EP1005362A4 - SYSTEME D'ENZYME CHLOROPEROXYDASE DESTINE A PRODUIRE DE L'ACIDE HYPOCHLOREUX ET DE L'HYPOCHLORITE $i(IN SITU) - Google Patents

SYSTEME D'ENZYME CHLOROPEROXYDASE DESTINE A PRODUIRE DE L'ACIDE HYPOCHLOREUX ET DE L'HYPOCHLORITE $i(IN SITU)

Info

Publication number
EP1005362A4
EP1005362A4 EP98910457A EP98910457A EP1005362A4 EP 1005362 A4 EP1005362 A4 EP 1005362A4 EP 98910457 A EP98910457 A EP 98910457A EP 98910457 A EP98910457 A EP 98910457A EP 1005362 A4 EP1005362 A4 EP 1005362A4
Authority
EP
European Patent Office
Prior art keywords
composition
hydrogen peroxide
fabric
enzyme
contacting
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.)
Withdrawn
Application number
EP98910457A
Other languages
German (de)
English (en)
Other versions
EP1005362A1 (fr
Inventor
Vickie L Humphrey
Michele Kortyna
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.)
Clorox Co
Original Assignee
Clorox Co
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 Clorox Co filed Critical Clorox Co
Publication of EP1005362A1 publication Critical patent/EP1005362A1/fr
Publication of EP1005362A4 publication Critical patent/EP1005362A4/fr
Withdrawn legal-status Critical Current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
    • C11D3/02—Inorganic compounds ; Elemental compounds
    • C11D3/04—Water-soluble compounds
    • C11D3/046—Salts
    • A—HUMAN NECESSITIES
    • A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
    • A01N—PRESERVATION OF BODIES OF HUMANS OR ANIMALS OR PLANTS OR PARTS THEREOF; BIOCIDES, e.g. AS DISINFECTANTS, AS PESTICIDES OR AS HERBICIDES; PEST REPELLANTS OR ATTRACTANTS; PLANT GROWTH REGULATORS
    • A01N63/00—Biocides, pest repellants or attractants, or plant growth regulators containing microorganisms, viruses, microbial fungi, animals or substances produced by, or obtained from, microorganisms, viruses, microbial fungi or animals, e.g. enzymes or fermentates
    • A01N63/50—Isolated enzymes; Isolated proteins
    • 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
    • C11D3/38654—Preparations containing enzymes, e.g. protease or amylase containing oxidase or reductase
    • 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
    • C11D3/39—Organic or inorganic per-compounds
    • C11D3/3942—Inorganic per-compounds

Definitions

  • the present invention generally relates to compositions and methods for using an enzymatic system for generating hypochlorous acid and hypochlorite in situ . More particularly, the invention pertains to use of a chloroperoxidase enzyme in the presence of a hydrogen peroxide source and a chloride salt.
  • hypochlorite based bleaches generally provide superior bleaching performance over competing varieties of bleach such as perborates, percarbonates, and peracids.
  • the most widely used hypochlorite bleach is common household liquid bleach which is approximately a 5.25 weight percent aqueous solution of sodium hypochlorite.
  • hypochlorite As a salt of a weak acid (hypochlorous acid) and a strong base (i.e. sodium hydroxide) , hypochlorite (-OC1 " ) exists in equilibrium (pKa ⁇ 7.5) with hypochlorous acid (HOC1) .
  • hypochlorite is more stable of the two and may be further stabilized by basic solutions.
  • the pH of common household bleach is usually maintained at alkaline levels between about 10.5 and 12 where virtually all of the species are in the hypochlorite form.
  • hypochlorite bleach is also used as a germicide.
  • hypochlorous acid has the potential to be a much more potent germicide than hypochlorite.
  • hypochlorite has only 1/80th of the germicidal potency of hypochlorous acid. Block, Disinfectants and Antiseptics , Lea & Febiger (publ.), (1991), 131-138.
  • hypochlorite Although many applications could use hypochlorite's combination of germicidal efficacy and superior bleaching ability, there may be certain limitations of use. For example, sodium hypochlorite is primarily available in liquid form. While liquids are convenient to use, unartful application can result in unintended splashing and spillage. As a result, a need exists for an alternative delivery of a hypochlorite based bleaching system.
  • a composition comprises a chloroperoxidase enzyme, a hydrogen peroxide source, a chloride salt and an adhering agent which tends to localize the enzyme to the fabric or surface being treated.
  • the composition may be formed either before delivery to the fabric or surface, or in the alternative, formed at the site being treated.
  • the enzymatic components chloroperoxidase and its substrates hydrogen peroxide and chloride ion
  • the enzyme catalyzes a reaction which results in the formation of hypochlorous acid.
  • hypochlorous acid pKa ⁇ 7.5
  • hypochlorite some fraction of the hypochlorous acid (pKa ⁇ 7.5) will then ionize to form hypochlorite.
  • the present invention is in the non-alkaline pH range (preferably between about 4 and about 8) , at least about
  • hypochlorous acid 10%, and more preferably at least about 20% of the hypochlorous acid will remain in the non-ionized form.
  • the components must be stored in such a way to prevent the enzymatic reaction from occurring prematurely.
  • One method for achieving this purpose is by separately storing the enzyme from at least one of its substrates.
  • chloroperoxidase, hydrogen peroxide source, chloride salt, and adhering agent all may be in a non-liquid form, thus preventing the enzymatic reaction from appreciably occurring until the composition is dissolved in aqueous solution.
  • Figure 1 The amount of hypochlorous acid generated by myeloperoxidase as a function of pH is graphically illustrated.
  • the present invention relates to compositions and methods for using an enzymatic bleaching system for generating hypochlorous acid and hypochlorite either immediately prior to delivery or in situ .
  • An embodiment of the invention comprises a chloroperoxidase enzyme, a hydrogen peroxide source, a chloride salt, and an adhering agent which tends to localize the enzyme to the fabric or surface being treated.
  • the composition must be present in aqueous solution. Because the use of the present invention
  • cleaning referring to the removal of soils without the use of an oxidizing agent
  • bleaches referring to the removal of stains using an oxidizing agent
  • disinfects referring to the destruction or prevention of the growth of microorganisms
  • disinfectant and “germicide” (referring to an agent that kills microorganisms) and their various conjugations are also used interchangeably unless implicitly or explicitly rendered otherwise.
  • chloroperoxidase which results in the formation of hypochlorous acid in the presence of hydrogen peroxide and a chloride salt may be used.
  • the chloroperoxidase of the present invention may be purified from known sources or may be produced using recombinant means by methods known in the art. See, for example, B.W. Griffin, Pero ⁇ idases in Chemistry and Biology, Volume 2, chapter 4, pages 86-131 (1991), incorporated herein by reference.
  • Preferred chloro- peroxidases are those whose optimal pH for activity is in the range of about 4 to about 8.
  • Especially preferred chloroperoxidases are those that exhibit good ther ostability as well as good stability towards commonly used components in detergents and other cleaning formulations.
  • Particularly preferred chloroperoxidases are myeloperoxidases. Cloroperoxidases from Curvularia inaequalis or Caldariomyces fumago are also preferred. Hydrogen Peroxide
  • Hydrogen peroxide or a generator capable of generating hydrogen peroxide may be used.
  • hydrogen peroxide is used to describe both hydrogen peroxide itself and a source for hydrogen peroxide unless implicitly or explicitly rendered otherwise.
  • sodium peroxide, sodium perborate or other salts of hydrogen peroxide are sources of hydrogen peroxide since each forms hydrogen peroxide upon dissolution.
  • Another example of a source of hydrogen peroxide is an oxidase with a suitable substrate.
  • Examples include but are not limited to: D-glucose oxidase and glucose; hexose oxidase and hexose; cholesterol oxidase and cholesterol; galactose oxidase and D-galactose; pyranose oxidase and pyranose; choline oxidase and choline; pyruvate oxidase and pyruvate; oxalate oxidase and oxalate; glycolate oxidase and glycolate; and D-amino acid oxidase and D-amino acid.
  • the desired hydrogen peroxide source is an enzyme, it may either be purified from known sources or may be produced using recombinant means by methods known in the art.
  • the chloride salt may be inorganic such as MgCl 2 , KC1, NaCl, ZnCl 2 , CaCl j , and NrJCl. Generally, metal inorganic salts are preferred. Alternatively, the chloride salts may be organic. Illustrative examples include but are not limited to triethylammonium chloride, pyridinium chloride, and tolonium chloride. However, for reasons of ready availability and economy, sodium chloride is particularly preferred. Quantity of the Enzymatic Components
  • the quantities of the enzymatic components will depend on a number of inter-related factors. However, because the present invention generally relies on generating the bleaching agents at the site being treated, substantially lesser amounts of bleaching agents are required to achieve the same bleaching activity as prior art hypochlorite solutions. In other words, since the effects of the bleaching agents are localized to the surface of the stain being treated, the effective concentration of the generated bleaching agents is substantially higher than the actual concentrations of the bleaching agents in solution. Because the cost of the chloroperoxidase enzyme is more than that of any of the other components, it is preferred to minimize the amount of enzyme necessary. Not surprisingly, the amount of enzyme will vary depending on the particular application.
  • the amount of enzyme in the inventive compositions is between about 1 ⁇ g/ml and about 10 mg/ml. Depending on the particular applications, ranges yielding between about 5 ⁇ g/ml and about 10 ⁇ g/ml, about 100 ⁇ g/ml and about 500 ⁇ g/ml, and about 1 mg/ml to about 5 mg/ml of chloroperoxidase in solution are preferred.
  • the optimal amounts of hydrogen peroxide and chloride salt depend on the desired pH of the aqueous solution where the enzymatic reaction is to take place.
  • the pH range for the present invention is preferably between about 4 and about 8 depending upon the ratio of hypochlorous acid to hypochlorite that is desired. For example, since hypochlorous acid is a much more potent germicide, if the intended application is primarily as a disinfectant, a more acidic pH between about 4 and about 5 will be desired. However, if intended application is primarily as a bleaching agent and a dual bleaching system is desired, a pH near the pKa or approximately 7.5 will be desired. In any event, in the pH range of the present invention, the amount of hypochlorous acid that remains non-ionized will be at least about 10% and more preferably at least about 20%.
  • the pH also affects the enzyme's affinity for its substrates.
  • the enzyme's affinity for chloride ion varies with pH and the concentration of hydrogen peroxide.
  • the enzyme's affinity for hydrogen peroxide also varies with pH and the concentration of chloride ion.
  • the ratio of chloride and hydrogen peroxide concentration may be derived from the following formula:
  • the chloride salt should be present such that the chloride concentration is between about 0.1 and about 15 weight percent, and preferably is between about 2 and about 10 weight percent.
  • typical values for hydrogen peroxide concentration are between about 0.001 and about 1 weight percent in the aqueous solution.
  • adhering agent Any compound or material that tends to localize the enzyme to the fabric or surface being treated may be used as an adhering agent. By keeping the enzymes at or relatively near the site being treated, adhering agents significantly increase the effective concentration of hypochlorous acid and hypochlorite at the desired site.
  • the adhering agent may be present in an amount between about 0.01 and about 10 weight percent, and preferably between about 0.1 and about 5 weight percent.
  • Surfactants useful in the present invention are generally either anionic or non-ionic and may be used alone or as mixtures of various surfactants.
  • anionic surfactants include but are not limited to: ammonium, substituted ammonium (for example, mono-, di-, and triethanola monium) , alkali metal and alkaline earth metal salts of C 6 -C 18 fatty acids and resin acids; linear and branched alkyl benzene sulfo- nates; alkyl sulfates; alkyl ether sulfates, alkane sulfonates, olefin sulfonates, hydroxyalkane sulfonates, acyl sarcosinates, and acyl N-methyltaurides.
  • non-ionic surfactants include linear ethoxylated alcohols such as those sold by Shell Chemical Company under the brand name NEODOLTM.
  • Other non-ionic surfactants include various linear ethoxylated alcohols with an average length of from about 6 to 16 carbon atoms and averaging about 2 to 20 moles of ethylene oxide per mole of alcohol; linear and branched, primary and secondary ethoxylated, propoxylated alcohols with an average length of about 6 to 16 carbons and averaging 0 to 10 moles of ethylene oxide and about 1 to 10 moles of propylene oxide per mole of alcohol; linear and branched alkyl- phenoxy (polyethoxy) alcohols, otherwise known as ethoxylated alkylphenols with an average chain length of 8 to 16 carbon atoms and averaging 1.5 to 30 moles of ethylene oxide per mole of alcohol.
  • the inventive composition may include other ingredients known in the art to either maintain or enhance the performance of the enzyme or the generated bleaching agents.
  • buffering agents may be used to maintain the aqueous solution at the desired pH.
  • Illustrative examples of buffering agents include but are not limited to carbonates, phosphates, silicates, borates, and mixtures thereof.
  • Buffering agents may be present in an amount between about 0.1 and about 30 weight percent.
  • the buffering agent is present in an amount between about 0.5 and about 10 weight percent in the aqueous solution where the enzymatic reaction is to occur.
  • Builders or chelating agents may also be added to the composition. If a builder or chelating agent is desired, typical amounts range from about 0.1 to about 30 weight percent, and preferably from about 1 to about 20 weight percent. Examples of builders include but are not limited to ethylenediaminetetraacetic acid, tartaric acid, citric acid, nitrilotriacetic acid, sodium carboxymethylsuccinic acid, sodium N-(2-hydroxy- ethyl)ethylenediaminetriacetic acid, N-dithyleneglycol- N,N-diacetic acid, diethylenetriaminepentaacetic acid, and mixtures thereof.
  • Potentiators agents that enhance the efficacy of enzyme activity and/or the generated bleaching agents, may also be included in an amount between about 0.1 to about 30 weight percent.
  • Potentiators are well known in the art and include builders, chelating agents, and enzyme stabilizers such as diethylaminoethanol.
  • Other optional ingredients include those that enhance the aesthetic appeal of the inventive composition such as fragrances and coloring agents.
  • Fragrances such as those commercially available from International Flavors and Fragrance Inc., may be included in an amount ranging from about 0.001 to about 2.0 weight percent.
  • a fragrance or mixture of fragrances is present in an amount from about 0.1 to about 1 weight percent.
  • coloring agents may be included in small amounts. Illustrative examples of widely used coloring agents include but are not limited to ultramarine blue and copper pthalocyanines and may be included in an amount from about 0.001 to about 0.1 weight percent.
  • compositions are an enzymatic one, proper care must be taken to prevent the enzymatic substrates from prematurely reacting. If the substrates are permitted to interact with the enzyme substantially before the inventive composition's intended use, the composition's effectiveness as a bleaching agent will degrade over time as the concentrations of the substrates are depleted.
  • either the chloroperoxidase or one of the substrates may be separately stored from the remainder of the composition.
  • the enzymatic composition may be formed in situ by delivering the components to the site in rapid succession.
  • the components may be admixed immediately before delivering the composition to the affected area.
  • a convenient storage means is a multiple chambered dispenser such as that disclosed in Beacha et al., U.S. Patent 4,585,150, issued April 29, 1986, and commonly assigned to The Clorox Company.
  • Another strategy is to store the enzyme, hydrogen peroxide source, and the chloride salt in a non-liquid form since the enzymatic reaction does not appreciably occur in the absence of a suitable aqueous medium.
  • Illustrative uses for the non-liquid form of the inventive composition include uses as an additive to dry laundry detergent or to a type of scouring powder for cleaning kitchens and bathrooms. In this context, the enzymatic reaction generating hypochlorous acid and hypochlorite will not occur until the composition comes into contact with an aqueous medium.
  • the inventive composition may be in the form of a solid, pre-treatment stick and either a liquid or dry laundry detergent.
  • the chloroperoxidase and one or more adhering agents may be part of the pre-treatment stick which is rubbed on the stain or area being treated, with the remaining ingredients being a part of the laundry detergent.
  • Suitable stick formulations are known in the art such as those described in Sabol, U.S. Patent 4,842,762; Barrett, Jr.
  • one preferred embodiment for a pre-treatment stick includes propylene glycol, nonylphenol ethoxylate, linear alcohol ethoxylate, dodecylbenzenesulfonic acid, and stearic acid.
  • inventive composition may be used in any application where a bleaching agent is desired.
  • a bleaching agent includes but are not limited to use as a laundry additive, as a laundry pre-treatment agent, a kitchen or bathroom all-purpose scouring powder, a liquid kitchen or bathroom cleaner and disinfectant, a mildew remover, a toilet bowl cleaner, and a general purpose germicide.
  • the inventive composition is used to clean a fabric or a surface by contacting the fabric or surface being treated with a composition that comprises an aqueous solution, a chloroperoxidase, a hydrogen peroxide source, and a chloride salt.
  • a composition that comprises an aqueous solution, a chloroperoxidase, a hydrogen peroxide source, and a chloride salt.
  • an adhering agent such as a surfactant promotes the tendency of the chloroperoxidase to adhere to the fabric or surface being treated.
  • enzymatic reaction will occur, generating hypochlorous acid in situ .
  • hypochlorous acid will ionize to form hypochlorite depending on the pH of the surrounding environment. Many of the benefits result from the in situ generation of the bleaching agents.
  • taurine Chloramine Assay The concentration of hypochlorous acid generated by myeloperoxidase, hydrogen peroxide and sodium chloride was measured using a taurine chloramine assay. Briefly, taurine (also known as 2-aminoethane- sulfonic acid, "TauNH 2 ”) reacts with the hypochlorous acid to form taurine chloramine (TauNHCl) which in turn reacts to form dithionitrobenzoic acid (DTNB) , the formation of which is measured by absorption spectros- copy.
  • taurine also known as 2-aminoethane- sulfonic acid, "TauNH 2 ”
  • tauNHCl taurine chloramine
  • DTNB dithionitrobenzoic acid
  • Standard absorbance curves were generated by measuring the absorbance at varying pHs of known concentrations of taurine chloramine. There was a generally linear relationship between absorbance and concentration of taurine chloramine. By comparing the absorbance of a myeloperoxidase reaction mixture with the appropriate standard curve, the amount of hypochlo- rous acid generated by the myeloperoxidase may be inferred.
  • Assays were performed by pipetting 1 ml samples into 12 x 75 mm test tubes and then adding 0.125 ml of 1 mM thionitrobenzoic acid ("TNB") to each sample. The resulting solutions were thoroughly mixed and allowed to stand in the dark for 10 to 15 minutes. The samples were mixed again before 200 ⁇ l of each sample were pipetted into triplicate microplate wells. The microplates were read at 412 nm. Table 1 shows results from representative myeloperoxidase reaction conditions.
  • Table 2 illustrates results using larger concentrati ⁇ ns of substrates. Either 5 ⁇ g/ml myeloperoxidase or 10 ⁇ g/ml myeloperoxidase ("MPO") was tested at 400 mM NaCl and 830 ⁇ M H202. TABLE 2
  • Fig. 1 graphically illustrates the data in Table 2, displaying the taurine chloramine generation by myeloperoxidase as a function of pH.
  • Fabric swatches spotted with ball point ink and blood were treated with an embodiment of the inventive composition which comprised of a 0.1 M phosphate buffer solution at pH 6.0 containing 10 ⁇ g/ml of myeloperoxidase, 0.83 mM H 2 0 2 , and 0.4 M NaCl. Because normal washings are generally insufficient, pretreatment is usually necessary for effective stain removal. Substantially improved results for both ink and blood stains were obtained using the inventive composition over the buffer control.
  • buffer control comprising the following: 0.4 M phosphate buffer (pH 5.5); 1.6 M NaCl; and 33.2 mM H 2 0 2 .
  • buffer control Using the buffer control as a base, the following solutions were tested against the grape, tea, and mildew spores:
  • buffer control 3. inventive embodiment A: buffer control with 1.3 mg/ml myeloperoxidase;
  • inventive embodiment B buffer control with 1.3 mg/ml myeloperoxidase and 0.4% SDS; and,
  • inventive embodiment C buffer control with 1.3 mg/ml myeloperoxidase and 0.4% NEODOLTM.
  • the inventive embodiments After 15 minutes, the ability of the compositions to remove the grape, tea, and mildew spore stains was assessed. In all cases, the inventive embodiments outperformed a comparable amount of liquid hypochlorite bleach, providing superior cleaning performance. In addition, SDS and NEODOLTM appear to enhance the overall cleaning performance of the inventive compositions.
  • the surface antimicrobial action of the inventive embodiments were tested.
  • the basic solution (referred to as “basic solution”) comprised: 0.1 M phosphate buffer (pH 5.5); 0.4 M NaCl; and 0.83 mM H 2 0 2 .
  • Inventive embodiment D includes basic solution with 10 ⁇ g/ml of myeloperoxidase.
  • Inventive embodiment E is 10 ⁇ g/ml of myeloperoxidase and 1% surfactant (NEODOLTM) in basic solution.
  • inventive compositions are powerful germicidal agents. This increased germicidal efficacy may be exploited in many potential applications especially since microbes attached to surfaces are harder to kill than the same microbes in solution.
  • An inventive embodiment, which was used to demonstrate this phenomenon comprised: 0.3 ⁇ g/ml of myeloperoxidase, 10 ⁇ M H 2 0 2 and 0.01 M NaCl in 0.02 M phosphate buffer (pH 7.0).

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  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Wood Science & Technology (AREA)
  • General Health & Medical Sciences (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Oil, Petroleum & Natural Gas (AREA)
  • Organic Chemistry (AREA)
  • Zoology (AREA)
  • Health & Medical Sciences (AREA)
  • Inorganic Chemistry (AREA)
  • Agronomy & Crop Science (AREA)
  • Biotechnology (AREA)
  • Microbiology (AREA)
  • Pest Control & Pesticides (AREA)
  • Plant Pathology (AREA)
  • Virology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Dentistry (AREA)
  • Environmental Sciences (AREA)
  • Detergent Compositions (AREA)

Abstract

L'invention concerne des compositions destinées à produire de l'acide hypochloreux et de l'hypochlorite in situ, ainsi que leur utilisation comme agents de blanchiment et/ou comme désinfectants. La composition de l'invention comporte une enzyme présentant une activité chloroperoxydase, une source de peroxyde d'hydrogène, un sel de chlorure et un agent d'adhésion tendant à localiser l'enzyme sur le tissu ou la surface traitée. L'acide hypochloreux et l'hypochlorite sont formés avantageusement sur le site d'action voulu ou près de celui-ci produisant un blanchiment efficace.
EP98910457A 1997-03-24 1998-03-16 SYSTEME D'ENZYME CHLOROPEROXYDASE DESTINE A PRODUIRE DE L'ACIDE HYPOCHLOREUX ET DE L'HYPOCHLORITE $i(IN SITU) Withdrawn EP1005362A4 (fr)

Applications Claiming Priority (5)

Application Number Priority Date Filing Date Title
US82379497A 1997-03-24 1997-03-24
US823794 1997-03-24
US97573197A 1997-11-21 1997-11-21
US975731 1997-11-21
PCT/US1998/005225 WO1998042370A1 (fr) 1997-03-24 1998-03-16 SYSTEME D'ENZYME CHLOROPEROXYDASE DESTINE A PRODUIRE DE L'ACIDE HYPOCHLOREUX ET DE L'HYPOCHLORITE $i(IN SITU)

Publications (2)

Publication Number Publication Date
EP1005362A1 EP1005362A1 (fr) 2000-06-07
EP1005362A4 true EP1005362A4 (fr) 2002-10-09

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EP98910457A Withdrawn EP1005362A4 (fr) 1997-03-24 1998-03-16 SYSTEME D'ENZYME CHLOROPEROXYDASE DESTINE A PRODUIRE DE L'ACIDE HYPOCHLOREUX ET DE L'HYPOCHLORITE $i(IN SITU)

Country Status (3)

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EP (1) EP1005362A4 (fr)
AU (1) AU6469698A (fr)
WO (1) WO1998042370A1 (fr)

Families Citing this family (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
GB2391020A (en) * 2002-07-20 2004-01-28 Reckitt Benckiser Nv Stain removal
WO2004009751A1 (fr) * 2002-07-20 2004-01-29 Reckitt, Benckiser, N., V. Composition de traitement de tache et procede
GB2594063A (en) * 2020-04-14 2021-10-20 Qures Group Ltd Solid composition for producing antibacterial, antiviral, antifungal and disinfectant solutions

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WO1989009813A1 (fr) * 1988-04-15 1989-10-19 Novo Nordisk A/S Additif de detergent pour le blanchissage de tissu
EP0500387A2 (fr) * 1991-02-21 1992-08-26 Exoxemis, Inc. Méthodes et compositions pour le traitement des infections et le contrôle de la flore utilisant l'haloperoxydase
WO1995027046A2 (fr) * 1994-03-31 1995-10-12 Unilever Nv Compositions antimicrobiennes enzymatiques comprenant des haloperoxydases
WO1996038548A1 (fr) * 1995-06-01 1996-12-05 Eoe, Inc. Formules activees par oxygene pour la desinfection ou la sterilisation
WO1999002640A1 (fr) * 1997-07-09 1999-01-21 The Procter & Gamble Company Compositions de lavage/nettoyage contenant une oxydoreductase

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US4847089A (en) * 1986-07-16 1989-07-11 David N. Kramer Cleansing and distinfecting compositions, including bleaching agents, and sponges and other applicators incorporating the same
US5389369A (en) * 1991-02-21 1995-02-14 Exoxemis, Inc. Halo peroxidase containing compositions for killing yeast and sporular microorganisms
US5453284A (en) * 1993-01-29 1995-09-26 Pellico; Michael A. Stabilized enzymatic dentifrice

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Publication number Priority date Publication date Assignee Title
WO1989009813A1 (fr) * 1988-04-15 1989-10-19 Novo Nordisk A/S Additif de detergent pour le blanchissage de tissu
EP0500387A2 (fr) * 1991-02-21 1992-08-26 Exoxemis, Inc. Méthodes et compositions pour le traitement des infections et le contrôle de la flore utilisant l'haloperoxydase
WO1995027046A2 (fr) * 1994-03-31 1995-10-12 Unilever Nv Compositions antimicrobiennes enzymatiques comprenant des haloperoxydases
WO1996038548A1 (fr) * 1995-06-01 1996-12-05 Eoe, Inc. Formules activees par oxygene pour la desinfection ou la sterilisation
WO1999002640A1 (fr) * 1997-07-09 1999-01-21 The Procter & Gamble Company Compositions de lavage/nettoyage contenant une oxydoreductase

Non-Patent Citations (1)

* Cited by examiner, † Cited by third party
Title
See also references of WO9842370A1 *

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AU6469698A (en) 1998-10-20
EP1005362A1 (fr) 2000-06-07
WO1998042370A1 (fr) 1998-10-01

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