EP1214044A2 - Procede de restructuration de fibres keratiniques - Google Patents

Procede de restructuration de fibres keratiniques

Info

Publication number
EP1214044A2
EP1214044A2 EP00974377A EP00974377A EP1214044A2 EP 1214044 A2 EP1214044 A2 EP 1214044A2 EP 00974377 A EP00974377 A EP 00974377A EP 00974377 A EP00974377 A EP 00974377A EP 1214044 A2 EP1214044 A2 EP 1214044A2
Authority
EP
European Patent Office
Prior art keywords
enzyme
substrate activity
alcohol
group
preferred
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
EP00974377A
Other languages
German (de)
English (en)
Inventor
Astrid Kleen
Oliver BRABÄNDER
Andrea SÄTTLER
Horst Höffkes
Ralf Otto
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.)
Henkel AG and Co KGaA
Original Assignee
Henkel AG and Co KGaA
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 Henkel AG and Co KGaA filed Critical Henkel AG and Co KGaA
Publication of EP1214044A2 publication Critical patent/EP1214044A2/fr
Ceased legal-status Critical Current

Links

Classifications

    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A61K8/66—Enzymes
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K8/00—Cosmetics or similar toiletry preparations
    • A61K8/18—Cosmetics or similar toiletry preparations characterised by the composition
    • A61K8/30—Cosmetics or similar toiletry preparations characterised by the composition containing organic compounds
    • A61K8/64—Proteins; Peptides; Derivatives or degradation products thereof
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
    • A61Q5/00—Preparations for care of the hair

Definitions

  • the invention relates to a method for restructuring keratin fibers.
  • Restructuring in the sense of the invention reduces the damage to keratin fibers caused by a wide variety of influences understand.
  • the restoration of natural strength plays an important role.
  • damaging influences are, for example, permanent wave treatments, oxidative dyeing or lightening of the flakes, as well as frequent washing, blow-drying and combing.
  • damage from environmental influences, such as UV light can occur.
  • Restructured fibers are characterized, for example, by an improved sheen, by an improved handle and by easier combing.
  • successful restructuring can be demonstrated physically as an increase in melting point compared to the damaged fiber.
  • a first subject of the present invention is therefore a process for restructuring keratin fibers, in which at least one enzyme of the transglutaminase type and (B) at least one active substance which has a substrate activity for the enzyme are applied to the fibers.
  • a second aspect of the present invention is also the achievement of a hair-setting effect on undamaged hair.
  • the method according to the invention can therefore also be used for setting the hair for special styling effects.
  • keratin fibers include furs, wool. Feathers and especially human hair understood.
  • transglutaminase (official name: protein-glutamine gamma-glutamyltransferase; EC 2.3.2.13). This enzyme preferably catalyzes the reaction of the amino acid residue glutamine within a protein with an alkylamine to form an N5-alkylgutamine protein with the release of ammonia.
  • An alkylamine which is preferred in nature and which plays a role in this reaction is the amino acid lysine or the amino acid residue lysine within a protein.
  • all enzymes with transglutaminase activity are suitable for carrying out the present invention.
  • transglutaminases obtained from guinea pig liver, Physarum p ⁇ lycephalum, Medicago sutiva or Bacillus subtilits are suitable.
  • Calcium-independent transglutaminases as described, for example, in EP-726 317-A2 and EP-397 606- ⁇ 1 and sold by Ajinomoto, are particularly preferred.
  • Commercial products Activa * WM and EB from Ajinomoto are preferred; Activa * WM is particularly preferred.
  • transglutaminases in cosmetic formulations are already known from the literature.
  • US Pat. No. 5,490,980 describes an agent for the treatment of human skin, hair or nails with which active ingredients containing a primary amine group are attached to the glutamine residues of the skin, hair or nails by means of transglutaminase.
  • this document does not contain any references to the subject matter of the present invention and the restructuring properties of this method.
  • active substance with substrate activity means all substances which can be attached to the hair by means of the transglutaminase. This can be done, for example, by networking the active ingredients with substrate activity with one another, that is to say by forming a type of shell around the hair. However, this can preferably also be done by covalent bonds of the active substances with substrate activity to the lysine and / or glutamine residues of the hair.
  • proteins are particularly suitable for these purposes. Protein hydrolyzates and their derivatives. Protein hydrolyzates are product mixtures that are obtained by acidic, basic or enzymatically catalyzed breakdown of proteins (proteins).
  • proteins and protein hydrolysates of both vegetable and animal origin can be used.
  • Animal proteins are, for example, elastin, collagen, keratin, silk and milk protein.
  • proteins of plant origin are soy, almond, pea, algae, potato and wheat protein.
  • proteins as such is preferred, other natural active substances with substrate activity, such as peptides, amino acids and corresponding derivatives, may also be used in their place. It is also possible, although less preferred, to use derivatives of the protein hydrolyzates, for example in the form of their fatty acid condensation products or cationically derivatized.
  • Casein, soy protein and wheat protein are particularly preferred. Casein is very particularly preferred.
  • substances which are synthetically functionalized with an H 2 NR group or an H : N (CO) -R 'group are used as active ingredients with substrate activity, where R and R' are are an unbranched C, - to C 8 alkylene group.
  • Particularly preferred functional groups are the groups H 2 N- (CH 2 ) 4 - and H : N- (CO) -CH : -CH, - derived from lysine or glutamine.
  • monomers such as lysine and glutamine
  • the active substances with substrate activity are contained in the agents used according to the invention preferably in amounts of 0.005 to 10% by weight, based on the total agent. Amounts of 0.01 to 2% by weight are particularly preferred.
  • the mass ratio of the enzyme of the transglutaminase type to the active substance with substrate activity is preferably 1: 4000 to 1: 1, particularly preferred is a mass ratio of 1: 2000 to 1:50.
  • the invention is not subject to any restrictions with regard to the timing of the method.
  • the two components (a) and (b) are applied to the fibers in this order.
  • a separate application of the components in the order (b) (a) is also according to the invention.
  • the enzyme preparation can in principle remain on the hair, in a preferred embodiment of the process according to the invention the preparation which contains the enzyme is rinsed out after an exposure time of 3 to 120 minutes. This rinsing can be done with pure water. Exposure times of 15 to 30 minutes have proven to be sufficient in most cases. Regardless of the course of the method according to the invention, it has proven to be advantageous to use the enzyme preparation at a temperature of 20 to 55 ° C., in particular 35 to 50 ° C.
  • Aqueous, alcoholic and oily preparations and mixtures thereof are particularly suitable according to the invention.
  • Aqueous preparations are particularly preferred. They can be, for example, solutions, dispersions, emulsions (water in oil emulsions, oil in water emulsions and multiple emulsions and PIT emulsions).
  • the pH of these preparations is generally 2 to 10, preferably 4 to 9 and particularly preferably 6 to 8.
  • the enzyme preparations are formulated in the form of a thickened solution.
  • the agents with thickeners such as agar, guar gum, alginates, xanthan gum, gum arabic, karaya gum, locust bean gum, linseed gums, dextrans, cellulose derivatives, e.g. B. methyl cellulose, hydroxyalkyl cellulose and carboxymethyl cellulose, starch fractions and derivatives such as amylose, amylopectin and dextrins, clays such. B. bentonite or fully synthetic hydrocolloids such.
  • the enzyme preparations are preferably formulated with low viscosity.
  • the enzyme preparations can contain all the usual constituents which are suitable for the treatment of keratin fibers, in particular human flakes.
  • Aqueous preparations are preferred. In the context of the inventions, aqueous preparations are understood to mean those compositions which contain at least 50% by weight of water, based on the total composition.
  • the enzyme preparation contains at least one surfactant. It can be both anionic, ampholytic, zwitterionic or act non-ionic surfactants as well as cationic surfactants.
  • the person skilled in the art can check a possible influence of the various surfactants on the activity of the transglutaminase-type enzyme, if necessary by simple preliminary tests.
  • a combination of anionic and nonionic surfactants or a combination of anionic and amphoteric surfactants is used.
  • Suitable anionic surfactants in agents according to the invention are all anionic surface-active substances suitable for use on the human body. These are characterized by a water-solubilizing, anionic group such as. B. a carboxylate, sulfate, sulfonate or phosphate group and a lipophilic alkyl group with about 10 to 22 carbon atoms.
  • anionic group such as. B. a carboxylate, sulfate, sulfonate or phosphate group and a lipophilic alkyl group with about 10 to 22 carbon atoms.
  • glycol or polyglycol ether groups, ester, ether and amide groups and hydroxyl groups can be contained in the molecule.
  • Non-ionic surfactants contain z.
  • B a polyol group, a polyalkylene glycol ether group or a combination of polyol and polyglycol ether group.
  • Such connections are, for example
  • Preferred nonionic surfactants are alkyl polyglycosides of the general formula R'O- (Z) ⁇ . These connections are characterized by the following parameters.
  • the alkyl radical R 1 contains 6 to 22 carbon atoms and can be either linear or branched. Primary linear and methyl-branched aliphatic radicals in the 2-position are preferred. Such alkyl radicals are, for example, 1-octyl, 1-decyl, 1-lauryl, 1-myristyl, 1-cetyl and 1-stearyl. 1-Octyl, 1 -decyl, 1-lauryl, 1-myristyl are particularly preferred. When using so-called "oxo alcohols" as starting materials, compounds with an odd number of carbon atoms in the alkyl chain predominate.
  • the alkyl polyglycosides which can be used according to the invention can contain, for example, only a certain alkyl radical R '. Usually, however, these compounds are made from natural fats and oils or mineral oils. In this case, the alkyl radicals R are mixtures corresponding to the starting compounds or corresponding to the respective working up of these compounds.
  • R ' consists essentially of C 8 - and C, 0 -alkyl groups, essentially of C 12 - and C 14 -alkyl groups, essentially of C 8 - to C, 6 -alkyl groups or essentially consists of C 12 to C 16 alkyl groups.
  • Any mono- or oligosaccharides can be used as sugar building block Z.
  • Sugar with 5 or 6 carbon atoms and the corresponding oligosaccharides are usually used.
  • sugars are glucose, fructose, galactose, arabinose, ribose, xylose, lyxose, allose, old rose, mannose, gulose, idose, talose and sucrose.
  • Preferred sugar units are glucose, fructose, galactose, arabinose and sucrose; Glucose is particularly preferred.
  • the alkyl polyglycosides which can be used according to the invention contain on average 1 1 to *> sugar units. Alkyl polyglycosides having ⁇ values of 1.1 to 1.6 are preferred. Alkyl glycosides in which ⁇ 1.1 to 1.4 are particularly preferred
  • the alkylglycosides can also be used to improve the fragrance components on the hair.
  • the person skilled in the art will therefore prefer that the effect of the parlumole on the hair going beyond the duration of the hair treatment is preferred use this substance class as a further ingredient of the preparations according to the invention
  • alkoxylated homologs of the alkyl polyglycosides mentioned can also be used according to the invention. These homologues can contain an average of up to 10 ethylene oxide and / or propylene oxide units per alkyl glycoside unit
  • Zwitterionic surfactants are surface-active compounds which carry at least one quaternary ammonium group and at least one -COO ( '- or -S0 3 ( ' group in the molecule.
  • Particularly suitable zwitterionic surfactants are the so-called betaines such as the N-alkyl-N, N-dimethylammomum glycate, for example the cocoalkyl-dimethylammonmm-glycinate, N-acyl-ammopropyl-N N-dimethylammonium glycinate, for example the cocoacylaminopropyl-dimethylammonium glycinate, and 2-alkyl- 3-carboxylmethyl-3-hydroxyethyl ⁇ m ⁇ dazohne with 8 to 18 carbon atoms in the alkyl or acyl group and the cocoacylaminoethylhydroxyethylcarboxymethylglycinate
  • a preferred zwitte ⁇ onic surfactant is known under the INCI name Cocamidopropyl Betaine fatty acid amide de ⁇ vat
  • ampholytic surfactants sub-am- pholytica surfactants are surface-active compounds which, apart from a C 8 -C, s alkyl or acyl group, contain at least one free amino group and at least one -COOH or -SO H group and are capable of forming internal salts.
  • ampholytic surfactants are N-alkyl- glycine, N-alkylpropionic acids, N-alkylaminobutyric acids, N-alkyliminodipropionic acids, N-hydroxyethyl-N-alkylamidopropylglycine, N-alkyltaurines, N-alkylsarcosines, 2-alkylaminopropionic acids and alkylaminoacetic acids each with about 8 to 18 carbon atoms in the alkyl group.
  • Particularly preferred ampholytic surfactants are N-cocoalkylaminopropionate, cocoacylaminoethyl aminopropionate and C l2 _, 8 acyl sarcosine.
  • the cationic surfactants used are, in particular, those of the quaternary ammonium compound, esterquat and amidoamine type.
  • Preferred quaternary ammonium compounds are ammonium halides, in particular chlorides and bromides, such as alkyltrimethylammonium chlorides, dialkyldimethylammonium chlorides and trialkylmethylammonium chlorides, e.g. B. cetyltrimethylammonium chloride, stearyltrimethylammonium chloride, distearyldimethylammonium chloride, lauryldimethylammonium chloride, lauryldimethylbenzylammonium chloride and tricetylmethylammonium chloride, and the compounds known under the INCI names Quaternium-27 and Quaternium-83 compounds imidazolium.
  • the long alkyl chains of the above-mentioned surfactants preferably have 10 to 18 carbon atoms.
  • Esterquats are known substances which contain both at least one ester function and at least one quaternary ammonium group as a structural element.
  • Preferred ester quats are quaternized ester salts of fatty acids with triethanolamine, quaternized ester salts of fatty acids with diethanolalkylamines and quaternized ester salts of fatty acids with 1,2-dihydroxypropyldialkylamines.
  • Such products are sold, for example, under the trademarks Stepantex ® , Dehyquart ® and Armocare ® .
  • alkylamidoamines are usually produced by amidation of natural or synthetic fatty acids and fatty acid cuts with dialkylaminoamines.
  • An invented According to the invention, particularly suitable compound from this group of substances is the lower part of the name Tegoamid "S 1 8 commercially available stearamidopropyl / dimethylamn
  • the compounds with alkylene groups used as surfactant can each be uniform substances. However, it is generally preferred to use native vegetable or animal raw materials in the production of these substances, so that mixtures of substances with different alkyl chain lengths depending on the respective raw material are obtained receipt
  • both products with a “normal” homolog distribution and those with a narrow homolog distribution can be used.
  • “Normal” homolog distribution includes mixtures of Homologs understood that are obtained in the reaction of fatty alcohol and alkylene oxide using alkali metals, alkali metal hydroxides or alkali metal alcoholates as catalysts.
  • narrow homolog distributions are obtained if, for example, hydrotalcites, alkaline earth metal salts of ether carboxylic acids, alkaline earth metal oxides, hydroxides or alcoholates are used as catalysts
  • the use of products with a narrow flomologist distribution can be preferred
  • the enzyme preparations used according to the invention preferably contain at least one oil component
  • Oil components suitable according to the invention are in principle all water-insoluble oils and fatty substances and their mixtures with solid paraffins and waxes.
  • water-soluble substances are those whose solubility in water at 20 ° C. is less than 0.1% by weight.
  • the melting point of the individual 01- or Fat components are preferably below about 40 ° C. 01 and fat components which can be liquid at room temperature, ie below 25 ° C. Be particularly preferred according to the invention.
  • a preferred group of oil components are vegetable oils.
  • vegetable oils are sunflower oil, olive oil, soybean oil, rapeseed oil, almond oil, jojobaol, orange oil, wheat germ oil, peach kernel oil and the liquid components of coconut oil
  • T ⁇ glyce ⁇ dole such as the liquid portions of beef tallow and synthetic T ⁇ glyce ⁇ dole are suitable
  • liquid paraffinols and synthetic hydrocarbons and di-n-alkyl ethers with a total of between 12 to 36 carbon atoms, in particular 12 to 24 carbon atoms, such as, for example, di-n- octyl ether, di-n-decyl ether, di-n-nonyl ether, di-n-undecyl ether, di-n-dodecyl ether, n-hexyl-n-octyl ether, n-octyl-n-decyl ether, n-decyl-n-undecyl ether, n-undecyl-n-dodecyl ether and n-hexyl-n-undecyl ether as well as di-tert-butyl ether, di-iso-pentyl ether, di-3-ethyl
  • Oil components which can likewise be used according to the invention are fatty acid and fatty alcohol esters.
  • the monoesters of fatty acids with alcohols having 3 to 24 carbon atoms are preferred. This group of substances involves the products of esterification of fatty acids with 8 to 24 carbon atoms, such as, for example, caproic acid.
  • Stearic acid Isostearic acid, oleic acid, elaidic acid, petrosine acid.
  • alcohols such as isopropyl alcohol, capron alcohol, caprylic alcohol, 2-ethylhexyl alcohol, capric alcohol, lauryl alcohol, isotridecyl alcohol, myristyl alcohol, cetyl alcohol.
  • Dicarboxylic acid esters such as di-n-butyl adipate and di- (2-ethylhexyl) adipate are also suitable.
  • Di- (2-ethylhexyl) succinate and di-isotridecylacelate as well as diol esters such as ethylene glycol dioleate, ethylene glycol di-isotridecanoate, propylene glycol di (2-ethylhexanoate), propylene glycol di-isostearate, propylene glycol di-pelargonate, butanediol -di-isostearate and neopentyl glycol di-capylate are oil components which can be used according to the invention.
  • fatty alcohols with 8 to 22 carbon atoms can also be used as oil components acting according to the invention.
  • the fatty alcohols can be saturated or unsaturated and linear or branched.
  • decanol, octanol, octenol, dodecenol can be used for the purposes of the invention.
  • the fatty alcohols derive from preferably natural fatty acids, usually from a recovery from the esters of the fatty acids Reduction can be assumed according to the invention.
  • Those fatty alcohol cuts that are produced by reducing naturally occurring triglycerides such as beef tallow, palmol, peanut oil, rubole, cottonseedol, soybean oil, sunflower oil and linseed oil or fatty acid esters resulting from their transesterification products with corresponding alcohols can also be used, and thus a mixture of different fatty alcohols
  • the enzyme preparations used according to the invention contain a care substance.
  • This care substance is preferably selected from cationic polymers and silicones
  • a first group of cationic polymers are the so-called “temporarily cationic" polymers. These polymers usually contain an amino group which is present as a quaternary ammonium group at certain pH values and is therefore cationic.
  • the permanent cationic polymers are preferred among the cationic polymers.
  • "permanently cationic” refers to those polymers which have a cationic group regardless of the pH of the agent. These are generally polymers which contain a quaternary nitrogen atom, for example in the form of an ammonium group.
  • Preferred cationic polymers are, for example, quaternized cellulose -De ⁇ vate, as they are commercially available under the names Celquat ® and Polymer JR ®
  • the compounds Celquat ® H 100, Celquat ® L 200 and Polymer JR ® 400 are preferred quaternized cellulose derivatives, polysiloxanes with quaternary groups, such as, for example Commercially available products Q2-7224 (manufacturer - Dow Corning, a stabilized trimethylsilylamodimethicone), Dow Corning ® 929 emulsion (containing a hydroxyl-ammo-modified silicone, which is also referred to as amodimefhicone), SM-2059 (manufacturer general Electric), SLM-55067 (manufacturer Wacker) and Abil ® - ⁇ uat 3270 and 3272 (manufacturer ller: Th Goldschmidt, diquaternary polydimethylsiloxanes, Oua
  • Polymeric dimethyldiallylammonium salts and their copolymers with esters and amides of acrylic acid and methacrylic acid are examples of such cationic polymers,
  • Copolymers of vinyl pyrrolidone with quaternized derivatives of dialkylamino alkyl acrylate and methacrylate such as vinyl pyrrolidone-dimethylaminoethyl methacrylate copolymers quaternized with diethyl sulfate.
  • vinyl pyrrolidone-dimethylaminoethyl methacrylate copolymers quaternized with diethyl sulfate.
  • Such compounds are available under the names Gafquat ® 734 and Gafquat ® 755 commercially, vinylpyrrolidone-vinyl imidazolium copolymers, such as those offered under the names Luviquat ® FC 370, FC 550, FC 905 and HM 552, quaternized polyvinyl alcohol, as well as the under the names Polyquaternium 2, Polyquaternium 17, Polyquaternium 18 and
  • Polyquaternium 27 known polymers with quaternary nitrogen atoms in the main polymer chain.
  • cationic polymers those under the names Polyquaternium-24 (commercial product e.g. Quatrisoft * LM 200), Polyquaternium-32, Polyquaternium-35 and Polyquaternium-37 (commercial products e.g. Salcare ® SC 92 and Salcare ® SC 95) known polymers.
  • copolymers of vinylpyrrolidone such as the commercial products Copolymer 845 (manufactured by ISP), Gaffix ® VC 713 (manufactured by ISP).
  • Gafquat ® ASCP 101 1 Gafquat ® HS 1 10, Luviquat ® 8155 and Luviquat ® MS 370 are available.
  • Cationic polymers preferred according to the invention are quaternized cellulose derivatives, polymeric dimethyldiallylammonium salts. Polyquaternium-27 and their copo- polymers and polymers of the type polyquaternium-2. Cationic cellulose derivatives, in particular the Flandels product Polymer * JR 400, and polymers of the type Polyquaternium-2, in particular the commercial product Mirapol * A-1 5, are very particularly preferred cationic polymers.
  • the cationic polymers are contained in the agents used according to the invention preferably in amounts of 0.05 to 10% by weight, based on the total agent. Quantities from 0.1 to 5% by weight are particularly preferred.
  • Ampho-polymers are also suitable as a care substance in combination with or as an alternative to cationic polymers.
  • Ampho-polymers are amphoteric polymers, ie polymers that contain both free amino groups and free - COOH or S0 3 H groups in the molecule and are capable of forming internal salts, zwitterionic polymers that contain quaternary ammonium groups and - Contain COO-- or -SO ,, - groups, and summarized those polymers which contain -COOH- or SO-, H groups and quaternary ammonium groups.
  • amphopolymer suitable is that available under the name Amphomer ® acrylic resin which is a copolymer of tert-butylaminoethyl methacrylate, N- (l, l, 3,3-tetramethylbutyl) -acrylamide and two or more monomers from the group Acrvlklare, Methacrylic acid and its simple esters.
  • preferred amphopolymers are composed of unsaturated carboxylic acids (e.g. acrylic and methacrylic acid), cationically derivatized unsaturated carboxylic acids (e.g.
  • acrylamidopropyl-trimethylammonium chloride and optionally other ionic or nonionic monomers, as for example in German Laid-open specification 39 29 973 and the state of the art cited therein.
  • Care substances that can be used according to the invention are furthermore silicone oils and silicone gums, in particular dialkyl and alkylarylsiloxanes, such as, for example, dimethyl polysiloxane and methylphenylpolysiloxane, and their alkoxylated and quaternized analogs.
  • silicone oils and silicone gums in particular dialkyl and alkylarylsiloxanes, such as, for example, dimethyl polysiloxane and methylphenylpolysiloxane, and their alkoxylated and quaternized analogs.
  • silicones are the products sold by Dow Corning under the names DC 190, DC 200 and DC 1401 and the commercial products DC 344 and DC 345 from Dow Corning.
  • Q2-7224 (manufacturer: Dow Corning; a stabilized trimethyl silyl amodimethicone), Do Corning ® 929 Emulsion (containing a hydroxylamino-modified silicone which is also known as amodimethicone), SM-2059 (manufacturer: General Electric), SLM -55067 (manufacturer: Wacker) as well as Abil ® -Quat 3270 and 3272 (manufacturer: Th. Goldschmidt; diquaternary polydimethylsiloxanes, Quaternium-80) and the commercial product Fancorsil ® LIM-1.
  • the product Dow Corning ® 1784 is a suitable anionic silicone oil.
  • the enzyme preparations can in principle contain all further components known to those skilled in the art for such cosmetic products.
  • auxiliaries and additives are, for example, nonionic polymers such as, for example, vinylpyrrolidone / vinyl acrylate copolymers, polyvinylpyrrolidone and vinylpyrrolidone / vinyl acetate copolymers and polysiloxanes,
  • Structurants such as maleic acid, lactic acid and amino acids hair conditioning compounds such as phospholipids, such as soybean lecithin.
  • Structurants such as maleic acid, lactic acid and amino acids
  • hair conditioning compounds such as phospholipids, such as soybean lecithin.
  • Solvents and mediators such as ethanol, isopropanol, ethylene glycol, propylene glycol, glycerin and diethylene glycol, active ingredients that improve fiber structure, in particular panthenol and mono-, di- and oligosaccharides such as, for example, glucose, galactose, fructose, fructose and lactose, quaternized amines such as methyl-l alkylamidoethyl-2-alkylimidazolinium methosulfate defoamers such as silicones, dyes for coloring the agent, Anti-dandruff agents such as piroctone olamine, zinc omadine and climbazole, light stabilizers, in particular derivatized benzophenones, cinnamic acid derivatives and triazines,
  • active ingredients that improve fiber structure in particular panthenol and mono-, di- and oligosaccharides such as, for example, glucose, galactose,
  • Substances for adjusting the pH such as customary acids, in particular edible acids and bases,
  • Active ingredients such as allantoin, pyrrolidone carboxylic acids and their salts as well as bisabolol, vitamins, provitamins and vitamin precursors, in particular those from groups A, B 3 , B 5 , B 6 , C, E, F and H,
  • Plant extracts such as green tea extracts. Oak bark, nettle, witch hazel, hops, chamomile, burdock root, horsetail, hawthorn, linden flowers, almond, aloe vera, spruce needle, horse chestnut, sandalwood, juniper, coconut, mango, apricot, lime.
  • Cholesterol Cholesterol
  • Consistency enhancers such as sugar esters, polyol esters or polyol alkyl ethers, fats and waxes such as walrus, beeswax, montan wax and paraffins, fatty acid alkanolamides,
  • Opacifiers such as latex, styrene / PVP and styrene / acrylamide copolymers pearlescent agents such as ethylene glycol mono- and distearate and PEG-3 distearate, pigments,
  • Stabilizing agent for hydrogen peroxide and other oxidizing agents blowing agents such as propane-butane mixtures, N 2 0, dimethyl ether, C0 2 and air.
  • a second subject of the invention is the use of (A) at least one enzyme of the transglutaminase type and (B) at least one active ingredient which has a substrate activity for the enzyme for the restructuring of keratin fibers.
  • a third subject of the invention is the use of (A) at least one enzyme of the transglutaminase type and (B) at least one active ingredient which has a substrate activity for the enzyme for strengthening keratin fibers.
  • a fourth object of the present invention is a two-part kit for restructuring keratin fibers, which contains a first preparation containing one (a) an active substance with substrate activity and a second composition containing (b) an enzyme of the transglutaminase type.
  • Strands from Alkinco (0.5 g, code 6634) were subjected to conventional permanent wave treatments with the commercial product Poly Lock-Normal permanent wave.
  • the fibers were exposed to the reducing solution (containing 7.9% by weight thioglycolic acid) in a first step for 40 minutes at room temperature, rinsed with pure water and then fixed at room temperature for 10 minutes (oxidation solution containing 2.6 % By weight hydrogen peroxide). After the oxidative treatment, the fibers were rinsed and dried.
  • the strands were each at a temperature of 50 ° C. for 60 minutes in 2 ml of an aqueous casein solution (30 mg / ml, with tris (hydroxymethyl) aminomethane (TRIS) -HC1-
  • the strands were each immersed at 50 ° C. for 60 minutes in 2 ml of an aqueous casein solution (30 mg / ml, adjusted to pH 7.6 with tris (hydroxymethyl) aminomethane (TRIS) -HC1 buffer).
  • an aqueous casein solution (30 mg / ml, adjusted to pH 7.6 with tris (hydroxymethyl) aminomethane (TRIS) -HC1 buffer).
  • the tresses were each ml at a temperature of 50 ° C for 60 minutes in 2 an aqueous transglutaminase solution (l, 2 mg / ml Activation ® WM corresponding to 0,012mg / ml active substance, with TRIS-FICL buffer at pH 7.6 adjusted) immersed , c) Evidence of the hair structuring effect using HP-DSC

Landscapes

  • Health & Medical Sciences (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Animal Behavior & Ethology (AREA)
  • General Health & Medical Sciences (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Birds (AREA)
  • Epidemiology (AREA)
  • Cosmetics (AREA)
  • Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)

Abstract

Procédé de restructuration de fibres kératiniques, qui consiste à appliquer sur les fibres (A) au moins une enzyme du type de la transglutaminase et (B) au moins un principe actif qui peut se fixer sur les fibres à l'aide de ladite enzyme. Ce procédé permet la restructuration de fibres endommagées.
EP00974377A 1999-09-22 2000-09-13 Procede de restructuration de fibres keratiniques Ceased EP1214044A2 (fr)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
DE1999145487 DE19945487A1 (de) 1999-09-22 1999-09-22 Verfahren zur Restrukturierung keratinischer Fasern
DE19945487 1999-09-22
PCT/EP2000/008924 WO2001021139A2 (fr) 1999-09-22 2000-09-13 Procede de restructuration de fibres keratiniques

Publications (1)

Publication Number Publication Date
EP1214044A2 true EP1214044A2 (fr) 2002-06-19

Family

ID=7922949

Family Applications (1)

Application Number Title Priority Date Filing Date
EP00974377A Ceased EP1214044A2 (fr) 1999-09-22 2000-09-13 Procede de restructuration de fibres keratiniques

Country Status (4)

Country Link
EP (1) EP1214044A2 (fr)
AU (1) AU1271001A (fr)
DE (1) DE19945487A1 (fr)
WO (1) WO2001021139A2 (fr)

Families Citing this family (11)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
DE10163052A1 (de) * 2001-12-21 2003-07-17 Henkel Kgaa Restrukturierung und Ausrüstung keratinischer Fasern
DE10356494A1 (de) * 2003-12-03 2005-07-07 Henkel Kgaa Verfahren zur dauerhaften Ausrüstung keratinischer Fasern mit Pflegewirkstoffen durch Carboxylesterhydrolasen
DE102004041568A1 (de) * 2004-08-26 2006-03-09 Henkel Kgaa Zubereitung mit enzymatisch katalysierter Freisetzung von Pflegestoffen für keratinische Fasern in situ
FR2876286B1 (fr) * 2004-10-07 2007-01-12 Oreal Procede de mise en forme de fibres keratiniques
WO2006040446A1 (fr) * 2004-10-07 2006-04-20 L'oreal Procédé de mise en forme de fibres kératiniques
WO2006040447A1 (fr) * 2004-10-07 2006-04-20 L'oreal Procédé de traitement cosmétique des fibres kératiniques et utilisation d'un inhibiteur de transglutaminase
FR2876285B1 (fr) * 2004-10-07 2007-11-16 Oreal Procede de traitement cosmetique des fibres keratiniques et utilisation d'un inhibiteur de transglutaminase
US9011828B2 (en) 2011-01-25 2015-04-21 Elc Management, Llc Compositions and methods for permanent straightening of hair
FR3006588B1 (fr) * 2013-06-07 2016-02-12 Isp Investments Inc Extrait peptidique de soja et son utilisation cosmetique pour renforcer la structure du cheveu
JP6889962B1 (ja) * 2021-01-07 2021-06-18 ミテジマ化学株式会社 獣毛の改質方法
WO2024116027A1 (fr) * 2022-11-28 2024-06-06 Uprising Science Private Limited Composition de soin capillaire, formulation et méthode de traitement et de gestion des cheveux

Family Cites Families (10)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2719166B2 (ja) * 1989-02-02 1998-02-25 鐘紡株式会社 毛髪化粧料組成物
JPH0395109A (ja) * 1989-09-08 1991-04-19 Kanebo Ltd 毛髪化粧料
EP0615745B1 (fr) * 1993-02-19 1997-05-02 Howard Green Compositions contenant des protéines à partir de corneocytes
US5490980A (en) * 1994-09-28 1996-02-13 Chesebrough-Pond's Usa Co., Division Of Conopco, Inc. Covalent bonding of active agents to skin, hair or nails
JP3567951B2 (ja) * 1995-10-12 2004-09-22 ライオン株式会社 毛髪処理剤及び毛髪処理方法
FR2740331B1 (fr) * 1995-10-25 1997-12-19 Sederma Sa Nouvelles compositions cosmetiques pour le traitement des cheveux et du cuir chevelu
DE19882746T1 (de) * 1997-04-03 2001-10-18 California Inst Of Techn Enzymvermittelte Modifikation von Fibrin für das Gewebs-Engineering
FR2767833B1 (fr) * 1997-08-29 2001-03-02 Oreal Polypeptide isole de l'epiderme et son utilisation
WO1999036570A2 (fr) * 1998-01-20 1999-07-22 Pericor Science Inc Liaison d'agents au tissu par transglutaminase
JP2002515555A (ja) * 1998-05-20 2002-05-28 ノボザイムス ノース アメリカ，インコーポレイティド 羊毛の酵素処理法

Non-Patent Citations (2)

* Cited by examiner, † Cited by third party
Title
None *
See also references of WO0121139A3 *

Also Published As

Publication number Publication date
WO2001021139A3 (fr) 2001-08-16
WO2001021139A2 (fr) 2001-03-29
AU1271001A (en) 2001-04-24
DE19945487A1 (de) 2001-03-29

Similar Documents

Publication Publication Date Title
EP1812117B1 (fr) Procede de restructuration de fibres keratiniques
EP1594448B1 (fr) Agents de traitement capillaire avec des melanges de tensioactifs
DE10005162A1 (de) Kosmetisches Mittel
DE10338883A1 (de) Verfahren zur Glättung keratinhaltiger Fasern
DE19523596A1 (de) Zubereitung zur Behandlung keratinischer Fasern
EP2020227B1 (fr) Dérivés de cellulose cationiques en cosmétique
DE19738303A1 (de) Verwendung einer Wirkstoffkombination und Mittel
EP1214044A2 (fr) Procede de restructuration de fibres keratiniques
DE19540853A1 (de) Haarbehandlungsmittel
DE102004024509B4 (de) Verfahren und Zubereitungen zur Restrukturierung von Haaren
DE19907715A1 (de) Zubereitungen zur Behandlung keratinischer Fasern
EP1154752B1 (fr) Preparations destinees au traitement de fibres keratiniques
EP1779845B1 (fr) Utilisation de dérivés de cellulose cationiques en cosmétique
DE102004045253A1 (de) Kationische Copolymere und ihre Verwendung in haarkosmetischen Zubereitungen
WO2006029757A1 (fr) Melange de principes actifs pour traiter des fibres keratiniques
DE102004041573A1 (de) Neues Mittel zur Behandlung keratinischer Fasern
DE10243038A1 (de) Haarbehandlungsmittel mit konditionierenden Eigenschaften
DE102004041568A1 (de) Zubereitung mit enzymatisch katalysierter Freisetzung von Pflegestoffen für keratinische Fasern in situ
DE10243037A1 (de) Haarbehandlungsmittel mit festigenden Eigenschaften
DE4317576A1 (de) Haarnachbehandlungsmittel
DE10162143A1 (de) Verfahren zur dauerhaften Verformung keratinischer Fasern und Mittel
EP1568348A1 (fr) Procédé d'apprêt permanent des fibres kératiniques par un conditionneur à l'aide d'un hydrolase d'ester carboxylique
DE102006059270A1 (de) Verwendung von Styphnolobium
DE102004024508A1 (de) Verfahren zur Restrukturierung keratinischer Fasern mit Dithiolen

Legal Events

Date Code Title Description
PUAI Public reference made under article 153(3) epc to a published international application that has entered the european phase

Free format text: ORIGINAL CODE: 0009012

17P Request for examination filed

Effective date: 20020313

AK Designated contracting states

Kind code of ref document: A2

Designated state(s): AT BE CH CY DE DK ES FI FR GB GR IE IT LI LU MC NL PT SE

17Q First examination report despatched

Effective date: 20060629

STAA Information on the status of an ep patent application or granted ep patent

Free format text: STATUS: THE APPLICATION HAS BEEN REFUSED

18R Application refused

Effective date: 20070127