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WO2001036577A1 - Procede de rinçage de textiles - Google Patents

Procede de rinçage de textiles Download PDF

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Publication number
WO2001036577A1
WO2001036577A1 PCT/EP2000/010912 EP0010912W WO0136577A1 WO 2001036577 A1 WO2001036577 A1 WO 2001036577A1 EP 0010912 W EP0010912 W EP 0010912W WO 0136577 A1 WO0136577 A1 WO 0136577A1
Authority
WO
WIPO (PCT)
Prior art keywords
fabric
reagent
antibody
process according
benefit agent
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.)
Ceased
Application number
PCT/EP2000/010912
Other languages
English (en)
Inventor
Mark John Berry
Donna Cochrane
Robert John Crawford
Paul James Davis
Sandra Hemmington
Neil James Parry
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.)
Hindustan Unilever Ltd
Unilever NV
Original Assignee
Hindustan Lever Ltd
Unilever NV
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 Hindustan Lever Ltd, Unilever NV filed Critical Hindustan Lever Ltd
Priority to AU15188/01A priority Critical patent/AU1518801A/en
Priority to EP00977489A priority patent/EP1230333A1/fr
Priority to BR0015562-4A priority patent/BR0015562A/pt
Priority to CA002390076A priority patent/CA2390076A1/fr
Publication of WO2001036577A1 publication Critical patent/WO2001036577A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

Links

Classifications

    • 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
    • C11D3/0005—Other compounding ingredients characterised by their effect
    • C11D3/001—Softening compositions
    • C11D3/0015—Softening compositions liquid
    • 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
    • C11D3/384—Animal products
    • C11D3/3845—Antibodies
    • 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
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/12—Soft surfaces, e.g. textile

Definitions

  • the present invention generally relates to a process for rinsing fabrics. More in particular, it relates to a process for rinsing fabrics whereby a benefit agent is delivered to a fabric during the rinse cycle of a washing process.
  • a conventional fabric cleaning process as it is carried out in an automated washing machine comprises a main wash cycle (which may comprise a number of sub-cycles) in which soiled fabrics are contacted with a liquid aqueous cleaning composition or wash liquor.
  • a main wash cycle which may comprise a number of sub-cycles
  • Such a composition comprises surfactants builders and optionally other ingredients such as enzymes, bleaching agents, etc.
  • the now cleaned fabrics are subjected to a rinse cycle in which the cleaning composition is removed by pumping it off and spinning the wash load followed by soaking in fresh water.
  • softening agents may be added which improve the feel of the washed fabrics .
  • Such softening agents conventionally comprise cationic softening compounds of the quaternary ammonium type.
  • Other benefit agents include perfumes.
  • compositions which are added during the rinse cycle have a relatively short contact time with the fabrics and most of the compounds are immediately removed again in the last centrifuge step.
  • O-A-98/00500 discloses a composition comprising a benefit agent attached to a peptide or protein deposition aid which has a high affinity for fabric.
  • the composition is claimed to effectively deposit the benefit agent onto the fabric during the wash cycle.
  • the transfer of textile dyes from one garment to another during a washing or rinsing process may be inhibited by adding antibodies against the textile dye to the wash or rinse liquid.
  • WO-A-98/07820 discloses amongst others rinse treatment compositions containing antibodies directed at cellulase and standard softener actives (such as DEQA) .
  • a process for rinsing fabrics whereby a benefit agent is delivered to a fabric during the rinse cycle of a washing process, said benefit agent being deposited onto the fabric by means of a reagent having a high binding affinity for the fabric.
  • a rinse composition for use in the process of the invention comprising a reagent having a high binding affinity for the fabric and a benefit agent.
  • the invention relates to a process for rinsing fabrics whereby a benefit agent is delivered to a fabric during the rinse cycle of a washing process.
  • the benefit agent can be selected from softening agents, finishing agents/ protective agents, fragrances (perfumes), bleaching agents.
  • softening agents are clays, cationic surfactants or silicon compounds.
  • finishing agents/ protective agents are polymeric lubricants, soil repelling agents, soil release agents, photo-protective agents (sunscreens), anti-static agents, dye-fixing agents, antibacterial agents and anti-fungal agents.
  • the fragrances or perfumes may be encapsulated, e.g. in latex microcapsules.
  • Suitable examples of bleaches are photobleaches .
  • Examples of photobleaches are given in EP-A-379 312 (British Petroleum) , which discloses a water-insoluble photobleach derived from anionically substituted porphine, and in EP-A-035 470 (Ciba Geigy) , which discloses a textile treatment composition comprising a photobleaching component.
  • the benefit agent is deposited onto the fabric by means of a reagent having a high binding affinity for the fabric.
  • a reagent having a high binding affinity for the fabric.
  • a specific example of such a reagent is for instance an antibody.
  • the degree of binding of a molecule A to another molecule B can be generally expressed by the chemical equilibrium constant K resulting from the following reaction:
  • binding of a molecule to the fabric is specific or not can be judged from the difference between the binding (K d value) of the molecule to one type of fabric, versus the binding to another type of fabric material.
  • said material will be a fabric such as cotton or polyester.
  • K d value the binding of a molecule to the fabric
  • the difference between the two binding constants should be minimally 10, preferably more than 100, and more preferably, more that 1000.
  • the reagent should bind to the fabric, with a K d lower than 10 ⁇ 4 M, preferably lower than 10 "6 M and could be 10 ⁇ 10 M or even less.
  • K d binding affinities
  • the weight efficiency of the reagent in the total rinse composition would be increased and smaller amounts of the reagent would be required.
  • Antibodies are specific binding proteins. Their function in nature is to protect against disease by recognising (and binding) foreign bodies, such as viruses or Bacteria, but not self-cells. Furthermore, methods are well-known in the art to generate antibodies that are specific for almost any protein, organic molecule, or cell surface, that is likely to be encountered. This binding specificity has been exploited in the Biotechnology industry, principally for medical diagnostics. For example, many home-based pregnancy test kits comprise an antibody that specifically binds to the pregnancy marker hormone, human chorionic gonadotropin (hCG) , but not to other hormones present in urine.
  • hCG human chorionic gonadotropin
  • Unilever has described the use of stain-specific antibodies to target bleaching enzymes exclusively to stains but not to dyes - thus achieving efficient stain removal without damaging surrounding fabric.
  • Antibodies are well known examples of molecules which are capable of binding specifically to compounds against which they were raised. Antibodies can be derived from several sources. From mice, monoclonal antibodies can be obtained which possess very high binding affinities. From such antibodies, Fab, Fv or scFv fragments, can be prepared which have retained their binding properties. Such antibodies or fragments can be produced through recombinant DNA technology by microbial fermentation. Well known production hosts for antibodies and their fragments are yeast, moulds or bacteria .
  • a class of antibodies of particular interest is formed by the Heavy Chain antibodies as found in Camelidae, like the camel or the llama.
  • the binding domains of these antibodies consist of a single polypeptide fragment, namely the variable region of the heavy chain polypeptide (HC-V) .
  • the binding domain consists of two polypeptide chains (the variable regions of the heavy chain (V h) and the light chain (Vi) ) .
  • Procedures to obtain heavy chain immunoglobulins from Camelidae, or ( functionalized) fragments thereof, have been described in WO-A-94/04678 (Casterman and Hamers) and WO-A- 94/25591 (Unilever and Free University of Brussels).
  • binding domains can be obtained from the V h fragments of classical antibodies by a procedure termed "camelization" .
  • the classical V h fragment is transformed, by substitution of a number of amino acids, into a HC-V-like fragment, whereby its binding properties are retained.
  • This procedure has been described by Riechmann et al. in a number of publications (J. Mol . Biol. (1996) 259, 957-969; Protein. Eng . (1996) 9, 531-537, Bio/Technology (1995) 13, 475-479) .
  • HC-V fragments can be produced through recombinant DNA technology in a number of microbial hosts (bacterial, yeast, mould), as described in WO-A-94/29457 (Unilever) .
  • fusion proteins that comprise an enzyme and an antibody or that comprise an enzyme and an antibody fragment are already known in the art.
  • One approach is described by Neuberger and Rabbits (EP-A-194 276) .
  • a method for producing a fusion protein comprising an enzyme and an antibody fragment that was derived from an antibody originating in Camelidae is described in WO-A-94/25591.
  • a method for producing bispecific antibody fragments is described by Holliger et al. (1993) PNAS 90, 6444-6448.
  • a particularly attractive feature of antibody binding behaviour is their reported ability to bind to a "family" of structurally related molecules.
  • a "family" of structurally related molecules For example, in Gani et al. (J. Steroid Biochem. Molec. Biol. 48, 277-282) an antibody is described that was raised against progesterone but also binds to the structurally-related steroids, pregnanedione, pregnanolone and 6-hydroxy-progesterone . Therefore, using the same approach, antibodies could be isolated that bind to a whole "family" of stain chromophores (such as the polyphenols, porphyrins, or caretenoids as described below) . A broad action antibody such as this could be used to treat several different stains when coupled to a bleaching enzyme.
  • stain chromophores such as the polyphenols, porphyrins, or caretenoids as described below
  • Peptides usually have lower binding affinities to the substances of interest than antibodies. Nevertheless, the binding properties of carefully selected or designed peptides can be sufficient to deliver the desired selectivity in an oxidation process.
  • a peptide which is capable of binding selectively to a fabric to which one would like to deliver a benefit agent can for instance be obtained from a protein which is known to bind to that specific fabric. An example of such a peptide would be a binding region extracted from an antibody raised against that fabric.
  • a suitable peptide could be analogous to the active center of a protein analogous to a non-catalytic binding domain of a protein, e.g. a receptor.
  • peptides that bind to such substance can be obtained by the use of peptide combinatorial libraries.
  • a library may contain up to 10 10 peptides, from which the peptide with the desired binding properties can be isolated.
  • R.A. Houghten Trends in Genetics, Vol 9, no &, 235-239.
  • Several embodiments have been described for this procedure (J. Scott et al., Science (1990) 249, 386-390; Fodor et al., Science (1991) 251, 767-773; K. Lam et al., Nature (1991) 354, 82-84; R.A. Houghten et al., Nature (1991) 354, 84-86).
  • Suitable peptides can be produced by organic synthesis, using for example the Merrifield procedure (Merrifield (1963) J.Am.Chem.Soc. 85, 2149-2154).
  • the peptides can be produced by recombinant DNA technology in microbial hosts (yeast, moulds, bacteria) (K.N. Faber et al. (1996) Appl. Microbiol. Biotechnol . 45, 72-79).
  • Pepidomimics In order to improve the stability and/or binding properties of a peptide, the molecule can be modified by the incorporation of non-natural amino acids and/or non-natural chemical linkages between the amino acids. Such molecules are called peptidomimics (H.U. Saragovi et al. (1991) Bio/Technology 10, 773-778; S. Chen et al. (1992)
  • the reagent has a high binding affinity for the fabric.
  • the reagent is a protein or a peptide, it may be that one part of its polypeptide chain is responsible for the binding affinity to the fabric, and part of the reagent comprises an enzyme part capable of providing a benefit.
  • the bleaching enzyme may be a fusion protein comprising two domains, which may be coupled by means of a linker.
  • the reagent having the high binding affinity may be covalently coupled to a benefit agent by means of a bivalent coupling agent such as glutardialdehyde.
  • a bivalent coupling agent such as glutardialdehyde.
  • the reagent having the high binding affinity is a peptide or a protein, it may also be coupled to the enzyme by constructing a fusion protein. In such a construct there would typically be a peptide linker between the binding reagent and the enzyme.
  • An example of a fusion of an enzyme and a binding reagent is described in Ducancel et al . Bio/technology 11, 601-605.
  • a further embodiment would be for the reagent with a high binding affinity to be a bispecific reagent.
  • a reagent could fulfil the requirement of accumulating the benefit agent on the fabric either by supplying said reagent together with the benefit agent as a pre-formed non-covalent complex or by supplying the two separately and allowing them to self-assemble either in the rinse liquor or on the fabric .
  • the rinse process of the invention is carried out using micro-particles sensitised with antibody, and configured such that the micro-particles are loaded with the benefit agent and the antibody has a high affinity or specificity for a substance (or "marker molecule" ) typically found on some regions of fabrics but not on others.
  • marker molecules include bleach-damaged dyes and microbes known to be associated with malodour.
  • the antibody targets the benefit agent to its intended site of action and binds it there.
  • Microbe-specific antibodies may target fragrance-containing particles to the regions of malodour. Thus, a more efficient use of expensive ingredients is achieved.
  • antibodies specific for bleach-damaged dyes can target dyed particles to faded regions, thus replenishing the colour lost in the main wash cycle.
  • micro-particles have been sensitised with antibody and used to generate a coloured end-point in medical diagnostic devices, when they are applied manually onto a test strip.
  • analogous particles are being specifically bound to some cotton swatches but not others, depending on which marker molecules are present on the swatches .
  • the binding of particles is being driven not by manual application but by agitating a bulk liquid phase (e.g. a rinse liquor) containing said particles and swatches.
  • the agitation increases the number of collisions between fabric and particles and thus increases specific binding: particles sensitised with specific antibody result in productive collisions and binding is permanent; particles sensitised with non-specific antibody result in non-productive collisions and do not bind permanently.
  • Such an agitation could be readily achieved during the rinse cycle in an automatic washing machine.
  • Another advantage of the present invention is that it is possible to target some benefit molecules to particular regions of fabric during the rinse.
  • dyes can be targeted to colour-bleached regions to replenish dye lost in the main wash or fragrance can be targeted to regions where it is most needed (i.e. those regions where microbes associated with malodour are present - such as the "underarm" regions).
  • methods for targeting small molecules (such as a dye or a fragrance) to particular regions of fabric have not previously been described. The inventors have approached this problem by loading small molecules (such as a dye) onto a micro-particle and then sensitising the particles with an antibody.
  • the advantage of this is that a single antibody binding event can deposit many dye molecules onto the target-region of fabric.
  • antibody-sensitised particles have been described previously (as component parts of medical diagnostic devices) they are used in a fundamentally different way: in the medical device, the particles are manually applied to the target surface (typically nitro-cellulose paper) and then eluted with a solution. If specific antibody is present, the particles remain stuck on. Otherwise they do not.
  • antibody-sensitised particles have not previously been used to target a small chemical compound (such as a dye or a fragrance) from a bulk liquid phase to a particular target site on a surface.
  • a small chemical compound such as a dye or a fragrance
  • the inventors have been able to achieve surprisingly specific binding to cotton swatches by agitating a bulk liquid phase (of rinse liquor or tap water) containing said particles and swatches.
  • An important embodiment of the invention is to use a binding reagent (as described above) that binds to several different types of fabrics. This would have the advantage of enabling a single benefit agent to be deposited to several different types of fabric.
  • the rinse compositions of the invention can be used in a detergent composition which is specifically suited for rinsing purposes, and this constitutes a second aspect of the invention.
  • WO-A-98/07820 discloses inter alia rinse treatment compositions containing antibodies directed at cellulase and standard softener actives such as DEQA.
  • the rinse product according to the present invention preferably contains no softener or low levels of softener active (e.g. HEQ) . If HEQ is present, the rinse product contains Sodium tripolyphosphate (STP) to stabilise antibody activity.
  • STP Sodium tripolyphosphate
  • the present inventors achieved much superior binding and specificity in rinse liquors (or tap water) by omitting typical softener compositions. They also achieved improved binding in the presence of softener compositions by adding salts, especially multivalent salts such as STP. It is also very surprising that the inventors have found antibodies to be active in rinse liquors (or tap water) . Previously published descriptions of specific antibody binding are typically in physiological strength buffer (0.15M NaCl) often supplemented with 0.15% surfactant. In many ways this mimics the environment in which the antibodies bind in nature, namely in serum which is approximately 0.15M NaCl, pH 7, and where serum albumin may be thought to act in an analogous way to a surfactant in that it reduces the opportunity for non-specific binding reactions .
  • the rinse composition comprises one or more benefit agents and optionally other conventional detergent ingredients.
  • the invention in its second aspect provides a rinse composition which comprises from 0.1 - 50 % by weight, based on the total composition, of one or more surfactants.
  • This surfactant system may in turn comprise 0 - 95 % by weight of one or more anionic surfactants and 5 - 100 % by weight of one or more nonionic surfactants.
  • the surfactant system may additionally contain amphoteric or zwitterionic detergent compounds, but this in not normally desired owing to their relatively high cost. It was found to be advantageous to also include cationic surfactants into the composition. Examples of suitable cationic surfactants are given in WO-A-97/03160 and WO-A-98/17767 (Procter&Gamble) .
  • nonionic and anionic surfactants of the surfactant system may be chosen from the surfactants described "Surface Active Agents” Vol. 1, by Schwartz & Perry, Interscience 1949, Vol. 2 by Schwartz, Perry & Berch, Interscience 1958, in the current edition of "McCutcheon ' s Emulsifiers and Detergents” published by Manufacturing Confectioners Company or in "Tenside-Taschenbuch” , H. Stache, 2nd Edn., Carl Hauser Verlag, 1981.
  • Suitable nonionic detergent compounds which may be used include, in particular, the reaction products of compounds having a hydrophobic group and a reactive hydrogen atom, for example, aliphatic alcohols, acids, amides or alkyl phenols with alkylene oxides, especially ethylene oxide either alone or with propylene oxide.
  • Specific nonionic detergent compounds are C 6 -C 22 alkyl phenol-ethylene oxide condensates, generally 5 to 25 EO, i.e. 5 to 25 units of ethylene oxide per molecule, and the condensation products of aliphatic C 8 - Ci 8 primary or secondary linear or branched alcohols with ethylene oxide, generally 5 to 40 EO.
  • Suitable anionic detergent compounds which may be used are usually water-soluble alkali metal salts of organic sulphates and sulphonates having alkyl radicals containing from about 8 to about 22 carbon atoms, the term alkyl being used to include the alkyl portion of higher acyl radicals.
  • suitable synthetic anionic detergent compounds are sodium and potassium alkyl sulphates, especially those obtained by sulphating higher C 8 -C ⁇ e alcohols, produced for example from tallow or coconut oil, sodium and potassium alkyl C 9 -Co benzene sulphonates, particularly sodium linear secondary alkyl C 10 -C 15 benzene sulphonates; and sodium alkyl glyceryl ether sulphates, especially those ethers of the higher alcohols derived from tallow or coconut oil and synthetic alcohols derived from petroleum.
  • the preferred anionic detergent compounds are sodium Cn-Cis alkyl benzene sulphonates and sodium C ⁇ 2 -C ⁇ e alkyl sulphates.
  • surfactants such as those described in EP-A- 328 177 (Unilever), which show resistance to salting-out, the alkyl polyglycoside surfactants described in EP-A-070 074, and alkyl monoglycosides .
  • Preferred surfactant systems are mixtures of anionic with nonionic detergent active materials, in particular the groups and examples of anionic and nonionic surfactants pointed out in EP-A-346 995 (Unilever) .
  • surfactant system which is a mixture of an alkali metal salt of a C1 6 -C18 primary alcohol sulphate together with a C ⁇ 2 -Ci 5 primary alcohol 3-7 EO ethoxylate.
  • the nonionic detergent is preferably present in amounts greater than 10%, e.g. 25-90% by weight of the surfactant system.
  • Anionic surfactants can be present for example in amounts in the range from about 5% to about 40% by weight of the surfactant system.
  • the rinsing detergent composition may take any suitable physical form, such as a powder, a tablet, an aqueous or non aqueous liquid, a paste or a gel.
  • the complex of benefit agent and reagent having a high affinity according to the invention will generally be used as a dilution in water of about 0.05 to 2%.
  • the rinse composition in accordance with the invention comprising the complex of the reagent having a high affinity for the fabric and the benefit aid can have any suitable form, i.e. the form of a granular composition, a liquid or a slurry of the enzyme, or with carrier material (e.g. as in EP-A-258 068 and the Savinase (TM) and Lipolase (TM) products of Novo Nordisk) .
  • carrier material e.g. as in EP-A-258 068 and the Savinase (TM) and Lipolase (TM) products of Novo Nordisk
  • a good way of adding the complex to a liquid rinse product is in the form of a slurry containing from 0.005 to 50 % by weight of the complex in an ethoxylated alcohol nonionic surfactant.
  • the rinse compositions of the invention comprise about 0.001 to 10 mg, preferably from 0.01 to 10 mg of antibody per liter of the rinse liquor in use.
  • a concentrated rinse composition before use will comprise about 1 to 1000 mg/1, preferably from 10 mg to 100 mg per liter of the rinse product .
  • Figure 1 a Graph showing the effects of wash and rinse liquors from Persil non-biological powder main wash on antibody binding activity (a specific anti-hCG monoclonal was used) compared to standard curves in PBST and tap water bench marks) .
  • Graph shows binding signal (optical density at 405nm) versus antibody concentration.
  • Figure 2 Graph showing the effects of wash and rinse liquors from Zeus liquid main wash on antibody binding activity (a specific anti-hCG monoclonal was used) compared to standard curves in PBST and tap water bench marks .
  • Graph shows binding signal (optical density at 405nm) versus antibody concentration.
  • Example 1 Antibody binding in Tap water to antigen.
  • Antibody activity was determined using an immuno- assay or ⁇ ELISA' .
  • the assay comprised a specially designed nylon peg sensitised with antigen.
  • a number of wash and rinse liquors were used to determine the effects on antibody activity. These liquors were obtained from wash cycles using standard Persil non-biological powder and Zeus (concentrated zeolite built) non-biological HDL formulation.
  • the pegs had to be rehydrated by immersing in phosphate buffer saline (PBS) [0.15M sodium chloride, 0.0075M di-sodium hydrogen ortho- phosphate and 0.0025M sodium di-hydrogen orthophosphate, pH7.2] or distilled water only if using tap water or wash/rinse liquor as antibody diluent, for 15 minutes.
  • PBS phosphate buffer saline
  • Mouse anti-hCG was assayed as a dilution curve, with concentrations starting at l ⁇ g/ml, in phosphate buffered saline + 0.015% v/v tween 20 (PBST) pH7.2.
  • Mouse anti-E3G was assayed as a negative control to allow assessment of non-specific binding and was also run in a dilution curve, with equal concentrations to the mouse anti-hCG.
  • the pegs were exposed to the various concentrations of anti-hCG and anti-E3G for 60 minutes, at room temperature, before washing in PBST. This was followed by exposure to Goat anti-mouse alkaline phosphatase conjugate, diluted in PBST, for 30 minutes at room temperature. After a final wash in PBST, the pegs were analysed for the amount of alkaline phosphatase bound by incubating in a colour generating substrate system (p-nitro-phenyl phosphate) where the more antibody bound the more colour is generated. The resulting colour was read in an ELISA plate reader at 405nm.
  • Figures 1 and 2 demonstrate the ability of the antibodies to bind to its antigen in tap water and rinse liquors.
  • Example 2 Binding antibody loaded particles to fabric senstised with antigen.
  • Results The results presented in the table below indicate the ability to target particles to an antigen on fabric via a specific antibody binding event in tap water. The greater the DE the greater the particle deposition. Table 1. Binding of targeted particles to cotton in tap water (non-shaking/static exposure)
  • Example 3 Functional bihead antibody molecule in tap water .
  • This example describes the confirmation that engineered antibody molecules (with the potential of large-scale exploitation) can function effectively in a non-buffered tap water environment.
  • Bi-head molecule (denoted 1349) will bind red wine stains (anti-polyphenolic) and the enzyme Glucose oxidase (Gox) .
  • Bi-Head 1349 was diluted at lO ⁇ g/per ml in tap water or Phosphate buffered saline + tween 20, PBST [0.01M Na 2 HPO 4 /NaH 2 PO 4 ,0.15M NaCl and 0.15% Tween 20] each containing 5 ⁇ g/ml Gox. Additionally a control of Gox only at 5 ⁇ g/ml was diluted in tap water or PBST to be used as a control.
  • the prepared solutions were dispensed in 1ml volumes to two stained swatches and two unstained swatches. Tap water and PBST only were added to two unstained swatches as a further control. Samples were left at 21°C( ⁇ 1) for 30 minutes without shaking. The samples were placed in bottle containing either tap water or PBST (as appropriate) and agitated on a rototorque (Cole Parmer instrument Co. Chicargo Model 7637-10) for 2 minutes. This rinsing process was repeated twice more. The swatches were then placed in a clean 24 well tissue culture plate and a substrate was added comprising 0.

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Abstract

La présente invention concerne un procédé de rinçage de textiles selon lequel un agent traitant bénéfique est ajouté aux textiles pendant le cycle de rinçage d'un processus de lavage; cet agent traitant bénéfique étant déposé dans le textile au moyen d'un réactif présentant une haute affinité pour ce textile.
PCT/EP2000/010912 1999-11-16 2000-11-03 Procede de rinçage de textiles Ceased WO2001036577A1 (fr)

Priority Applications (4)

Application Number Priority Date Filing Date Title
AU15188/01A AU1518801A (en) 1999-11-16 2000-11-03 Process for rinsing fabrics
EP00977489A EP1230333A1 (fr) 1999-11-16 2000-11-03 Procede de rin age de textiles
BR0015562-4A BR0015562A (pt) 1999-11-16 2000-11-03 Processo para a rinsagem de tecidos, e, composição de rinsagem para uso no mesmo
CA002390076A CA2390076A1 (fr) 1999-11-16 2000-11-03 Procede de rincage de textiles

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
EP99309098 1999-11-16
EP99309098.4 1999-11-16

Publications (1)

Publication Number Publication Date
WO2001036577A1 true WO2001036577A1 (fr) 2001-05-25

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PCT/EP2000/010912 Ceased WO2001036577A1 (fr) 1999-11-16 2000-11-03 Procede de rinçage de textiles

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EP (1) EP1230333A1 (fr)
AR (1) AR026492A1 (fr)
AU (1) AU1518801A (fr)
BR (1) BR0015562A (fr)
CA (1) CA2390076A1 (fr)
WO (1) WO2001036577A1 (fr)
ZA (1) ZA200203573B (fr)

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6946501B2 (en) 2001-01-31 2005-09-20 The Procter & Gamble Company Rapidly dissolvable polymer films and articles made therefrom
US7316994B2 (en) 2002-11-01 2008-01-08 The Procter & Gamble Company Perfume polymeric particles
US8187580B2 (en) 2002-11-01 2012-05-29 The Procter & Gamble Company Polymeric assisted delivery using separate addition
WO2015078943A1 (fr) 2013-11-28 2015-06-04 Unilever Plc Améliorations concernant des agents bénéfiques encapsulés

Citations (5)

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DE19621224A1 (de) * 1996-05-25 1997-11-27 Henkel Kgaa Verfahren zur Inhibierung der Farbübertragung
WO1998000500A1 (fr) * 1996-07-01 1998-01-08 Unilever Plc Composition detergente
WO1998007821A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite cellulolytique regulee par anticorps
WO1998056885A2 (fr) * 1997-06-13 1998-12-17 Unilever N.V. Enzymes de blanchiment
JPH1161639A (ja) * 1997-08-25 1999-03-05 Dainippon Jochugiku Co Ltd 洗濯用抗菌仕上げ剤

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Publication number Priority date Publication date Assignee Title
DE19621224A1 (de) * 1996-05-25 1997-11-27 Henkel Kgaa Verfahren zur Inhibierung der Farbübertragung
WO1998000500A1 (fr) * 1996-07-01 1998-01-08 Unilever Plc Composition detergente
WO1998007821A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite cellulolytique regulee par anticorps
WO1998056885A2 (fr) * 1997-06-13 1998-12-17 Unilever N.V. Enzymes de blanchiment
JPH1161639A (ja) * 1997-08-25 1999-03-05 Dainippon Jochugiku Co Ltd 洗濯用抗菌仕上げ剤

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Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6946501B2 (en) 2001-01-31 2005-09-20 The Procter & Gamble Company Rapidly dissolvable polymer films and articles made therefrom
US7547737B2 (en) 2001-01-31 2009-06-16 The Procter & Gamble Company Rapidly dissolvable polymer films and articles made therefrom
US7316994B2 (en) 2002-11-01 2008-01-08 The Procter & Gamble Company Perfume polymeric particles
US8187580B2 (en) 2002-11-01 2012-05-29 The Procter & Gamble Company Polymeric assisted delivery using separate addition
WO2015078943A1 (fr) 2013-11-28 2015-06-04 Unilever Plc Améliorations concernant des agents bénéfiques encapsulés

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BR0015562A (pt) 2002-09-03
CA2390076A1 (fr) 2001-05-25
ZA200203573B (en) 2003-07-30
EP1230333A1 (fr) 2002-08-14
AU1518801A (en) 2001-05-30

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