CH619002A5 - Composition for protecting skin and hair. - Google Patents

Description

35 The present invention relates to an agent for protecting skin and hair against the harmful effects of harsh materials, in particular detergents, and against adverse climatic conditions, which contains a non-enzymatic modified protein in combination with a surface-active agent.

The agents according to the invention accordingly contribute to keeping the skin and hair in good condition.

The adverse effects of surfactant-containing preparations on keratin are known. These 45 effects are believed to be caused by the surfactant penetrating the keratin surface, resulting in the leaching of oils and moisturizing components which are essential for the good condition of the keratin. This penetration of surface-active agents and the leaching out of essential oils also influences the ability of keratin, particularly in the case of skin, to retain water in the tissue, and this results in a poor state of the keratinous material.

55 Many attempts have been made to create preparations that improve the condition of the skin and hair. The use of protein on skin and hair as a cosmetic treatment is likely to be older than historical records. Milk casein has been used as a rejuvenating beauty product, and more recently it has been recommended for use in toilet soaps. GB-PS No. 1 160 485 recommends the incorporation of partially degraded proteins, which have a gel strength of zero bloom grams, into detergent preparations and lotions for use on the skin, as dishwashing liquids, etc.

DE-OS No. 2 151 739 and No. 2 151 740 describe certain fat derivatives of aminolysates of low molecular weight

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weight described, which are suitable for use in shampoos. GB-PS No. 1 122 076 describes the production of low molecular weight alcohol-soluble protein esters which are suitable for use in hairspray compositions. Various low molecular weight polypeptides or modified polypeptides are commercially available and are recommended for use in cosmetic and shampoo formulations, for example Hydro Pro 220, Hydro Pro 330, Maypon 4C, marketed by Stepan Chemical Company will ; Wilson X250, Wilson X1000 j »and Wilson Aqua Pro, which are launched by the Wilson Chemical Company. However, it has been found that none of these preparations are particularly effective in protecting keratin against the action of harsh detergents, and this is particularly true when the 15 proteins of the detergent preparation itself are incorporated. The softening effect of these preparations can often be improved by adding greasy or oily materials; however, when used in dishwashing liquids, this leads to a loss of foaming power or to aesthetic changes which are generally considered undesirable by the consumer.

Even when applied to keratin, the agents according to the invention exert their effect in foaming detergent solutions and do not lead to any loss of foam or cleaning power in the detergent solutions containing them.

In the context of the following description, a "modified protein" is understood to mean a product which, in contrast to a "derived protein", is obtained in one or more stages by chemical or biological modification of a precursor protein, a precursor protein is a non-enzymatic protein selected from natural, derived, synthetic or biosynthetic proteins, and a derived protein is the product of the hydrolytic, ammoniolytic, enzymatic or thermal degradation of a protein material.

The agent according to the invention is characterized in that

that it contains 0.1 to 90% by weight of surfactant and that the non-enzymatic modified protein has an average molecular weight above 5000 and an isoionic point at more than pH 6 and, due to the modification, one or more of the following functional ones Groups contains:

the different R groups can be the same or different.

Among the modified proteins above, those proteins are preferred in which R1 has the general formula

-CH2- (CHQV (CH2) q-Q '

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in which Q1 is R2, SR2, OR2, N (R2) 2, S (R2) 2, N (R2) 3 or OCOR3, where R2 is hydrogen or R3 and R3 is an alkyl or alkenyl radical having up to 20 carbon atoms , p represents O and q represents 0 to (5-p).

Generally, R1 will contain no more than 8 carbon atoms and up to 2 heteroatoms, which may be the same or different. Preferred classes of modified proteins that fall under the above definitions are those in which R1 is represented by:

1.CH2-CH-OH- (CH2) r-H, where r = 0 to 6,

2. CH2- (CH2) r-H, where r = 0 to 7, and, (CH2) S-H, where r = 1 to 4

3. (CH2) 3-N;

-C-W-Q; -N-X-Q; -O-Y-Q; -S-Z-Q;

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where C, N, O and S represent carbon, nitrogen, oxygen or sulfur atoms which are part of the unmodified starting protein,

-Z- represents a direct bond or carbonyl, so

-Y- represents -Z-, sulfonyl or phosphonyl,

-X— stands for -Y- or> C = NR,

-W- stands for -X-, -NX-, -OY- or -SZ- and

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Q stands for-RI, -SR ', - OR1, -NR2, -SR2 or-NR3,

in which

R represents hydrogen or —R1 and

R1 is an alkyl, alkenyl, aryl, cycloalkyl or heterocyclic radical, the alkyl or alkenyl radicals 6 being optionally interrupted by heteroatoms and optionally being substituted by nonionogenic and / or cationic radicals, and where R is no longer than 20 linked carbon atoms in the alkyl or alkenyl radicals. gs

In a given modified protein, the functional groups need not all be identical. Also

N (CH2) t-H and s and t stand for 0 to 3, is represented.

Protein modification can be carried out using the normal methods used in the production of proteins with functional substituents. In general, the reactive centers on which modification is carried out are protein side chains which contain acidic or basic groups, such as carboxyl groups, amino, sulfhydryl, aliphatic or phenolic hydroxyl groups, imidazole or guani-dinogroups, or which have a reactive aromatic group Show ring, as in tyrosine. A preferred modified protein has carboxylic acid ester or amide groups as substituents which are derived from the carboxylic acid groups of the unmodified substrate. The ester can be obtained from the protein and the corresponding alcohol by suspending the protein in the anhydrous alcohol at a temperature between 0 and 25 ° C and at an acid concentration of 0.02 to 0.10 molar for several days. Alternatively, hydroxyalkyl esters can be obtained by reacting the protein with an epoxide, e.g. But-l-enoxide. Esterified products can also be obtained by reaction with diazoacetic acid esters or amides. Amides can be formed from the protein carboxylic acid group by reaction with a water-soluble carbodiimide and an amine. This can simultaneously lead to the formation of phenolic groups of tyrosine or sulfhydryl groups of cysteine, O-arylisoureas or S-alkylisothioureas being obtained.

- -rf

According to another embodiment of the invention, the proteins can be alkylated or alkylated via amino, hydroxyl or sulfhydryl groups. Acylation can be effected using the appropriate acid anhydride or N-carboxyanhydride. In the latter case, this leads to acylation, which predominantly attacks amino groups. In the former case, the modification, if the acid anhydride is cyclic, leads to acidic substituents which can be neutralized, for example, by esterification. Reactions analogous to acylation can also be carried out. For example, e-amino groups of proteins can be selectively replaced by the more basic guanidino groups by treatment with an O-alkylisourea or S-alkylisothiourea.

Sulfonic acid esters or sulfonamide derivatives of proteins can, for example, by reacting the hydroxy or

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Amino groups of the protein can be prepared with sulfonyl halides. These modified proteins can again be used to obtain further modifications by cleaving the alkyl / oxygen bond of the sulfonate. In this way, for example, hydroxyl groups can be replaced by S-alkyl groups.

There are other ways to form alkylated or arylated proteins. S-alkylation or N-alkylation of sulfhydryl or amino groups can be carried out by nucleophilic substitution in the case of halogen acetates of haloacetamides or by addition of multiple carbon bonds which are conjugated, for example, to cyanide, such as in acrylonitrile, or to an imido group, such as in maleimides , can be effected. N-alkylation can also be carried out by means of sodium borohydride reduction of the imines which are formed in the condensation of protein amine groups with aliphatic aldehydes or ketones. Arylation of sulfhydryl, amino or hydroxy groups can be carried out by nucleophilic substitution of halogen, especially fluorine, in activated halogenobenzene derivatives; will.

The proteins for the agents according to the invention can be modified in numerous other ways. In addition, the guanidine groups of arginine can be modified by reaction 25 with 1,2-dicarbony derivatives such as cyclohexanedione or phenylglyoxal.

The precursor proteins, which can be used in the agents in modified form, can be selected from natural, derived, synthetic or biosynthetic proteins.

Typical natural proteins include intracellular proteins and globular proteins, such as those found in blood plasma and milk. Derived proteins can be obtained from many sources, for example by hydrolytic, ammoniolytic, thermal or enzymatic degradation of globular or structural proteins, such as keratin, collagen, fibrinogen, myosin, whey protein, casein or vegetable proteins, such as those derived from cereals, bean cheese (Soy curd) or the protein-rich residues from the production of seed oil. A particularly suitable derived protein is gelatin, which is the product of the (usually acid or base catalyzed) hydrolysis of skin or bone collagen and which can have an average molecular weight which varies from 5000 to 200,000 and even higher 45. Other highly suitable precursor proteins include total casein and soybean protein; synthetic proteins such as polylysine and proteins obtained from unicellular microorganisms such as bacteria.

The molecules of a protein vary widely in size and complexity, and the molecular weight of a protein is therefore necessarily an inaccurate measure. The molecular weight of a protein can be specified by defining the molecular weight distribution of the protein molecule, but it is customary to specify 55 as the mean molecular weight of the protein sample,

because an average molecular weight is measured by most physical methods. However, such an average is only an approximate indication of the actual molecular weight distribution of the sample. In addition, the average molecular weight measured can vary from one measurement method to another. So-called molecular weights averaged in terms of numerical values are usually obtained by measuring the osmotic pressure, diffusion rates, etc., while molecular weights averaged in terms of weight are measured, for example, by ultracentrifuge methods. In the present description, use is generally made of viscosity measurements of buffered solutions for the determination of average protein molecular weights. As is known, the intrinsic viscosity of a buffered protein solution depends primarily on the total length of the protein coil and is relatively independent of; the type of side chains and end groups of the protein. There is therefore a relationship between the intrinsic viscosity and the average molecular weight, M, of the protein, which can be expressed according to the Staudinger equation as follows rij = K.Ma,

where K and a for a particular protein source, e.g. for gelatin derived from calf skin (see Macromolecular Chemi-1 stry of Gelatin, page 72, by A. Veiss), are constants. The intrinsic viscosity is the reduced specific viscosity at infinite dilution of the protein solution and is defined as follows with regard to the actual viscosities measured in a viscometer:

Relative viscosity measured viscosity of the protein in buffered solution measured viscosity of the buffered solution

Specific viscosity rj sp = rj rel - 1

Reduced specific viscosity

Intrinsic viscosity

"Hsp

Concentration (c) of the protein solution lim c> o

The constants K and a, which are used in the determination of the molecular weights of modified gelatin derived from calf skin, are used as follows (according to J. Bello, H.R. Bello and J.R. Vinograd, Biochimica Et Biophysica Acta, 57, 222-229; 1962):

K = 2.9 X IO "4 a = 0.62.

The modified proteins as used in the present invention have molecular weights greater than 5,000. In particular, their molecular weights should preferably be greater than about 10,000, more preferably greater than 15,000, and generally they will range from 20,000 to 200,000 lie.

In connection with the total molecular weight of the modified protein, it is preferred that at least the larger fraction of the molecular weight comes from the precursor protein. Desirably, the precursor protein makes up between 80% and 99%, preferably between 90% and 96%, of the total molecular weight of the modified protein.

Protein molecules that have both acidic and basic side chains are charged in both acidic and basic solutions and are therefore of an amphoteric nature. The number of such acidic and basic residues in a protein molecule can be measured by titration with a monobasic strong acid (e.g. dilute nitric acid) or an acidic strong base (e.g. sodium hydroxide solution), and the results are conveniently recorded in mmol / g.

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net, which is the number of millimoles of acid or base required to neutralize 1 g of the protein. Modified proteins of the type used according to the invention have a basic side chain content which is preferably greater than 0.1 mmol / g, in particular greater than 0.5 5 mmol / g and expediently greater than 0.8 mmol / g. They have an acidic side chain content which is preferably less than 1.5 mmol / g, in particular less than 1.1 mmol / g, and desirably less than 0.8 mmol / g.

The modified proteins as used according to the invention preferably have proportionally fewer anionic side chains and more non-polar or cationic side chains than the corresponding unmodified proteins from which they are derived. The modification thus generally leads to an increase in the hydrophobicity and can lead to an increase in the pH of the isoionic point, i.e. the pH at which the same concentrations of protein anions and cations exist in solution.

The modified proteins for use in the agents according to the invention preferably have a pH of the 211 isoionic point of more than 6.5, in particular more than 7.2 and desirably more than 8.0.

The pH of the isoionic point of the above-mentioned protein may differ somewhat from the pH of the isoelectric point of the protein, although the differences are usually small. The isoelectric point is determined by the anion / cation equilibrium of all ions in the measured sample, including non-protein ions; the isoionic point, on the other hand, is determined by the anion / cation balance of the protein ion alone. The pH of the isoionic 30 point can be determined in the following way.

Acidic amberlite resin (IR 120) and basic amberlite resin (IR 400) are washed with several parts by volume of water, filtered and mixed in a ratio of 0.4: 1. With minimal heating, a 1 V2 wt .-% protein solution (20 35 ml) is prepared, allowed to cool to constant temperature and mixed with the resin mixture (4.2 g), whereupon the solution is stirred for 5 minutes, the mixture is filtered and the pH of the filtrate is the pH of the isoionic point of the protein. The optimal choice of protein for any particular agent depends to some extent on the use pH of the agent, i.e. the pH of the carrier when applied to keratin. Depending on the type of application, this use pH can be the pH of the agent itself or the pH of an aqueous solution or dispersion of the agent at a use concentration which can be as low as 0.01%.

In view of the fact that the agents contain modified proteins, it is preferred if the pH of the agent or an aqueous solution or dispersion of the agent at the use concentration is lower than (pl + 2), where pl is the pH Isoionic point value of the modified protein. More preferably this usage pH is lower than (pl + 0.5), desirably 55 lower than (pl - 0.7), and even more desirably lower than (pl - 1.4). In addition, modified proteins which have a pl greater than 9.6 can be used satisfactorily at a pH between (pl + 2) and pl. 60

The use pH of the agents according to the invention can vary widely depending on the purpose and the type of use of the agents. Liquid or cream-like agents intended for shampoos, hand creams, or cosmetic lotions are generally applied directly to skin or hair 65, and the use pH is the pH of the agent itself. This can be any pH in the Generally range from 4 to 9. Detergents such as liquid dishwashing detergents, bath additives and granular or liquid heavy duty detergents are generally used in a large excess of water, and the use pH is the pH of an aqueous solution of the detergent at a concentration generally in the range of 0.01% to 2% by weight. Builder-free detergents, which are used, for example, as liquid mild detergents, will have a use pH of about 7; high performance scaffold containing detergents generally have a use pH in the alkaline range up to a pH of about 11. Soap bars are applied to the skin as an aqueous solution or dispersion of the constituents of the soap bar in a concentration which is generally Range is 5 to 15 wt .-%. The pH of the soap dispersion can vary from 5.5 to 9.5 depending on the type of soap bar used.

The preferred agents according to the present invention have a use pH in the range from 4 to 11, in particular in the range from 5 to 9.5, and particularly preferably in the range from 5.5 to 7.5.

The modified proteins are preferably produced by modification of the protein precursor side chains which contain free car-boxyl groups or free basic, in particular primary amino groups. In particular, the modification of acid groups is preferably carried out by oxyalkylation and esterification (corresponding to a substitution

O

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of -C OR1 as —WQ) or amidation (corresponding to the

O

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Substitution of -C NHR1 as -WQ). On the other hand, the basic groups are preferably modified in the form of alkylation (corresponding to the substitution of -R1 as -XQ). It should be borne in mind that the acylation of, for example, primary amino groups destroys the basic character of such groups, the general effect in the absence of other types of modification in a lowering of the pH of the isoionic point of the protein in the range from 4.5 to 5 , 5 is. N-acylation can therefore not be used as a type of modification unless there is another compensating modification by which the pI of the N-acylated protein increases to more than 6.

Particularly preferred modified proteins for use in the context of the invention include esterification or hydroxyalkylation products of high molecular weight gelatins which result from the acidic or basic hydrolysis of materials such as animal skin or bones. Such modified proteins have proportionally fewer carboxyl groups and more carboxyl ester groups than the unmodified proteins. Lower alkyl or hydroxyalkyl ester derivatives are preferred. They can be prepared simply by acid catalyzed esterification with the corresponding alcohol, in which case the reaction primarily attacks the protein carboxylic acid functions, or alternatively they can be prepared by treatment with an alkylene oxide, in which case the esterification by hydroxyalkylation of other reactive groups, for example primary amino groups, can be accompanied. The extent of such N-hydroxyalkylation depends primarily on the pH conditions used. If the pH of the reaction medium is kept in the acidic range during the reaction, the extent of the N-hydroxyalkylation is rather less than if the pH is allowed to rise during the reaction. The effect of N-hydroxyalkylation is

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an increase in the hydrophobicity of the protein but a decrease in the isoionic point of the protein. The benefit in terms of conditioning effectiveness is therefore relatively small compared to the effect of esterification in terms of conditioning effectiveness. The extent of the modification is preferably such that at least 5%, in particular 20% and expediently at least 35% of the free acidic side chains of the protein are esterified. The modified proteins can be present in the agents according to the invention in an amount up to 50% by weight, but generally in an amount between 1% by weight and 10% by weight, preferably between 2% by weight and 6% by weight. % of the agent is available. They are therefore effective keratin conditioning agents even at relatively low concentrations.

Surfactant materials which can be used in the compositions according to the invention can be selected from the water-soluble soaps and synthetic, anionic, nonionic, cationic, zwitterionic and amphoteric detergents as described below. Preferably the surfactants are foaming detergents or emulsifiers.

A. Anionic soap and synthetic non-soap detergents.

This class of detergents includes common alkali soaps, such as the sodium, potassium, ammonium, alkylammonium and alkylolammonium salts of higher fatty acids, which contain from about 8 to 24 carbon atoms and preferably from about 10 to about 20 carbon atoms. Suitable fatty acids can be obtained from natural sources, such as from vegetable or animal esters (e.g. palm oil, coconut oil, babasu oil, soybean oil, castor oil, tallow, whale and fish oils, fat, lard and their mixtures). The fatty acids can also be produced synthetically (e.g. by oxidation of petroleum or by hydrogenation of carbon monoxide according to the Fischer-Tropsch process). Resin acids are suitable, such as rosin and such resin acids in tall oil. Naphthenic acids are also suitable. Sodium and potassium soaps can be obtained by direct saponification of the fats and oils or by neutralization of the free fatty acids, which are obtained in a separate manufacturing process. The sodium, potassium and triethanolium salts of the mixtures of fatty acids derived from coconut oil and tallow, e.g. Sodium or potassium tallow and coconut soap.

This class of detergents also includes water-soluble salts, especially the alkali metal salts of organic sulfuric acid reaction products which contain in their molecular structure an alkyl radical with about 8 to about 22 carbon atoms and a sulfonic acid or sulfuric acid ester residue. (The term "alkyl" also includes the alkyl portion of higher acyl residues.) Examples of this group of synthetic detergents which form part of the preferred compositions of the present invention are the alkali metal, e.g. Sodium or potassium alkyl sulfates, especially those obtained by sulfating the higher alcohols (having 8 to 18 carbon atoms), the latter being formed by reducing the glycerides of tallow or coconut oil; the alkali metal olefin sulfonates having 8 to 24 carbon atoms are described, for example, in US Pat. No. 3,332,880 and the alkali metal alkyl glyceryl ether sulfonates, especially those of the higher alcohols derived from tallow and coconut oil, other anionic detergents include the alkali metal alkyl benzene sulfonates in which the alkyl group contains from about 9 to about 15 carbon atoms, including those in the U.S. Pat 'n No. 2 220 099 and No. 2 477 383 types described (the alkyl radical can be a straight or branched aliphatic chain); Sodium coconut oil fat

acid monoglyceride sulfates and sulfonates; Salts of alkylphenol ethylene oxide ether sulfate with about 1 to about 12 units of ethylene oxide per molecule and in which the alkyl radicals contain 8 to about 18 carbon atoms; the reaction product of fatty acids esterified with isethionic acid and neutralized with sodium hydroxide, for example the fatty acid is oleic acid or derived from coconut oil; Sodium or potassium salts of fatty acid amide of a methyl tauride, in which the fatty acids e.g. are derived from coconut oil; Sodium or potassium β-acetoxy or β-acetamidoalkanesulfonates, wherein the alkane has 8 to 22 carbon atoms; and others as are known per se, a number of which are described in particular in U.S. Patent Nos. 2,286,921, 2,486,922 and 2,396,278, respectively.

Other synthetic anionic detergents useful in the invention are the alkyl ether sulfates. These materials have the formula R20 (C2H40) XS03M, in which R2 is alkyl or alkenyl with about 8 to about 24 carbon atoms, x = 1 to 30 and M is a salt-forming cation from the group of the alkali metal, ammonium, dimethyl, trimethyl -, Triethyl, dimethanol, diethanoi, trimethanol and triethanol ammonium salts mean.

Suitable alkyl ether sulfates are condensation products of ethylene oxide and monohydric alcohols with about 8 to about 24 carbon atoms. The radical R 2 preferably has from 18 to 18 carbon atoms. The alcohols can be derived from fats, e.g. Coconut oil or tallow, derived, or can be synthetic. Lauryl alcohol and straight chain alcohols derived from tallow are preferred in the context of the invention. Such alcohols are reacted with 1 to 12 and in particular 6 molar parts of ethylene oxide and the resulting mixture of molecular species, e.g. have an average of 6 moles of ethylene oxide per mole of alcohol, is sulfated and neutralized.

Specific examples of suitable alkyl ether sulfates are sodium coconut alkyl ethylene glycol ether sulfate, lithium tallow alkyl triethylene glycol ether sulfate and sodium tallow alkyl hexaoxy ethylene sulfate.

Preferred for reasons of excellent cleaning properties and easy availability are the alkali metal coconut and tallow alkyloxyethylene ether sulfates, which contain on average about 1 to about 10 oxyethylene residues. The alkyl ether sulfates are described in U.S. Patent No. 3,332,876.

B. Nonionic synthetic detergents.

Nonionic synthetic detergents can be broadly defined as compounds that result from the condensation of alkylene oxide groups (hydrophilic in nature) with an organic hydrophobic compound, which may be aliphatic or alkyl aromatic in nature. The length of the hydrophilic or polyoxyalkylene residue that is condensed with any particular hydrophobic group can be easily adjusted to provide a water-soluble compound that has the desired degree of equilibrium between hydrophilic and hydrophobic elements.

A known class of nonionic synthetic detergents is available, for example, on the market under the trade name "Pluronic". These compounds are formed by the condensation of ethylene oxide with a hydrophobic base, which is formed by the condensation of propylene oxide with propylene glycol. The hydrophobic portion of the molecule which shows water insolubility has a molecular weight of about 1500 to 1800. The addition of polyoxyethylene residues to this hydrophobic portion leads to an increase in the water solubility of the molecule as a whole and the liquid character of the product is maintained to the point where the polyoxyethylene content makes up about 50% of the total weight of the condensation product.

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Other suitable nonionic synthetic detergents include:

1. The polyethylene oxide condensates of alkylphenol, e.g. the condensation products of alkylphenols having an alkyl group of about 6 to 12 carbon atoms in either a straight or branched chain configuration with ethylene oxide, the ethylene oxide being present in amounts corresponding to 5 to 25 moles of ethylene oxide per mole of alkylphenol. The alkyl substituent in such compounds can be derived, for example, from polymerized propylene, diisobutylene, octene or nonene.

2. Those resulting from the condensation of ethylene oxide with the product resulting from the reaction of propylene oxide with ethylene diamine. Examples include compounds that contain from about 40% to about 80% by weight polyoxyethylene and a molecular weight from about 5000 to about

11,000 and result from the reaction of ethylene oxide groups with a hydrophobic base, which is the reaction product of ethylenediamine and excess propylene oxide, the base having a molecular weight in the order of 2500 to 3000, satisfactory.

3. The condensation product of aliphatic alcohols having 8 to 24 carbon atoms in either a straight or branched chain configuration with ethylene oxide, e.g. a coconut alcohol / ethylene oxide condensate with 5 to 30 moles of ethylene oxide per mole of coconut alcohol, the coconut alcohol fraction having 10 to 14 carbon atoms.

4. Nonionic detergents, including nonylphenol condensed with either about 10 or about 30 moles of ethylene oxide per mole of phenol and the condensation products of coconut alcohol averaging either about 5.5 or about 15 moles of ethylene oxide per mole of alcohol and the condensation product of about 15 moles of ethylene oxide with 1 mole of tridecanol.

Other examples include dodecylphenol condensed with 12 moles of ethylene oxide per mole of phenol; Dinonylphenol condensed with 15 moles of ethylene oxide per mole of phenol; Dodecyl mercaptan condensed with 10 moles of ethylene oxide per mole of mercaptan; bis- (N-2-hydroxyethyl) lauramide; Nonylphenol condensed with 20 moles of ethylene oxide per mole of nonylphenol; Myristyl alcohol condensed with 10 moles of ethylene oxide per mole of myristyl alcohol; Lauramide condensed with 15 moles of ethylene oxide per mole of lauramide; and diisooctylphenol condensed with 15 moles of ethylene oxide.

5. A detergent of the general formula R3R4R5N - »O (amine oxide detergent), wherein R3 is an alkyl group having about 10 to about 28 carbon atoms, 0 to about 2 hydroxyl groups and 0 to about 5 ether bonds, at least one of the radicals R3 being one Represents alkyl group, contains about 10 to about 18 carbon atoms and 0 ether bonds and each of the radicals R4 and R5 is selected from the group consisting of alkyl radicals and hydroxyalkyl radicals having 1 to about 3 carbon atoms.

Specific examples of amine oxide detergents include: dimethyl dodecyl amine oxide, dimethyl tetradecyl amine oxide, ethyl methyl tetradecyl amine oxide, cetyl dimethyl amine oxide, dimethyl stearyl amine oxide, cetyl ethyl propyl amine oxide, diethyl dodecyl amine oxide, diethyl tetradecyl amine bis (2-hydroxyl dodyl) bis (2-hydroxyl dodyl) bis (2), l-hydroxypropylamine oxide, (2-hydroxypropyl) methyltetradecylamine oxide, dimethyloleylamine oxide, dimethyl- (2-hydroxydodecyl) amine oxide and the corresponding decyl, hexadexyl and octadecyl homologues of the above compounds.

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6. A detergent with the general formula R3-S -R4, wherein R3 and R4 have the meaning given above.

Specific examples of sulfoxide detergents include: dodecylmethylsulfoxide, tetradecylmethylsulfoxide, 3-hydroxy-tridecylmethylsulfoxide, 3-methoxytridecylmethylsulfoxide, 3-hydroxy-4-dodecoxybutylmethylsulfoxide, octadecyl-2-hydrodoxyethylsulfoxide.

7. The ammonia, monoethanol and diethanolamides of fatty acids with an acyl residue that has from about 8 to about 18 carbon atoms. These acyl residues are usually derived from naturally occurring glycerides, e.g. Coconut oil, palm oil, soybean oil and tallow, but can also be of synthetic origin, e.g. from the oxidation of petroleum or the hydrogenation of carbon monoxide using the Fischer-Tropsch process.

C. Ampholytic synthetic detergents.

Ampholytic synthetic detergents can be generally referred to as derivatives of aliphatic or aliphatic derivatives of heterocyclic secondary and tertiary amines, in which the aliphatic radical can be straight-chain or branched, and in which one of the aliphatic substituents contains about 8 to 18 carbon atoms and at least one anionic water-solubilizing group, e.g. Contains carboxy, sulfo or sulfato. Examples of compounds that fall under this definition are sodium 3- (dodecylamino) propionate, sodium 3- (dodecylamino) propane-1-sulfonate, sodium 2- (dodecylamino) ethyIsulfate, sodium 2 - (dimethylamino) octadecanoate, disodium 3- (N-carboxymethyldodecylamino) propane-l-sulfo-nate, disodium octadecyliminodiacetate, sodium l-carboxyme-thyI-2-undecyimidazole and sodium N, N-bis- (2- hydroxyethyl) -2-sulfato-3-dodecoxypropylamine.

D. Zwitterionic synthetic detergents.

Zwitterionic synthetic detergents can be generally referred to as derivatives of aliphatic quaternary ammonium and phosphonium or tertiary sulfonium compounds, in which the cationic atom can be part of a heterocyclic ring and in which the aliphatic radical can be straight-chain or branched and one of the aliphatic substituents is about 3 to Contains 18 carbon atoms, at least one aliphatic substituent having an anionic water-solubilizing group, for example Carboxy, sulfo or sulfato has. Examples of compounds that fall under this definition are 3- (N, N-dimethyl-N-hexadecylammonio) -2-hydroxypropane-1 sulfonate, 3 - (N, N-dimethyl-N-hexadecylam-monio) propane -l -sulfonate, 2- (N, N-dimethyl-N-dodecylammonio) acetate, 3- (N, N-dimethyl-N-dodecylammonio) propionate, 2- (N, N-dimethyl-N- octadecylammonio) ethyl sulfate, 2- (S-methyl-S-tert.-hexadecylsulfonio) -ethane-l-sulfonate, 3- (S-methyl-S-dodecylsulfonio) propionate, 4- (S-methyl-S-tetrade -cylsulfonio) butyrate, l- (2-hydroxyethyl) -2-undecylimidazolium-l-acetate, 2- (trimethylammonio) octadecanoate, 3- [N, N-bis (2-hydroxyethyl) -N-octadecylammonio ] -2-hydroxypropane-1-sulfonate and 3- (N, N-dimethyl-Nl-methylalkylammo-nio) -2-hydroxypropane-l-sulfonate, wherein alkyl has an average length of 13.5 to 14.5 Has carbon atoms.

Some of these detergents are described in U.S. Patent Nos. 2,129,264; No. 2,178,353; No. 2,774,786; No. 2,813,898; and no.

2,828,332.

E. Cationic detergents.

Cationic detergents include those that have the general formula

Have R6-N (R7) 3 + An,

wherein R6 is an alkyl chain with about 8 to about 20 carbon atoms

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8th

each R7 is selected from the group consisting of alkyl and alkanol groups having 1 to 4 carbon atoms and benzyl groups, where there is normally no more than one benzyl group, and two R7 groups either through a carbon-carbon ether or through 5 an imino bond can be linked to form a ring structure, and represents an halogen atom, a sulfate group, nitrate group or other pseudohalogen group. Specific examples are coconut alkyl trimethyl amine chloride, dodecyl dimethyl benzyl bromite and dodecyl methyl 10 morpholinochloride.

The soap and anionic, nonionic and zwitterionic non-soap surfactants mentioned above can be used as the only surfactants, or the various 1s examples can be mixed together in the practice of the invention. Anionic and nonionic surfactants are particularly preferred. The amount of surfactant incorporated into the preparations depends on the intended use of the particular approach. So it is in relation to the weight of the preparation as such when it is applied directly to the skin, e.g. as a cosmetic lotion, or at the concentration at which it is used as a solution in, for example, dishwashing water or bath water. In most 25 cases, a content in the range from 0.1% by weight to 90% by weight of the preparation is suitable. In particular, detergents for cleaning purposes will generally contain between about 5% and 50% by weight of the surfactant, while cosmetic preparations will generally contain between 0.1% and 30% and 10% by weight of the surfactant .

The invention is applicable to various preparations which come into contact with keratin in the normal course of use, e.g. Dishwashing liquids, hand or face creams, body lotions, hair shampoos, bath additives, high-performance detergents, detergents for hard surfaces, soap bars, etc. The physical form of the detergent can also vary widely, from granular solids to gels and creams to viscous or mobile. 40 liquid assets. Dishwashing detergents are generally liquid and include mixtures of water and foaming detergents. Granular detergent preparations, on the other hand, can contain some water or be anhydrous. Cosmetic and related agents will generally have a base containing a mixture of water, emulsifier and oil, and the physical condition of these agents will be that of oil-in-water or water-in-oil emulsions. However, it is also contemplated that cosmetic-like agents according to the invention may be in the form of gels 50 containing the modified protein and water and optionally containing a protective agent such as methyl alcohol. However, other cosmetic-like agents can contain some water or be anhydrous, but contain a mixture of modified protein, oil and foaming surface active agent. Such agents are particularly suitable as bath additives.

The preferred liquid or granular detergents for use as, for example, high-performance detergents, 60 dishwashing detergents or shampoos contain between 5% by weight and 50% by weight of foaming detergent. In particular, the foaming detergent is selected from:

a. up to 45% by weight of a water-soluble hydrocarbon sulfate of the general formula R20 (C2H40) nSO3M, in which 65 R2 is a straight or branched, saturated or unsaturated aliphatic hydrocarbon radical having 8 to 24 carbon atoms or one having an aliphatic, straight-chain or branched hydrocarbon group having 8 to 18 carbon atoms is substituted benzene; n represents 1 to 12; and M represents an alkali metal, ammonium, dimethyl, trimethyl, triethyl, dimethanol, diethanoi, trimethanol or triethanol ammonium salt;

b. up to 45% by weight of a water-soluble hydrocarbon sulfonate of the general formula R2S03M;

c. up to 45% by weight of a water-soluble hydrocarbon sulfate of the general formula R20S03M;

d. up to 40% by weight of the ammonia, monoethanol and diethanolamides of fatty acid with an aryl radical with 8 to 18 carbon atoms;

e. up to 40% by weight of the condensation product of 3 to 25 moles of an alkylene oxide, preferably ethylene or propylene oxide, and one mole of an organic, hydrophobic compound of an aliphatic or alkylaromatic nature, the latter having 8 to 24 carbon atoms.

Another component that can be incorporated into the agents according to the invention is a water-soluble buffer material. The purpose of the buffer is to adjust the pH range that maximizes the conditioning effectiveness of these agents. If the protein has a pI up to about pH 8, e.g. type B gelatin, i.e. gelatin made by base catalyzed hydrolysis of collagen, the optimal use pH range is about 5.5 to 7, and this requires the use of a mild acidic buffer material. Suitable acidic buffers can be: acetic acid, citric acid, malic acid, gluconic acid, maleic acid, lactic acid, tartaric acid, propionic acid, butyric acid, malonic acid, polymaleic acid, polyitaconic acid, glutaric acid, citraconic acid; Benzene pentacarboxylic acid and benzene hexacarboxylic acid; Succinic acid, ethylenediaminetetraacetic acid and nitriloacetic acid; as well as the weakly acidic salts thereof. If a protein has a pI greater than about pH 9, the optimal use pH range is about 7 or higher and this may require the use of basic buffer materials. These can be selected from the basic salts of the organic acids, as mentioned above, or from the more common alkaline inorganic buffer materials, such as alkali metal phosphates, polyphosphates, carbonates, silicates and borates. Acidic buffer materials are generally used in proportions of up to 15% by weight, preferably up to 5% by weight, of an agent. Alkaline buffer materials can be used up to about 40% by weight in a granular detergent, or up to about 5% by weight in a liquid detergent.

The liquid detergents or gels according to the invention generally contain a carrier based on water and / or water-soluble solvent. Suitable solvents include Q2-8 mono and dialanols, e.g. Ethanol, butanol, methylpropanol-1 and -2, amylol or pentanol, butanediol, toluene, benzylcarbinol, ethylene glycol monobutyl ether, propylene glycol propyl ether and diethylene glycol dimethyl ether. They are generally present in amounts of up to 15% by weight of the agent. Additional components of liquid detergents include foam enhancers such as the higher alkyl amine oxides and alkylolamides of carboxylic acids having 10 to 14 carbon atoms, thickeners, protective agents, opacifiers, perfumes, dyes, fluorescent agents, opacifying agents, bactericides, hydrophobic oily materials and hydrotropics.

Commonly used hydrotropes include common lower alkyl aryl sulfonates such as sodium and potassium toluenesulfonate, xylene sulfonate, benzenesulfonate and cumene sulfonate. Urea and lower alkanol hydrotropes such as methanol, ethanol, propanol and butanol can also be used.

Hydrophobic oily materials suitable for use in the present compositions include animal

9

619 002

see vegetable and mineral oils and waxes, e.g. Beeswax, walrus and carnauba wax; Fatty alcohols such as stearyl, myristyl and cetyl alcohol; Fatty esters and partial esters such as isopropyl myristate, glyceryl monostearate; Fatty acids such as stearic acid; Lanolin and cholesterol derivatives; and silicone oils. s

The agents according to the invention and in particular the cosmetic creams or lotions can also contain components which are intended to increase the moisturizing effectiveness of the agents. Suitable components include lower aliphatic alcohols having about 2 to about 6 in carbon atoms and 2 to 3 hydroxy groups, e.g. 1,4-butanediol, 1,2-propylene glycol, glycerin. Other suitable components include urea or urea derivatives such as guanidine, pyrrolidone or allantoin.

Solid granular detergents can contain foam enhancers, 15 foam suppressants, bleach, anti-soiling agents, enzymes, enzyme and bleach activators, fluorescent agents, builders, and other normal components of granular detergents. Solid bars can also contain additives such as fatty acids, salts, skin creams and 20 oils.

Oxyalkylation of the proteins.

The following procedure is a typical method that can be used to oxyalkylate proteins. , 5 In this case the method is described with reference to the oxybutylation of gelatin. 10 g of gelatin obtained by base hydrolysis with a molecular weight of approximately 80,000 and a pH of the isoionic point of approximately 5.35 are dissolved in 500 ml of water and the pH of the solution is adjusted to 7.5 with sodium hydroxide solution The solution is heated with stirring to a constant temperature of 27 ° C. and 65 ml of but-1-enoxide are added, and the reaction is allowed to proceed for 26 hours, during which time the pH with the addition of sulfuric acid below 8 , 0. 35 At the end of this period, the pH of the isoionic point of the hydroxybutylated gelatin is determined to be 7.8 by measurement using a mixed ion exchange bed, and after the excess but-1-enoxide has been evaporated, the solution is slowly dialyzed for 6 hours in order to Remove salts and low molecular weight material, and the modified gelatin is finally obtained by freeze drying, the product is then washed with methanol / ether 1: 1 and then with ether, followed by it is brought to dryness. The hydroxy-butylated gelatin has an intrinsic viscosity (measured in a pH 4.5 buffer solution containing 0.15 moles of sodium chloride, 0.1 moles of sodium acetate and 0.1 moles of acetic acid) of 0.301, which corresponds to the empirical equation of Staudinger and the values of the constants K and a according to Bello, Bello and Vinograd correspond to an average molecular weight of 73,000.

The percentage of gelatin esterification, as measured by titration, was 43%, while the percentage of N-alkylation, as measured by Van Slyke determination of primary amino groups, was 61%. 5 5

The above method or variations thereof can be used to produce modified gelatins that have different substituents and physical characteristics. For example, maintaining the pH of the reaction medium in the acidic range reduces the extent of the N-hydroxyalkylation that occurs during the reaction. Modified higher molecular weight gelatins can be prepared using higher molecular weight starting materials. Ethylene or propylene oxides can be used in place of but-1-65 enoxide to produce the corresponding oxyalkylated derivatives. Other types of proteins can also be used in place of base hydrolyzed gelatin; for example gelatin obtained by acid hydrolysis, or proteins such as casein, gliadin, soybean protein, zein and serum or egg albums. Other procedures can also be used to prepare oxyalkylated derivatives, e.g. the reaction with anhydrous alkylene carbonates.

Protein esterification.

Protein derivatives in which only the carboxylate groups have been modified can be prepared by the following procedure. 10 g of gelatin with a gel strength of about 140 bloom g and an isoionic point of about 5.3, the size of which corresponds to a mesh size

60 mesh sieves has been ground, is stirred at room temperature in a 0.036N solution of concentrated sulfuric acid (1.76g) in 1000 ml of absolute methanol. After standing for about 20 hours with occasional shaking, the methanolic solution is decanted from the solid, which is washed with methanol and then with ether, after which it is dried in a desiccator at a pressure of 0.1 mm Hg. Acidic residues are removed from the product by stirring the gelatin in ten times the weight of water with the addition of 5N sodium hydroxide solution until a pH of 6 is reached. The swollen grains are melted at 40 ° C., whereby a clear liquid is obtained which solidifies to a gel at 4 ° C. and is dried in a stream of air. Salts and low molecular weight material are removed from the product by autodialysis, after which the product is dried as indicated above.

The pH of the isoionic point of the methyl ester derivatives of gelatin, measured by mixed bed ion exchange, was 7.8. Its intrinsic viscosity, measured in a buffer solution of pH 4.5, was 0.31, corresponding to an average molecular weight of 70,000. The percentage of methyl esterification was 44%.

Aminalkylamide derivatives of the proteins.

Protein derivatives with high pH values of the isoionic point can be prepared, for example, by modifying the protein carboxylic acid groups to give carboxylic acid aminoalkylamide groups as follows.

A solution of 10 ml of N, N-dimethylethylenediamine in 80 ml of water is prepared and its pH is adjusted to 4.5 with sulfuric acid. 2 g of gelatin, which has a gel strength of about 240 bloom g, is added together with 4 g of N-cyclohexyl-N- [2- (4-B-morpholinyl) ethyl] carbodiimidemethyl-p-toluenesulfonate. The pH of the solution is adjusted to 4.8 and the solution is then left at about 25 ° C

Stand for 61 hours. It is diluted with water and then dialyzed slowly for about 14 hours, during which time the pH rises to about 7.5. Finally, the product is isolated by freeze drying and then vacuum drying in a desiccator. The 2- (N, N-dimethylamino) ethyl amide derivative of gelatin has the following characteristics:

pH of the isoionic point Intrinsic viscosity Average molecular weight Percentage of modified carboxylic acid groups

= 10.5

0.49 = 162,000

= 42%.

Skin conditioning tests.

Conditioning performance was measured by both in vitro and in vivo tests, and a high degree of agreement was found between the two test methods. The in vitro test (called calfskin occlusivity test) is based on the rate of perspiration of water through a sample of calfskin, which is mixed with a 0.15% aqueous solution of a detergent composition (at 18 ° hardness),

619 002

10th

that contains the protein is brought into contact. The occlusiveness of the protein was measured as a reduction in water transpiration for the protein-containing surfactant solution compared to that for water.

The in vivo test used was a hand immersion test (HIT). This test was carried out on the basis of 16 people (32 hands) per product in a multiproduct test, the hands being balanced in terms of the differences between the right hand and the left hand, so that 32 hands, 16 right and 16 left hands per product, have been tested. Each person immersed their left and right hands in different solutions over three consecutive 10 minute periods within half an hour a day, etc. for 3 weeks, 5 days a week. The treatment solutions were replenished every 10 minutes. The hands were removed from the solution every 2 minutes and immersed again.

The hands were assessed on the first Monday (before immersion) and every Friday of the test. The assessment was made on the basis of a scale ranging from 0 to 10 (perfect), regarding the overall condition of the hand, on the basis of a scale ranging from 0 to 10 (perfect) regarding skin flaking, and on a scale ranging from 0 to 10 (perfect) Scale, regarding the nail assessment. HIT grades for protein / surfactant solutions were determined and applied using a scale on which a 0.15% aqueous solution of the surface agent from Standard II (see Table V) was given the HIT grade 0 and a hand care lotion, which was applied in an amount of 1 mg / cm2 to which HIT grade 100 was assigned.

Examples 1-13

A number of oxybutylated gelatins made by the methods described above were compared for their conditioning benefits that they show in aqueous surfactant solutions. The modified proteins were made with varying molecular weights, isoionic points, degrees of O-alkylation, degrees of N-alkylation, etc. They were incorporated into various liquid detergent compositions of Examples 1 to 13, which are given in Table V. Examples 1 through 4 illustrate the effect (see Table I) of changing molecular weight on the conditioning performance of oxybutylated gelatins. It can be seen that oxybutylated gelatins with molecular weights in the range of 5,000 to 200,000 are all effective when providing conditioning benefits in aqueous surfactant solutions, but these benefits are most pronounced with modified proteins in the higher molecular weight range, i.e. above about 20,000. However, proteins that have lower molecular weights of about 5,000 or even lower still provide useful conditioning benefits.

Examples 6-9 illustrate the effect of changing the pH of the isoionic point on conditioning performance at a constant pH of application to skin (pH 7). It can be seen that the conditioning performance is very sensitive to the pH of the isoionic point (p1), with modified proteins having a p1 value above 8 and preferably above 8.5 being most effective for a given molecular weight value.

It can also be seen that performance is reduced to some extent at pI values below the pH of the application.

The effect of the concentration of the modified protein in the surfactant is demonstrated by comparing Examples 1, 10 and 11. The optimal protein concentration is about 4% by weight of the composition, with only minor advantages being obtained by increasing the protein content to 5% by weight. With an incorporation quantity of 2% by weight, however, conditioning advantages are reduced by more than 50%.

The conditioning performance of Examples 1, 2 and 3 as a function of the pH of the application to keratin is shown in Table IV. The optimal pH range for conditioning effectiveness is obviously below the pH of the io isoionic point of the protein, with the conditioning effectiveness generally being reduced for pH values above the isoionic point. Compared to the solution of the surface-active agent used as a control (Standard II), however, there are conditioning advantages with a somewhat lower value even above the higher pH range.

The last two entries in Table I, namely Examples 12 and 13, illustrate incorporation of the same modified protein as used in Example 1 into a surfactant solution based on paraffin sulfonate and alkyl ether sulfate. Although Examples 12 and 13 show less efficacy than most of the previous examples, the calf skin test shows that the compositions of Examples 12 and 13 have a greater mildness than the same liquid detergent compositions (Standard III) that do not have a modified protein contain.

Table I also shows the manual immersion test data for Examples 1 to 3 and 11. This data shows

that such modified proteins that have a molecular weight of 3o greater than about 1500 and a pH of the isoionic point of greater than about 8 help protect keratin from the deleterious effects of detergent solutions based on keratin at pH about 7 are applied, are particularly effective. In particular, the compositions of Examples 1 to 3 showed that from dilute aqueous solutions of surface-active agents, at least 1 hour of the conditioning benefits are obtained that are obtained with a hand care lotion that is applied directly to the skin surface. In addition, in five three-week hand-immersion tests, the composition of Example 1 left the hands and nails in a significantly better condition with 95% reliability than with the composition of Standard II.

Another advantage of the above proteinaceous compositions is that there is essentially no reduction in the volume or stability of the foam associated with the detergent composition itself. It has also been found that the above compositions have excellent storage stability and yet the surfactant has the effect of increasing the stability of the protein against hydrolysis at about pH 7 by a factor of up to about 6.

Examples 14-19

Table II compares the conditioning performance of various 55 modified proteins incorporated into surface active agent formulations as defined in Table V. Again, it can be seen that the modified high molecular weight, high isoionic point 60 proteins according to the present invention are particularly effective to provide in vitro ocelusivity benefits of aqueous surfactant solutions.

The conditioning performance of the agent of Example 17 as a function of the application pH on keratin is shown in Table IV. This modified protein has a very high pH of the isoionic point (about 10.5) and is over a wide pH range below the pH of the isoionic point and up to 2 pH units above the pH of the isoionic Effective. The effectiveness

11

619 002

decreases at application pH values that are higher than (pl + 2). In contrast to most of the other examples, where the conditioning performance at pH values below the p1 of the modified protein is relatively insensitive to the hardness of the treatment solution, the means of Example 17 above this pH value is somewhat more effective in the absence of free water hardness. This is the case with pH values from 9.3 to 9.5

Calf skin occlusiveness grade 4.5 at 0 ° hardness, but only 1.5 at 18 ° hardness.

Examples 20 to 26 The following examples are illustrative, but not limiting, of liquid detergents according to the present invention. All percentages mean% by weight.

Examples:

20 21 22 23 24 25 26

Dimethyldodecyl

amine oxide

8th%

4%

2%

4%

2%

4%

3 '

Coconut alcohol ethy

lenoxide (6) condensate

15

7

6

7

2nd

7

6

Diethanol-C12_i6-fat

acid amide

2nd

3rd

2nd

2nd

Coconut alcohol ethy

lenoxide (3) sulfate,

Sodium salt

10th

9

14

10th

12

14

Ci3_i8 "paraffin sulfate,

Sodium salt

10th

9

9

10th

12

Ci2_i4-a-01efinsuIfonat,

Ammonium salt

12

urea

8th

6

10th

8th

6

10th

more technical, with metha

nol denatured alcohol

11

13

13

13

13

12

13

Modified gelatin *

2nd

4th

4th

4th

5

3rd

4th

water

rest

* = Modified gelatin: hydroxybutyl derivative; Molecular weight 25,000; pH of the isoionic point 9.1; Percentage of O-alkylated side chains 48; Percentage of N-alkylated side chains 20.

The above agents are milder to the skin and hair than the corresponding agents containing no modified protein and there is essentially no reduction in the volume or stability of the foam formed by the detergent. Substantially the same cleaning and conditioning performance is obtained when the modified protein in the example above is replaced by the oxybutylated product of casein, which has been purified by the Hammarsten method, the modified casein having a pI of 8.8, a percentage of the O -alkylated side chains of 40% and a percentage of N-alkylated side chains of 61%.

Examples 27-32

Examples: 27 28 29 30 31 32

Coconut alcohol ethylene oxide (3) sulfate, ammonium salt 16 18 18 12 Coconut alcohol ethylene

oxide (9) sulfate, sodium salt 22 14

C13_i 8-paraffin sulfonate,

Sodium salt 10 8 14 10 5 8

Ci2_i4-a-01efinsulfonate,

Ammonium salt 8 10

Cio-14-alkylbenzene,

Sodium salt 5 14

Modified gelatin * 4 3 4 2 5 3

technical alcohol denatured with methanol 10 11 13 10 13 8

Water rest

* = Modified gelatin: hydroxyethyl derivative; Molecule Essentially the same cleaning and conditioning weight 80,000; pH of the isoionic point 8.3; Prostation is obtained when the modified protein is replaced by a percentage of O-alkylated side chains 47; Percentage of N-alkylated, methyl, ethyl, propyl, or butyl ester of gelatin replaced side chains 40.

619 002

12

which has a molecular weight of about 80,000 and a pH of the isoionic point of 8 to 9.5.

Example 33

A foaming oil bath that shows foaming and skin conditioning properties has the following composition.

Glycerin

Triethanolamine

borax

Glyceryl monostearate methyl p-hydroxybenzoate Modified gelatin * water

Rest on

6.0 1.5 0.9 2.0 0.25 5.0 100.00

Parts by weight: 40 56 1

Hexadecyldimethylamine oxide mineral oil water oxybutylated gelatin:

Molecular weight 90,000;

pH of the isoionic point 8.8;

Percentage of O-alkylated side chains 45;

Percentage of N-alkylated side chains 40 4

Example 34

A soap bar that is mild to the skin has the following composition:

Real side (tallow / coconut in the ratio 50:50)

free fatty acid moisture skin cream

N, N-dimethylethylenediamine derivative of gelatin:

pH of the isoionic point 10.5;

Molecular weight 100,000; Percentage of O-alkylated side chains 42

Parts by weight:

78.5 7.6 9.3 0.5

* = Modified gelatin: hydroxypropyl derivative; Molecular weight 80,000; pH of the isoionic point 9.2; Percentage of O-alkylated side chains 35; Percentage of N-alkylated side chains 61.

Example 36

i s A protein-based hair cream detergent has the following composition.

Parts by weight:

20 Tegamin S-13 +

Phosphoric acid (85%) methyl p-hydroxybenzoate glyceryl monostearate Modified casein * water

Rest on

4th

0.6 0.2 1.5 8.0 100.00

4.0

+ = Tegamin S-13 is a dialkylaminoalkylstearamide, which is brought to the market by the Goldschmidt Chemical Company.

30 * = modified casein: oxybutyl derivative; pH of the isoionic point 8.8; Percentage of O-alkylated side chains 40; Percentage of N-alkylated side chains 61.

Example 37

35 A cosmetic gel for use on the face and hands has the following composition.

Parts by weight:

Example 35

A moisturizing hand cream has the following composition.

Stearic acid

mineral oil

Cetyl alcohol

Parts by weight:

12 2

0.6

• ♦ o ethyl alcohol

Methyl p-hydroxybenzoate Modified gelatin * water

Rest on

10 0.3 15

100.00

* = Modified gelatin: oxybutyl derivative; pH of the isoionic point 9.6; Molecular weight 15,000; Percentage of O-alkylated side chains 24; Percentage of N-alkylated side chains 43.

Table I

Conditioning performance of oxybutylated gelatins at pH 7.

Example% by weight of the percentage, pH value, molecular in vitro

Protein set the set of desiso-Iar-Occlusi-

in the O-alky- N-alky- ionic weight: quantity:

Combination: Rating: Points:

setting:

Manual immersion test:

Overall condition:

Cutaneous

pungs

Status:

1

4th

45

40

8.8

190,000

8.2

64

44

2nd

4th

44

39

9.0

80,000

7.7

61

53

3rd

4th

48

20th

9.1

25,000

6.4

68

42

4th

4th

24th

43

9.6

15,000

4.6

-

-

5

4th

-

17th

9.1

9,000

3.1

-

-

6

4th

47

30th

8.9

80,000

8.3

-

-

13

619 002

Conditioning performance of oxyhutylated gelatins at pH 7.

Example weight Ç? the percentage-percent-pH-value molecule-in-vitro protein set the set that of the isolar-occlusive

in the O-Alky- N-AIky- ionic weight: vity:

Combination: Rating: Points:

Settlement:

Hand immersion test:

Total skin dander condition: Pung condition:

7

4th

49

59

7.9

100,000

5.9

-

-

8th

4th

39

-

6.9

80,000

4.7

-

-

9

6

56

52

6.2

80,000

<1

-

-

10th

5

45

40

8.8

190,000

7.8

-

-

11

2nd

45

40

8.8

190,000

5.3

31

33

12

4th

45

40

8.8

190,000

2.3

-

-

13

4th

45

40

8.8

190,000

2.5

-

-

default

I _____ 0 '

II - - - - - -6.1 0 0

III -3.6 0 -12

Table II

Conditioning performance of various modified proteins at pH 7.

Example:

Modified reagent / protein:

% By weight protein in the

Percentage of O-alky

Percentage of the N-alky

pH value molecule in vitro of the occlusive

ionic weight: vity:

Together:

lation:

Point:

setting:

(a)

(b)

(c)

(d)

(e)

(f)

(G)

14

Ethylene oxide /

gelatin

4th

47

40

8.3

80,000

6.4

15

Propylene oxide /

gelatin

4th

35

61

9.2

80,000

4.4

2nd

But-l-enoxide /

gelatin

4th

44

39

9.0

80,000

7.7

16

Methanol /

gelatin

4th

35

9.0

100,000

2.7

17th

N, N-dimethyl

ethylenediamine /

gelatin

4th

42

7

10.5

100,000

3.0

18th

But-l-enoxide /

Casein

4th

40

61

8.8

-

3.2

19th

But-l-enoxide /

Soybean

protein

4th

-

-

8.5

-

6.0

default

IV

Superpro 16 C.

6

-

-

5-6

1,000

<-7

V

Hydropro 230

6

-

-

6.5

300

+0.1

VI

Crotein SPC

6

-

-

5-5.5

10,000

-6.1

VII

Crotein SPO

6

-

-

5-5.5

2,000

-1.2

VIII

Wilson X 250

6

-

-

6

1,000

-3.4

IX

Wilson X 1000

6

-

-

5

10,000

-6.7

619 002

14

Table III

Conditioning performance of various precursor proteins.

Protein% by weight protein usage pH of the molecular in vitro

in the total pH: isoionic weight: occlusive

setting: point: vity:

Type A * 4 6 7.7 75 000 5.3

cationic to all

Polylysine ** 4 7 pH values> 70,000

Default:

X 4 7 4.5 140 000 -6.1

* Isatinic gelatin produced by acid catalyzed hydrolysis of collagen

Point 7.7, isoelectric point 8.4, molecular weight approx. 75,000 ** synthetic polypeptide, polylysine, isoionic point> 11, molecular weight 70,000 and above

Table IV

Conditioning performance as a function of the application pH.

Application Standard II: Example 1: Example 2: Example 3: Example 17: Standard X: application pH:

2.5 - 1.3 - -5.0

5.7

8.2 7.7 6.4 3.0 6.1

-1.5 1.5 - 1.5

-2.7 1.4

-6.2 -1.3 - 1.5

-6.0 -3.7 - 1.0

- - - 3.5

3.8

- - - -1.2

4.0

-

4.5

5.0

8.5

5.5

-

6.0

-5.3

6.5

-

7.0

-6.1

7.5

-

8.0

-6.2

8.5

-

9.0

-6.5

9.3

-7.3

10.0

-

10.5

-

11.0

-5.2

11.5

12.0

12.5

M

Table V

Together

Example:

Default:

setting:

1.4

6.7,

2:

3.5:

8: 9:

10:

11:

12:

13:

I: II:

ni:

IV:

X:

15,

14,

-

18,

16,

IX:

19:

17, 21:

(a)

(b)

(c)

(d)

(e)

(g) (h)

(i)

(j)

(k)

(I)

(m) (n)

(O)

(p)

(q)

Ammonium linear-C12_14-alkylbenzene-

sulfonate 18.4 18.4 18.4 18.4 18.4 18.4 18.4 18.4 - - - 18.4 - 18.4 18.4

Sodium linear C12_I4-

alcohol sulfate,

including

3 ethylene oxide residues 18.4 18.4 18.4 18.4 18.4 18.4 18.4 18.4 13.5 18.4 - 18.4 13.5 18.4 18.4

Sodium C14 paraffinsul

fonat ____ ____ 27.0 18.4 - - 27.0 -

15 619 002

Contin. Tab. V:

(a) (b) (c) (d) (e) (f) (g) (h) (i) (j) (k) (1) (m) (n) (o) (p) (q ) Lauric acid

ethanol 2.0 2.0 2.0 2.0 2.0 4.5 4.5 4.5 4.5 - 2.0 - 4.5 - 2.0 2.0

Urea 10.0 - 6.0 10.0 10.0 - - - 8.0 6.0 12.0 - 10.0 technical,

Verg ^ Hte ^ Spirit 13 '° 13' ° 13 '° 15> ° U> 4 13' ° 13> ° 13 '° 13' ° 7> ° 10 '° "13> ° 7' ° 13 '° l3' °

Protein * 4.0 4.0 4.0 4.0 4.0 4.0 6.0 5.0 2.0 4.0 4.0 - - - 6.0 4.0 Water,

Remaining to 100 100 100 100 100 100 100 100 100 100 100 100 100 100 100 100 * = protein incorporated as grains that contain about 10% water.

C.

Claims (12)

619 002 PATENT CLAIMS 1. Agent for protecting skin and hair against the harmful effects of harsh materials, in particular detergents, and against adverse climatic conditions, which contains a non-enzymatic modified protein in combination with a surface-active agent, characterized in that it contains 0, Contains 1 to 90% by weight of surfactant and that the non-enzymatic modified protein has an average molecular weight above 5000 and an isoionic point at more than pH 6 and, as a result of the modification, contains one or more of the following functional groups: I I -Ç-W-Q; -N-X-Q; -O-Y-Q; -S-Z-Q; in which C, N, O and S represent carbon, nitrogen, oxygen or sulfur atoms which are part of the unmodified starting protein, —Zr- represents a direct bond or carbonyl, -Y- represents -Z-, sulfonyl or phosphonyl, -X- stands for -Y-or> C = NR, I. -W- stands for -X-, -NX-, -OY- or-SZ- and Q represents -R1, -SR1, -OR1, -NR2, -SR2 or - NR3, in which R represents hydrogen or —R1 and R1 represents an alkyl, alkenyl, aryl, cycloalkyl or heterocyclic radical, the alkyl or alkenyl radicals optionally being interrupted by heteroatoms and optionally being substituted by nonionic and / or cationic radicals , and wherein R has no more than 20 interconnected carbon atoms in the alkyl or alkenyl radicals. 2. Composition according to claim 1, characterized in that R1 of the formula: -CH2- (CHQ1) p- (CH2) q-Q1 ® © in which Q1 is R2, SR2, OR2, N (R2) 2, S (R2) 2, N (R2) 3 or OCOR3, where R2 is hydrogen or R3 and R3 is an alkyl or alkenyl radical having up to 20 carbon atoms , and wherein p = 0 or 1 and q = 0 to (5 - p). 3. Composition according to claim 1 or 2, characterized in that R1 contains up to 8 carbon atoms and up to 2 heteroatoms. 4. Means according to claim 1, characterized in that R1 of the formula -CH2-CHOH- (CH2) r -H corresponds, in which r = 0 to 6. 5. Means according to claim 1, characterized in that R1 of the formula -CH2- (CH2) r -H corresponds, where r = 0 to 7. 6. Composition according to claim 1, characterized in that R1 of the formula H2) s-H - (CH2) r — N (CH2) t-H where r = 1 to 4 and s and t = 0 to 3. 7. Composition according to one of the claims 1 to 6, characterized in that at least one of the functional groups of the modified protein is introduced into side chains of the unmodified starting protein containing carboxyl groups. s 8. Composition according to claim 7, characterized in that WQ the group O II -COR1 Kl means. 9. Composition according to claim 8, characterized in that R1 corresponds to the formula given in claim 4 and the modified protein is an oxyalkylated protein 15, whose oxyalkyl groups are derived from an alk-l-enoxide. 10. Composition according to claim 8, characterized in that R1 corresponds to the formula given in claim 5 and the modified protein is an esterified protein, 2o whose ester groups are derived from a primary alcohol, 11. Means according to claim 7, characterized in that WQ the group O II 25 -C NHR1 means. 12. Composition according to claim 11, characterized in that R1 corresponds to the formula io given in claim 6 and that the modified protein is an amidated protein whose amide groups are derived from an alkylenediamine.