Classifications

• • C—CHEMISTRY; METALLURGY
  • C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
  • C09K—MATERIALS FOR MISCELLANEOUS APPLICATIONS, NOT PROVIDED FOR ELSEWHERE
  • C09K3/00—Materials not provided for elsewhere
• • C—CHEMISTRY; METALLURGY
  • C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
  • C09D—COATING COMPOSITIONS, e.g. PAINTS, VARNISHES OR LACQUERS; FILLING PASTES; CHEMICAL PAINT OR INK REMOVERS; INKS; CORRECTING FLUIDS; WOODSTAINS; PASTES OR SOLIDS FOR COLOURING OR PRINTING; USE OF MATERIALS THEREFOR
  • C09D7/00—Features of coating compositions, not provided for in group C09D5/00; Processes for incorporating ingredients in coating compositions
• • 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
  • 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
  • A61K8/72—Cosmetics or similar toiletry preparations characterised by the composition containing organic macromolecular compounds
  • A61K8/73—Polysaccharides
• • 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
  • A61K8/72—Cosmetics or similar toiletry preparations characterised by the composition containing organic macromolecular compounds
  • A61K8/81—Cosmetics or similar toiletry preparations characterised by the composition containing organic macromolecular compounds obtained by reactions involving only carbon-to-carbon unsaturated bonds
  • A61K8/8141—Compositions of homopolymers or copolymers of compounds having one or more unsaturated aliphatic radicals, each having only one carbon-to-carbon double bond, and at least one being terminated by only one carboxyl radical, or of salts, anhydrides, esters, amides, imides or nitriles thereof; Compositions of derivatives of such polymers
  • A61K8/8147—Homopolymers or copolymers of acids; Metal or ammonium salts thereof, e.g. crotonic acid, (meth)acrylic acid; Compositions of derivatives of such polymers
• • 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
  • A61K8/72—Cosmetics or similar toiletry preparations characterised by the composition containing organic macromolecular compounds
  • A61K8/81—Cosmetics or similar toiletry preparations characterised by the composition containing organic macromolecular compounds obtained by reactions involving only carbon-to-carbon unsaturated bonds
  • A61K8/8141—Compositions of homopolymers or copolymers of compounds having one or more unsaturated aliphatic radicals, each having only one carbon-to-carbon double bond, and at least one being terminated by only one carboxyl radical, or of salts, anhydrides, esters, amides, imides or nitriles thereof; Compositions of derivatives of such polymers
  • A61K8/8152—Homopolymers or copolymers of esters, e.g. (meth)acrylic acid esters; Compositions of derivatives of such polymers
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61Q—SPECIFIC USE OF COSMETICS OR SIMILAR TOILETRY PREPARATIONS
  • A61Q19/00—Preparations for care of the skin
• • C—CHEMISTRY; METALLURGY
  • C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
  • C09D—COATING COMPOSITIONS, e.g. PAINTS, VARNISHES OR LACQUERS; FILLING PASTES; CHEMICAL PAINT OR INK REMOVERS; INKS; CORRECTING FLUIDS; WOODSTAINS; PASTES OR SOLIDS FOR COLOURING OR PRINTING; USE OF MATERIALS THEREFOR
  • C09D7/00—Features of coating compositions, not provided for in group C09D5/00; Processes for incorporating ingredients in coating compositions
  • C09D7/40—Additives
  • C09D7/43—Thickening agents
  • C09D7/44—Combinations of two or more thickening agents
• • C—CHEMISTRY; METALLURGY
  • C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
  • C09K—MATERIALS FOR MISCELLANEOUS APPLICATIONS, NOT PROVIDED FOR ELSEWHERE
  • C09K23/00—Use of substances as emulsifying, wetting, dispersing, or foam-producing agents
• • C—CHEMISTRY; METALLURGY
  • C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
  • C09K—MATERIALS FOR MISCELLANEOUS APPLICATIONS, NOT PROVIDED FOR ELSEWHERE
  • C09K3/00—Materials not provided for elsewhere
  • C09K3/18—Materials not provided for elsewhere for application to surfaces to minimize adherence of ice, mist or water thereto; Thawing or antifreeze materials for application to surfaces
  • C09K3/185—Thawing materials
• • C—CHEMISTRY; METALLURGY
  • C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
  • C09K—MATERIALS FOR MISCELLANEOUS APPLICATIONS, NOT PROVIDED FOR ELSEWHERE
  • C09K8/00—Compositions for drilling of boreholes or wells; Compositions for treating boreholes or wells, e.g. for completion or for remedial operations
  • C09K8/60—Compositions for stimulating production by acting on the underground formation
• • C—CHEMISTRY; METALLURGY
  • C09—DYES; PAINTS; POLISHES; NATURAL RESINS; ADHESIVES; COMPOSITIONS NOT OTHERWISE PROVIDED FOR; APPLICATIONS OF MATERIALS NOT OTHERWISE PROVIDED FOR
  • C09K—MATERIALS FOR MISCELLANEOUS APPLICATIONS, NOT PROVIDED FOR ELSEWHERE
  • C09K8/00—Compositions for drilling of boreholes or wells; Compositions for treating boreholes or wells, e.g. for completion or for remedial operations
  • C09K8/60—Compositions for stimulating production by acting on the underground formation
  • C09K8/62—Compositions for forming crevices or fractures
  • C09K8/66—Compositions based on water or polar solvents
  • C09K8/68—Compositions based on water or polar solvents containing organic compounds
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
  • A61K2800/00—Properties of cosmetic compositions or active ingredients thereof or formulation aids used therein and process related aspects
  • A61K2800/40—Chemical, physico-chemical or functional or structural properties of particular ingredients
  • A61K2800/48—Thickener, Thickening system
• • C—CHEMISTRY; METALLURGY
  • C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
  • C08L—COMPOSITIONS OF MACROMOLECULAR COMPOUNDS
  • C08L5/00—Compositions of polysaccharides or of their derivatives not provided for in groups C08L1/00 or C08L3/00

Definitions

• the present invention relates to the use of a synergistic mixture of water-soluble, thickening polymers and hydrophobins for thickening aqueous phases and the degradation of the thickening effect by cleaving the protein.
• the invention further relates to a thickening composition of water-soluble polymers, hydrophobins and water.
• Water-soluble, thickening polymers are used in many fields of technology, for example in the field of cosmetics, in food, for the production of cleaning agents, printing inks, emulsion paints or in the production of oil.
• polymers with thickening effect a multiplicity of chemically different polymers are used, for example biopolymers such as xanthan, starch, gelatin, modified biopolymers such as hydroxyethylcellulose, hydroxypropylcellulose or carboxymethylcellulose or synthetic polymers such as polyvinyl alcohols, polyacrylic acids or partially crosslinked polyacrylic acids or polyacrylamides, and in particular Copolymers of (meth) acrylic acid with other monomers.
• biopolymers such as xanthan, starch, gelatin
• modified biopolymers such as hydroxyethylcellulose, hydroxypropylcellulose or carboxymethylcellulose
• synthetic polymers such as polyvinyl alcohols, polyacrylic acids or partially crosslinked polyacrylic acids or polyacrylamides, and in particular Copolymers of (meth) acrylic acid with other monomers.
• Another class of thickening polymers are the so-called associative thickeners. These are water-soluble polymers which have side or terminal hydrophobic groups, such as longer alkyl chains. In aqueous solution, such hydrophobic groups can associate with themselves or with other hydrophobic group-containing substances. As a result, an associative network is formed, through which the medium is thickened. Examples of such polymers are disclosed in EP 013 836 A1 or WO 2006/16035.
• Hydrophobins are small proteins of about 100 to 150 amino acids, which are characteristic of filamentous fungi, for example Schizophyllum commune. They usually have 8 cysteine units. They form relatively low-viscosity solutions in water at a low concentration of up to about 3% by weight, while more concentrated solutions finally become gelatinous.
• EP 1 252 516 discloses the coating of various substrates with a hydrophobin-containing solution at a temperature of 30 to 80 0 C. Further, for example, the use as demulsifier (WO 2006/103251) as evaporation retarders (WO 2006/128877) or soiling inhibitor (WO 2006/103215).
• WO 2006/103253 discloses drilling muds containing hydrophobins. The formulations may contain, in addition to the hydrophobins, a wide variety of other components, including polymers or copolymers, such as polyacrylamides.
• WO 96/41882 proposes the use of hydrophobins as emulsifiers, thickeners, surface-active substances, for hydrophilicizing hydrophobic surfaces, for improving the water resistance of hydrophilic substrates, for producing oil-in-water emulsions or for water-in-oil emulsions in front. Furthermore, pharmaceutical applications such as the preparation of ointments or creams and cosmetic applications such as skin protection or the production of hair shampoos or hair rinses are proposed.
• thickening polymers For some applications of thickening polymers, it is desirable that the thickening effect also be reversed.
• a typical example of this is the so-called "fracturing" process in the course of petroleum production, where a solution of a thickening polymer is forced into a borehole, which creates new cracks in the petroleum formation, which better cleans the oil from the formation After completion of fracturing, however, the viscosity of the polymer solution should be reduced again so that the polymer solution does not clog the cracks formed.
• oxidizing agents has been proposed for the degradation of the polymers.
• biopolymers such as polysaccharides
• degradation enzymes that split the polymer chain at certain points.
• the object of the invention was to provide a thickening composition in which the thickening effect can be "switched off” again in a simple manner.
• hydrophobins and water-soluble polymers synergistically cooperate and form well-thickening compositions even at low concentrations.
• the thickening effect can, if desired, be eliminated in a simple manner by splitting the hydrophobin, for example with the aid of enzymes. Cleavage of the thickening polymer itself is not required. Accordingly, the use of a synergistic mixture for thickening aqueous phases was found, wherein the mixture
• At least one water-soluble, thickening polymer (A), and at least one hydrophobin (B), At least one water-soluble, thickening polymer (A), and at least one hydrophobin (B),
• weight ratio (A) / (B) is 5: 1 to 1:10, and wherein the amounts are based on the sum of all components of the aqueous phase.
• At least one water-soluble, thickening polymer (A) is used for thickening.
• Suitable water-soluble, thickening polymers (A) generally have a number-average molar mass M n of from 1000 to 10 000 000 g / mol, preferably from 10 000 to 1 000 000 g / mol on.
• the polymers (A) used can be completely miscible with water, without this being imperative for carrying out the invention. However, they must dissolve in water at least to such an extent that the use according to the invention is possible. As a rule, the polymers (A) used should have a solubility in water of at least 50 g / l, preferably 100 g / l and particularly preferably at least 200 g / l.
• water-soluble also refers to alkali-soluble emulsions (ASE) of polymers.
• thickening polymer is used in this invention in a manner known in principle for those polymers which significantly increase the viscosity of aqueous solutions even in comparatively low concentrations.
• Suitable water-soluble, thickening polymers (A) comprise hydrophilic groups in addition to carbon and hydrogen in such an amount that the polymers (A) become water-soluble at least in certain pH ranges.
• they are functional groups which comprise O and / or N atoms.
• the O and / or N atoms may be part of the main chain of the polymer and / or be arranged laterally or terminally.
• C O
• ether groups -O- in particular polyethylene oxide groups - (CH 2 -CH 2 -O-) n -, where n is preferably from 1 to 200,
• Examples of preferred functional groups include hydroxy groups -OH, carboxyl groups -COOH, sulfonic acid groups -SO 3 H, carboxamide groups -C (O) -NH 2 and polyethylene oxide groups - (CH 2 -CH 2 -O-) n-, where n is preferably from 1 to 200 stands.
• Water-soluble, thickening polymers (A) suitable for carrying out the invention generally have a numerical ratio of oxygen and nitrogen atoms to the total number of oxygen and nitrogen and carbon atoms (no + nn) / (nc + no + nn) from 0.2 to 0.5, preferably 0.3 to 0.46.
• the thickening polymers may be naturally occurring polymers, modified natural polymers or synthetically produced polymers.
• Naturally occurring thickening polymers include, for example, polypeptides such as gelatin or casein.
• polysaccharides may also be polysaccharides, wherein the term should also include modified polysaccharides.
• polysaccharides include starch, xanthans or glucans.
• modified polysaccharides include hydroxyethylcellulose, hydroxypropylcellulose, hydroxypropylmethylcellulose or carboxymethylcellulose.
• xanthans or glucans can be used.
• synthetic polymers include poly (meth) acrylic acid or its salts, poly (meth) acrylic acid-containing copolymers or their salts, polyacrylamides, polyvinylpyrrolidone. rolidone, polyvinyl alcohol or polyethylene glycols. They may also be crosslinked poly (meth) acrylic acids or poly (meth) acrylic acid copolymers, provided that the crosslinking is not so strong that it impairs the water solubility of the polymers.
• the polyacrylic acids may be solutions of polyacrylic acid or copolymers thereof or also precipitation polymers based on polyacrylic acid, which may also be slightly crosslinked.
• alkali-soluble emulsions of (meth) acrylic acid copolymers include alkali-soluble emulsions of (meth) acrylic acid copolymers. Such copolymers are present in the acidic pH range as comparatively low-viscosity emulsions in water. In the alkaline range, the polymers dissolve in the aqueous phase and increase their viscosity significantly.
• Alkali-soluble emulsions are, for example, copolymers which contain (meth) acrylic acid and hydrophobic comonomers, in particular (meth) acrylic esters, in particular C 1 -C 4 -alkyl (meth) acrylates, such as methyl (meth) acrylate, ethyl (meth ) acrylate or n-butyl (meth) acrylate.
• the amount of (meth) acrylic acid is usually 10 to 50 wt.%
• hydrophobic associating polymers may be hydrophobic associating polymers. These are understood in a manner known in principle to be water-soluble polymers which have lateral or terminal hydrophobic groups, such as, for example, longer alkyl chains. In aqueous solution, such hydrophobic groups can associate with themselves or with other hydrophobic group-containing substances, which causes a strong thickening effect.
• Examples of preferred hydrophobically associating polymers include copolymers comprising acidic monomers, preferably (meth) acrylic acid, and at least one (meth) acrylic acid ester, wherein the ester group comprises a hydrocarbon radical R 1 having at least 6 carbon atoms, preferably 8 to 30 carbon atoms. These may be preferably linear aliphatic hydrocarbon radicals or hydrocarbon radicals comprising aromatic units, in particular ⁇ -aryl-substituted alkyl radicals.
• R 3 is preferably a polyalkylene oxide group - (CH 2 -CH (R 4 ) -O-) n -, where n is a number from 2 to 100, preferably 5 to 50, and R 4 is independently H or CH 3 with the proviso that it is at least 50 mol%, preferably at least 80 mol% of the radicals R 4 is H.
• R 4 is exclusively H.
• the other monomers may be finally (meth) acrylic acid act.
• further (meth) acrylic esters, in particular C 1 -C 4 -alkyl (meth) acrylates, such as methyl (meth) acrylate, ethyl (meth) acrylate or n-butyl (meth) acrylate to be present.
• alkali-soluble emulsions can be obtained which additionally have hydrophobic associating groups.
• hydrophobically associating polymers include hydrophobically modified cellulose ethers, hydrophobically modified polyacrylamides, hydrophobically modified polyethers, for example polyethylene glycol terminated with C 6 -C 30 -hydrocarbon groups or hydrophobically associating polyurethanes which comprise polyether segments and terminal hydrophobic groups.
• At least one hydrophobin (B) is furthermore used for thickening.
• hydrophobins is intended to mean polypeptides of the general structural formula (I)
• X is selected for each of the 20 naturally occurring amino acids (Phe, Leu, Ser, Tyr, Cys, Trp, Pro, His, GIn, Arg, Ne Met, Thr, Asn, Lys, VaI, Ala, Asp, Glu, GIy) can stand.
• the radicals X may be the same or different.
• the indices standing at X each represent the number of amino acids in the respective subsequence X
• C stands for cysteine, alanine, serine, glycine, methionine or threonine, at least four of the radicals named C being cysteine
• the indices n and m independently represent natural numbers between 0 and 500, preferably between 15 and 300.
• the polypetides according to the formula (I) are further characterized by the property that at room temperature after coating a glass surface, they increase the contact angle of a water droplet of at least 20 °, preferably at least 25 ° and particularly preferably 30 °, in each case compared with the contact angle an equally large drop of water with the uncoated glass surface.
• the amino acids designated C to C 8 are preferably cysteines; However, they can also be replaced by other amino acids of similar space filling, preferably by alanine, serine, threo- nin, methionine or glycine. However, at least four, preferably at least 5, particularly preferably at least 6 and in particular at least 7 of the positions C to C 8 should consist of cysteines. Cysteines can either be reduced in the proteins according to the invention or form disulfide bridges with one another. Particularly preferred is the intramolecular formation of CC bridges, in particular the formation of at least one, preferably 2, more preferably 3 and most preferably 4 intramolecular disulfide bridges. In the exchange of cysteines described above by amino acids of similar space filling, it is advantageous to exchange in pairs those C positions which are capable of forming intramolecular disulfide bridges with one another.
• cysteines, serines, alanines, glycines, methionines or threonines are also used in the positions marked X, the numbering of the individual C positions in the general formulas may change accordingly.
• X, C and the indices standing at X and C have the above meaning
• the subscripts n and m are numbers between 0 and 350, preferably 15 to 300
• the proteins continue through the characterized above contact angle change, and it is further at least 6 of the radicals C is cysteine. Most preferably, all of the C radicals are cysteine.
• the proteins are further characterized by the abovementioned contact angle change, and at least 6 of the C named residues are cysteine. Most preferably, all of the C radicals are cysteine.
• radicals X n and X m may be peptide sequences that are naturally also linked to a hydrophobin. However, one or both of the residues may be peptide sequences that are not naturally linked to a hydrophobin. Including such radicals X N and / or X m are to be understood, in which a naturally occurring in a hydrophobin peptide sequence is extended by a non-naturally occurring in a hydrophobin peptide sequence. If X n and / or X m are naturally non-hydrophobin-linked peptide sequences, such sequences are generally at least 20, preferably at least 35 amino acids long. They may, for example, be sequences from 20 to 500, preferably 30 to 400 and particularly preferably 35 to 100 amino acids.
• Such a residue, which is not naturally linked to a hydrophobin, will also be referred to below as a fusion partner.
• the proteins may consist of at least one hydrophobin part and one fusion partner part which in nature do not coexist in this form. Fusion-hydrophobins from fusion partner and hydrophobin part have been disclosed for example in WO 2006/082251, WO 2006/082253 and WO 2006/131564.
• the fusion partner portion can be selected from a variety of proteins. Only a single fusion partner can be linked to the hydrophobin moiety, or several fusion partners can also be linked to a hydrophobin moiety, for example at the amino terminus (X n ) and at the carboxy terminus (X m ) of the hydrophobin moiety. However, it is also possible, for example, to link two fusion partners with a position (X n or X m ) of the protein according to the invention.
• fusion partners are proteins that occur naturally in microorganisms, in particular in E. coli or Bacillus subtilis.
• fusion partners are the sequences yaad (SEQ ID NO: 16 in WO 2006/082251), yaae (SEQ ID NO: 18 in WO 2006/082251), ubiquitin and thioredoxin.
• fragments or derivatives of said sequences which comprise only a part, for example 70 to 99%, preferably 5 to 50%, and particularly preferably 10 to 40% of said sequences, or in which individual amino acids or nucleotides are opposite the said sequence are changed, wherein the percentages in each case refers to the number of amino acids.
• the fusion hydrophobin in addition to the fusion partner mentioned as one of the groups X n or X m or as a terminal component of such a group on a so-called affinity domain (affinity tag / affinity tail) on.
• affinity domains include (His) k, (Arg) k, (Asp) k, (Phe) k or (Cys) k groups, wherein k is generally a natural number of 1 to 10. It may preferably be a (His) k group, where k is 4 to 6.
• the group X n and / or m X may consist exclusively of such an affinity domain or a naturally or non-naturally linked to a hydrophobin radical X n and X m is extended by a terminal affinity domain.
• hydrophobins used according to the invention may also be modified, for example by glycosylation, acetylation or else by chemical crosslinking, for example with glutaraldehyde.
• a characteristic of the hydrophobins or their derivatives used according to the invention is the change of surface properties when the surfaces are coated with the proteins. The change in the surface properties can be experimentally determined, for example, by measuring the contact angle of a water drop before and after coating the surface with the hydrophobin and determining the difference between the two measurements.
• contact angle measurements is known in principle to the person skilled in the art.
• the measurements refer to room temperature and water drops of 5 ⁇ l and the use of glass slides as substrate.
• the exact experimental conditions for an exemplary method for measuring the contact angle are shown in the experimental part.
• the fusion proteins used according to the invention have the property of increasing the contact angle by at least 20 °, preferably at least 25 °, particularly preferably at least 30 °, in each case compared with the contact angle of a water droplet of the same size with the uncoated glass surface.
• hydrophobins for carrying out the present invention are the hydrophobins of the type dewA, rodA, hypA, hypB, sc3, basfi, basf2. These hydrophobins including their sequences are disclosed, for example, in WO 2006/82251. Unless stated otherwise, the sequences given below refer to sequences disclosed in WO 2006/82251. An overview table with the SEQ ID numbers is in WO 2006/82251 on page 20. Unless expressly stated otherwise, all SEQ IDs cited below refer to the SEQ IDs cited by WO2006 / 82251.
• fusion proteins yaad-Xa-dewA-his (SEQ ID NO: 20), yaad-Xa-rodA-his (SEQ ID NO: 22) or yaad-Xa-basfl-his (SEQ ID NO: 24) with the polypeptide sequences given in parentheses and the nucleic acid sequences coding therefor, in particular the sequences according to SEQ ID NO: 19, 21, 23.
• yaad-Xa-dewA-his SEQ ID NO: 20
• proteins which, starting from the amino acid sequences shown in SEQ ID NO.
• Particularly suitable derivatives for carrying out the present invention are from yaad-XadewA-his (SEQ ID NO: 20), yaad-Xa-rodA-his (SEQ ID NO: 22) or yaad-Xa-basf1-his (SEQ ID NO: 24) derivatives derived from truncation of the yaad fusion partner.
• yaad-XadewA-his SEQ ID NO: 20
• yaad-Xa-rodA-his SEQ ID NO: 22
• yaad-Xa-basf1-his SEQ ID NO: 24
• the truncated residue should comprise at least 20, preferably at least 35, amino acids.
• a truncated radical having 20 to 293, preferably 25 to 250, particularly preferably 35 to 150 and for example 35 to 100 amino acids can be used.
• An example of such a protein is yaad40-Xa-dewA-his (SEQ ID NO: 26 in WO 2007/014897), which has a reduced to 40 amino acids yaad residue.
• a cleavage site between the hydrophobin and the fusion partner or the fusion partners can be used to cleave off the fusion partner and release the pure hydrophobin in underivatized form (for example by BrCN cleavage to methionine, factor Xa, enterokinase, thrombin, TEV cleavage Etc.).
• hydrophobins used in the invention can be prepared chemically by known methods of peptide synthesis, such as by Merrifield solid phase synthesis.
• Naturally occurring hydrophobins can be isolated from natural sources by suitable methods. As an example, let Wösten et. al., Eur. J Cell Bio. 63, 122-129 (1994) or WO 96/41882.
• the production of fusion proteins can preferably be carried out by genetic engineering processes in which a nucleic acid sequence coding for the fusion partner and a hydrophobin part, in particular DNA sequence, are combined in such a way that the desired protein is produced in a host organism by gene expression of the combined nucleic acid sequence ,
• a production method for example, is disclosed by WO 2006/082251 or WO 2006/082253.
• the fusion partners greatly facilitate the production of hydrophobins. Fusion hydrophobins are produced in the mentioned genetic engineering methods with significantly better yields than hydrophobins without fusion partners.
• the fusion hydrophobins produced by the host organisms according to the genetic engineering process can be worked up in a manner known in principle and purified by known chromatographic methods.
• the simplified work-up and purification process disclosed in WO 2006/082253, pages 11/12 can be used.
• the fermented cells are first separated from the Fermetationsbrühe, digested and the cell debris of the inclusion bodies (inclusion bodies) separately. The latter can be done advantageously by centrifuging.
• the inclusion bodies for example by acids, bases and / or detergents in principle known Be opened up way to release the fusion hydrophobins.
• the inclusion bodies with the fusion hydrophobins used according to the invention can generally be completely dissolved within about 1 h already using 0.1 M NaOH.
• the solutions obtained can -ggf. after adjusting the desired pH, without further purification, to carry out this invention.
• the fusion hydrophobins can also be isolated from the solutions as a solid. The isolation can preferably be carried out by means of spray granulation or spray drying, as described in WO 2006/082253, page 12.
• the products obtained by the simplified work-up and purification process comprise, in addition to residues of cell debris, usually about 80 to 90% by weight of proteins.
• the amount of fusion hydrophobins is generally from 30 to 80% by weight with respect to the amount of all proteins.
• the isolated products containing fusion hydrophobins can be stored as solids and dissolved for use in the respective desired media.
• the fusion hydrophobins can be used as "pure" hydrophobins for the practice of this invention. Cleavage is advantageously carried out after isolation of the inclusion bodies and their dissolution.
• a combination of at least one water-soluble, thickening polymer (A) and at least one hydrophobin (B) is used for thickening aqueous phases.
• A water-soluble, thickening polymer
• B hydrophobin
• Aqueous phases include water or an aqueous solvent mixture.
• Further solvent components in an aqueous solvent mixture are water-miscible solvents, for example alcohols such as methanol, ethanol or propanol.
• the proportion of water in a solvent mixture is generally at least 75% by weight with respect to the sum of all solvents used, preferably at least 90% by weight, more preferably at least 95% by weight and most preferably exclusively water is used.
• the aqueous phases may contain further, dissolved or dispersed therein inorganic or organic components.
• Type and amount of other components depend on the type of aqueous phase.
• the amount of all thickening polymers (A) together will be determined by those skilled in the art according to the desired viscosity of the composition. It may also depend on the type and molar mass of the polymer (A) and other components present in the aqueous phase to be thickened. It is generally 0.01 to 2.5 wt.% With respect to the sum of all components of the composition, preferably 0.1 to 2 wt.%, Particularly preferably 0.25 to 1, 5 wt.% And for example 0.5 to 1% by weight.
• the amount of hydrophobins (B) is determined by one skilled in the art according to the desired viscosity of the composition. It may also depend on the other components present in the aqueous phase to be thickened.
• the amount of hydrophobin (B) to be used is as a rule 0.1 to 2.5% by weight, based on the sum of all components of the aqueous phase, preferably 0.2 to 2% by weight and more preferably 0.25 to 1% by weight. ,
• the water-soluble polymers (A) and the hydrophobins (B) are used in the weight ratio (A) / (B) of 5: 1 to 1:10.
• the weight ratio (A) / (B) is preferably 3: 1 to 1: 2.
• the water-soluble polymers (A) and the hydrophobins (B) are added in the respective amounts and ratios of the aqueous phase to be thickened.
• components (A) and (B) are preferably each dissolved separately in water or in an aqueous solvent mixture and, with intensive mixing, in each case added separately to the aqueous phase to be thickened.
• the thickening effect begins with the mixing of components (A) and (B).
• aqueous phases can be, for example, liquid washing and cleaning agent formulations, such as, for example, detergents, washing aids, such as pre-spotters, fabric softeners, cosmetic formulations, pharmaceutical formulations, foods, coating compositions, formulations for textile production, textile printing pastes, printing inks, printing pastes for textile printing, paints, pigment slurries, aqueous formulations for foam production, formulations for the construction industry, such as concrete mixtures, formulations for petroleum production, such as drilling muds or formulations for acidizing or fracturing or deicing mixtures, for example for airplanes.
• liquid washing and cleaning agent formulations such as, for example, detergents, washing aids, such as pre-spotters, fabric softeners, cosmetic formulations, pharmaceutical formulations, foods, coating compositions, formulations for textile production, textile printing pastes, printing inks, printing pastes for textile printing, paints, pigment slurries, aqueous formulations for foam production, formulations for the construction industry, such as concrete mixture
• the thickening of the aqueous phase it is optionally possible after the thickening of the aqueous phase to reduce the thickening effect again.
• at least one agent is added to the aqueous phase, which is capable of cleaving peptide bonds in the hydrophobin. Due to the cleavage of the hydrophobin, the thickening effect is at least significantly reduced or even eliminated, depending on the type of composition.
• the cleavage can be carried out by means of conventional chemical agents; for example, it may be a BrCN cleavage.
• enzymes can be used for the targeted cleavage of certain peptide bonds.
• proteases are used for cleaving the hydrophobins.
• this embodiment can be used advantageously in the field of mineral oil production for the treatment of underground oil-bearing formations.
• a solution of the water-soluble polymer (A) and the hydrophobin (B) is forced through a borehole into the crude oil-bearing formation.
• This pressure treatment creates new cracks in the petroleum formation that allow oil to flow better from the formation to the wellbore.
• Such a treatment is also termed "fracturing.”
• a solution containing the agent which can cleave peptide bonds preferably a protease solution
• a solution containing the agent which can cleave peptide bonds preferably a protease solution
• a solution containing the agent which can cleave peptide bonds is pressed into the formation, which cleaves the hydrophobins, the viscosity
• the thickened aqueous phase decreases again, advantageously avoiding the thickened aqueous phase clogging the newly formed cracks and thus negating the success of the fracturing treatment.
• an aircraft may first be deiced with a mixture thickened according to the invention. After defrosting, the remainder of the mixture may be treated with a peptide-bond cleaving agent, preferably a protease solution, so that the residues of the deicing mixture do not contaminate the airfield.
• a peptide-bond cleaving agent preferably a protease solution
• the invention relates to a synergistic composition which comprises at least one aqueous phase, 0.01 to 2.5% by weight of at least one water-soluble, thickening polymer (A), and at least 0.1 to 2.5% by weight .% of at least one hydrophobin (B), with the proviso that the weight ratio (A) / (B) is from 5: 1 to 1:10, and wherein the amounts are based on the sum of all components of the aqueous phase.
• Preferred polymers (A), hydrophobins (B), amounts and preferred other parameters have already been mentioned above.
• the aqueous phases thickened according to the invention show a pronounced time-dependent behavior, ie, when the thickened aqueous phase shears, its viscosity decreases. After the end of the shear stress, the viscosity of the aqueous phase decreases again to. If a thickening polymer (A) already shows time-dependent behavior, the time-dependent effect generally increases as a result of the addition of hydrophobins.
• A1 to A3 are three different commercially available alkali-soluble dispersions of acrylates, A4 and A5 are precipitation polymers and A6 is a biopolymer.
• Alkali-soluble polyacrylate aqueous dispersion, pH approx. 3, emulsion polymer
• Alkali-soluble polyacrylate aqueous dispersion, pH approx. 3, emulsion polymer
• hydrophobin A a fusion hydrophobin with the complete Fusion partner yaad used (yaad-Xa-dewA-his, hereinafter called hydrophobin A) and a fusion hydrophobin with a reduced to 40 amino acids fusion partner yaad40-Xa-dewA-his (hydrophobin B).
• hydrophobin B a fusion hydrophobin with a reduced to 40 amino acids fusion partner yaad40-Xa-dewA-his
• the viscosity of the aqueous solutions was measured in accordance with the specifications DIN 51550, DIN 53018 and DIN 53019 with a conventional rotational viscometer (Brookfield ® model-RV-03 viscometer) at a speed of 20 revolutions per minute with the spindle no. 64 at 20 0 C. , The viscosities were measured on the one hand immediately after mixing or after adjusting the pH. The time-dependent flow behavior was determined by measuring the viscosity as a function of time while the viscometer was running.
• Table 1 shows the initial value.
• Figure 1 shows the viscosities of solutions of polymer A1 at pH 9 versus time (curve 1: only 1.2% polymer; curve 2: 1% polymer + 0.5% hydrophobin type A; curve 3: 1% polymer + 0.5% hydrophobin type B).
• curve 1 only 1.2% polymer
• curve 2 1% polymer + 0.5% hydrophobin type A
• curve 3 1% polymer + 0.5% hydrophobin type B

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• 2010
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