03-28 | 2000-10-03 | Fuji Oil Company Limited | Soybean protein hydrolysate, process for producing the same, and meat products and drinks using the same |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
DE60117405T2 (en) | protein hydrolyzate | |
JP3609648B2 (en) | Novel protein deamidase, gene encoding it, production method thereof and use thereof | |
JP3153237B2 (en) | Protein hydrolyzate | |
DE69917716T2 (en) | Protein-deamidating enzyme, gene coding therefor, process for the preparation and use thereof | |
JPH0665280B2 (en) | Protein gelling agent and protein gelling method using the same | |
TWI284537B (en) | Blood-viscosity reducing agent | |
JP3142001B2 (en) | Method for removing bitterness from enzymatic hydrolysis protein | |
JP5035586B2 (en) | Meat softener containing proteolytic enzyme powder and method for modifying meat using the meat softener | |
WO2000073429A1 (en) | Enzyme liquor and process for producing the same, enzyme preparation, protease preparations and protease-producing bacterium | |
JP3470441B2 (en) | Fermentation accelerator and method for producing fermentation accelerator | |
JP4278831B2 (en) | Enzyme solution and its production method, enzyme agent, proteolytic enzyme agent, proteolytic enzyme producing bacterium | |
JP2556109B2 (en) | Material for meat grain | |
JPH0646799A (en) | Decomposed protein and pickle solution containing it | |
JPH0775569A (en) | Novel transglutaminase | |
JP4401555B2 (en) | A novel chymotrypsin-like protease, a method for producing the same, and a method for producing a protein degradation product containing a novel chymotrypsin-like protease. | |
JP4295387B2 (en) | Method for producing degradable peptides | |
SUNG et al. | Improvement of the Functionality of Soy Protein by Introduction of New Thiol Groups through a Papain‐catalyzed Acylation | |
EP0631733B1 (en) | Enzymic agent for improving the tenderization of meat | |
JP2590373B2 (en) | New surimi and its manufacturing method | |
EP4317428A1 (en) | Enzyme composition for food | |
JP2001178398A (en) | Fermented seasoning and method of producing the same | |
CA1325133C (en) | Method for preparation of tastable matters consisting mainly of low molecular weight peptides | |
KR0127099B1 (en) | Novel bacillus sp. and producing method of protease | |
JP7317497B2 (en) | New meat quality improving agent and method of using the same | |
WO2024135764A1 (en) | Enzyme composition for producing food |