JPH0790300A - Washing agent and washing method - Google Patents
Washing agent and washing methodInfo
- Publication number
- JPH0790300A JPH0790300A JP5273262A JP27326293A JPH0790300A JP H0790300 A JPH0790300 A JP H0790300A JP 5273262 A JP5273262 A JP 5273262A JP 27326293 A JP27326293 A JP 27326293A JP H0790300 A JPH0790300 A JP H0790300A
- Authority
- JP
- Japan
- Prior art keywords
- lipase
- cellulase
- rinsing
- washing
- enzyme
- 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
- 238000005406 washing Methods 0.000 title abstract description 21
- 238000000034 method Methods 0.000 title description 7
- 102000004882 Lipase Human genes 0.000 claims abstract description 43
- 108090001060 Lipase Proteins 0.000 claims abstract description 43
- 239000004367 Lipase Substances 0.000 claims abstract description 42
- 235000019421 lipase Nutrition 0.000 claims abstract description 42
- 102000004190 Enzymes Human genes 0.000 claims abstract description 33
- 108090000790 Enzymes Proteins 0.000 claims abstract description 33
- 229940088598 enzyme Drugs 0.000 claims abstract description 33
- 108010059892 Cellulase Proteins 0.000 claims abstract description 31
- 229940106157 cellulase Drugs 0.000 claims abstract description 31
- 230000000694 effects Effects 0.000 claims abstract description 20
- 230000001461 cytolytic effect Effects 0.000 claims description 3
- 230000002366 lipolytic effect Effects 0.000 claims description 3
- 239000012487 rinsing solution Substances 0.000 claims description 3
- 239000004744 fabric Substances 0.000 abstract description 22
- 239000003795 chemical substances by application Substances 0.000 abstract description 18
- 150000002632 lipids Chemical class 0.000 abstract description 8
- 239000007788 liquid Substances 0.000 abstract description 5
- 229920002678 cellulose Polymers 0.000 abstract description 3
- 239000001913 cellulose Substances 0.000 abstract description 3
- 239000003513 alkali Substances 0.000 abstract 4
- 239000003599 detergent Substances 0.000 description 13
- 239000003921 oil Substances 0.000 description 13
- 235000019198 oils Nutrition 0.000 description 13
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 11
- 238000011156 evaluation Methods 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 229920000742 Cotton Polymers 0.000 description 6
- 108091005804 Peptidases Proteins 0.000 description 6
- VLKZOEOYAKHREP-UHFFFAOYSA-N n-Hexane Chemical compound CCCCCC VLKZOEOYAKHREP-UHFFFAOYSA-N 0.000 description 6
- 239000004006 olive oil Substances 0.000 description 6
- 235000008390 olive oil Nutrition 0.000 description 6
- 238000011084 recovery Methods 0.000 description 6
- 102000035195 Peptidases Human genes 0.000 description 4
- 239000003945 anionic surfactant Substances 0.000 description 4
- 239000003093 cationic surfactant Substances 0.000 description 4
- 238000001035 drying Methods 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 238000003860 storage Methods 0.000 description 4
- 241000228245 Aspergillus niger Species 0.000 description 3
- 241000223198 Humicola Species 0.000 description 3
- 241000235395 Mucor Species 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 241000235527 Rhizopus Species 0.000 description 3
- 239000004902 Softening Agent Substances 0.000 description 3
- 239000000654 additive Substances 0.000 description 3
- 239000007844 bleaching agent Substances 0.000 description 3
- 239000007850 fluorescent dye Substances 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 241000131386 Aspergillus sojae Species 0.000 description 2
- 241001148466 Janthinobacterium lividum Species 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- UYXTWWCETRIEDR-UHFFFAOYSA-N Tributyrin Chemical group CCCC(=O)OCC(OC(=O)CCC)COC(=O)CCC UYXTWWCETRIEDR-UHFFFAOYSA-N 0.000 description 2
- 241000223261 Trichoderma viride Species 0.000 description 2
- 241000235015 Yarrowia lipolytica Species 0.000 description 2
- 239000006103 coloring component Substances 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 239000008187 granular material Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 235000019626 lipase activity Nutrition 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 102000004169 proteins and genes Human genes 0.000 description 2
- 108090000623 proteins and genes Proteins 0.000 description 2
- 229910052938 sodium sulfate Inorganic materials 0.000 description 2
- 235000011152 sodium sulphate Nutrition 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- UFTFJSFQGQCHQW-UHFFFAOYSA-N triformin Chemical compound O=COCC(OC=O)COC=O UFTFJSFQGQCHQW-UHFFFAOYSA-N 0.000 description 2
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 2
- LDVVTQMJQSCDMK-UHFFFAOYSA-N 1,3-dihydroxypropan-2-yl formate Chemical compound OCC(CO)OC=O LDVVTQMJQSCDMK-UHFFFAOYSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 1
- 241001465318 Aspergillus terreus Species 0.000 description 1
- BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 241000223221 Fusarium oxysporum Species 0.000 description 1
- 241000233732 Fusarium verticillioides 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
- 241001480714 Humicola insolens Species 0.000 description 1
- 244000112675 Lablab purpureus Species 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 102000004317 Lyases Human genes 0.000 description 1
- 108090000856 Lyases Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000332006 Microtrombidium pusillum Species 0.000 description 1
- 241000729876 Niveus Species 0.000 description 1
- 241000228143 Penicillium Species 0.000 description 1
- 241000303962 Rhizopus delemar Species 0.000 description 1
- 239000004115 Sodium Silicate Substances 0.000 description 1
- 241001085826 Sporotrichum Species 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 241001136494 Talaromyces funiculosus Species 0.000 description 1
- 241000223258 Thermomyces lanuginosus Species 0.000 description 1
- 241000209140 Triticum Species 0.000 description 1
- 235000021307 Triticum Nutrition 0.000 description 1
- 229910021536 Zeolite Inorganic materials 0.000 description 1
- 241000179532 [Candida] cylindracea Species 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 1
- 239000001639 calcium acetate Substances 0.000 description 1
- 235000011092 calcium acetate Nutrition 0.000 description 1
- 229960005147 calcium acetate Drugs 0.000 description 1
- 159000000007 calcium salts Chemical class 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 150000002009 diols Chemical class 0.000 description 1
- HNPSIPDUKPIQMN-UHFFFAOYSA-N dioxosilane;oxo(oxoalumanyloxy)alumane Chemical compound O=[Si]=O.O=[Al]O[Al]=O HNPSIPDUKPIQMN-UHFFFAOYSA-N 0.000 description 1
- 238000010981 drying operation Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 230000009088 enzymatic function Effects 0.000 description 1
- 238000006266 etherification reaction Methods 0.000 description 1
- 230000003631 expected effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 239000002035 hexane extract Substances 0.000 description 1
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000000414 obstructive effect Effects 0.000 description 1
- 210000000496 pancreas Anatomy 0.000 description 1
- 239000002304 perfume Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 235000002639 sodium chloride Nutrition 0.000 description 1
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 1
- 229910052911 sodium silicate Inorganic materials 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000010457 zeolite Substances 0.000 description 1
Landscapes
- Detail Structures Of Washing Machines And Dryers (AREA)
- Detergent Compositions (AREA)
Abstract
Description
【0001】[0001]
【産業上の利用分野】本発明は、布、衣類等の洗濯すす
ぎ剤及び洗濯すすぎ方法に関し、特に、弱アルカリ性条
件下で活性を有する脂質分解酵素(以下、リパーゼと称
する。)及び弱アルカリ性条件下で活性を有するセルロ
ーズ分解酵素(以下、セルラーゼと称する。)の少なく
とも1種を含む洗濯すすぎ剤及びリパーゼ若しくはセル
ラーゼの少なくとも1種又はこれら両者の所定量を洗濯
すすぎ液中に添加してすすぎを行うことを特徴とする洗
濯すすぎ方法に関する。BACKGROUND OF THE INVENTION 1. Field of the Invention The present invention relates to a laundry rinsing agent for clothes, clothes and the like, and a method for washing and rinsing it, and more particularly to a lipolytic enzyme (hereinafter referred to as lipase) having activity under weak alkaline conditions and a weak alkaline condition. A rinsing agent containing at least one cellulolytic enzyme having the following activity (hereinafter, referred to as cellulase) and at least one lipase or cellulase, or a predetermined amount of both of them is added to the washing rinsing solution for rinsing. A method of washing and rinsing characterized by performing.
【0002】[0002]
【従来技術とその問題点】布、衣類等の洗濯に使用する
洗剤に酵素を添加することは、従来より既に広く行われ
ている。しかし、蛋白質である酵素は一般に比較的不安
定な物質であり、特に、高アルカリ性で、酵素阻害作用
の強い陰イオン界面活性剤が高濃度で存在し、しかも、
各種の添加剤の存在する洗濯条件下では、分解を受け易
く酵素本来の性能を充分に発揮させることは上相当に困
難であり、その為実際に使用できる酵素の種類も著しく
制約を受ける。2. Description of the Related Art The addition of enzymes to detergents used for washing clothes, clothes, etc. has been widely practiced. However, enzymes that are proteins are generally relatively unstable substances, and in particular, they are highly alkaline and have a high concentration of an anionic surfactant having a strong enzyme inhibitory action, and
Under the washing conditions in which various additives are present, it is susceptible to decomposition and it is extremely difficult to sufficiently exhibit the original performance of the enzyme. Therefore, the kind of enzyme that can be actually used is significantly restricted.
【0003】そこで、従来よりかかる過酷な条件下でも
比較的安定で高い活性を有する酵素の開発が盛んに行わ
れており、それなりに優れた機能を発揮する酵素も見出
されてはいるが、必ずしも充分満足すべき状態とは言い
難い。また、酵素の機能を出来るだけ活用する為に、障
害となる洗剤の存在しない洗濯前工程での“前浸漬”に
酵素を使用することが提唱されているが、手間が掛かる
為か現実には普及していない。他方、洗濯後工程として
洗濯すすぎ液中に柔軟仕上げを目標とした陽イオン界面
活性剤の添加が行われているが、酵素類の添加・使用に
ついては本発明者等の知る限りでは知られてはいない。
布、衣類等の洗剤用酵素として従来より広く用いられて
いる酵素は、大部分が蛋白分解酵素(プロテアーゼ)で
あり、リパーゼやセルラーゼを洗剤用酵素として使用し
た例は比較的少ない。Therefore, an enzyme having a comparatively stable and high activity under such severe conditions has been actively developed, and an enzyme having an excellent function has been found. It is not always possible to say that the situation is completely satisfactory. Also, in order to utilize the enzyme function as much as possible, it has been proposed to use the enzyme in "pre-soaking" in the pre-washing step where there is no obstructive detergent, but in reality it may be time-consuming. Not popular. On the other hand, as a post-washing step, a cationic surfactant for the purpose of softening is added to the wash rinsing liquid, but addition and use of enzymes are known as far as the present inventors know. There isn't.
Most of the enzymes that have hitherto been widely used as detergent enzymes for cloth, clothes, etc. are proteolytic enzymes (proteases), and there are relatively few cases where lipase or cellulase is used as a detergent enzyme.
【0004】[0004]
1、脂質汚れの除去について 衣類に付着した脂質汚れは、陰イオン界面活性剤を用い
た一般の洗濯では、充分には除去し難い為、リパーゼを
添加した洗剤が開発されたが(特開昭63−6869
7、米国特許4011169、英国特許129361
3)、前述の通り高アルカリ性且つ高濃度の陰イオン界
面活性剤の存在する条件下では、充分にその機能を発揮
し難く、漂白剤、蛍光染料等の添加剤によりリパーゼが
失活したり、更に、洗剤成分として広く用いられている
蛋白分解酵素(プロテアーゼ)により、それ自体蛋白質
であるリパーゼが分解し失活する場合もある。従って、
予めリパーゼを配合した洗剤を用いても脂質汚れの除去
は充分でない場合が多い。1. Removal of lipid stains Lipid stains on clothes are difficult to remove sufficiently by general washing with an anionic surfactant, so a lipase-added detergent was developed. 63-6869
7, US Patent 4011169, British Patent 129361
3) As described above, under conditions where a highly alkaline and high-concentration anionic surfactant is present, it is difficult to sufficiently exhibit its function, and lipase is inactivated by additives such as bleaching agents and fluorescent dyes. Further, lipase, which is a protein itself, may be decomposed and inactivated by a proteolytic enzyme (protease) widely used as a detergent component. Therefore,
In many cases, the removal of lipid stains is not sufficient even with the use of a lipase-mixed detergent.
【0005】2)染色木綿布の柔軟について 染色木綿布は、一般に洗濯を繰り返すと色が白っぽくな
り柔軟性が失われる。陽イオン界面活性剤を有効成分と
する従来のすすぎ剤では柔軟性は或程度回復するが、色
調は回復しない。セルラーゼを洗剤に配合して柔軟性を
回復させる方法が提案されているが(英国特許1368
599、特公昭61−16316)、前述のリパーゼと
同様に高アルカリ性且つ高濃度の陰イオン界面活性剤が
存在する条件下では、セルラーゼの機能が充分発揮され
ず、洗剤添加成分である蛋白分解酵素プロテアーゼ、漂
白剤、蛍光染料、香料等により失活する場合もあり期待
した通りの効果が得られていない。かかる状況に鑑み、
本発明が解決しようとする課題は、布、衣類等に付着し
た脂質汚れの除去及び染色木綿布等の柔軟性の回復と、
白っぽくなった色調の回復を効果的に行う方法を確立す
ることである。2) Softness of dyed cotton cloth Generally, when dyed cotton cloth is repeatedly washed, its color becomes whitish and its flexibility is lost. A conventional rinse agent containing a cationic surfactant as an active ingredient recovers flexibility to some extent, but not color tone. A method of recovering flexibility by incorporating cellulase into a detergent has been proposed (British Patent 1368).
599, Japanese Examined Patent Publication No. 61-16316), in the presence of a highly alkaline and high-concentration anionic surfactant as in the case of the lipase described above, the function of cellulase is not sufficiently exerted, and a proteolytic enzyme which is a detergent additive component. It may be inactivated by protease, bleaching agent, fluorescent dye, fragrance, etc., and the expected effect is not obtained. In view of this situation,
The problem to be solved by the present invention is to remove lipid stains adhering to cloth, clothes and the like and to restore the flexibility of dyed cotton cloth,
The aim is to establish a method for effectively recovering the white color.
【0006】[0006]
【課題を解決する手段】本発明者は上記課題の解決の為
種々研究を重ねた結果、リパーゼの機能を充分に発揮し
易い条件の揃うすすぎ工程に、リパーゼを使用すること
により衣類の脂質汚れが効果的に除去され、また、セル
ラーゼを洗濯すすぎ工程に使用することにより染色木綿
布の柔軟性の回復と、白っぽくなった色調の回復をさせ
ることに成功した。即ち、本発明は、洗濯すすぎ液中
に、リパーゼの少なくとも1種を30〜8,000LU
/L及び/又はセルラーゼの少なくとも1種を5〜20
0CU/L添加することを特徴とする洗濯すすぎ方法及
びかかる目的に使用するリパーゼ及びセルラーゼの少な
くとも1種を含む洗濯すすぎ剤を提供せんとするもので
ある。Means for Solving the Problems The inventors of the present invention have conducted various studies to solve the above problems, and as a result, by using lipase in a rinsing step in which the conditions where the function of lipase is easily exhibited sufficiently, lipid stains on clothes can be obtained. Was effectively removed, and by using cellulase in the washing and rinsing process, the softness of the dyed cotton cloth was restored, and the whitish color tone was restored. That is, the present invention provides 30 to 8,000 LU of at least one lipase in the wash rinsing solution.
/ L and / or at least one cellulase of 5 to 20
The present invention provides a laundry rinsing method characterized by adding 0 CU / L, and a laundry rinsing agent containing at least one of lipase and cellulase used for such purpose.
【0007】以下、本発明について更に詳細に説明す
る。本発明に使用されるリパーゼは、弱アルカリ性(p
H7.0〜8.0程度)で活性を有するリパーゼであれ
ば、必ずしも制限はなく使用可能であるが、特にトリグ
リセリド分解性能の高いリパーゼ(トリアシルグリセロ
ール・リパーゼ)が望ましい。尚、酸性或いは高アルカ
リ性で最高活性を示すリパーゼであっても、弱アルカリ
性で実用に充分な活性を示すリパーゼであれば当然使用
できる。The present invention will be described in more detail below. The lipase used in the present invention is weakly alkaline (p
A lipase having an activity of about H 7.0 to 8.0) can be used without any limitation, but a lipase (triacylglycerol lipase) having a high triglyceride decomposing ability is particularly preferable. It should be noted that even a lipase that exhibits the highest activity under acidic or highly alkaline conditions can naturally be used as long as it is weakly alkaline and exhibits sufficient activity for practical use.
【0008】本発明に使用されるリパーゼについて代表
的なものを示せば、例えば、動物由来のもとしては豚の
すい臓より抽出したリパーゼ(Pancreatic
lypase)、植物由来のもとしては小麦胚芽より抽
出したリパーゼ、微生物由来のもとしてはキャンディダ
・シリンドラセア(Candida cylindra
cea)の産生するリパーゼ、キャンディダ・リポリテ
ィカ(Candidalipolytica)の産生す
るリパーゼ、リゾプス・アルヒザス(Rhizopus
arrhizus)の産生するリパーゼ、リゾプス・
デェレマー(Rhizopus delemar)の産
生するリパーゼ、リゾプス・ニヴェウス(Rhizop
us niveus)の産生するリパーゼ、クロモバク
テリウム・ビスコサム(Chromodacte−ri
um Viscosum)の産生するリパーゼ、ムコー
ル・ミエイ(Mucor miehei)の産生するリ
パーゼ、ムコール・プシラス(Mucor pusil
las)の産生するリパーゼ、シュウドモナス・メフィ
チカ(Pseudomonas mephitica)
の産生するリパーゼ、フミコーラ・ラヌギノザ(Hum
icola lanuginosa)の産生するリパー
ゼ、フミコーラ・インソレンス(Humicola i
nsolens)の産生するリパーゼ、フミコーラ・ブ
レビスポラ(Humicola brevispor
a)の産生するリパーゼ、フザリウム・オキシスポラム
(Fusarium oxysporum)の産生する
リパーゼ、アスペルギラス・ニガー(Aspergil
lus niger)の産生するリパーゼ、アスペルギ
ラス・オリゼー(Aspergillus oryze
a)の産生するリパーゼ等が使用できる。これらのリパ
ーゼは、着色成分を除去し可及的高純度で使用すること
が望ましいのは当然である。Typical examples of the lipase used in the present invention include, for example, lipase (Pancreatic) extracted from pig pancreas, which is of animal origin.
lyase), lipase extracted from wheat germ as plant-derived one, and Candida cylindrace as microbial-derived one.
cea) produced by Candida lipolytica, Rhizopus lipase produced by Candida lipolytica
lipase produced by arrhizus), Rhizopus
Rhizop, a lipase produced by Rhizopus delemar
lipase produced by us niveus, Chromodoacte-ri
um Viscosum) -produced lipase, Mucor miehei-produced lipase, Mucor pusil (Mucor pusil)
Las) -produced lipase, Pseudomonas mephitica
Produced by Humicola lanuginosa (Hum
Humicola insolens (Humicola i), a lipase produced by icola lanuginosa
Humicola brevispor, lipase produced by Nsolens
a) lipase produced by Fusarium oxysporum, Aspergillus niger
Aspergillus oryze, a lipase produced by L. niger
The lipase produced by a) can be used. As a matter of course, it is desirable that these lipases be used in the highest possible purity by removing the coloring components.
【0009】本発明におけるリパーゼの使用量として
は、必ずしも厳密な制限はないが、一つの目安として、
すすぎ液における初期のリパーゼ活性が1リットル当た
り30〜8,000LU、より好ましくは300〜4,
000LUとなるように用いるのが適当である。尚、リ
パーゼ活性の単位LU(Lipase Unit)は、
トリブチリンをPVAを乳化剤としてpH7,温度37
℃で作用させた場合、1分間に1.0マイクロモル当量
の脂肪酸を遊離する酵素の力価を1単位とする。(酵素
利用ハンドブック、地人書館、昭和56年、230頁参
照)The amount of lipase used in the present invention is not necessarily strictly limited, but as one guideline,
The initial lipase activity in the rinse solution is 30 to 8,000 LU per liter, more preferably 300 to 4,
It is suitable to use it so that it becomes 000 LU. The unit LU (Lipase Unit) of lipase activity is
Tributyrin with PVA as an emulsifier, pH 7, temperature 37
When it is allowed to act at 0 ° C, the titer of the enzyme that releases 1.0 micromolar equivalent of fatty acid per minute is defined as 1 unit. (See page 230, Enzyme Handbook, Jijijinkan, 1981)
【0010】また、本発明に使用されるセルラーゼとし
ては、弱アルカリ性で結晶性のセルロースを分解する能
力を有するセルラーゼであれば必ずしも制限はなく使用
できる。本発明に使用されるセルラーゼについて代表的
なものを示せば、例えば、トリコデルマ・ビリデ(Tr
ichoderma viride)の産生するセルラ
ーゼ,アスペルギラス・ニガー(Aspergillu
s niger)の産生するセルラーゼ,アスペルギラ
ス・ソヤ(Aspergillus sojae)の産
生するセルラーゼ、アスペルギラス・テレウス(Asp
ergillus terreus)の産生するセルラ
ーゼ、ペニシリウム・フニクロサム(Penicill
ium funiculosum)の産生するセルラー
ゼ、ペニシリウム・プシラム(penicilluiu
m pusillum)の産生するセルラーゼ、フミコ
ーラ・イソレンス(Humicola isolen
s)の産生するセルラーゼ、フサリウム・モニリフォル
ム(Fusarium moniliforme)の産
生するセルラーゼ、リゾプス・デレマー(Rhizop
us delemar)の産生するセルラーゼ、スポロ
トリカム・ディモルフォスポラム(Sporotric
hum dimorphosporum)の産生するセ
ルラーゼ等が使用できる。これらのセルラーゼは、リパ
ーゼと同様に着色成分を除去し可及的高純度で使用する
ことが望ましい。The cellulase used in the present invention can be used without limitation as long as it is a cellulase having a weak alkaline and ability to decompose crystalline cellulose. Typical examples of the cellulase used in the present invention are shown in, for example, Trichoderma viride (Tr
Aspergillus niger (Aspergillus niger) produced by ichoderma viride
cellulase produced by Aspergillus sojae, Aspergillus terreus (Asp) produced by Aspergillus sojae
ergillus terreus cellulase, Penicillium funiculosum
cellulase produced by ium funiculosum, penicillium
Humicola isolen, a cellulase produced by M. pusillum.
cellulase produced by s), a cellulase produced by Fusarium moniliforme, Rhizopus delemer (Rhizop)
cellulase produced by Us delemar, Sporotrichum dimorphosporum (Sporotric)
and cellulase produced by hum dimorphosporum) can be used. It is desirable that these cellulases be used in the highest possible purity by removing the coloring components as in the case of lipase.
【0011】本発明におけるセルラーゼの使用量として
は、必ずしも厳密な制限はないが、一つの目安として、
すすぎ液における初期のセルラーゼ活性が1リットル当
たり5〜200CU、より好ましくは20〜80CUと
なるように用いる。尚、セルラーゼ活性の単位CU(C
ellulase Unit)は、エーテル化度0.5
5〜0.65のCMCを基質として、温度50℃,pH
7で作用させた場合、1分間にグルコース1.0マイク
ロモル当量に相当する還元糖を遊離させる酵素の力価を
1CUとする(酵素利用ハンドブック、地人書館、昭和
56年,301頁参照)。The amount of cellulase used in the present invention is not strictly limited, but one guideline is as follows.
It is used so that the initial cellulase activity in the rinse solution is 5 to 200 CU per liter, more preferably 20 to 80 CU. The unit of cellulase activity, CU (C
ellulase Unit) has an etherification degree of 0.5
Using CMC of 5 to 0.65 as a substrate, temperature 50 ° C, pH
When 7 is used, the titer of the enzyme that liberates reducing sugar equivalent to 1.0 micromolar equivalent of glucose per minute is 1 CU (see Handbook of Enzyme Use, Jijijinkan, 1981, p. 301). .
【0012】本発明に係わるすすぎ剤は、主成分として
リパーゼまたはセルラーゼの少なくとも一種、或いは両
者を含む液状或いは顆粒状の組成物として使用する。液
状の場合は、酵素の保存安定性を計る為ジオール、ポリ
オール、例えばエチレングリコールの含水溶液が使用さ
れる。また、保存安定剤として酵素によっては、少量の
カルシウム塩、ほう酸塩、蟻酸、中性界面活性剤の添加
が有効な場合がある。必要によっては、酵素をマイクロ
カプセル化したり、グリコール中に懸濁状態として保存
安定性を高めることも出来る。The rinsing agent according to the present invention is used as a liquid or granular composition containing, as a main component, at least one of lipase and cellulase, or both. In the case of a liquid, an aqueous solution of a diol or a polyol such as ethylene glycol is used to measure the storage stability of the enzyme. Depending on the enzyme, it may be effective to add a small amount of calcium salt, borate, formic acid, or a neutral surfactant as a storage stabilizer. If necessary, the enzyme can be microencapsulated or suspended in glycol to improve storage stability.
【0013】酵素は、乾燥状態では比較的安定であるた
め、粒剤の保存安定性は良好であるが、溶解性を考慮す
る必要がある。賦形材としては、乳糖、スターチ、塩化
ナトリウム、硫酸ナトリウム等を使用することが出来
る。また、粒剤の分解性を良くし、且つ酵素の分散性を
良くするため、少量の中性界面活性剤、或いは陽イオン
界面活性剤を使用することも出来る。また、洗濯仕上が
りを良くする為、少量の香料、漂白剤、蛍光染料等も酵
素を阻害しない限り本発明のすすぎ剤に添加することが
出来る。Since the enzyme is relatively stable in a dry state, the storage stability of the granule is good, but the solubility must be taken into consideration. Lactose, starch, sodium chloride, sodium sulfate and the like can be used as the excipient. Further, in order to improve the degradability of the granule and the dispersibility of the enzyme, it is possible to use a small amount of a neutral surfactant or a cationic surfactant. Further, in order to improve the washing finish, a small amount of perfume, bleaching agent, fluorescent dye or the like can be added to the rinse agent of the present invention as long as it does not inhibit the enzyme.
【0014】製剤品中のリパーゼ及びセルラーゼの組成
については、必ずしも制限はないが通常は、リパーゼに
ついては製剤1ml当たり300〜80,000LU、
より好ましくは3,000〜40,000LU、また、
セルラーゼの組成については製剤1ml当たり50〜
2,000CU、より好ましくは200〜800CUと
なるように用いるのが適当であり、使用に際しては5,
000〜15,000倍通常は1万倍程度に希釈、即
ち、洗濯すすぎ液10リットル当たり1ミリリットル程
度の量が用いられる。The composition of lipase and cellulase in the preparation is not necessarily limited, but normally, lipase is usually 300 to 80,000 LU per 1 ml of the preparation,
More preferably 3,000-40,000 LU,
The composition of cellulase is 50 ~ per 1 ml of the preparation.
It is suitable to use 2,000 CU, more preferably 200 to 800 CU.
000 to 15,000 times, usually diluted about 10,000 times, that is, an amount of about 1 milliliter per 10 liters of the washing and rinsing liquid is used.
【0015】[0015]
【実施例】以下に代表的な実施例を示し、本発明につい
て更に具体的に説明する。但し、これらは本発明につい
ての理解を容易にする為の単なる例示であり、従って、
本発明はこれらのみに限定されないことは勿論のこと、
これらの例によって何ら制限されないことはで言うまで
もない。EXAMPLES The present invention will be described more specifically by showing typical examples below. However, these are merely examples for facilitating the understanding of the present invention, and therefore,
Of course, the present invention is not limited to these,
It goes without saying that these examples are not limiting in any way.
【0016】実施例 1 試験布としては、10cm×10cmの寸法の木綿布に
オリーブオイル300mgを含浸後、室温で約1週間程
放置したものを用いた。オリーブオイルの含浸量は、含
浸時に正確に秤量脂、各試験布ごとに記録した。この試
験布をソックスレー抽出器を用い、ノルマルヘキサン抽
出し高速液クロマトグラフィーにてオリーブオイル定量
すると、回収率は平均96%であった。この試験布を、
Terg−0−Tometer試験器で、洗浄した。Example 1 As a test cloth, a cotton cloth having a size of 10 cm × 10 cm impregnated with 300 mg of olive oil and left at room temperature for about 1 week was used. The amount of olive oil impregnated was accurately recorded for each test cloth when weighed with fat. When this test cloth was extracted with normal hexane using a Soxhlet extractor and olive oil was quantified by high performance liquid chromatography, the recovery rate was 96% on average. This test cloth
Washed on Terg-0-Tometer tester.
【0017】洗浄条件は下記の様である: 洗剤 :JIS K3371無リン洗剤 洗剤濃度:0.133% 温度 :30℃ 時間 :15分間 反転数 :105CPM 浴比 :6枚/1000ml 尚、JISK3371記載の洗剤組成は、LAS15
%、ゼオライト17%、珪酸ナトリウム5%、炭酸ナト
リウム3%、CMC1%、残り硫酸ナトリウムである。The washing conditions are as follows: Detergent: JIS K3371 phosphorus-free detergent Detergent concentration: 0.133% Temperature: 30 ° C. Time: 15 minutes Reversal number: 105 CPM Bath ratio: 6 sheets / 1000 ml Incidentally, JISK3371 description The detergent composition is LAS15
%, Zeolite 17%, sodium silicate 5%, sodium carbonate 3%, CMC 1%, and the remaining sodium sulfate.
【0018】次に、下記成分のすすぎ剤を用いてすすぎ
を行った。 すすぎ剤組成: リパーゼ(Candida cylindracea
由来):25,000LU/ml セルラーゼ(Fusarium moniformi由
来):300CU/ml トライトンX−207 :1.5容量% 酢酸カルシウム :0.6g/1
000ml エチレングリコール :65容量% 水分 :バランス すすぎ条件は下記の様である: すすぎ剤濃度:0.01%(第1回目) すすぎ時間 :5分間 反転数 :105CPM 繰り返し数 :3回 但し、すすぎ剤は、第1回目のすすぎについてのみ添加
した。すすぎ終了後、試験布は室温で風乾した。Next, rinsing was performed using the rinsing agents of the following components. Rinse agent composition: lipase (Candida cylindracea)
Derived): 25,000 LU / ml Cellulase (from Fusarium monoformi): 300 CU / ml Triton X-207: 1.5% by volume calcium acetate: 0.6 g / 1
000 ml Ethylene glycol: 65% by volume Moisture: Balance Rinsing conditions are as follows: Rinsing agent concentration: 0.01% (1st time) Rinsing time: 5 minutes Inversion number: 105 CPM Repeat number: 3 times However, rinsing agent Was added only for the first rinse. After the rinsing was completed, the test cloth was air dried at room temperature.
【0019】上記操作による洗浄−すすぎ−乾燥を3回
繰り返した後、試験布に残留している油脂分をソックス
レー抽出器を用い、ノルマルヘキサンで抽出した。ノル
マルヘキサン抽出液は、濃縮後常法に従い高速液体クロ
マトグラフィーで定量した。その結果、トリグリセリ
ド、ジグリセリド、モノグリセリドの合計を残留油脂分
とした場合、残留油脂分量の初期油脂分量に対する割合
は平均31%であった。尚、初期油脂分量は、オリーブ
オイルの試験布含浸量に平均回収率96%を乗じ値とし
た。After washing, rinsing, and drying were repeated three times by the above operation, the oil and fat remaining on the test cloth was extracted with normal hexane using a Soxhlet extractor. The normal hexane extract was concentrated and then quantified by high performance liquid chromatography according to a conventional method. As a result, when the total amount of triglyceride, diglyceride and monoglyceride was used as the residual oil and fat content, the ratio of the residual oil and fat content to the initial oil and fat content was 31% on average. The initial amount of oil / fat was determined by multiplying the amount of olive oil impregnated with the test cloth by an average recovery rate of 96%.
【0020】実施例 2 すすぎ剤の効果を調べる為にすすぎ剤を使用せず、実施
例1と同様な操作を行ったところ残留油脂成分量の初期
油脂分量に対する割合は平均53%であった。Example 2 In order to investigate the effect of the rinsing agent, the same operation as in Example 1 was carried out without using the rinsing agent, and the ratio of the residual oil and fat component amount to the initial oil and fat content was 53% on average.
【0021】実施例 3 緑色の木綿タオルを、市販の粉石鹸を用いて市販全自動
洗濯機で洗濯し天日乾燥した。この洗濯を25回繰り返
したところ、タオル地は柔軟感が失われ、且つ緑色の色
調も白っぽくなった。このタオル地を10cm×10c
mの正方形に切断し、オリーブオイル350mgを含浸
させ1週間室温で放置したものを試験布とした。尚、ノ
ルマルヘキサン抽出によるオリーブオイルの回収率は、
平均95%であった。この試験布を用いて、浴比を3枚
/1000mlとした以外は実施例1と同様な条件で洗
浄を行った。Example 3 A green cotton towel was washed in a commercially available fully automatic washing machine with commercially available powdered soap and dried in the sun. When this washing was repeated 25 times, the towel cloth lost its softness and the green color tone became whitish. This towel cloth is 10cm × 10c
A test cloth was cut into m squares, impregnated with 350 mg of olive oil, and allowed to stand at room temperature for 1 week. The recovery rate of olive oil by normal hexane extraction is
The average was 95%. Using this test cloth, washing was performed under the same conditions as in Example 1 except that the bath ratio was 3 sheets / 1000 ml.
【0022】次いで、下記組成のすすぎ剤を用いてすす
ぎを行った。 すすぎ剤組成: リパーゼ(Pseudmonas mephitica
由来):32,000LU/ml セルラーゼ(Trichoderma viride
由来):480CU/ml トライトンX−207 :2.5容量
% エチレングリコール :62 容量
% 水分 :バランス すすぎの条件及び乾燥条件は、実施例1と同様であっ
た。Next, rinsing was performed using a rinsing agent having the following composition. Rinse Agent Composition: Lipase (Pseudomonas mephitica)
Origin: 32,000 LU / ml cellulase (Trichoderma viride)
Origin): 480 CU / ml Triton X-207: 2.5% by volume Ethylene glycol: 62% by volume Moisture: Balance The conditions of rinsing and drying were the same as in Example 1.
【0023】洗濯−すすぎ−乾燥の操作を3回繰り返し
た後に、柔軟性の回復と色調の回復について評価した。
評価の結果は実施例4に纏めてある。柔軟性と色調を評
価した後に、試験布をソックスレー抽出器を用いノルマ
ルヘキサンで抽出し油脂分を測定したところ、残留油脂
分量の初期油脂分量に対する割合は平均36%であっ
た。After the washing-rinsing-drying operation was repeated three times, the recovery of flexibility and the recovery of color tone were evaluated.
The evaluation results are summarized in Example 4. After evaluating the flexibility and color tone, the test cloth was extracted with normal hexane using a Soxhlet extractor, and the oil and fat content was measured. The ratio of the residual oil and fat content to the initial oil and fat content was 36% on average.
【0024】実施例 4 市販の柔軟仕上げ剤を用いた以外は、実施例3と同様に
して洗濯−すすぎ−乾燥を行った。すすぎは市販の柔軟
仕上げ剤(主成分:陽イオン表面活性剤)を添付された
使用説明書に従い、第1回目のすすぎに0.022%
(0.22ml/1000ml)使用した。Example 4 Washing-rinsing-drying was performed in the same manner as in Example 3 except that a commercially available softening agent was used. Rinse is 0.022% for the first rinse according to the instructions attached with a commercially available softening agent (main component: cationic surfactant).
(0.22 ml / 1000 ml) was used.
【0025】洗濯−すすぎ−乾燥を3回繰り返した後、
得られた試験布を実施例3で得られた試験布と比較し、
柔軟性、色調を12人からなるパネルにより評価した。
結果を以下に示す。(柔軟性回復の評価−12人の評価分布) 実施例3サンプル:変わらず 0、やや良い 3、良い
6、非常に良い 3 実施例4サンプル:変わらず 0、やや良い 4、良い
7、非常に良い 1(色調回復の評価−12人の評価分布) 実施例3サンプル:変わらず 3、やや良い 5、良い
4 実施例4サンプル:変わらず11、やや良い 1、良い
0After repeating washing-rinsing-drying three times,
The test cloth obtained was compared with the test cloth obtained in Example 3,
The flexibility and color tone were evaluated by a panel of 12 people.
The results are shown below. (Evaluation of recovery of flexibility-12 people's evaluation distribution) Example 3 sample: 0 unchanged, somewhat good 3, good 6, very good 3 Example 4 sample: 0 unchanged, slightly good 4, good 7, very good Good 1 (Evaluation of color tone recovery-12 people's evaluation distribution) Example 3 sample: unchanged 3, somewhat good 5, good 4 Example 4 sample: unchanged 11, slightly good 1, good 0
【0026】パネルによる評価結果は、柔軟性の回復に
付いては陽イオン柔軟仕上剤と同等の効果であるが、色
調の回復に付いては本発明によるすすぎ剤が、優れた効
果を示している。パネル評価の終了後、実施例4サンプ
ルを、ソックスレー抽出器を用いノルマルヘキサンで抽
出し残留油脂分を定量した。残留油脂分量の初期油脂分
量に対する割合は平均59%であった。The results of the evaluation by the panel show that the softening agent has the same effect as that of the cationic softening finishing agent, but the rinsing agent of the present invention has an excellent effect of restoring the color tone. There is. After the panel evaluation was completed, the sample of Example 4 was extracted with normal hexane using a Soxhlet extractor to quantify the residual oil and fat content. The ratio of the residual oil / fat content to the initial oil / fat content was 59% on average.
Claims (2)
解酵素(リパーゼ)及び弱アルカリ性条件下で活性を有
するセルローズ分解酵素(セルラーゼ)の少なくとも1
種を含む洗濯すすぎ剤。At least one of a lipolytic enzyme (lipase) having an activity under weak alkaline conditions and a cellulolytic enzyme (cellulase) having an activity under weak alkaline conditions.
Laundry rinse containing seeds.
活性を有する脂質分解酵素(リパーゼ)の少なくとも1
種を30〜8,000LU/L及び/又は弱アルカリ性
条件下で活性を有するセルローズ分解酵素(セルラー
ゼ)の少なくとも1種を5〜200CU/L添加してす
すぎを行うことを特徴とする洗濯すすぎ方法。2. At least one of lipolytic enzymes (lipases) having activity in mildly alkaline conditions in a wash rinsing solution.
30 to 8,000 LU / L and / or 5 to 200 CU / L of at least one cellulolytic enzyme (cellulase) having activity under weakly alkaline conditions, and rinsing is carried out, characterized by comprising rinsing .
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP5273262A JPH0790300A (en) | 1993-09-24 | 1993-09-24 | Washing agent and washing method |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP5273262A JPH0790300A (en) | 1993-09-24 | 1993-09-24 | Washing agent and washing method |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH0790300A true JPH0790300A (en) | 1995-04-04 |
Family
ID=17525384
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP5273262A Pending JPH0790300A (en) | 1993-09-24 | 1993-09-24 | Washing agent and washing method |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0790300A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0976838A1 (en) * | 1998-05-06 | 2000-02-02 | Rhone-Poulenc Nutrition Animale | Enzymes mixture |
| DE102024208390A1 (en) | 2024-09-04 | 2026-03-05 | Henkel Ag & Co. Kgaa | Textile washing processes |
-
1993
- 1993-09-24 JP JP5273262A patent/JPH0790300A/en active Pending
Cited By (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0976838A1 (en) * | 1998-05-06 | 2000-02-02 | Rhone-Poulenc Nutrition Animale | Enzymes mixture |
| WO1999057325A3 (en) * | 1998-05-06 | 2000-04-06 | Rhone Poulenc Animal Nutrition | Enzymes mixture |
| DE102024208390A1 (en) | 2024-09-04 | 2026-03-05 | Henkel Ag & Co. Kgaa | Textile washing processes |
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