JPH08322456A - Production of biscuits - Google Patents

Production of biscuits

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Publication number
JPH08322456A
JPH08322456A JP13256495A JP13256495A JPH08322456A JP H08322456 A JPH08322456 A JP H08322456A JP 13256495 A JP13256495 A JP 13256495A JP 13256495 A JP13256495 A JP 13256495A JP H08322456 A JPH08322456 A JP H08322456A
Authority
JP
Japan
Prior art keywords
enzyme
units
lipoxygenase
protease
amylase
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.)
Granted
Application number
JP13256495A
Other languages
Japanese (ja)
Other versions
JP2964215B2 (en
Inventor
Kazuhisa Sugimoto
和久 杉本
Yoshifumi Okamura
喜史 岡村
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Ezaki Glico Co Ltd
Original Assignee
Ezaki Glico Co Ltd
Priority date (The priority date 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 date listed.)
Filing date
Publication date
Application filed by Ezaki Glico Co Ltd filed Critical Ezaki Glico Co Ltd
Priority to JP13256495A priority Critical patent/JP2964215B2/en
Publication of JPH08322456A publication Critical patent/JPH08322456A/en
Application granted granted Critical
Publication of JP2964215B2 publication Critical patent/JP2964215B2/en
Anticipated expiration legal-status Critical
Expired - Fee Related legal-status Critical Current

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Abstract

PURPOSE: To obtain the subject product good in a swelling property, improved in a crispy texture, and good in meltability in mouths, by adding amylase and/or protease and lipoxygenase. CONSTITUTION: This method for producing a biscuit comprises adding enzymes selected from (A) lipoxygenase, (B) amylase and (C) protease to a biscuit dough before baked, subjecting the mixture to an enzymatic treatment generally at 15-50 deg.C for 30min to 12hr, molding the treated dough and subsequently baking the molded product. The enzyme A, the enzyme B and the enzyme C are preferably used in amounts of 120000-65000 units, <=10000 units and <=75 units, respectively, per kg of wheat four. A commercially available enzyme preparation is preferably used as the enzyme A. For example, an α-type enzyme may be used as the enzyme B. For example, the enzyme originated from papaya may be used as the enzyme C.

Description

【発明の詳細な説明】Detailed Description of the Invention

【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 which melt well in the mouth and have a crispy 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] Biscuits, cookies,
Crackers, pies, etc. have been manufactured using wheat flour as a main raw material. In this production, in order to improve the swelling and texture of the finished product, lipoxygenase has been made to act on the mixed dough (Japanese Patent Publication No. 4-6323, Japanese Patent Laid-Open No. 6-32323).
3-254939). However, even with these processes,
Some products are not satisfactory in terms of mouthfeel and crispness, and a new method for further improving them has been strongly desired.

【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 diligent efforts, the present inventor has conducted a first invention in which a pre-baking dough is enzymatically treated by using lipoxygenase in combination with at least one of amylase and protease. The invention described in 1, 3, or 5 is referred to as the first, second, or third invention, respectively. The same shall apply hereinafter), and the second invention in which a dough before baking is treated with an enzyme in combination with ethyl alcohol, or a lipoxygenase is used. The above problems are solved by the third invention in which at least one kind of amylase or protease is used in combination with ethyl alcohol and the dough before baking is subjected to enzyme treatment.

【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 and pies.

【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。
The lipoxygenase may be a commercially available enzyme agent.
The activity of the lipoxygenase used in the present invention is measured by the measuring method described below. The amount of lipoxygenase is 5 per 1 kg of wheat flour on which the enzyme acts.
000 to 100,000 units is good, and even 12,000
A range of ˜65,000 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, as the amylase used in combination with lipoxygenase, so-called α-type amylase derived from microorganisms such as plants and molds can be used, and it is used in the range of 15,000 units or less, preferably 10,000 units or less according to the amylase activity measuring method described later. To 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。
The protease used in combination with lipoxygenase according to the present invention may be of plant origin such as papaya or microbial origin such as mold, and the activity of the protease is 100 units or less, preferably 75 units by the method for measuring protease activity described later. 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, ethyl alcohol includes foods containing ethyl alcohol, such as sake and whiskey. The amount of alcohol used is 10% by weight or less based on the flour. There is no particular limitation on the method of addition of alcohol and the timing as long as a high concentration of alcohol does not touch the enzyme and inactivate the enzyme.

【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] Biscuit dough, lipoxygenase according to the first invention, the second invention or the third invention, respectively,
Enzymatic treatment is performed by the action of protease, amylase and ethyl alcohol. The treatment conditions need to be adjusted depending on the type of enzyme and the amount added, 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 a predetermined enzyme action time can be ensured, the addition timing and order in the method for producing a normal baked confectionery are not limited, and for example, it can be dispersed in wheat flour, or dissolved or dispersed in water added during kneading and added. .

【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。
The treated dough is appropriately molded and fired by a conventional method. Although the added enzyme is inactivated by firing, it may be intentionally inactivated by steam treatment, warm bath treatment, or the like during the molding process. Depending on the type of biscuit, sugar, nuts, etc. may be sprinkled or alkali, egg yolk, etc. may be applied during the molding process.

【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、O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 method described below. That is, 0.2 mM Am saturated with O 2
3 ml of monium linoleate solution (pH
9.0, 0.1M Borate-HCl buffer
(including r), 0.3 ml of an appropriately diluted enzyme solution is added, the reaction is performed at 25 ° C., and the absorbance at 234 nm in the reaction solution 3 minutes and 5 minutes after the start of the reaction is measured. Under the above conditions, the amount of enzyme that increases the absorbance at 234 nm by 0.001 per minute is defined as 1 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 amylase activity is measured by the method described below. That is, 1 ml of 0.5% soluble starch solution
(PH 5.0, 0.05M Acetate buff
er is included. ) Add an appropriately diluted enzyme solution to 40 ℃
After reacting for 30 minutes in Somogyi-Nelso
The reducing sugar produced by the n method is quantified. Under the above-mentioned conditions, 1 unit is the enzymatic force that produces 1 mg of reducing sugar as glucose.

【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 protease is measured by the method described below. That is, 5 ml of 0.6% casein solution (p
H7.5, 0.05 M phosphate buf
1 ml of an appropriately diluted enzyme solution was added to the fer, and the mixture was reacted at 30 ° C. for 10 minutes, and the precipitation reagent (concentration in sample,
5 ml of a mixed solution consisting 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 produced at 275 nm is quantified. Under these conditions, 1μ as tyrosine per minute
The enzyme power to generate mol is 1 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。
[Effect] Lipoxygenase, amylase and protease are all effective enzymes for improving the texture of bread and baked confectionery after baking, but their effects are limited. According to the present application, it is possible to obtain a further effect by using them together. Moreover, although 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 per 1 kg of flour, the action time can be extremely shortened or the action temperature can be reduced. It is difficult to control the production process, for example, because it must be extremely low. Further, even if 5000 units or less of lipoxygenase is used, the object of the present application can be achieved for the time being, 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 / kg of flour
Although it is possible to achieve the object by using ethyl alcohol in an amount of g or more, the moldability is likely to deteriorate because the growth of gluten is inhibited. Further, since alcohol is a volatile substance, there is a danger in the firing process, which 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 manufactured by a conventional method. The specifications of the enzymes used in the test product formulations (Formulations 1 to 3) were commercially available lipoxygenase agents (Nagase Biochemical, soybean-derived, with a specific activity of 124).
000 U / g) 0.04 g, that is, 4960 units by the above-mentioned lipoxygenase titer measurement method, and biozyme F which is a fungal-derived enzyme as an amylase agent (Amano Pharmaceutical Co., Ltd. 57,000 U / g)
0.008 g, that is, 456 units by the above-mentioned amylase titer measurement method and purified papain conc as a protease agent (Nagase Biochemical Co., Ltd., plant-derived and having a specific activity of 725
U / g) was added in an amount of 0.004 g, that is, 2.9 units were added individually or in combination by the above-mentioned protease titer measurement method, and after enzyme treatment at 30 ° C. for 60 minutes, molding and baking were performed. As a comparative example, a composition was prepared in which an enzyme other than lipoxygenase was not mixed at all.

【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 of the obtained biscuits was evaluated by 10 panelists based on the evaluation standard table shown in Table 2, and the average result is shown in Table 3. Furthermore, a three-point comparative study was conducted between Comparative Example and Formulation 3, and it was found that there was a difference between the two tissues 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 trial-produced by a conventional method based on the composition shown in Table 4. The specifications of the enzyme used in the test product formulation (formulation 4) were commercially available lipoxygenase agents (produced by Nagase Biochemical Co., Ltd., derived from soybean, with a specific activity of 124000 U).
/ G) of 0.04 g, that is, 4960 units by the above-mentioned lipoxygenase titer measuring method and 8 g of food grade ethyl alcohol (66%) were added, followed by enzyme treatment at 30 ° C for 60 minutes, followed by molding and baking. As a comparative example, a composition was prepared in which enzymes other than lipoxygenase and ethyl alcohol were not added at all.

【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 formulation shown in Table 6, a biscuit was manufactured by a conventional method. The specifications of the enzyme used in the test product formulation (Formulation 5 to 7) were commercially available lipoxygenase agents (Nagase Biochemical Co., Ltd., soybean-derived specific activity 124
000 U / g) 0.04 g, that is, 4960 units by the above-mentioned lipoxygenase titer measurement method, and biozyme F which is a fungal-derived enzyme as an amylase agent (Amano Pharmaceutical Co., Ltd. 57,000 U / g)
0.008 g, that is, 456 units by the above-mentioned amylase titer measurement method and purified papain conc as a protease agent (Nagase Biochemical Co., Ltd., plant-derived and having a specific activity of 725
U / g) 0.004 g, that is, 2.9 units by the above-mentioned protease titer measurement method, food grade ethyl alcohol (6
6%) 8 g, added individually or in combination, and 3
After enzyme treatment at 0 ° C. for 60 minutes, it was molded and baked. As a comparative example, a composition was prepared in which enzymes other than lipoxygenase and ethyl alcohol were not added at all.

【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 of the obtained biscuits was evaluated by 10 panelists based on the evaluation standard table shown in Table 2, and the average result is shown in Table 7. Furthermore, a three-point comparative study was carried out between the comparative example and the formulation 7, and it was found that there was a difference between the two structures at a risk rate 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 trial-produced by a conventional method based on the composition shown in Table 8. The specifications of the enzymes used in the test product formulations (Formulations 8 to 10) are commercially available lipoxygenase agents (produced by Nagase Biochemical Co., Ltd., derived from soybean, and have a specific activity of 12).
4000 U / g), that is, 6200 units by the above-mentioned lipoxygenase titer measurement method, and bioactivity F which is an enzyme derived from mold as an amylase agent (manufactured by Amano Pharmaceutical Co., α-type derived from mold) 57,000 U / g)
0.01 g, that is, 5 by the above-mentioned amylase titer measuring method.
70 units of purified papain conc as a protease agent (Nagase Biochemical, plant-derived, specific activity 725U
/ G) 0.007 g, that is, 5 units by the above-mentioned protease titer measurement method, food grade ethyl alcohol (66%)
8 g of each was added alone or in combination, and after enzyme treatment at 30 ° C. for 60 minutes, molding and firing were performed. As a comparative example, a composition was prepared in which enzymes other than lipoxygenase and ethyl alcohol were not added at all.

【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 of the obtained biscuits was evaluated by 10 panelists based on the evaluation standard table shown in Table 2, and the average result is shown in Table 9. Furthermore, a three-point comparative study was conducted between Comparative Example and Formulation 10, and it was found that there was a difference between the two structures at a risk rate 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 swelling property of the dough is improved, the crispy feeling which is one of the preferable tastes is improved as compared with the conventional one, and the melting in the mouth and the mouthfeel are greatly improved as compared with the conventional one. .

Claims (6)

【特許請求の範囲】[Claims] 【請求項1】 焼成前のビスケット生地にアミラーゼ及
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, which comprises adding at least one of amylase and protease and lipoxygenase to a biscuit dough before baking, performing enzyme treatment, and then molding and baking.
【請求項2】 小麦粉1kgあたり酵素量として150
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 is 150 per kg of wheat flour.
The method for producing biscuits according to claim 1, wherein 00 units or less of amylase, 100 units or less of protease, and 5000 to 100000 units of lipoxygenase are used.
【請求項3】 焼成前のビスケット生地にリポキシゲナ
ーゼ及びエチルアルコールを添加し、酵素処理を行った
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, which comprises adding lipoxygenase and ethyl alcohol to an unbaked biscuit dough, performing enzyme treatment, and then molding and baking.
【請求項4】 小麦粉1kgあたり5000〜1000
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 1 kg of wheat flour
The process for producing biscuits according to claim 3, wherein 00 units of lipoxygenase and 0.1 kg or less of ethyl alcohol are used.
【請求項5】 焼成前のビスケット生地にアミラーゼ及
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. Production of biscuits, characterized in that at least one of amylase and protease, lipoxygenase and ethyl alcohol are added to the biscuit dough before baking, and the mixture is subjected to enzyme treatment, followed by molding and baking. Law.
【請求項6】 小麦粉1kgあたり15000単位以下
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. 15000 units or less of amylase, 100 units or less of protease, and 500 per kg of wheat flour.
0 to 100,000 units of lipoxygenase and 0.1k
The method for producing biscuits according to claim 5, wherein ethyl alcohol of g or less is used.
JP13256495A 1995-03-31 1995-04-20 Manufacturing method of biscuits Expired - Fee Related JP2964215B2 (en)

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
JP7-112250 1995-03-31
JP11225095 1995-03-31
JP13256495A JP2964215B2 (en) 1995-03-31 1995-04-20 Manufacturing method of biscuits

Publications (2)

Publication Number Publication Date
JPH08322456A true JPH08322456A (en) 1996-12-10
JP2964215B2 JP2964215B2 (en) 1999-10-18

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ID=26451468

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Country Status (1)

Country Link
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Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5942262A (en) * 1996-03-19 1999-08-24 Gist-Brocades Biscuit doughs and biscuits products and methods of producing same
WO2002020730A2 (en) 2000-09-05 2002-03-14 Novozymes A/S Manganese lipoxygenase
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

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5942262A (en) * 1996-03-19 1999-08-24 Gist-Brocades Biscuit doughs and biscuits products and methods of producing same
WO2002020730A2 (en) 2000-09-05 2002-03-14 Novozymes A/S Manganese lipoxygenase
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

Also Published As

Publication number Publication date
JP2964215B2 (en) 1999-10-18

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