JP2964215B2 - Manufacturing method of biscuits - Google Patents
Manufacturing method of biscuitsInfo
- Publication number
- JP2964215B2 JP2964215B2 JP13256495A JP13256495A JP2964215B2 JP 2964215 B2 JP2964215 B2 JP 2964215B2 JP 13256495 A JP13256495 A JP 13256495A JP 13256495 A JP13256495 A JP 13256495A JP 2964215 B2 JP2964215 B2 JP 2964215B2
- Authority
- JP
- Japan
- Prior art keywords
- lipoxygenase
- units
- enzyme
- protease
- ethyl alcohol
- 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 - Fee Related
Links
- 235000015895 biscuits Nutrition 0.000 title claims description 23
- 238000004519 manufacturing process Methods 0.000 title claims description 11
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 36
- 102000004190 Enzymes Human genes 0.000 claims description 31
- 108090000790 Enzymes Proteins 0.000 claims description 31
- 102000003820 Lipoxygenases Human genes 0.000 claims description 31
- 108090000128 Lipoxygenases Proteins 0.000 claims description 31
- 239000004365 Protease Substances 0.000 claims description 20
- 235000019441 ethanol Nutrition 0.000 claims description 20
- 108091005804 Peptidases Proteins 0.000 claims description 17
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 17
- 239000004382 Amylase Substances 0.000 claims description 14
- 102000013142 Amylases Human genes 0.000 claims description 14
- 108010065511 Amylases Proteins 0.000 claims description 14
- 235000019418 amylase Nutrition 0.000 claims description 14
- 238000000465 moulding Methods 0.000 claims description 9
- 235000013312 flour Nutrition 0.000 claims description 8
- 241000209140 Triticum Species 0.000 claims description 2
- 235000021307 Triticum Nutrition 0.000 claims description 2
- 229940088598 enzyme Drugs 0.000 description 27
- 239000000203 mixture Substances 0.000 description 23
- 230000000694 effects Effects 0.000 description 18
- 235000019419 proteases Nutrition 0.000 description 13
- 238000009472 formulation Methods 0.000 description 12
- 230000000052 comparative effect Effects 0.000 description 10
- 238000000034 method Methods 0.000 description 10
- 238000010304 firing Methods 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 238000004448 titration Methods 0.000 description 8
- 239000003795 chemical substances by application Substances 0.000 description 7
- 239000000047 product Substances 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 6
- 241000196324 Embryophyta Species 0.000 description 4
- 244000068988 Glycine max Species 0.000 description 4
- 235000010469 Glycine max Nutrition 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 108090000526 Papain Proteins 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 238000011156 evaluation Methods 0.000 description 3
- 229940055729 papain Drugs 0.000 description 3
- 235000019834 papain Nutrition 0.000 description 3
- 238000013441 quality evaluation Methods 0.000 description 3
- 241001137251 Corvidae Species 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 102220483782 Myb/SANT-like DNA-binding domain-containing protein 1_A21D_mutation Human genes 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 235000009508 confectionery Nutrition 0.000 description 2
- 235000014510 cooky Nutrition 0.000 description 2
- 235000012495 crackers Nutrition 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 235000015108 pies Nutrition 0.000 description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 2
- OYHQOLUKZRVURQ-HZJYTTRNSA-M 9-cis,12-cis-Octadecadienoate Chemical compound CCCCC\C=C/C\C=C/CCCCCCCC([O-])=O OYHQOLUKZRVURQ-HZJYTTRNSA-M 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 240000006432 Carica papaya Species 0.000 description 1
- 235000009467 Carica papaya Nutrition 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 108010068370 Glutens Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 235000008429 bread 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
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 235000013345 egg yolk Nutrition 0.000 description 1
- 210000002969 egg yolk Anatomy 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 235000021312 gluten Nutrition 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000004898 kneading Methods 0.000 description 1
- 229940049918 linoleate Drugs 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 239000011259 mixed solution Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000002522 swelling effect Effects 0.000 description 1
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 235000015041 whisky Nutrition 0.000 description 1
Landscapes
- Bakery Products And Manufacturing Methods Therefor (AREA)
Description
【0001】[0001]
【産業上の利用分野】本発明は口溶けが良くサクサクし
た食感を有するビスケット類を製造する方法に関するも
のである。BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a method for producing biscuits having a mouthfeel and a crisp texture.
【0002】[0002]
【従来の技術と問題点】従来、ビスケット、クッキー、
クラッカー、パイ等は小麦粉を主原料として製造されて
きた。この製造において出来上がり製品の膨化や食感を
改良するため、混合生地にリポキシゲナーゼを作用させ
ることが行われてきた(特公平4−6323、特開昭6
3−254939)。しかしながらこれらの処理でも、
なお口どけやサクサク感といった製品の食感面で満足で
きないものがあり、それを一層改良する新たな方法が強
く望まれていた。[Prior art and problems] Conventionally, biscuits, cookies,
Crackers, pies and the like have been produced mainly from flour. In this production, lipoxygenase is allowed to act on the mixed dough in order to improve the puffiness and texture of the finished product (Japanese Patent Publication No. 4-6323;
3-254939). However, even in these processes,
Some products, such as mouthfeel and crispness, are unsatisfactory in terms of the texture of the product, and there has been a strong demand for a new method for further improving the texture.
【0003】[0003]
【問題点を解決するための手段】本発明者は鋭意工夫を
行った結果、リポキシゲナーゼをアミラーゼまたはプロ
テアーゼの内の1種類以上と併用して焼成前の生地に酵
素処理する第1発明(請求項1,3又は5に記載の発明
をそれぞれ第1,第2又は第3発明という。以下同
じ)、リポキシゲナーゼをエチルアルコールとを併用し
て焼成前の生地に酵素処理する第2発明、又はリポキシ
ゲナーゼをアミラーゼまたはプロテアーゼの内の1種類
以上とエチルアルコールと併用し焼成前の生地にて酵素
処理する第3発明によって、上記の問題点を解決したも
のである。Means for Solving the Problems As a result of the inventor's devising, the first invention in which lipoxygenase is used in combination with at least one of amylase and protease to enzyme-treat the dough before firing (claim) The invention described in 1, 3, or 5 is referred to as a first, second, or third invention, respectively. The same applies hereinafter), a second invention in which lipoxygenase is used in combination with ethyl alcohol for enzyme treatment of dough before baking, or a lipoxygenase. The above-mentioned problems have been solved by the third invention in which one or more kinds of amylase or protease and ethyl alcohol are used in combination and enzyme treatment is performed on the dough before firing.
【0004】本発明にいうビスケット類の種類として
は、ビスケット、クッキー、クラッカー、パイなどが挙
げられる。The types of biscuits referred to in the present invention include biscuits, cookies, crackers, pies and the like.
【0005】リポキシゲナーゼは市販の酵素剤でよい。
本発明に用いるリポキシゲナーゼの力価は後述する測定
方法により活性を測定するが、使用量としては酵素を作
用させる小麦粉1kgあたりリポキシゲナーゼ活性が5
000〜100000単位が良く、さらには12000
〜65000単位の範囲が好ましい。[0005] Lipoxygenase may be a commercially available enzyme preparation.
The activity of the lipoxygenase used in the present invention is measured by the measurement method described below.
000-100,000 units is good, and 12,000
A range of ~ 65000 units is preferred.
【0006】本発明においてリポキシゲナーゼと併用す
るアミラーゼは植物やカビ等の微生物起源の所謂α型も
のを用いることができ、後述するアミラーゼ活性測定方
法により15000単位以下、好ましくは10000単
位以下の範囲において使用する。In the present invention, the amylase used in combination with the lipoxygenase may be a so-called α-form derived from a microorganism such as a plant or a mold, and may be used in an amount of 15,000 units or less, preferably 10,000 units or less according to the amylase activity measuring method described later. I do.
【0007】本発明によりリポキシゲナーゼと併用する
プロテアーゼはパパイア等の植物若しくはカビ等の微生
物起源のものを用いることができ、後述するプロテアー
ゼ活性測定方法により、プロテアーゼの活性が100単
位以下、好ましくは75単位以下の範囲で使用する。According to the present invention, a protease to be used in combination with lipoxygenase may be derived from a plant such as papaya or a microorganism such as fungi. Use within the following range.
【0008】本願においてエチルアルコールとは、エチ
ルアルコールを含む食品をもこれに含めることとし、例
えば清酒、ウイスキー等が挙げられる。使用量は小麦粉
に対しアルコールとして10重量%以下にする。高濃度
のアルコールが酵素に触れ、酵素が失活するような事さ
え無いようにすれば、アルコールの添加方法、時期も特
に問わない。In the present application, the term "ethyl alcohol" includes foods containing ethyl alcohol, such as sake and whiskey. The amount used is 10% by weight or less as an alcohol based on flour. The method and timing of adding the alcohol are not particularly limited as long as the high concentration alcohol does not touch the enzyme and the enzyme is not deactivated.
【0009】ビスケット類の生地に、第1発明、第2発
明又は第3発明のそれぞれに従ってリポキシゲナーゼ、
プロテアーゼ、アミラーゼ、エチルアルコールを作用さ
せ、酵素処理を行う。処理条件は酵素の起源による種類
及び添加量に応じて調節する必要があるが、一般には処
理温度は15℃〜50℃、処理時間は30分〜12時間
とすることができる。所定の酵素作用時間さえ確保でき
れば、通常の焼菓子の製造方法中における添加時期、順
序は問わず、たとえば小麦粉中に分散させたり、混練中
に行う加水に溶解若しくは分散して投入することができ
る。[0009] Biscuits dough may contain lipoxygenase according to the first, second or third invention, respectively.
Enzyme treatment is carried out by the action of protease, amylase and ethyl alcohol. The treatment conditions need to be adjusted according to the type and amount of the enzyme depending on the origin, but generally the treatment temperature can be 15 ° C to 50 ° C and the treatment time can be 30 minutes to 12 hours. As long as the predetermined enzyme action time can be ensured, the timing of addition in a normal method for producing baked confectionery can be added regardless of the order, for example, it can be dispersed in wheat flour or dissolved or dispersed in water added during kneading. .
【0010】処理の終わった生地は常法によって、適宜
成形、焼成する。添加した酵素は焼成によって失活する
が、成形工程中に水蒸気処理、温浴処理等によって意図
的に失活させてもよい。ビスケット類の種類によっては
成形工程中に砂糖、ナッツ等をふりかけたり、アルカ
リ、卵黄等を塗布してもよい。[0010] The finished dough is appropriately molded and baked by a conventional method. The added enzyme is inactivated by firing, but may be intentionally inactivated by steam treatment, hot bath treatment, or the like during the molding step. Depending on the type of biscuits, sugar, nuts or the like may be sprinkled during the molding step, or alkali or egg yolk may be applied.
【0011】リポキシゲナーゼの活性は次に述べる方法
で測定する。すなわち、O2飽和した0.2mM Am
monium linoleate 溶液3ml(pH
9.0、0.1M Borate−HCl buffe
rを含む)に適当に希釈した酵素液を0.3ml加えて
25℃で反応を行い、反応開始後3分後と5分後の反応
液における234nmの吸光度を測定する。上記条件の
もとで1分間に234nmの吸光度を0.001増加さ
せる酵素量を1単位とする。The activity of lipoxygenase is measured by the following method. That is, O 2 saturated 0.2 mM Am
3 ml of monium linoleate solution
9.0, 0.1 M Borate-HCl buffer
The reaction solution is added at 0.3 ° C. to the reaction solution at 25 ° C., and the absorbance at 234 nm of the reaction solution is measured 3 minutes and 5 minutes after the start of the reaction. The amount of the enzyme that increases the absorbance at 234 nm by 0.001 per minute under the above conditions is defined as one unit.
【0012】アミラーゼの活性は次に述べる方法にて測
定する。すなわち、可溶性でんぷん0.5%溶液1ml
(pH5.0、0.05M Acetate buff
erを含む。)に適当に希釈した酵素液を加え、40℃
において30分間反応後、Somogyi−Nelso
n法で生成する還元糖を定量する。上記の条件において
グルコースとして1mgの還元糖量を生成する酵素力を
1単位とする。The activity of amylase is measured by the following method. That is, 1 ml of 0.5% soluble starch solution
(PH 5.0, 0.05M Acetate buff
er. )), Add an appropriately diluted enzyme solution,
Reaction for 30 minutes in Somogyi-Nelso
The reducing sugar produced by the n method is quantified. The enzymatic power for producing 1 mg of reducing sugar as glucose under the above conditions is defined as one unit.
【0013】プロテアーゼの活性は次に述べる方法にて
測定する。すなわち、カゼイン0.6%溶液5ml(p
H7.5、0.05 M phosphate buf
ferを含む)に適当に希釈した酵素液1mlを加えて
30℃で10分間反応し、沈殿試薬(試料中の濃度、
0.11Mのトリクロロ酢酸、0.22Mの酢酸ナトリ
ウム、0.33Mの酢酸からなる混合溶液)5mlを加
えて反応をとめ、そのまま20分間放置する。この上清
を得て275nmにおいて生成するチロシン相当量を定
量する。この条件において1分間にチロシンとして1μ
molを生成する酵素力を1単位とする。The activity of the protease is measured by the method described below. That is, 5 ml of a 0.6% casein solution (p
H7.5, 0.05 M phosphate buf
1 ml of an appropriately diluted enzyme solution, and reacted at 30 ° C. for 10 minutes. The precipitation reagent (concentration in the sample,
5 ml of a mixed solution of 0.11 M trichloroacetic acid, 0.22 M sodium acetate, and 0.33 M acetic acid) was added to stop the reaction, and the mixture was allowed to stand for 20 minutes. The supernatant is obtained and the amount of tyrosine generated at 275 nm is determined. Under these conditions, 1 μm of tyrosine per minute was used.
The enzymatic power for producing mol is defined as one unit.
【0014】[0014]
【作用】リポキシゲナーゼ、アミラーゼ及びプロテアー
ゼはいずれもパンや焼菓子の焼成後の組織改良に効果の
ある酵素であるが単独ではその効果に限界がある。本願
により、それらを併用することによって、より一層の効
果を得ることが可能となった。また、小麦粉1kgあた
り酵素量として100000単位以上のリポキシゲナー
ゼ、15000単位以上のアミラーゼ又は100単位以
上のプロテアーゼを使用しても本願の目的は一応達成で
きるが、作用時間を極端に短くしたり、作用温度を極端
に低くとらねばならなかったりする等、生産工程のコン
トロールが難しくなる。更に5000単位以下のリポキ
シゲナーゼを使用しても、本願の目的は一応達成できる
が、長時間の作用時間を要するし実用にならない。[Function] Lipoxygenase, amylase and protease are all enzymes that are effective in improving the texture of bread and baked confectionery after baking, but the effects of these enzymes alone are limited. According to the present application, it is possible to obtain a further effect by using them in combination. The purpose of the present application can be achieved by using 100,000 units or more of lipoxygenase, 15,000 units or more of amylase, or 100 units or more of protease as an enzyme amount per 1 kg of flour. It is difficult to control the production process, for example, it is necessary to keep the temperature extremely low. Further, the use of lipoxygenase of 5000 units or less can achieve the object of the present application, but it requires a long action time and is not practical.
【0015】本願において小麦粉1kgあたり0.1k
g以上のエチルアルコールを使用しても目的を達成する
ことは可能であるが、グルテンの成長を阻害する為に成
形性が悪化し易い。また、アルコールが揮発物である為
に焼成工程に危険が伴い、実用的ではない。In the present application, 0.1 k per kg of flour
Although the purpose can be achieved by using g or more of ethyl alcohol, the moldability is liable to deteriorate due to the inhibition of gluten growth. In addition, since alcohol is a volatile substance, the firing step involves danger and is not practical.
【0016】[0016]
【実施例】以下に実施例により本発明をさらに詳細に説
明する。The present invention will be described in more detail with reference to the following examples.
【0017】(実施例1)表1の配合に基づき、常法に
よりビスケットを試作した。テスト品配合(配合1〜配
合3)に使用した酵素の諸元は市販のリポキシゲナーゼ
剤(ナガセ生化学社製、大豆由来のもので比活性124
000U/g)を0.04gつまり前述のリポキシゲナ
ーゼ力価測定法にて4960単位分と、アミラーゼ剤と
してカビ由来の酵素であるビオザイムF(天野製薬社
製、カビ由来のα型のもので比活性57000U/g)
を0.008gつまり前述のアミラーゼ力価測定法にて
456単位分とプロテアーゼ剤として精製パパインコン
ク(ナガセ生化学社製、植物由来のもので比活性725
U/g)を0.004gつまり前述のプロテアーゼ力価
測定法にて2.9単位分をそれぞれ単独あるいは複合し
て添加し、30℃で60分間酵素処理後、成形・焼成し
た。比較例としてはリポキシゲナーゼ以外の酵素を全く
配合しない配合のものを作成した。(Example 1) Based on the composition shown in Table 1, a biscuit was trial-produced by a conventional method. The specifications of the enzymes used in the test product formulations (formulations 1 to 3) were commercially available lipoxygenase agents (manufactured by Nagase Biochemical Co., Ltd., derived from soybean, specific activity of 124).
000 U / g) as 0.04 g, that is, 4960 units in the lipoxygenase titration method described above, and a specific activity of biozyme F (a mold derived from Amano Pharmaceutical Co., Ltd .; 57000U / g)
0.008 g, that is, 456 units by the above-mentioned amylase titration method and purified papain conc (produced by Nagase Biochemical Co., Ltd., plant-derived, specific activity of 725) as a protease agent.
U / g) was added singly or in combination of 2.9 units by the protease titration method described above, and the mixture was subjected to an enzyme treatment at 30 ° C. for 60 minutes, followed by molding and firing. As a comparative example, a composition not containing any enzyme other than lipoxygenase was prepared.
【0018】得られたビスケットの品質評価をパネラー
数10人で表2に示す評価基準表に基づいて行い、その
平均の結果を表3に示す。更に比較例と配合3において
は3点比較調査を実施し、5%の危険率で両者の組織に
は差があるとの結果をえた。The quality evaluation of the obtained biscuit was performed by 10 panelists based on the evaluation criteria table shown in Table 2, and the average result is shown in Table 3. Further, a three-point comparative study was conducted for Comparative Example and Formulation 3, and the result was that there was a difference between the two structures at a risk rate of 5%.
【0019】[0019]
【表1】 [Table 1]
【0020】[0020]
【表2】 [Table 2]
【0021】[0021]
【表3】 [Table 3]
【0022】(実施例2)表4の配合に基づき、常法に
よりビスケットを試作した。テスト品配合(配合4)に
使用した酵素の諸元は市販のリポキシゲナーゼ剤(ナガ
セ生化学社製、大豆由来のもので比活性124000U
/g)を0.04gつまり前述のリポキシゲナーゼ力価
測定法にて4960単位分と、食品用エチルアルコール
(66%)8gを添加し、30℃で60分間酵素処理
後、成形・焼成した。比較例としてはリポキシゲナーゼ
以外の酵素、エチルアルコールともに全く添加しない配
合のものを作成した。(Example 2) Biscuits were experimentally produced based on the composition shown in Table 4 by an ordinary method. The specifications of the enzyme used in the test product formulation (formulation 4) were a commercially available lipoxygenase agent (manufactured by Nagase Biochemical Co., Ltd., derived from soybean and having a specific activity of 124000 U)
/ G) was added to 0.04 g, that is, 4960 units for the lipoxygenase titration method described above, and 8 g of food-grade ethyl alcohol (66%), and subjected to enzyme treatment at 30 ° C. for 60 minutes, followed by molding and firing. As a comparative example, an enzyme other than lipoxygenase and a mixture in which ethyl alcohol was not added at all were prepared.
【0023】[0023]
【表4】 [Table 4]
【0024】[0024]
【表5】 [Table 5]
【0025】(実施例3)表6の配合に基づき、常法に
よりビスケットを試作した。テスト品配合(配合5〜配
合7)に使用した酵素の諸元は市販のリポキシゲナーゼ
剤(ナガセ生化学社製、大豆由来のもので比活性124
000U/g)を0.04gつまり前述のリポキシゲナ
ーゼ力価測定法にて4960単位分と、アミラーゼ剤と
してカビ由来の酵素であるビオザイムF(天野製薬社
製、カビ由来のα型のもので比活性57000U/g)
を0.008gつまり前述のアミラーゼ力価測定法にて
456単位分とプロテアーゼ剤として精製パパインコン
ク(ナガセ生化学社製、植物由来のもので比活性725
U/g)を0.004gつまり前述のプロテアーゼ力価
測定法にて2.9単位分、食品用エチルアルコール(6
6%)8gをそれぞれ単独あるいは複合して添加し、3
0℃で60分間酵素処理後、成形・焼成した。比較例と
してはリポキシゲナーゼ以外の酵素、エチルアルコール
ともに全く添加しない配合のものを作成した。(Example 3) Based on the composition shown in Table 6, a biscuit was trial-produced by a conventional method. The specifications of the enzymes used in the test product formulations (Formulations 5 to 7) were commercially available lipoxygenase agents (manufactured by Nagase Biochemical Co., Ltd., derived from soybean, specific activity of 124).
000 U / g) as 0.04 g, that is, 4960 units in the lipoxygenase titration method described above, and a specific activity of biozyme F (a mold derived from Amano Pharmaceutical Co., Ltd .; 57000U / g)
0.008 g, that is, 456 units by the above-mentioned amylase titration method and purified papain conc (produced by Nagase Biochemical Co., Ltd., plant-derived, specific activity of 725) as a protease agent.
U / g) of 0.004 g, that is, 2.9 units by the above-mentioned protease titration method, and ethyl alcohol (6
6%) 8 g each alone or in combination,
After the enzyme treatment at 0 ° C. for 60 minutes, molding and firing were performed. As a comparative example, an enzyme other than lipoxygenase and a mixture in which ethyl alcohol was not added at all were prepared.
【0026】得られたビスケットの品質評価をパネラー
数10人で表2に示す評価基準表に基づいて行い、その
平均の結果を表7に示す。更に比較例と配合7において
は3点比較調査を実施し、0.1%の危険率で両者の組
織には差があるとの結果をえた。The quality evaluation of the obtained biscuit was performed by 10 panelists based on the evaluation criteria table shown in Table 2, and the average result is shown in Table 7. In addition, a three-point comparative study was performed on the comparative example and formulation 7, and the result was that there was a difference between the two structures at a risk of 0.1%.
【0027】[0027]
【表6】 [Table 6]
【0028】[0028]
【表7】 [Table 7]
【0029】(実施例4)表8の配合に基づき、常法に
よりビスケットを試作した。テスト品配合(配合8〜配
合10)に使用した酵素の諸元は市販のリポキシゲナー
ゼ剤(ナガセ生化学社製、大豆由来のもので比活性12
4000U/g)を0.05gつまり前述のリポキシゲ
ナーゼ力価測定法にて6200単位分と、アミラーゼ剤
としてカビ由来の酵素であるビオザイムF(天野製薬社
製、カビ由来のα型のもので比活性57000U/g)
を0.01gつまり前述のアミラーゼ力価測定法にて5
70単位分とプロテアーゼ剤として精製パパインコンク
(ナガセ生化学社製、植物由来のもので比活性725U
/g)を0.007gつまり前述のプロテアーゼ力価測
定法にて5単位分、食品用エチルアルコール(66%)
8gをそれぞれ単独あるいは複合して添加し、30℃で
60分間酵素処理後、成形・焼成した。比較例としては
リポキシゲナーゼ以外の酵素、エチルアルコールともに
全く添加しない配合のものを作成した。(Example 4) Biscuits were experimentally produced based on the composition shown in Table 8 by an ordinary method. The specifications of the enzyme used in the test product formulation (formulation 8 to formulation 10) are commercially available lipoxygenase agents (manufactured by Nagase Biochemical Co., Ltd., derived from soybean, specific activity of 12).
4000 U / g) of 0.05 g, that is, 6200 units by the lipoxygenase titration method described above, and a specific activity of biozyme F (a mold derived from Amano Pharmaceutical Co., Ltd .; 57000U / g)
Is 0.01 g, that is, 5
70 units and purified papain conch (produced by Nagase Biochemical Co., Ltd. as a protease agent and having a specific activity of 725 U
/ G) is 0.007 g, that is, 5 units by the protease titer described above, and ethyl alcohol for food (66%)
8 g of each was added alone or in combination, and the mixture was subjected to an enzyme treatment at 30 ° C. for 60 minutes, followed by molding and firing. As a comparative example, an enzyme other than lipoxygenase and a mixture in which ethyl alcohol was not added at all were prepared.
【0030】得られたビスケットの品質評価をパネラー
数10人で表2に示す評価基準表に基づいて行い、その
平均の結果を表9に示す。更に比較例と配合10におい
ては3点比較調査を実施し、0.1%の危険率で両者の
組織には差があるとの結果をえた。The quality evaluation of the obtained biscuit was carried out by 10 panelists based on the evaluation criteria table shown in Table 2, and the average result is shown in Table 9. In addition, a three-point comparative study was conducted on the comparative example and formulation 10, and the result was that there was a difference between the two structures at a risk of 0.1%.
【0031】[0031]
【表8】 [Table 8]
【0032】[0032]
【表9】 [Table 9]
【0033】[0033]
【効果】本発明により、生地の膨化性が良くなり、好ま
しい味質の1つであるサクサク感が従来のものと比較し
て向上しており、口溶け、口あたりも従来に比べ大きく
改善された。[Effect] According to the present invention, the dough has good swelling properties, and the crispness, which is one of the preferable taste qualities, is improved as compared with the conventional one, and the dissolution in the mouth and the mouth feel are greatly improved as compared with the conventional one. .
───────────────────────────────────────────────────── フロントページの続き (56)参考文献 特開 昭63−254939(JP,A) 特開 平1−165332(JP,A) 特開 昭62−166831(JP,A) 特開 平5−23095(JP,A) 特開 平4−311338(JP,A) 特開 昭60−241842(JP,A) 特開 平7−147881(JP,A) 特公 平4−6323(JP,B2) (58)調査した分野(Int.Cl.6,DB名) A21D 2/00 A21D 8/00 ──────────────────────────────────────────────────続 き Continuation of front page (56) References JP-A-63-254939 (JP, A) JP-A-1-165332 (JP, A) JP-A-62-166831 (JP, A) JP-A 5- 23095 (JP, A) JP-A-4-311338 (JP, A) JP-A-60-241842 (JP, A) JP-A-7-147881 (JP, A) JP-B-4-6323 (JP, B2) (58) Field surveyed (Int. Cl. 6 , DB name) A21D 2/00 A21D 8/00
Claims (6)
びプロテアーゼのうちの1種類以上とリポキシゲナーゼ
とを添加し、酵素処理を行った後、成形・焼成を行うこ
とを特徴とするビスケット類の製造法。1. A method for producing biscuits, comprising adding at least one of amylase and protease and lipoxygenase to biscuit dough before baking, performing enzyme treatment, and then performing molding and baking.
00単位以下のアミラーゼ、100単位以下のプロテア
ーゼ、5000〜100000単位のリポキシゲナーゼ
を使用することを特徴とする請求項1に記載のビスケッ
ト類の製造法。2. The amount of enzyme per kg of wheat flour is 150
The method for producing biscuits according to claim 1, wherein an amylase of 100 units or less, a protease of 100 units or less, and lipoxygenase of 5,000 to 100,000 units are used.
ーゼ及びエチルアルコールを添加し、酵素処理を行った
後、成形・焼成を行うことを特徴とするビスケット類の
製造法。3. A method for producing biscuits, comprising adding lipoxygenase and ethyl alcohol to biscuit dough before baking, performing enzyme treatment, and then performing molding and baking.
00単位のリポキシゲナーゼと0.1kg以下のエチル
アルコールを使用することを特徴とする請求項3に記載
のビスケット類の製造法。4. 5000 to 1000 per kg of flour
4. The method for producing biscuits according to claim 3, wherein 00 units of lipoxygenase and 0.1 kg or less of ethyl alcohol are used.
びプロテアーゼのうちの1種類以上とリポキシゲナーゼ
及びエチルアルコールを添加し、酵素処理を行ったあ
と、成形・焼成を行うことを特徴とするビスケット類の
製造法。5. A method for producing biscuits, wherein one or more of amylase and protease, lipoxygenase and ethyl alcohol are added to a biscuit dough before baking, followed by enzyme treatment, followed by molding and baking. Law.
のアミラーゼ、100単位以下のプロテアーゼ、500
0〜100000単位のリポキシゲナーゼと、0.1k
g以下のエチルアルコールを使用することを特徴とする
請求項5に記載のビスケット類の製造法。6. 1kg or less of amylase, 100 or less of protease, 500kg or less per kg of flour.
0-100,000 units of lipoxygenase, 0.1 k
The method for producing biscuits according to claim 5, wherein less than g of ethyl alcohol is used.
Priority Applications (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP13256495A JP2964215B2 (en) | 1995-03-31 | 1995-04-20 | Manufacturing method of biscuits |
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
JP11225095 | 1995-03-31 | ||
JP7-112250 | 1995-03-31 | ||
JP13256495A JP2964215B2 (en) | 1995-03-31 | 1995-04-20 | Manufacturing method of biscuits |
Publications (2)
Publication Number | Publication Date |
---|---|
JPH08322456A JPH08322456A (en) | 1996-12-10 |
JP2964215B2 true JP2964215B2 (en) | 1999-10-18 |
Family
ID=26451468
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP13256495A Expired - Fee Related JP2964215B2 (en) | 1995-03-31 | 1995-04-20 | Manufacturing method of biscuits |
Country Status (1)
Country | Link |
---|---|
JP (1) | JP2964215B2 (en) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2002020730A2 (en) | 2000-09-05 | 2002-03-14 | Novozymes A/S | Manganese lipoxygenase |
Families Citing this family (2)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
ATE218809T1 (en) * | 1996-03-19 | 2002-06-15 | Dsm Nv | COMBINATION OF ENZYMES |
CN102308863A (en) * | 2011-09-30 | 2012-01-11 | 东莞市华美食品有限公司 | Enzyme-modified crisp biscuit preparation method |
-
1995
- 1995-04-20 JP JP13256495A patent/JP2964215B2/en not_active Expired - Fee Related
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2002020730A2 (en) | 2000-09-05 | 2002-03-14 | Novozymes A/S | Manganese lipoxygenase |
Also Published As
Publication number | Publication date |
---|---|
JPH08322456A (en) | 1996-12-10 |
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