JPH0353360B2 - - Google Patents
Info
- Publication number
- JPH0353360B2 JPH0353360B2 JP371483A JP371483A JPH0353360B2 JP H0353360 B2 JPH0353360 B2 JP H0353360B2 JP 371483 A JP371483 A JP 371483A JP 371483 A JP371483 A JP 371483A JP H0353360 B2 JPH0353360 B2 JP H0353360B2
- Authority
- JP
- Japan
- Prior art keywords
- enzyme
- calcium sulfate
- enzymes
- anhydrous
- weight
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired
Links
- 102000004190 Enzymes Human genes 0.000 claims description 25
- 108090000790 Enzymes Proteins 0.000 claims description 25
- OSGAYBCDTDRGGQ-UHFFFAOYSA-L calcium sulfate Chemical compound [Ca+2].[O-]S([O-])(=O)=O OSGAYBCDTDRGGQ-UHFFFAOYSA-L 0.000 claims description 11
- 150000002978 peroxides Chemical class 0.000 claims description 9
- 239000007844 bleaching agent Substances 0.000 claims description 8
- 239000003381 stabilizer Substances 0.000 claims description 6
- 229940095672 calcium sulfate Drugs 0.000 claims description 5
- 239000013078 crystal Substances 0.000 claims description 5
- 229940095564 anhydrous calcium sulfate Drugs 0.000 claims description 3
- 229940088598 enzyme Drugs 0.000 description 23
- 150000003839 salts Chemical class 0.000 description 8
- 230000000694 effects Effects 0.000 description 6
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 5
- 239000001301 oxygen Substances 0.000 description 5
- 229910052760 oxygen Inorganic materials 0.000 description 5
- 238000004061 bleaching Methods 0.000 description 4
- 230000009849 deactivation Effects 0.000 description 4
- VTIIJXUACCWYHX-UHFFFAOYSA-L disodium;carboxylatooxy carbonate Chemical compound [Na+].[Na+].[O-]C(=O)OOC([O-])=O VTIIJXUACCWYHX-UHFFFAOYSA-L 0.000 description 4
- -1 sodium percarbonate Chemical class 0.000 description 4
- 229940045872 sodium percarbonate Drugs 0.000 description 4
- ZAMOUSCENKQFHK-UHFFFAOYSA-N Chlorine atom Chemical compound [Cl] ZAMOUSCENKQFHK-UHFFFAOYSA-N 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 108010056079 Subtilisins Proteins 0.000 description 3
- 102000005158 Subtilisins Human genes 0.000 description 3
- 239000000460 chlorine Substances 0.000 description 3
- 229910052801 chlorine Inorganic materials 0.000 description 3
- 230000003301 hydrolyzing effect Effects 0.000 description 3
- 238000000034 method Methods 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 108010022999 Serine Proteases Proteins 0.000 description 2
- 102000012479 Serine Proteases Human genes 0.000 description 2
- WQYVRQLZKVEZGA-UHFFFAOYSA-N hypochlorite Chemical compound Cl[O-] WQYVRQLZKVEZGA-UHFFFAOYSA-N 0.000 description 2
- 239000002736 nonionic surfactant Substances 0.000 description 2
- LCPVQAHEFVXVKT-UHFFFAOYSA-N 2-(2,4-difluorophenoxy)pyridin-3-amine Chemical compound NC1=CC=CN=C1OC1=CC=C(F)C=C1F LCPVQAHEFVXVKT-UHFFFAOYSA-N 0.000 description 1
- 108090000915 Aminopeptidases Proteins 0.000 description 1
- 102000004400 Aminopeptidases Human genes 0.000 description 1
- 108090000087 Carboxypeptidase B Proteins 0.000 description 1
- 102000003670 Carboxypeptidase B Human genes 0.000 description 1
- 108010080937 Carboxypeptidases A Proteins 0.000 description 1
- 102000000496 Carboxypeptidases A Human genes 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 108060005980 Collagenase Proteins 0.000 description 1
- 102000029816 Collagenase Human genes 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 102000004317 Lyases Human genes 0.000 description 1
- 108090000856 Lyases Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 108090000787 Subtilisin Proteins 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 229910052925 anhydrite Inorganic materials 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- ZOMBKNNSYQHRCA-UHFFFAOYSA-J calcium sulfate hemihydrate Chemical compound O.[Ca+2].[Ca+2].[O-]S([O-])(=O)=O.[O-]S([O-])(=O)=O ZOMBKNNSYQHRCA-UHFFFAOYSA-J 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 229960002424 collagenase Drugs 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 108010059345 keratinase Proteins 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 239000002304 perfume Substances 0.000 description 1
- 239000000049 pigment Substances 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 229960001922 sodium perborate Drugs 0.000 description 1
- CHQMHPLRPQMAMX-UHFFFAOYSA-L sodium persulfate Substances [Na+].[Na+].[O-]S(=O)(=O)OOS([O-])(=O)=O CHQMHPLRPQMAMX-UHFFFAOYSA-L 0.000 description 1
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229960001322 trypsin Drugs 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Detergent Compositions (AREA)
Description
【発明の詳細な説明】
本発明は無機過酸化物と酵素とを含有する漂白
剤組成物に関し、特には、酵素の失活を抑制し保
存安定性の改善された衣類用漂白剤組成物に関す
る。
過炭酸ナトリウムに代表される無機過酸化物
は、次亜塩素酸塩のような塩素系漂白剤に比べて
使用できる繊維が多いこと、色・柄物にも使用で
きること、塩素系漂白剤特有の臭いがないことな
どの勝れた性質を有しており、酸素系漂白剤とし
て広く用いられるようになつている。
しかしながら、酸素系漂白剤は衣類に付着した
種々の汚れに対する漂白効果が塩素系漂白剤に比
べて劣るために漂白効果の向上が試みられ、特に
落ちにくいと認識されている蛋白、油脂、澱粉汚
れに対しては、酵素を酸素系漂白剤と併用して汚
れを除去する方法が知られている。ところが一方
において、酸素系漂白剤に酵素を添加したものは
特に酵素が失活しやすく、長期間に亘つて安定に
保つておくことが極めて困難であつた。このよう
な酵素含有漂白剤の保存安定性を改善する方法と
しては特定の無水塩を添加することが提案されて
おり、ある程度の効果は認められているが(特開
昭57−73100号公報)、その作用要因については何
ら指摘されてない。
本発明者らは、酵素を含む酸素系漂白剤におけ
る酵素活性の安定性に対する作用要因について鋭
意検討した結果、結晶構造を有する硫酸カルシウ
ムおよび硫酸カルシウム1/2水塩を配合すること
により保存安定性を改善しうることを見出し、こ
の知見に基づいて本発明を完成するに至つた。
すなわち、本発明の酵素含有漂白剤組成物は以
下の(A)〜(C)成分を含むことを特徴とする。
(A) 無機過酸化物、
(B) 酵素、
(C) ()〜()から選ばれる少なくとも1種
の安定化剤。
() 結晶形が六方晶形である無水硫酸カルシ
ウム、
() 硫酸カルシウム1/2水塩。
(A)成分の無機過酸化物の具体例としては過炭酸
ナトリウム、過硼酸ナトリウム、過硫酸ナトリウ
ムなどが例示され、この中でも過炭酸ナトリウム
は低温における漂白効果が優れている点で好まし
い。
硫酸カルシウムについては一般に無水塩、1/2
水塩および2水塩が認められており、また、結晶
系では斜方晶系および六方晶系の無水塩、三方晶
系の1/2水塩、単斜晶系の2水塩に類別され、六
方晶系の無水塩は可溶性の型の無水石コウとよ
ばれている。そしてこの中で、六方晶系の無水塩
および三方晶系の1/2水塩が酵素の安定化剤とし
て特異的に働く。
本発明では、安定化剤として、無機過酸化物の
共存下における酵素安定性に特異的な効果を示す
前記()〜()の少なくとも一種が用いら
れ、この安定化剤の配合量は(A)〜(C)成分中の0.1
〜20重量%が好ましく、特に好ましくは0.5〜5
重量%である。この量が0.1重量%以下では添加
効果が必ずしも十分ではなく、また、20重量%を
越えると、無機過酸化物の量が減少し、漂白作用
上好ましくない。
本発明で使用される酵素としては、水の付加、
除去を促進する加水分解酵素、酸化還元を促進す
る酸化還元酵素、基を1つの分子から他の分子へ
転移し汚れを変質させて除去を促進する転移酵
素、分子間の結合を切断し汚れを分解して除去を
促進するリガーゼ、リアーゼ、汚れを化学的に変
質して除去を促進する酵素が適当であり、これら
の中でも加水分解酵素が好ましく、加水分解酵素
の中でもプロテアーゼが特に好ましい。プロテア
ーゼの具体例としては、セリンプロテアーゼ、ペ
プシン、トリプシン、キモトリプシン、コラーゲ
ナーゼ、ケラチナーゼ、エステラーゼ、スブチリ
シン、パパイン、カルボキシペプチターゼAおよ
びB、アミノペプチターゼが挙げられ、この中で
もセリンプロテアーゼが好ましい。これらの酵素
は、たとえば以下の市販品として入手することも
できる。
アルカラーゼ;ノボ・インダストリー社
エスペラーゼ;ノボ・インダストリー社
ビロプラーゼ;長瀬産業(株)
マクサターゼ;ギスト・プロゲデス社
ALD−2;明治製菓(株)
スペラーゼ;フアイザー社(株)
酵素の配合量は(A)〜(C)成分中の0.01〜5重量%
が適当である。
また、本発明では上記(A)〜(C)の必須成分の他
に、酵素の失活を促進したり、無機過酸化物に悪
影響を与えない範囲で、陰イオン界面活性剤、非
イオン界面活性剤、無機あるいは有機ビルダー、
香料、顔料、螢光剤などの種々の添加剤を添加す
ることができる。
以上説明したように、本発明によれば、無機過
酸化物および酵素を含む漂白剤組成物に結晶系が
六方晶系である無水硫酸カルシウムまたは硫酸カ
ルシウム1/2水塩を添加することにより、酵素の
失活を抑制し、保存安定性を向上させることがで
きる。
実施例
過炭酸ナトリウム79〜98.9重量%、酵素(アル
カラーゼ2.0T)1重量%に対し安定化剤を0.1〜
20重量%含有してなる酵素含有漂白剤組成物を調
製し、ポリ容器ボトルに密封保存し、45℃で30日
間放置して保存した後、酵素の活性残存率を
Casein−275mμ吸収法で求めた。結果を表−1
に示す。
【表】DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a bleach composition containing an inorganic peroxide and an enzyme, and more particularly to a bleach composition for clothing that suppresses enzyme deactivation and has improved storage stability. . Inorganic peroxides, such as sodium percarbonate, can be used for more fibers than chlorine bleaches such as hypochlorite, can be used for colored and patterned fabrics, and have the characteristic odor of chlorine bleaches. It has excellent properties such as being free from oxidation, and has become widely used as an oxygen bleach. However, oxygen bleaches are less effective than chlorine bleaches in bleaching various types of stains attached to clothing, so attempts have been made to improve the bleaching effect, especially for protein, oil, and starch stains that are known to be difficult to remove. A known method for removing stains is to use enzymes in combination with oxygen bleach. On the other hand, however, in oxygen bleaches containing enzymes, the enzymes are particularly susceptible to deactivation, making it extremely difficult to keep them stable for long periods of time. As a method of improving the storage stability of such enzyme-containing bleaches, it has been proposed to add a specific anhydrous salt, and although it has been found to be effective to some extent (Japanese Patent Laid-Open Publication No. 73100/1983) , nothing has been pointed out regarding its effect. As a result of intensive investigation into factors affecting the stability of enzyme activity in oxygen-based bleaches containing enzymes, the present inventors found that by incorporating calcium sulfate and calcium sulfate 1/2 hydrate, which have a crystal structure, storage stability can be improved. The present inventors have discovered that the present invention can be improved, and have completed the present invention based on this knowledge. That is, the enzyme-containing bleach composition of the present invention is characterized by containing the following components (A) to (C). (A) an inorganic peroxide, (B) an enzyme, and (C) at least one stabilizer selected from () to (). () Anhydrous calcium sulfate whose crystal form is hexagonal; () Calcium sulfate hemihydrate. Specific examples of the inorganic peroxide of component (A) include sodium percarbonate, sodium perborate, and sodium persulfate. Among these, sodium percarbonate is preferred because it has an excellent bleaching effect at low temperatures. For calcium sulfate, generally anhydrous salt, 1/2
Aquatic salts and dihydrate salts are recognized, and the crystal systems are classified into orthorhombic and hexagonal anhydrous salts, trigonal half-hydrate salts, and monoclinic dihydrate salts. The hexagonal anhydrous salt is called the soluble form of anhydrite. Among these, hexagonal anhydrous salts and trigonal hemihydrate salts specifically act as enzyme stabilizers. In the present invention, as a stabilizer, at least one of the above () to () is used, which has a specific effect on enzyme stability in the coexistence of an inorganic peroxide, and the amount of this stabilizer is (A ) ~ 0.1 in (C) component
~20% by weight is preferred, particularly preferably 0.5~5%
Weight%. If this amount is less than 0.1% by weight, the effect of addition is not necessarily sufficient, and if it exceeds 20% by weight, the amount of inorganic peroxide decreases, which is not preferable in terms of bleaching action. The enzyme used in the present invention includes water addition,
Hydrolytic enzymes that promote removal; oxidoreductases that promote redox; transferases that transfer groups from one molecule to another, altering the dirt and promoting removal; and cleavage of bonds between molecules to remove dirt. Suitable are ligases and lyases that decompose and promote removal, and enzymes that chemically alter stains and promote removal. Among these, hydrolytic enzymes are preferred, and among hydrolytic enzymes, proteases are particularly preferred. Specific examples of proteases include serine protease, pepsin, trypsin, chymotrypsin, collagenase, keratinase, esterase, subtilisin, papain, carboxypeptidase A and B, and aminopeptidase, and among these, serine protease is preferred. These enzymes can also be obtained as, for example, the following commercial products. Alcalase; Esperase, Novo Industries; Viroplase, Novo Industries; Maxatase, Nagase Sangyo; ALD-2, Gist Progedes; Sperase, Meiji Seika Co., Ltd. (C) 0.01 to 5% by weight of component
is appropriate. In addition to the above essential components (A) to (C), the present invention also includes anionic surfactants, nonionic surfactants, and nonionic surfactants to the extent that they do not promote enzyme deactivation or adversely affect inorganic peroxides. activators, inorganic or organic builders,
Various additives such as perfumes, pigments, fluorescent agents, etc. can be added. As explained above, according to the present invention, by adding anhydrous calcium sulfate or calcium sulfate 1/2 hydrate having a hexagonal crystal system to a bleach composition containing an inorganic peroxide and an enzyme, Enzyme deactivation can be suppressed and storage stability can be improved. Example: 79 to 98.9% by weight of sodium percarbonate, 1% by weight of enzyme (Alcalase 2.0T) and 0.1 to 0.1% of stabilizer
An enzyme-containing bleach composition containing 20% by weight was prepared, sealed in a plastic container bottle, and left to stand at 45°C for 30 days.
It was determined by Casein-275mμ absorption method. Table 1 shows the results.
Shown below. 【table】
Claims (1)
六方晶系である無水硫酸カルシウムおよび硫酸カ
ルシウム1/2水塩から選ばれる安定化剤を含有す
ることを特徴とする酵素含有漂白剤組成物。1 characterized by containing (A) anhydrous peroxide, (B) an enzyme, and (C) a stabilizer selected from anhydrous calcium sulfate and calcium sulfate 1/2 hydrate whose crystal system is a hexagonal system. Enzyme-containing bleach composition.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP371483A JPS59129300A (en) | 1983-01-12 | 1983-01-12 | Enzyme containing bleaching agent composition |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP371483A JPS59129300A (en) | 1983-01-12 | 1983-01-12 | Enzyme containing bleaching agent composition |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS59129300A JPS59129300A (en) | 1984-07-25 |
| JPH0353360B2 true JPH0353360B2 (en) | 1991-08-14 |
Family
ID=11564985
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP371483A Granted JPS59129300A (en) | 1983-01-12 | 1983-01-12 | Enzyme containing bleaching agent composition |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS59129300A (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE19501120A1 (en) * | 1995-01-17 | 1996-07-18 | Henkel Kgaa | Enzyme-containing bleaching detergent |
-
1983
- 1983-01-12 JP JP371483A patent/JPS59129300A/en active Granted
Also Published As
| Publication number | Publication date |
|---|---|
| JPS59129300A (en) | 1984-07-25 |
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