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WO1991006574A1 - Procede de preparation d'acides peroxycarboxyliques - Google Patents

Procede de preparation d'acides peroxycarboxyliques Download PDF

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Publication number
WO1991006574A1
WO1991006574A1 PCT/DK1990/000277 DK9000277W WO9106574A1 WO 1991006574 A1 WO1991006574 A1 WO 1991006574A1 DK 9000277 W DK9000277 W DK 9000277W WO 9106574 A1 WO9106574 A1 WO 9106574A1
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Prior art keywords
antibody
compound
general formula
catalyst
transition state
Prior art date
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Ceased
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PCT/DK1990/000277
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English (en)
Inventor
Sven Erik Godtfredsen
Ole Kirk
Frederik BJÖRKLING
Liselotte Bjerre Christensen
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Novo Nordisk AS
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Novo Nordisk AS
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Publication of WO1991006574A1 publication Critical patent/WO1991006574A1/fr
Anticipated expiration legal-status Critical
Ceased legal-status Critical Current

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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
    • C11D3/39—Organic or inorganic per-compounds
    • C11D3/3902—Organic or inorganic per-compounds combined with specific additives
    • 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
    • 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
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/0002—Antibodies with enzymatic activity, e.g. abzymes
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
    • C12P7/00—Preparation of oxygen-containing organic compounds
    • C12P7/40—Preparation of oxygen-containing organic compounds containing a carboxyl group including Peroxycarboxylic acids

Definitions

  • the present invention relates to a novel process for the preparation of peroxycarboxylic acids. Also, the present 5 invention relates to a catalyst for use in the process, as well as a detergent additive and a detergent composition containing the catalyst.
  • Peroxycarboxylic acids are frequently used for a number of
  • peroxycarboxylic acids for bleaching under laundry conditions (e.g. as described in "Chemistry of long-chain peroxy acids under laundry conditions", T.A.B.M. Bols an, R. Kok and A.D. Vreugdenhil, J. Am. Oil Chem. Soc.
  • the peroxycarboxylic acid is usually formed in situ, by the reaction of a precursor (an "activator”, e.g. tetraacetyl-ethylenediamine (TAED) or nonanoyloxybenzenesulphonate (NOBS) , as described in the reference cited above) with a perhydroxyl anion.
  • an activator e.g. tetraacetyl-ethylenediamine (TAED) or nonanoyloxybenzenesulphonate (NOBS) , as described in the reference cited above
  • TAED tetraacetyl-ethylenediamine
  • NOBS nonanoyloxybenzenesulphonate
  • Peroxycarboxylic acids are also commonly employed in the field of organic synthesis, as a wide variety of organic molecules may be oxidized by means of these reagents.
  • the various uses of peroxycarboxylic acids are exhaustively described in the art, e.g. in Comprehensive Organic Chemistry edited by Barton and
  • the present invention relates to a process for the preparation of a compound of the general formula (I)
  • R is an organic residue, in particular a linear or branched alkyl group, an aryl group or an alkyl aryl group each of which is optionally substituted with one or more hydroxy, alkoxy, nitro, amino, alkylamino, sulfonato, sulfo, a ido, halo or carboxy groups, the process comprising reacting a compound of the general formula (II)
  • X is an oxygen or nitrogen atom
  • R 1 has the meaning indicated above for R, or is a hydrogen atom or a carbohydrate residue, with hydrogen peroxide in the presence of a catalytic antibody raised against an analogue of a transition state of the reaction and capable of binding to said transition state.
  • catalytic antibody is intended to indicate an antibody which has the catalytic activity of an enzyme in that it is able to bind selectively to the transition state of a given reaction whereby the transition state is stabilized. In this way, the activation energy required for the reaction in question is decreased, and the rate of the reaction is consequently increased.
  • a transition state may be defined as an unstable intermediate which cannot be isolated as it is extremely short-lived. Consequently, it is not possible to raise antibodies against it.
  • An analogue of a transition state may be defined as a stable substance which has those characteristics of the corresponding transition state, such as charge or configuration, which provide it with identical or nearly identical antigenic determinant(s) so that catalytic antibodies raised against the analogue are also able to bind to the transition state itself when present in a reaction so as to provide a catalytic effect.
  • the preparation and use of catalytic antibodies is described in, e.g., A. Tramontano, A.A. A mann and R.A. Lerner, J. Am. Chem. Soc. 110, 1988, pp. 2282-2286; A. Tramontano, K.D. Janda and R.A. Lerner, Science 234, 19 Dec. 1986, pp.
  • R, R 1 and X are as defined above.
  • R may be a linear alkyl group, in particular a linear alkyl group with 1-19 carbon atoms, preferably 2-13 carbon atoms, more preferably 5-11 carbon atoms, and most preferably 7-9 carbon atoms.
  • the compound (II) is an optically active compound, it is possible to employ a racemate or one of the enantio er forms of the compound (II) for reaction with hydrogen peroxide. The process of the invention may thus be employed for the synthesis of optically active peroxycarboxylic acids.
  • X may be oxygen
  • R 1 may be a carbohydrate residue, preferably a monosaccharide, more preferably a methyl, ethyl or propyl glycoside, and most preferably a methyl, ethyl or propyl glucoside.
  • R. may be an aryl group which is preferably substituted with one or more sulfoxy, sulfono or hydroxy groups.
  • the transition state may, for instance, be the following tetrahedral structure
  • suitable transition state analogs useful for raising appropriate antibodies are phosphonate esters of the general formula (III)
  • R and R 1 are as indicated above. These analogs differ from the transition state itself by being stable compounds which may be employed to raise antibodies capable of binding the transition state of the reaction described above.
  • Examples of specific phosphonate esters for use in the present process arep-nitrophenyl-(4-carboxybutane) phosphonate, p-sulfophenyl- l(4-carboxybutane) phosphonate or 1'-0-ethylglucosyl-(4- carboxybutane) phosphonate.
  • phosphonate esters are relatively small molecules and may not in themselves be used for immunization purposes. In order to have an immunizing effect, they should therefore be bound (either directly or by means of a linking group such as a mercaptan, a succinimide or the like) to a suitable carrier molecule such as bovine serum albumin or keyhole limpet he ocyanin to form a conjugate which may then be used for immunization. Transition state analogue- carrier conjugates may, for instance, be produced by the method described in WO 88/09380.
  • the antibody employed in the process of the invention may be a polyclonal antibody.
  • Polyclonal antibodies may be prepared by immunizing a suitable animal (such as rabbits, goats, horses, sheep, mice, chickens, rats and guinea pigs) with the transition state analogue (in particular phoshonate ester) carrier conjugate (suitably dissolved or dispersed in a physiologically acceptable solvent or diluent) and isolating the antibody from the serum in a manner known per se (cf. A. Johnstone and R. Thorpe, I munochemistry in Practice, 2nd Ed. Blackwell Scientific publications, 1987, pp. 30-34 and 48-55).
  • monoclonal antibodies it is, however, usually preferred to employ monoclonal antibodies as these have become easy to produce in large quantities and in a high degree of purity. Furthermore, they exhibit great uniformity. Alternatively, it is possible to use a fragment of a monoclonal antibody, e.g. a Fab 1 , F(ab') 2 or other fragment. Monoclonal antibodies may be prepared by fusing cells producing the antibody with myeloma cells of an established cell line, selecting and cloning the resulting hybridoma cells and growing them in a suitable medium to produce the antibody and isolating the antibody from the culture, e.g. as described in A. Johnstone and R. Thorpe, op. cit. pp. 35-43.
  • the antibody may also be produced by the method described in WO 88/09380.
  • a further method of producing antibodies may be to cultivate a host cell transformed with a recombinant DNA vector which carries a DNA sequence encoding the antibody or a fragment thereof as well as DNA sequences encoding functions permitting 5 the expression of the DNA sequence encoding the antibody, in a culture medium under conditions permitting the expression of the antibody and recovering the antibody from the culture.
  • Preparation of antibodies by recombinant DNA techniques is, for instance, described in M. Better et al., Science 240, 1988, p. 101041; and CR. Wood et al. , Nature 314, 1985, p. 446.
  • a DNA fragment encoding the antibody may, for instance, be isolated by establishing a cDNA or geno ic library of an antibody-producing cell line and screening for positive clones by conventional procedures such as by hybridization to 15 oligonucleotide probes synthesized on the basis of the full or partial amino acid sequence of the antibody or by selecting for clones producing an antibody which is reactive with the appropriate transition state analog.
  • the DNA sequence may be inserted into a suitable 0 replicable expression vector comprising appropriate promotor, operator and terminator sequences permitting the antibody to be expressed in a particular host organism, as well as an origin of replication enabling the vector to replicate in the host organism in question.
  • the resulting expression vector may then be transformed into a suitable host cell, such as a fungal cell, preferred examples of which are a species of Asper ⁇ illus, most preferably Asperqillus oryzae or Aspercrillus niger.
  • Fungal cells may be transformed by a process involving protoplast formation and 0 transformation of the protoplasts followed by regeneration of the cell wall in a manner known per se.
  • the use of Asperqillus as a host microorganism is described in EP 238,023 (of Novo In- dustri A/S).
  • the host cell may also be a yeast cell, such as a strain of Saccharo yces spp. or Schizosaccharo yces spp. , in particular Saccharomyces cerevisiae.
  • the host organism may be a bacterium, in particular strains of Streptomyces and Bacillus, or E. coli.
  • the transformation of bacterial cells may be performed according to conventional methods, e.g. as described in Sambrook, Fritsch and Maniatis, Molecular Cloning: A Labora ⁇ tory Manual, Cold Spring Harbor, New York 1989.
  • the medium used to cultivate the transformed host cells may be any conventional medium suitable for growing the host cells in question.
  • the expressed antibody may conveniently be secreted into the culture medium and may be recovered therefor by well- known procedures including separating the cells from the medium by centrifugation or filtration, precipitating proteinaceous components of the medium by means of a salt such as ammonium sulphate, followed by chromatographic procedures such as ion exchange chromatography, affinity chromatography, or the like.
  • the present invention relates to a catalyst for use in the process according to the invention, which catalyst comprises a catalytic antibody raised against an analogue of a transition state of the reaction of a compound of the general formula II
  • R and R 1 are as indicated above, with hydrogen peroxide, said antibody being capable of binding said transition state.
  • the present invention relates to a detergent additive which comprises the catalyst of the invention.
  • the detergent additive of the invention may suitably be in the form of a non-dusting granulate, a liquid, in particular a stabilized liquid, or a protected antibody.
  • Non- dusting granulates may be produced in a manner analogous to that of producing enzyme granulates, e.g., as disclosed in US 4,106,991 and 4,661,452 (both to Novo Industri A/S) and may optionally be coated by methods known in the art.
  • Liquid antibody preparations may, for instance, be stabilized by adding a polyol such as propylene glycol, a sugar or sugar alcohol, lactic acid or boric acid according to established methods. Other stabilizers are well known in the art.
  • Protected antibodies may be prepared according to the method disclosed in EP 238,216 (for enzymes).
  • the detergent additive may further include one or more enzymes, such as proteases, lipases, cellulases, peroxidases or amylases or a combination thereof, conventionally included in detergent additives.
  • the catalytic antibody included in the detergent additive should be one which is resistant to the action of such enzymes, in particular that of protease. This may be accomplished by selection for antibodies which are stable in the presence of protease, by formulating the antibody so that the contact with protease will be minimized (e.g. as a granulate) , or by modifying the protease cleavage site(s) on the antibody, e.g. by protein engineering in a manner known per se.
  • the present invention relates to a detergent composition which comprises a catalyst according to the invention.
  • the catalyst may preferably be present in an amount corresponding to 0.01-100 mg of catalyst per litre of washing liquors.
  • the detergent composition additionally comprises a compound of the general formula II
  • the detergent composition of the invention may be formulated in any convenient form, e.g. as a powder or liquid.
  • the antibody may be stabilized in a liquid detergent by the inclusion of stabilizers as indicated above.
  • the detergent composition may further include hydrogen peroxide precursors such as perborates or percarbonates.
  • the pH of a solution of the detergent composition of the invention will be in the range of 7-12 and in some instances in the range of 7.0-10.5.
  • Detergent enzymes such as proteases, lipases, cellulases or amylases or a combination of two or more of these may be included in the detergent compositions of the invention, either separately or in a combined additive as described above.
  • the antibody should be one which is resistant to the action of such enzymes, notably that of protease as explained above.
  • the detergent composition of the invention may comprise one or more surface-active agents, such as anionic surfactants (e.g. linear alkyl benzene sulfonates, fatty alcohol sulfates, fatty alcohol ether sulfates, ⁇ -olefin sulfonates or soaps) , non ⁇ ionic surfactants (e.g. fatty alcohol ethoxylates, nonylphenol ethoxylates, fatty acid esters of sucrose and glucose, alkyl glycosides or esters of polyoxyethoxylated alkyl glycosides) , cationic surfactants and/or zwitterionic surfactants.
  • anionic surfactants e.g. linear alkyl benzene sulfonates, fatty alcohol sulfates, fatty alcohol ether sulfates, ⁇ -olefin sulfonates or soaps
  • non ⁇ ionic surfactants e.g. fatty alcohol e
  • Liquid and powder detergents may be formulated substantially as described in "Frame formulations for liquid/powder heavy-duty detergents" in J. Falbe, Surfactants in Consumer Products. Theory, Technology and Application, Springer Verlag, 1987.
  • a liquid heavy-duty detergent may comprise anionic surfactants, non-ionic surfactants, suds controlling agents, enzymes, foam boosters, builders, formulation aids, optical brighteners, stabilizers, fabric softeners, fragrances, dyestuffs and water.
  • a powder heavy-duty detergent may comprise anionic surfactants, non-ionic surfactants, suds controlling agents, foam boosters, chelating agents, ion exchangers, alkalis cobuilders, bleaching agents, bleach activators, bleach stabilizers, fabric softeners, antiredeposition agents, enzymes, optical brighteners, anticorrosion agents, fragrances, dyestuffs and blueing agents, formulation aids, fillers and water.
  • the catalytic antibody may be used per se. It is, however, possible to immobilize the antibody in order to facilitate the recovery of the peroxycarboxylic acids produced by the present process.
  • the immobilization procedures used to immobilize the antibody may be analogous to the established procedures for immobilizing enzymes (cf. for instance K. Mosbach, ed. , "Immobilized Enzymes", Methods in Enzy ology 44, Academic Press, New York, 1976) and include cross-linking of cell homogenates, covalent coupling to insoluble organic or inorganic supports, entrapment in gels and adsorption to ion exchange resins or other adsorbent materials.
  • Suitable support materials for the immobilized antibody are, for instance, plastics (e.g. polypropylene, polystyrene, polyvinylchloride, polyurethane, latex, nylon, teflon, dacron, polyvinylacetate, polyvinylalcohol or any suitable copolymer thereof) , polysaccharides (e.g. agarose or dextran) , ion exchange resins (both cation and anion exchange resins) , silicon polymers (e.g.
  • siloxane or silicates (e.g. glass) .
  • a particularly preferred resin is a weakly basic anion exchange resin which may be a polystyrene-, acrylic- or phenyl-formaldehyde-type resin. Examples of commercially available polyacrylic-type resins are Lewatit E 1999/85 (registered trademark of Bayer, Federal Republic of Germany) and Duolite ES-568 (registered trademark of Rohm & Haas, FRG) .
  • Immobilization of antibodies to this type of resin may be carried out according to EP 140 542 (disclosing the immobilization of enzymes) .
  • Immobilization to phenyl-formaldehyde-type resins may be done according to the procedure of DK 85/878 (disclosing the immobilization of enzymes) .
  • An example of a commercially available acrylic-type resin is Lewatit E2001/85 (registered trademark of Bayer, FRG) .
  • Another convenient material for immobilizing antibodies is an inorganic support, such as a silicate.
  • the antibody may be attached to the support by adsorption cr by covIER coupling, eg. as described in K. Mosbach, ed. , op.cit. (for enzymes).
  • the process according to the method of the invention may be carried out in the compound (II) itself (which in this case also acts as a solvent) or in solvents such as water, aqueous buffer solutions or organic solvents.
  • solvents such as water, aqueous buffer solutions or organic solvents.
  • Some preferred organic solvents are hydrocarbons such as hexane, cyclohexane, heptane, benzene and toluene, methylene chloride and hexachloroethane, acetonitrile, dimethylforma ide, dioxane and tetrahydrofurane. It is preferred to employ solvents in which the compound (II) and products of the reaction are highly soluble and in which the antibody maintains a good stability and activity.
  • the temperature at which the reaction of the compound (II) takes place is not believed to be critical, but may conveniently be in the range of about 20-100 °C, such as about 30-80 °C.
  • the hydrogen peroxide employed according to the process of the invention may be added as such to the reaction mixture either at the beginning of the reaction or at a desired rate in the course of the reaction.
  • a precursor of hydrogen peroxide such precursors being compounds which give rise to the generation of hydrogen peroxide in situ for reaction with the compound (II) , such as percarbonates or perborates.
  • the water generated in the course of the process according to the invention may, if desired, be removed by methods known in the art such as by distillation, exposure to dessicants etc.
  • Peroxycarboxylic acid references were prepared according to the method described by W.E. Parker, C. Ricciuti, CL. Ogg and D. Swern, J. Am. Chem. Soc. 1955, 77, 4037.
  • Percarboxylic acid levels may be monitored, also when hydrogen peroxide is present together with the peroxycarboxylic acid, by methods known in the art, e.g. by iodometry at 5 * C, as described by Sully and Williams in Analyst, 1962, 87, 653.
  • Hydrolysis of p-nitrophenol butyrate was monitored spectrophoto etrically by monitoring the absorbance at 400 nm using a Hewlett Packard HP 8452A diode array spectrophotometer.
  • Preparation and testing of catalytic antibodies capable of catalyzing the perhydrolysis of p-nitrophenol butyrate by hydrogen peroxide (as shown in Reaction Scheme I below) :
  • the selected carrier was KLH (Keyhole Limpet Hemocyanin) .
  • the conjugate was prepared by adding N-hydroxysuccinimide (4mg) , dicyclohexyl carbodiimide (7.4mg) and pyrrolidinopyridin (0.4mg) in CH 2 C1 2 (2ml) to compound 4 (lOmg) .
  • the mixture was allowed to react for 20 h at 20°C
  • the dicyclohexyl urea formed was removed by filtration and KLH (5.3mg) in H 2 0 (1ml) was added slowly.
  • the reaction proceeded for 2 h.
  • the product was dialyzed 24 h against H 2 0.
  • the resulting product had 0.29 mg hapten coupled to 5,3 mg KLH (monitored by hydrolysis of p- nitrophenol) .
  • mice were immunized three times at bi-weekly intervals. In the first immunization each mouse was injected subcutaneously with 100 ⁇ l of conjugate mixed with 100 ⁇ l of Freunds's complete adjuvant (corresponding to 0.4 ⁇ g of compound 4) . The two following immunizations had 100 ⁇ l of conjugate mixed with 100 ⁇ l of Freunds • s incomplete adjuvant (corresponding to 2 ⁇ g of compound 4) . Eyeblood samples were redrawn from all four mice and serum was analyzed by ELISA using hapten coupled to BSA as antigen (Hapten was coupled to BSA following the same principles as with KLH) . All four mice showed good titers.
  • Monoclonal antibodies were prepared by standard techniques first described by Kohler and Milstein, Nature 1975, 256, 495. Thus, the spleen from one mouse was removed and carefully dissected and disrupted. Fusion with sp2 myeloma cells was carried out in the presence of polyethylene glycol. The resulting hybridoma cells were seeded in 960 microtiter wells using selective medium (HAT) . After two weeks of growth, the supernatants were analyzed in the above mentioned ELISA. Fourty-eight selected hybridomas were further screened in an ELISA where BSA-coupled and free hapten were allowed to compete for the antibodies. Among these, seven hybridomas were selected, and monoclonal antibodies were obtained from the hybridoma tissue cultures.
  • Hybridoma supernatants were concentrated, the pH was adjusted to 8.5 and the monoclonal antibodies were then purified by adsorption on to Protein G Sepharose and eluted with citrate buffer pH 3.0.
  • the monoclonal antibodies were all of IgG 2 subclass.
  • Catalysis was monitored in an assay using 1 ml phosphate buffer (50 mM, pH 8 or 9) containing 0.5 mM p-nitrophenyl butyrate and 1.5 mM H 2 0 2 and 2 ⁇ M antibody (if present) .
  • the reactions were initiated by addition of p-nitrophenol butyrate.
  • Table 1 below shows the catalysis obtained with three different monoclonal antibodies, namely F37A12, F35B9 and F48A6.
  • F37A12 and F48A6 catalyses both the hydrolysis and the perhydrolysis of p-nitrophenyl butyrate.
  • F35B9 does not catalyze the reaction at all, presumably because it preferentially binds the starting material.
  • F48A6 is capable of catalyzing the formation of 98% peroxybutanoic acid relative to the total amount of p- nitrophenol released.

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Abstract

Dans le procédé décrit qui sert à préparer un composé représenté par la formule générale (I), où R représente un résidu organique , tel que notamment un groupe alkyle linéaire ou ramifié, un groupe aryle ou un groupe alkylaryle, dont chacun est éventuellement substitué par un ou plusieurs groupes hydroxy, alkyloxy, alkoxy, nitro, amino, alkylamino, sulfoxy, sulfono, amido, halo ou carboxy, un composé représenté par la formule générale (II) R-CO-X-R1, où X représente un atome d'oxygène ou d'azote et R1 représente R décrit ci-dessus ou un atome d'hydrogène ou un résidu d'hydrates de carbone, et est amené à entrer en réaction avec un peroxyde d'hydrogène en présence d'un anticorps catalytique dressé contre un analogue d'un état de transition de la réaction et capable de liaisons avec cet état de transition. Cet anticorps catalytique peut être utilisé comme composant de détergents pour la production d'agents de blanchiment à base d'acide peroxycarboxylique pendant des opérations de lavage ou comme catalyseur pour des opérations de synthèse organique.
PCT/DK1990/000277 1989-11-02 1990-10-31 Procede de preparation d'acides peroxycarboxyliques Ceased WO1991006574A1 (fr)

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DK547589A DK547589D0 (da) 1989-11-02 1989-11-02 Fremgangsmaade til fremstilling af organiske forbindelser
DK5475/89 1989-11-02

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EP (1) EP0494985A1 (fr)
JP (1) JPH05503507A (fr)
AU (1) AU6634290A (fr)
DK (1) DK547589D0 (fr)
WO (1) WO1991006574A1 (fr)

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WO1998006812A1 (fr) * 1996-08-16 1998-02-19 The Procter & Gamble Company Compositions detergentes ayant une activite enzymatique controlee par des anticorps
WO1998006810A1 (fr) * 1996-08-16 1998-02-19 The Procter & Gamble Company Compositions detergentes a activite lipolytique regulee par des anticorps
WO1998006811A1 (fr) * 1996-08-16 1998-02-19 The Procter & Gamble Company Compositions detergentes a activite proteolytique regulee par des anticorps
WO1998007818A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite amylolytique regulee par anticorps
WO1998007821A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite cellulolytique regulee par anticorps
WO1998007824A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes comprenant un anticorps d'oxydo-reductase
EP0912674A1 (fr) * 1996-07-05 1999-05-06 Unilever N.V. Compositions detergentes
US6277806B1 (en) * 1998-12-11 2001-08-21 Unilever Home & Personal Care Usa, Division Of Conopco, Inc. Bleaching enzymes and detergent compositions comprising them
US10414787B2 (en) 2013-03-14 2019-09-17 Mars, Incorporated Flavor composition containing HMG glucosides
US12096768B2 (en) 2019-08-07 2024-09-24 Ecolab Usa Inc. Polymeric and solid-supported chelators for stabilization of peracid-containing compositions

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US6352968B1 (en) 1996-07-05 2002-03-05 Lever Brothers Company, Division Of Conopco, Inc. Detergent compositions
WO1998007821A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite cellulolytique regulee par anticorps
WO1998007819A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite proteolytique regulee par anticorps
WO1998006812A1 (fr) * 1996-08-16 1998-02-19 The Procter & Gamble Company Compositions detergentes ayant une activite enzymatique controlee par des anticorps
WO1998007823A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes ayant une activite cellulolytique regulee par un anticorps
WO1998007817A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite lipolytique regulee par anticorps
WO1998007822A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes ayant une activite amylolytique regulee par un anticorps
WO1998007824A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes comprenant un anticorps d'oxydo-reductase
WO1998007818A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite amylolytique regulee par anticorps
WO1998007816A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes contenant un anticorps dirige contre une oxydoreductase
WO1998007820A1 (fr) * 1996-08-16 1998-02-26 The Procter & Gamble Company Compositions detergentes possedant une activite enzymatique regulee par anticorps
WO1998006811A1 (fr) * 1996-08-16 1998-02-19 The Procter & Gamble Company Compositions detergentes a activite proteolytique regulee par des anticorps
WO1998006810A1 (fr) * 1996-08-16 1998-02-19 The Procter & Gamble Company Compositions detergentes a activite lipolytique regulee par des anticorps
US6277806B1 (en) * 1998-12-11 2001-08-21 Unilever Home & Personal Care Usa, Division Of Conopco, Inc. Bleaching enzymes and detergent compositions comprising them
US10414787B2 (en) 2013-03-14 2019-09-17 Mars, Incorporated Flavor composition containing HMG glucosides
US12096768B2 (en) 2019-08-07 2024-09-24 Ecolab Usa Inc. Polymeric and solid-supported chelators for stabilization of peracid-containing compositions

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JPH05503507A (ja) 1993-06-10
EP0494985A1 (fr) 1992-07-22
AU6634290A (en) 1991-05-31

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