EP4134423A1 - Composition de prétraitement de blanchisserie pulvérisable - Google Patents

Composition de prétraitement de blanchisserie pulvérisable Download PDF

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Publication number
EP4134423A1
EP4134423A1 EP21190970.0A EP21190970A EP4134423A1 EP 4134423 A1 EP4134423 A1 EP 4134423A1 EP 21190970 A EP21190970 A EP 21190970A EP 4134423 A1 EP4134423 A1 EP 4134423A1
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EP
European Patent Office
Prior art keywords
composition
stains
enzyme
acid
forgoing
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EP21190970.0A
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German (de)
English (en)
Inventor
William Shore
Mika Zammit
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Henkel AG and Co KGaA
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Henkel AG and Co KGaA
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Priority to EP21190970.0A priority Critical patent/EP4134423A1/fr
Priority to AU2022207323A priority patent/AU2022207323A1/en
Publication of EP4134423A1 publication Critical patent/EP4134423A1/fr
Pending legal-status Critical Current

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    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/0043—For use with aerosol devices
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2065—Polyhydric alcohols
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/22—Carbohydrates or derivatives thereof
    • C11D3/222—Natural or synthetic polysaccharides, e.g. cellulose, starch, gum, alginic acid or cyclodextrin
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/38—Products with no well-defined composition, e.g. natural products
    • C11D3/386—Preparations containing enzymes, e.g. protease or amylase
    • C11D3/38663—Stabilised liquid enzyme compositions
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2075—Carboxylic acids-salts thereof
    • C11D3/2082—Polycarboxylic acids-salts thereof
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/16—Organic compounds
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2075—Carboxylic acids-salts thereof
    • C11D3/2086—Hydroxy carboxylic acids-salts thereof
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
    • C11D3/48—Medical, disinfecting agents, disinfecting, antibacterial, germicidal or antimicrobial compositions

Definitions

  • the present invention refers to a sprayable aqueous laundry pre-treatment composition comprising a multi-enzyme blend and Xanthan gum, a method for and the use of the inventive composition in stain removal as well as an aerosol dispenser comprising the inventive composition.
  • Removal of difficult stains is usually attempted in two steps.
  • the stained fabric is contacted with a stain-removing pretreatment composition.
  • the pretreated fabric is then washed with a laundry detergent composition or dry cleaned.
  • US 4,648,987 introduces a laundry prewash composition having a suitable detergency for dealing with a variety of spots and stains normally encountered in various fabrics, the composition being thickened to enhance its localized application to the fabric spots and stains.
  • the suggested aqueous laundry prewash composition comprises a cosurfactant system including a first hydrophobic nonionic surfactant for loosening oil soluble material from the fabric and a second hydrophilic nonionic surfactant for loosening water soluble material from the fabric, the hydrophobic nonionic surfactant being an oil soluble ethoxylated alcohol with about eight to eighteen carbon atoms and an average of about two to five ethylene oxide groups per molecule, the hydrophilic nonionic surfactant being a water soluble ethoxylated alcohol with about eight to eighteen carbon atoms and an average of about five to fifteen ethylene oxide groups per molecule, the cosurfactant system forming about 3.7-10.5 wt.-% of the composition, a hydrotrope
  • WO 2016/202572 relates to a laundry pretreatment composition which is claimed to be especially useful against stained cotton or polycotton fabrics.
  • the pretreatment composition disclosed comprises 0.5 to 15 wt.-% of a surfactant which is a non-ionic surfactant or an ethoxylated anionic surfactant; 0.5 to 8 wt.-% of at least one non-neutralized fatty acid having a pKa greater than 5 at 20 °C, 0.5 to 5 wt.-% of at least one organic acid having a pKa of 2 to 5 at 20 °C; and 0.5 to 10 wt.-% of a water-insoluble fatty acid ester.
  • a surfactant which is a non-ionic surfactant or an ethoxylated anionic surfactant
  • 0.5 to 8 wt.-% of at least one non-neutralized fatty acid having a pKa greater than 5 at 20 °C 0.5 to 5 wt.-
  • Detergent enzymes are biological enzymes that are used with detergents. They catalyze the reaction between stains and water, thus aiding in stain removal.
  • the use of enzymes in detergents has a number of advantages. For example, the water temperature for washing can be reduced by using detergent enzymes which perform well in cold water, allowing low-temperature washes and eliminating the need for heated water. Further, delicate materials such as wool or silk can be damaged or fade in high-temperature washes. Low-temperature washes with detergent enzymes can prevent such damages, allowing the consumer to choose clothes from a wider range of materials.
  • Enzymes can act as respiratory sensitizers and at high concentrations proteolytic enzymes can also irritate skin and eyes.
  • enzyme-containing spray products for household cleaning must meet various REACH requirements and suppliers of enzymes as well as downstream users have obligations related to these requirements.
  • an assessment of the airborne enzyme exposure must be conducted when including enzymes in sprayable products. Enzyme exposure, expressed as concentration of airborne enzyme protein, of consumers and professionals derived from use of spray products must be evaluated to demonstrate safety prior to marketing.
  • D.A. Basketter et al conducted several studies which are summarized in "Studies conducted for defining occupational and consumer exposure limits for enzyme protein respiratory allergens under REACH", Toxicology 268 (2010) 165-170 . According to the conducted studies, the highest levels of exposure were observed with laundry trigger sprays.
  • foams One approach to reduce the generation of enzyme-bearing aerosols is the use of foams.
  • foam products tend to sit on the surface of the fabric rather than penetrating the stain and are thus less effective as stain removers for fabrics.
  • a sprayable laundry pre-treatment composition which comprises a multi-enzyme blend for effective stain removal while the formation of aerosols is decreased by incorporating Xanthan gum.
  • a first object of the present invention is therefore a sprayable aqueous laundry pre-treatment composition comprising:
  • Laundry pre-treatment sprays should generally be able to remove different kinds of stains.
  • stain sheets have been established which comprise stains of natural oils such as olive oil, mechanical oils, sebaceous stains as well stains caused by everyday occurrences such as coffee or make-up. It was surprisingly found that the variety of stains could be effectively removed using a multi-enzyme blend which comprises multiple enzymes which target different stain sources such as protein, starch, pectin, gum, fat, oil, and grease, with protein being one of the major concerns as they are found in sweat, blood, grass, chocolate, dairy products and coffee.
  • the multi-enzyme blend comprises protease and at least one further enzyme selected from the group consisting of amylase, lipase, pectate lyase, serine endoprotease, cellulase and mannanase.
  • proteases to be used in the present invention are the subtilisins BPN' from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis, the protease PB92, the subtilisins 147 and 309, the protease from Bacillus lentus, subtilisin DY and the enzymes thermitase, proteinase K and the proteases TW3 and TW7, which can be assigned to subtilases but no longer to subtilisins in the narrower sense.
  • Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase ® from the company Novozymes.
  • Subtilisins 147 and 309 are marketed under the trade names Esperase ® and Savinase ® , respectively, by Novozymes.
  • Protease variants are derived from the protease from Bacillus lentus DSM 5483.
  • Other useful proteases are e.g.
  • proteases marketed under the trade names Durazym ® , Relase ® , Everlase ® , Nafizym ® , Natalase ® , Kannase ® , Progress Uno 101L ® and Ovozyme ® by the company Novozymes the proteases marketed under the trade names Purafect ® , Purafect ® OxP, Purafect ® Prime, Excellase ® , Properase ® , Preference P100 ® and Preference P300 ® from Danisco/DuPont, Lavergy pro 104 LS ® from BASF, Protosol ® from Advanced Biochemicals Ltd., the enzymes available under the trade name Wuxi@ from Wuxi Snyder Bioproducts Ltd, the enzymes available under the trade names Proleather ® and Protease P ® from Amano Pharmaceuticals Ltd, and the enzyme available under the trade name Proteinase K-16 from Kao Corp.
  • proteases from Bacillus gibsonii and Bacillus pumilus which are disclosed in WO 2008/086916 , WO 2007/131656 , WO 2017/215925 , PCT/EP2021/054688 and PCT/EP2021/054689 .
  • Further advantageously applicable proteases are disclosed in, for example. WO 91/02792 , WO 2008/007319 , WO 93/18140 , WO 01/44452 , GB 1243784 A , WO 96/34946 , WO 02/029024 and WO 03/057246 .
  • Stenotrophomonas maltophilia in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius, Bacillus lichenformis as well as Bacillus sphaericus.
  • Suitable lipases to be used in the present invention include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa ) as described in EP 0258068 and EP 0305216 , lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g., P. alcaligenes or P. pseudoalcaligenes ( EP 0218272 ), P. cepacia ( EP 0331376 ), P. sp.
  • Thermomyces e.g. from T. lanuginosus (previously named Humicola lanuginosa ) as described in EP 0258068 and EP 0305216
  • lipase from strains of Pseudomonas some of these now renamed to Burkholderi
  • strain SD705 ( WO 95/06720 & WO 96/27002 ), P. wisconsinensis ( WO 96/12012 ), GDSL-type Streptomyces lipases ( WO 2010/065455 ), lipase from Thermobifida fusca ( WO 2011/084412 ), Geobacillus stearothermophilus lipase ( WO 2011/084417 ), lipase from Bacillus subtilis ( WO 2011/084599 ), and lipase from Streptomyces griseus ( WO 2011/150157 ) and S. pristinaespiralis ( WO 2012/137147 ).
  • Preferred lipases include, for example, those originally obtainable from Humicola lanuginosa ( Thermomyces lanuginosus ) or further developed therefrom, in particular those with one or more of the following amino acid exchanges starting from the said lipase in positions D96L, T213R and/or N233R, particularly preferably T213R and N233R.
  • Lipases are marketed, for example, by the company Novozymes under the trade names Lipolase ® , Lipolase ® Ultra, LipoPrime ® , Lipozyme ® and Lipex ® .
  • Another advantageously applicable lipase is available under the trade name Lipoclean ® from the company Novozymes.
  • Preferred commercial lipase products include Lipolase TM , Lipex TM , Lipolex TM and Lipoclean TM (Novozymes A/S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades).
  • Suitable pectate lyases for use in the present invention are in particular pectate lyase (EC 4.2.2.2) which catalyzes the eliminative cleavage of (1,4)-alpha-D-glacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
  • pectate transeliminase polygalacturonic transeliminase and endopectin methyltranseliminase.
  • the systematic name is (1,4)-alpha-D-galacturonan lyase.
  • preference is given to pectate lyase derived from Bacillus.
  • Particular preference is given to XPect 1000L as commercially available from Novozymes, Denmark.
  • Amylases for use in the present invention may also be referred to by synonymous terms, for example, 1,4- ⁇ -D-glucan glucanohydrolase or glycogenase.
  • Amylases preferred according to the invention are alpha-amylases.
  • the decisive factor in determining whether an enzyme is an alpha-amylase within the meaning of the invention is its ability to hydrolyze ⁇ -(1,4)-glycoside bonds in poylsaccharides, in particular amylose and starch. In this way, they cause the degradation of starch-containing soils on the cleaning material.
  • the decomposition products are dextrins and maltose, glucose and branched oligosaccharides.
  • amylases are the ⁇ -amylases from Bacillus licheniformis, Bacillus amyloliquefaciens or Bacillus stearothermophilus and, in particular, their further developments improved for use in detergents or cleaning agents.
  • the enzyme from Bacillus licheniformis is available from the company Novozymes under the name Termamyl ® and from the company Danisco/Genencor under the name Purastar ® ST. Further development products of this ⁇ -amylase are available from Novozymes under the trade names Duramyl ® and Termamyl ® ultra, from Danisco/Genencor under the name Purastar ® OxAm and from Daiwa Seiko Inc.
  • Keistase ® The ⁇ -amylase from Bacillus amyloliquefaciens is marketed by the company Novozymes under the name BAN ® , and derived variants of the ⁇ -amylase from Bacillus stearothermophilus under the names BSG ® and Novamyl ® , also from the company Novozymes. Furthermore, the ⁇ -amylase from Bacillus sp. A 7- 7 (DSM 12368) and the cyclodextrin-glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) should be highlighted for this purpose.
  • amylolytic enzymes disclosed in international patent applications WO 2003/002711 , WO 2003/054177 and WO 2007/079938 are applicable, the disclosure of which is therefore expressly referred to or the disclosure content of which is therefore expressly included in the present patent application.
  • fusion products of all the molecules mentioned are applicable.
  • further developments of ⁇ -amylase from Aspergillus niger and A. oryzae available under the trade names Fungamyl ® from the company Novozymes are suitable.
  • Mannanase is defined in the context of the present invention as an enzyme that hydrolyses compounds known as mannans. Mannanases are enzyme catalyzing hydrolyses of 1,4-beta-D-mannosidic linkages in mannans, galactomannans, glucomannans, and galactoglucomannans. Mannans are polysaccharides with a backbone of ⁇ -1,4-linked D-mannopyranosyl residues, which can contain galactose or acetyl substitutions and may have glucose residues in the backbone.
  • the main enzyme type participating in the degradation of mannans are endo-1,4- ⁇ -mannanases (EC 3.2.1.78), which hydrolyze the internal glycoside bonds in the mannan backbone.
  • a mannanase enzyme comprising a polypeptide having mannan endo-1,4-beta-mannosidase activity (EC 3.2.1 .78) that catalyzes the hydrolysis of 1,4-beta-D-mannosidic linkages in mannans, galactomannans and/or glucomannans is preferred.
  • endo-1,4- ⁇ -mannanases can be found in glycoside hydrolase families 5, 26 and 113.
  • Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mannanases are included.
  • the mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B . agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens.
  • Commercially available mannanases are Mannaway (Novozymes A/S), and EFFECTENZ TM M1000 from Dupont.
  • Preferred mannanases include the GH5 mannanase obtained from Bacillus bogoriensis described in WO 1999/064619 .
  • mannanases include any of the GH26 Mannanases, mannanase from Preussia aemulans mature sequence of SEQ ID NO: 2 of WO 2017/021515 , mannanase from Yunnania penicillata mature sequence of SEQ ID NO: 2 of WO 2017/021516 , mannanase from Myrothecium roridum mature sequence of SEQ ID NO: 2 of WO 2017/021517 , mannanase from Chaetomium brasiliense mature sequence of SEQ ID NO: 2 of WO 2017/021518 , mannanases from Ascobolus stictoideus or mannanase from Chaetomium virescens SEQ ID NO: 3 and 6 from WO 2015/040159 .
  • the multi-enzyme blend comprises a mixture of protease, lipase, amylase, pectate lyase and mannanase.
  • stains such as sweat stains, blood, grass, chocolate, dairy products, ready-made sauces, baby foods, dressings, fruit stains, tooth paste, body lotion, grease and oil could be effectively removed.
  • compositions according to the present invention comprise at least one organic acid in an amount of 0.1 to 1.0 wt.-%, based on the total weight of the inventive composition.
  • organic acid is selected from the group consisting of glycolic acid, citric acid, acetic acid, maleic acid, lactic acid and mixtures thereof.
  • citric acid is used due to its favorable chelating properties and odor characteristics.
  • the laundry pre-treatment composition of the present invention is in particular designed for the removal of organic stains.
  • alkaline pH was found to be most effective. Therefore, the inventive composition preferably has a pH of 6 to 10, more preferably 6 to 9.
  • Preferred non-ionic surfactants in the inventive composition are alkoxylated alcohols in which the alkanol is a C9 to C20-alkanol, preferably C12 to C18-alkanol, wherein the number of moles alkylene oxide is from 5 to 20.
  • the alkanol is a fatty alcohol with 10 to 20 carbon atoms, preferably 12 to 18 carbon atoms, and which contain 5 to 9, preferably 5 to 8, alkoxy groups per mole.
  • the composition according to the invention comprises Xanthan gum. It was surprisingly found that by adding Xanthan gum to the composition according to the present invention, the enzyme exposure could be significantly reduced and kept below the threshold of 15 ng/m 3 while at the same time the composition remained sprayable.
  • Xanthan gum is generally believed to have a cellulose-like backbone or chain composed of repeating ⁇ -D-(1,4) glucose units. A side chain is connected to the number three position of every other glucose unit. The side chains consist of a terminal ⁇ -D-mannose unit glycosidically linked to the number 4 position of a ⁇ -D-glucuronic acid which in turn is linked to the number 2 position of an ⁇ -D-mannose unit that contains an acetyl group at the number 6 position.
  • the composition according to the invention comprises Xantham gum in an amount of at least 0.15 wt.-%, preferably in an amount of 0.2 to 1.0 wt.-%, based on the total weight of the sprayable composition. It was surprisingly found that keeping the content of Xantham gum within the claimed range, enzyme exposure could be kept secularly below the threshold of 15 ng/m 3 while at the same time maintaining the composition in a sprayable form without any foaming tendencies.
  • composition according to the invention further comprises at least one preservative, preferably in an amount of 0.2 to 2.0 wt.-%, more preferably 0.5 to 1.5 wt.-%, based on the total weight of the inventive composition, respectively.
  • the preservative belongs to the group of isothiazolinones. In an especially preferred embodiment, the preservative is selected from methylisothiazolinone and benzisothiazolinone.
  • a further object of the present invention is the use of a composition according to the present invention for removing stains from fabrics, in particular for the removal of oily stains and/or sebaceous stains.
  • Another object of the present invention is a method for removing stains from fabric comprising contacting the stain with 0.5 to 5 ml of a composition according to the present invention, followed by cleaning the fabric with aqueous laundry detergent or by dry cleaning.
  • the composition employed in the method according to the invention is sprayable. Therefore, the composition is preferably applied by spraying the composition onto the stain.
  • the pre-treatment is followed by a further washing step. This washing step may be a manual washing or washing in a machine or dry cleaning. Any suitable detergent may be used.
  • the composition of the present invention is preferably ambient-active. Accordingly, the second step of the method according to the invention is preferably carried out at temperatures of less than 40 °C, preferably less than 30 °C. Further, the temperature is preferably more than 15 °C, preferably more than 20 °C.
  • composition according to the invention is provided as a spray as this was found to be the most effective method of application. Therefore, another object of the present invention is an aerosol dispenser comprising the composition according to the present invention.
  • the dispenser according to the invention is rechargeable.
  • Table 1 shows an example of a pre-treatment laundry composition in line with the present invention.
  • Laundry pre-treatment composition Component [wt.-%] water 92.4 preservative * 0.1 citric acid 0.5 Xanthan gum 0.2 sodium hydroxide 0.6
  • Glycerin 0.5 non-ionic surfactant 5.0 perfume 0.1 multi-enzyme blend 0.5 total 100 *) 2-methyl-2H-isothiazol-3-one/1,2-benzisothiazol-3(2H)-one
  • the prepared composition was obtained as a clear and colorless liquid with a pH of 8.0 and a viscosity (RV, 20 °C) of 500 to 700 MPas.
  • Table 2 Stain set coffee w/ milk sauce: spaghetti starch: rice (coloured) blood, milk, ink ENZ pigment, oil, low milk content motor oil/ pigments clay: yellow, modelling sebum w/ carbon black clay (standard) make-up (fluid) olive oil w/ carbon black GCS red wine (not aged) GCS lipstick: red (diluted) GCS grass GCS ice cream: chocolate GCS
  • Table 3 Washing cycles Parameter Pre-Treater PSR Machine Type Front Top Cycle Cotton Regular Water Temperature Setting Cold Cold Water Setting Automatic Low/Medium Wash Water Volume (litres) 15 to 16 45 to 47 Water Hardness (ppm as Ca 2+ ) 50 to 80 50 to 80 Wash Temperature (°C) 19 to 21 19 to 21 Wash Time (minutes) 65 to 70 10 to 12 Spin Speed (rpm) 1200 1000 Total Cycle Time (minutes) 127 to 137 47 to 50 Appendix Cloth 2kg White mixed fabric
  • the pretreatment composition according to the invention was compared with several comparative compositions:
  • Exposure measurements were carried out according to " Exposure measurements of enzymes for risk assessment of household cleaning spray products" of the International Association for Soaps, Detergents and Maintenance Products (AISE) of July 2020 .
  • a schematic representation of the distances between spray bottle, textile target and air filter is shown in Figure 6 .
  • test protocol is as follows:
  • Air-sampling equipment is used to collect airborne enzymes during the application of the spray on the textile. After air sampling, the filters are analyzed for enzyme protein collected during the air sampling. The testing showed that already the addition of 0.1 wt.-% of Xantham gum reduced the enzyme exposure significantly, addition of 0.2 wt.-% of Xantham gum kept the exposure securely below the critical threshold of 15 ng/m 3 without affecting the spraying properties of the pre-treatment composition according to the invention.

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EP21190970.0A 2021-08-12 2021-08-12 Composition de prétraitement de blanchisserie pulvérisable Pending EP4134423A1 (fr)

Priority Applications (2)

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EP21190970.0A EP4134423A1 (fr) 2021-08-12 2021-08-12 Composition de prétraitement de blanchisserie pulvérisable
AU2022207323A AU2022207323A1 (en) 2021-08-12 2022-07-25 Sprayable laundry pre-treatment composition

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EP21190970.0A EP4134423A1 (fr) 2021-08-12 2021-08-12 Composition de prétraitement de blanchisserie pulvérisable

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Citations (39)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB1243784A (en) 1967-10-03 1971-08-25 Novo Terapeutisk Labor As Proteolytic enzymes, their production and use
US4648987A (en) 1985-02-13 1987-03-10 The Clorox Company Thickened aqueous prewash composition
EP0218272A1 (fr) 1985-08-09 1987-04-15 Gist-Brocades N.V. Enzymes lipolytiques et leur usage dans des compositions détergentes
EP0258068A2 (fr) 1986-08-29 1988-03-02 Novo Nordisk A/S Additif enzymatique pour détergent
EP0305216A1 (fr) 1987-08-28 1989-03-01 Novo Nordisk A/S Lipase recombinante de humicola et procédé de production de lipases recombinantes de humicola
EP0331376A2 (fr) 1988-02-28 1989-09-06 Amano Pharmaceutical Co., Ltd. ADN recombinant, bactérie du genre pseudomonas le contenant et son utilisation dans un procédé de production de lipase
WO1991002792A1 (fr) 1989-08-25 1991-03-07 Henkel Research Corporation Enzyme proteolytique alcaline et procede de production
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