NO742652L - - Google Patents

Description

Detergents with a keratin-protecting effect.

The present invention relates to compositions which protect keratin-containing materials, such as skin and hair, from the damaging effects of detergents or other materials with an adverse effect, such as solvents etc., as well as harsh climatic conditions.

The composition according to the present invention therefore helps

to maintain keratin-containing materials in good condition. The invention also relates to a method for treating keratin.

The destructive effects of compositions containing surfactants on keratin are well known. It is believed that these effects are due to the penetration of surface-active agents into the keratin surface, which leads to the "leaching" of oil and humectants, which are necessary to keep the keratin in good condition. This penetration of the surfactant and "leaching" of essential oils affects the keratin's ability, especially for skin, to retain water within the tissue, which in turn leads to a flat condition for the keratin-containing material.

Many attempts have previously been made to provide compositions to maintain or improve the conditions of hair and skin. Adding protein to the skin and hair as a cosmetic treatment probably goes back to prehistoric times. Casein in the form of milk has long been used as a recognized beauty agent and has more recently been recommended for use in toilet soaps. British Patent No. 1,160,485 describes the inclusion of partially degraded proteins, with a gel strength of zero "Bloom" g, in detergent compositions and creams for application to skin, such as dishwashing liquids.

OLS 2.151.739 and OLS 2.151.74o describe certain fat derivatives

of low-molecular aminolysates, suitable for use in shampoos. British Patent No. 1,122,076 describes the preparation of protein esters, soluble in low-molecular alcohols, which are useful in hairspray compositions. Various low-molecular polypeptides or modified polypeptides are commercially available and recommended for use in cosmetics and shampoo compositions, for example "Hydro Pro 22o", "Hydro Pro 33o", "Maypon 4C" (Stepan Chemical Company), "Wilson X25o", "Wilson Xlooo" and "Wilson Aqua Pro" (Wilson Chemical Company). However, it has been found that none of these compositions are particularly effective in protecting keratin against the action of powerful detergents, and this is especially the case when the proteins are incorporated into the detergent composition itself. The mitigating effect of these compositions can often be improved by the addition of fatty or oily materials, but when used in liquid dishwashing detergents this usually does not lead to

loss of foaming ability and aesthetic changes, which are generally considered undesirable by the consumer.

The present invention therefore provides protein-containing compositions which are particularly effective with regard to protecting keratin-containing materials, such as skin and hair, against the damaging effect of detergents and other sharp materials and against severe climatic conditions, and which are even effective when they keratin is applied in foaming detergent solutions, without this resulting in a loss of foaming or washing ability for detergent solutions containing the proteins.

According to a feature of the present invention, a composition for the protection of keratinous material against the damaging effects of detergents and other harsh environments comprises an effective amount of a modified protein, as defined in the following and which has a molecular weight greater than 5ooo and an isoionic point greater than pH 6 and where the modified protein is incorporated into a compatible carrier further comprising a surfactant or a cosmetic base material.

In this description, modified protein means a product, other than a derived protein, obtained in one or more steps by chemical or biochemical modification of a precursor protein, a precursor protein being a non-enzymatic protein selected from natural, derived, synthetic or biosynthetic proteins and a derivative protein is a product of hydrolytic,. aminolytic, enzymatic or thermal degradation of a protein material.

According to another feature of the invention, a composition for the protection of keratin-containing materials from the damaging effects of detergents and other harsh environments comprises an effective amount of precursor protein, as previously defined, with an average molecular weight greater than 5ooo and with an isoionic point (in the following sometimes denoted by p1) greater than 6, the precursor protein being incorporated into a compatible carrier which further contains a foaming detergent, the pH of the composition or an aqueous solution or dispersion of the composition at consumer concentration being less than

(pl - o,7).

According to a further feature of the invention, a method is provided for protecting keratin-containing material from the damaging effects of detergents or other sharp materials, which method comprises treating keratin with a composition or an aqueous solution or dispersion of

a composition, as defined above.

The preferred modified proteins for use in the compositions or in the method according to the present invention have functional groups obtained as a result of the modifications and comprise one or more of: C-W-Q; N-X-Q; O-Y-Q; S-Z-T where C, N, 0 and S represent carbon, nitrogen, oxygen and sulfur atoms respectively,

which atoms form part of the precursor protein,

_Z--means a direct bond or carbonyl group,

-Y- means -Z-, sulfonyl or phosphonyl groups,

-X-- means -Y- or C=NR groups

-tf- means -X-, -NX, -0Y- or SZ groups, and

111 © ©

Q means -R , -SR , -OR , -NR 2 , -SR 2 , -NR 2

in which R means a hydrogen atom or -r\ where R1 gmeans one or more alkyl, alkenyl, aryl, cycloalkyl or heterocyclyl groups, with interspersed heteroatoms or functional groups imparting color or fluorescence possibly between the alkyl or alkenyl groups etc. and may optionally be substituted with non-ionic or cationic groups, and where R does not contain more than 20 contiguous carbon atoms in the alkyl or alkenyl groups.

In a given modified protein, all these groups do not of course need to be identical, furthermore the different R groups can be the same or different.

Of the above modified proteins, those in which

1

R has the formula

2 7°7 ? 2 ?

wherein Q1 is R2, SR2', OR2, NR2, SR2, NR2or 0(C=0)R<3>,

2 3 3 in which R is a hydrogen atom or R , where R is an alkyl or alkenyl group with up to

2o carbon atoms. J-

t

In general, R 1 will contain no more than 8 carbon atoms and up to 2 heteroatoms, which may be the same or different. Preferred classes of modified protein falling within the above definitions are those in which R"<*>" is represented by

The protein modification can be carried out by common methods such as. are used in the production of proteins with functional substituents. In general, the reactive centers at which the modification is carried out are the protein side chains, which include acidic or basic groups such as carboxylic acid groups, amino, sulfhydryl, aliphatic or phenolic hydroxy groups, imidazole or guanidino groups, or side chains containing a reactive, aromatic ring such as in tyrosine. A preferred modified protein has as substituents carboxylic acid esters or amide groups derived from the carboxylic acid groups in the unmodified substrate. The ester can be obtained from protein and the appropriate alcohol by suspending the protein in anhydrous alcohol at a temperature in the range o - 25° and at an acid concentration of o.o2 - o.loM for several days. Alternatively, -hydroxyalkyl esters can be prepared by reacting the protein with an epoxide, for example but-1-enoxide. Esterified products can also be prepared by reaction with diazoacetic acid esters or amides. Amides can be prepared from protein carboxylic acid groups by reaction with a water-soluble carbodiimide and amine. This can simultaneously lead to a modification of the phenol groups in tyrosine or sulfhydryl groups in cysteine, respectively to give O-arylisoureas and S-alkylisothioureas.

In other embodiments of the invention, the proteins can be acylated or alkylated via the amino, hydroxy or sulfhydryl groups. Acylation can be carried out using the appropriate acid anhydride or N-carboxylic anhydride. In the latter case, this leads to acylation essentially of the amino groups. In the former case, if the acid anhydride is cyclic, the modification will lead to acidic substituents which must be neutralized, for example by esterification. Reactions analogous to acylation can also be carried out, for example the proteins' ε-amino groups can be selectively replaced with more basic guanidino groups by treatment with O-alkylisourea or S-alkylisothiourea.

Sulfonate esters or sulfonamide derivatives of the proteins can be prepared, for example, by reacting the protein's hydroxy or amino groups with sulfonyl halides. These modified proteins can in turn be used to produce further modifications by cleaving the alkyl-oxygen bond in the sulphonate. In this way, for example, hydroxy groups can be replaced, for example, with S-alkyl groups.

Other routes are also available for the preparation of alkylated or arylated proteins. Thus, S-alkylation or N-alkylation of the sulfhydryl groups of the amino groups can be carried out by nucleophilic substitution on halogen acetates or by addition to unsaturated carbon-carbon bonds which are conjugated with e.g. cyanide, as in acrylonitrile, or an imido group, as in maleimides. N-alkylation can also be carried out by means of sodium borohydride reduction of imiher obtained by condensation of proteinamine 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 halobenzene derivatives.

The proteins in the composition according to the invention can be modified in a number of other ways. For example, proteins easily undergo electrophilic substitution reactions, which allow the modification of cysteines to cystines by reaction with an iodine-

donor followed by an alkylmercamptan. Substitution of the aromatic ring with nitro groups using tetranitromethane as nitrating agent or with diazonium groups is also possible.

In addition, the guanidino groups in arginine can be modified by reaction with 1,2-dicarbonyl derivatives such as cyclohexanedione or phenylglyoxal.

The precursor proteins suitable for use, after modification in the compositions according to the invention, can be selected from natural, derived, synthetic or biosynthetic proteins.

Typical natural proteins include intracellular proteins or globular proteins such as those found in blood plasma and milk. Derived proteins can be obtained from many sources, e.g. by^hydrolytic, aminolytic, thermal or enzymatic degradation of<g>lobular or structural proteins, such as keratin, collagen, fibrinogen, myosin, whey egg white, casein or vegetable proteins, such as those obtained from grains, soybean pulp or protein-rich residues from seed oil production. A particularly suitable derived protein is gelatin which is a hydrolysis product (usually acid or basic catalysed) of collagen from skins and bones and which can have an average molecular weight in the range of 5ooo - 2oo.ooo and higher. Other highly desirable precursor proteins include whole casein and soybean protein, synthetic proteins such as polylysine and proteins obtained from single-celled microorganisms.

The precursor proteins whose isoionic point is greater than the pH

6 are also applicable for direct use, i.e. without modification in certain compositions according to the present invention. In particular, such precursor proteins comprise acidic hydrolysis products of, for example, collagen. These include the so-called type A gelatins. Other suitable proteins include polyamino acids such as polylysine and certain single cell proteins. However, it has been found that compositions according to the invention comprising precursor proteins are significantly less effective than those containing modified proteins. The latter are therefore highly preferred. Particularly preferred proteins for use in compositions according to the invention have distinctive values for molecular weight and isoionic point pH and these will be discussed in detail.

It will be understood that the molecules of protein vary greatly with regard to their size and complexity and that the molecular weight for a protein is an imprecise quantity. The molecular weight of a protein can be specified by defining the molecular weight distribution of the molecules in the protein, but it is instead common to define the average molecular weight of the protein sample,

because it is the average molecular weight that is measured by most physical techniques. Such an average molecular weight is only an approximation for the real molecular weight distribution of the sample. It will also be understood that determination of the mean molecular

weight can vary from one measuring technique to another. Usually, the so-called average molecular weights are determined by measuring osmotic pressure, diffusion rate, etc., while weighted average molecular weights are determined, for example, by ultracentrifuge techniques. In the present description, viscometric measurements of buffered protein solutions are used to determine the protein's average molecular weight. It is known that the limiting viscosity of a buffered protein solution is primarily dependent on the total length of the protein helix and that it is relatively independent of the nature of the side chains and end groups in the protein. There is therefore a relationship between intrinsic viscosity and the average molecular weight,

M, of the protein which can be expressed as

where K and a are constants,

for example, gelatin derived from calf skin (see Macromolecular Chemistry of Gelatin, page 72

by A. Veiss).

The limiting viscosity is reduced to specific viscosity by infinite dilution of the protein solution is defined with respect to the relevant viscosity, measured with a viscometer, as follows:

The constants, K and a, used in the calculation of molecular weights of gelatin derived from calf skin, were as follows from J. Bello, H.R. Bello and J.R. Vinograd, Biochimica Et Biophysica Acta, 57, 222-9, (1962)

K = 2.9 x lo<-4>

a = -o.62

Precursor and modified proteins according to the present invention have molecular weights greater than 3oo and preferably greater than 2ooo and even more advantageously more than 5ooo. More particularly, their molecular weight is greater than lo.ooo and further preferably greater than 15.ooo and will usually be in the range of 2o.ooo - 2oo.ooo.

Of the total molecular weight of the modified protein, it is preferred that at least the main part is derived from the precursor protein. Advantageously, the precursor protein provides 80-99%, preferably 90-96% of the total molecular weight of the modified protein.

.Protein molecules with both acidic and basic side chains are charged in both acidic and basic solutions and are therefore amphoteric in nature. The number of such acidic and basic groups in the protein molecule can be determined by titration with a monovalent, strong acid (for example dilute nitric acid) or base (for example a sodium hydroxide solution) and the results are stated

conventionally as mmol/g, the number of mmol of the acid or base required to neutralize 1 g of protein.

Modified proteins according to the present invention have a basic side chain content preferably greater than 0.1 mmol/g,

more preferably greater than 0.5 mmol/g and more advantageously greater than 0.8 mmol/g. They have an acidic side chain content preferably less than 1.5 mmol/g and more preferably less than 1.1 mmol/g and substantially more preferably less than 0.8 mmol/g.

The modified proteins according to the present 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 modifications thus generally lead to an increase in the hydrophobicity and can lead to an increase in the isoionic pH value, i.e.

the pH value at which equal concentrations of protein anions and cations are found in the solution.

Preferably, the modified or precursor proteins used in the composition of the present invention have an isoionic pH value greater than 6.5, more preferably greater than 7.2 and most preferably greater than 8.0.

The isoionic pH value of the protein. discussed above may differ slightly from the protein's isoelectric pH value, although the difference is usually small. The isoelectric point can be determined by the anion/cation balance of all the 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 ions thereof. The isoionic pH value can be determined as follows: "Amberlite" acid resin "IR 12o" and basic resin "IR 4oo" are washed with several volumes of water, filtered and mixed in the ratio o.4:1. A 1.5% by weight protein solution (20 ml) is prepared by minimal heating and allowed to stand overnight at a constant temperature, after which the resin mixture (4.2 g) is added and the solution is stirred for 5 min, after which the mixture is filtered and the pH value of the filtrate is the protein's isoionic pH value.

The optimal choice of protein for a particular composition is to some extent dependent on the pH value of the composition in use, i.e. the pH value of the carrier when applied to keratin. This application pH value may, depending on the application type, be the composition's own pH value or it may be the pH value of an aqueous solution or dispersion of the composition at an application concentration which may be as low as o.ol%.

Regarding the compositions comprising modified proteins

it is preferred that the pH value of the composition or an aqueous solution or dispersion of the composition at use concentration is less than (pI +2) where pI is the isoionic pH value of the modified protein. More preferred use-

The pH is less than (pl + o.5), more preferably less than (pl - o.7) and most preferably less than (pl - 1.4). In addition, modified proteins with a pI greater than 9.6 can be satisfactorily used at a pH between (pI + 2) and pI-.

With regard to the compositions according to the invention comprising precursor protein, it has previously been stated that the pH value for the composition or an aqueous solution or dispersion of the composition at the use concentration must be less than (pl - o.7). It is also preferred that this pH value in use is less than (pl - 1.4) and generally less than pH 7.

The use pH value for the composition according to the present invention can vary widely, of course depending on the purpose and method of use of the compositions. Liquids or cream compositions composed for shampoos, hand creams or cosmetic liquids are generally applied directly to hair or skin and the use pH value in this case is the pH of the composition itself. This one could be

any pH range, generally 4-9. Detergent compositions such as liquid dishwashing compositions, bath compositions and coarse powder or powdered detergents are usually used in a large excess of water and the use pH value is the pH value of an aqueous solution of the composition

at a concentration which is usually in the range of 0.1 - 2% by weight. Building salt-free detergent compositions, for example for use in delicate washing liquids, will usually have a use pH value of

about. 7, built-in detergents generally have a use pH in the alkaline range up to pH approx. 11. Bar soap compositions are applied to the skin as an aqueous solution or dispersion of bar soap ingredients in a concentration that is usually in the range of 5-15% by weight. The pH of the soap dispersion can vary depending on the type of seaweed soap used and is in the range of pH 5.5-9.5.

The preferred compositions according to the present invention have a use pH in the range 4-11, more preferably in the range 5-9.5 and most preferably in the range 5.5-7.5. Forioper proteins are generally incorporated into liquid detergent compositions in the pH range 5.5-6.9.

Modified proteins according to the present invention are produced by modifying the side chains of the protein precursor, comprising free carboxylic acid groups or free basic, especially primary amino groups. In particular, the modification of the acid groups is carried out by oxyalkylation and esterification (corresponding to a substitution with a fj<*>, instead of WQ) or amidation (corresponding to a substituted <COR>

eration of 0, , instead of WQ) . Modification of basic groups

. , CNHR J__e.. e ^ .. ^

on the other hand, is preferably carried out in the form of alkylation (corresponding to the substitution of -R"<*>" instead of XQ). It should be noted that acylation, for example of primary amino groups - destroys the basic character of such groups and the general effect in the absence of other types of modifications is to lower the protein's isoionic pH value to the range 4.5 - 5.5. N-acylation is therefore preferably not used as a single-modification method if no other modifications are used that raise the pI of the N-acylated protein to over 6.

Particularly preferred modified proteins according to the present invention include esterified or hydroxyalkylated products of high molecular weight gelatins derived by acid or basic hydrolysis of materials such as animal skin or bone.

Such modified proteins have proportionally fewer carboxylic acid groups and more carboxylic acid ester groups than unmodified proteins. Lower alkyl or hydroxyalkyl derivatives are preferred. These can be produced simply by an acid-catalyzed esterification with the appropriate alcohol, in which case the reaction takes place primarily at the protein's carboxylic acid groups, or alternatively, can be produced by treatment with alkylene oxide, in which case a hydroxyalkylation can also take place alongside the esterification of other reactive groups, for example of primary amino groups. The degree of such;. N-hydroxyalkylation is primarily dependent on the pH conditions used. If the pH of the reaction •-•medium

is kept in the acidic range during the course of the reaction, the degree of N-alkylation is significantly less than if the pH is allowed to rise during the reaction. The effect of the N-hydroxyalkylation leads to an increase in the protein's hydrophobicity and a lowering of the protein's isoionic point. However, the net effect with regard to the conditioning effect is relatively small compared to the effect of the esterification on the conditioning efficiency. Preferably, the degree of modification is such that at least 5%, more preferably 2o?4 and most preferably at least 35%

of the free, acidic side chains in the protein esterified. The modified proteins can be present in the composition according to the present invention in an amount of up to 50% by weight, but generally in an amount in the range 1-1o% by weight, preferably in the range 2-6% by weight of the composition. They are thus effective keratin conditioners even in relatively low concentrations.

The surface-active materials that can be used in the compositions according to the present invention can be selected from water-soluble soaps or synthetic anionic, non-ionic, cationic, zwitterionic and amphotic detergents, described in the following, preferably they are surface-active agents, foaming detergents or emulsifiers.

A. Anionic soap and non-soap synthetic detergents.

This class of detergents includes ordinary alkali soaps, such as sodium, potassium, ammonium alkylammonium and alkyloammonium salts of higher fatty acids containing 2-24 carbon atoms, preferably 10-20 carbon atoms. Suitable fatty acids can be obtained from natural sources such as for example from vegetable or animal esters (for example palm oil, coconut oil, babassu oil, soybean oil, castor oil, tallow, whale and fish oils, fats, tallow and mixtures thereof). The fatty acids can also be produced synthetically (for example by oxidizing petroleum or hydrogenating carbon monoxide by the Fischer Tropsch process). Resin acids obtained from tall oil are also usable. Naphthenic acids. are also applicable. Sodium and Kalim soaps can be produced by direct saponification of fats or oils or by neutralization of free fatty acids, which are produced by a separate manufacturing process. Particularly useful are sodium, potassium and triethanolamine salts of mixtures of fatty acids obtained from coconut oil, tallow, for example sodium or potassium tallow and coconut soap.

This class of wash agents also includes water-soluble salts, especially alkali metal salts of organic sulfuric acid reaction products, which in the molecular structure contain an alkyl group containing 8-22 carbon atoms and a sulphonic acid or sulfuric acid ester group. (Included in the term alkyl is the alkyl part of higher acyl groups). Examples of this group of synthetic detergents, which form part of the preferred compositions according to the present invention, are alkali metal, for example sodium or potassium alkyl sulphonates, especially those obtained by sulphonation of higher alcohols (Cg - C^g) obtained by reduction of glycerides in tallow or coconut oil, alkali metal olefin sulfonates with 8-24 carbon atoms as described for example in US patent 3,332,880, alkali metal. alkyl glyceryl ether sulfonates, especially those obtained from higher ethers of higher alcohols derived from tallow and coconut oil e. Other anionic detergents include alkali metal alkylbenzene sulfonates, in which the alkyl group contains 9-15 carbon atoms, including those described in US Patent Nos. 2,220. o99 and 2,477,383 (the alkyl group can be straight chain or - branched), sodium coconut oil fatty acid monoglyceride sulfates and sulfonates, salts of alkyl phenplethylene oxide ether sulfate with 1-12 ethylene oxide units per molecule and in which the alkyl groups contain 8-18 carbon atoms, the reaction product of fatty acids esterified with isothionic acid and neutralized with sodium hydroxide, where for example the fatty acid is oleic acid derived from coconut oil, sodium or potassium salts of fatty acid amide of a methyl tauride in which the fatty acid is for example derived from coconut oil , sodium or potassium-(3-acetoxy-or |3-acetamido-alkanesulfonates where the alkane group contains 8-22 carbon atoms, as well as others known in the state of the art, some of which are stated in US patents no. 2,286,921, 2,486,922 and 2,396,278.

Other useful synthetic anionic detergents are alkyl ether sulfonates. These connections have<*>the general

2 2

formula R 0 (C2H40)xSO3M wherein R is alkyl.. or alkenyl of 8-24 carbon atoms, x is 1-3o, and M is a salt-forming cation comprising alkali metal, ammonium, dimethyl, trimethyl, triethyl, dimethanol, diethanol, trimethanol and triethanol ammonium salts.

The alkyl ether sulphates according to the present invention are condensation products of ethylene oxide and monohydric alcohols with 8-24 carbon atoms. Preferably, R 2 contains 14-18 carbon atoms. The alcohols can be derived from fat, for example coconut oil or tallow, or can be synthetic. Lauryl alcohol and straight chain alcohols derived from tallow are preferred. Such alcohols are reacted with 1-12, especially 6 mol of ethylene oxide and the resulting mixture, for example containing on average 6 mol of ethylene oxide per mol of alcohol, is sulphonated and neutralized.

Particular examples of alkyl ether sulfates according to the present invention are sodium coconut alkyl ethylene glycol ether sulfate, lithium tallow alkyl triethylene glycol ether sulfate and sodium tallow alkyl hexoxyethylene sulfate.

Because of the excellent cleaning properties and the easy availability of alkali metal coconut and tallow alkyloxyethylene ether sulfates, with an average of 1-10 oxyethylene units per mol, are particularly preferred. The alkyl ether sulfates are described in

US Patent No. 3,332,876.

B. Non-ionic, synthetic liquid active agents.

Non-ionic, synthetic detergents can be broadly defined as compounds obtained by condensation of alkylene oxide groups (with a hydrophilic nature) with an organic hydrophobic compound,

which may be aliphatic or alkylaromatic in nature. The length of the hydrophilic or polyoxyalkylene group fused with a particular hydrophobic group can be easily adjusted to provide a water-soluble compound with the desired degree of balance between hydrophilic and hydrophobic elements.

For example, a well-known class of nonionic synthetic detergents is commercially available under the trade name "Pluronic". These compounds are formed by condensing ethylene oxide with a hydrophobic base formed by condensing propylene oxide with propylene glycol. The hydrophobic part of the molecule, which is naturally not water-soluble, has a molecular weight in the range 15oo - 18oo. The addition of polyoxyethylene groups to this hydrophobic part tends to increase the water solubility of the molecule as a whole and the product's liquid character is preserved up to a point where the polyoxyethylene content is approx. 50% of the total weight of the condensation product.

Other suitable nonionic synthetic detergents include: 1. Polyethylene oxide condensates of alkylphenol, for example the condensation product of alkylphenol with an alkyl group containing 6-12 carbon atoms in either a straight or branched chain, with ethylene oxide, the ethylene oxide being present in an amount equivalent to 5-25 mol of ethylene oxide per moles of alkylphenol. The alkyl substituent in such compounds can, for example, be derived from polymerized propylene, diisobutylene, octene or nonene. 2. Those derived from the condensation of ethylene oxide with the product obtained by reacting propylene oxide with ethylenediamine. Such compounds contain e.g. 4o - 80 weight- % polyoxyethylene and has a molecular weight in the range 5ooo - 11.ooo, and is obtained by reacting the ethylene oxide group with a hydrophobic base consisting of the reaction product of ethylenediamine and an excess of propylene oxide. Such bases with a molecular weight of the order of 2 are satisfactory. 5oo - 3,000. 3. The condensation product of an aliphatic alcohol with 8 - 24 carbon atoms either in a straight chain or branched

chain, with ethylene oxide, for example. a coconut alcohol-ethylene oxide condensate with 5 - 30 moles of ethylene oxide per

mole of coconut alcohol, the coconut alcohol fraction contains lo - 14 carbon atoms.

4. Non-ionic detergents including nonylphenol condensed with either lo - 30 moles of ethylene oxide per moles of phenol and the condensation products of coconut alcohol with an average of either 5.5 to 15 moles of ethylene oxide per moles of alcohol and the condensation product of approx. 15

mol of ethylene oxide with 1 mol of tridecanol. u

Other examples include dodecylphenol condensed with 12 moles of ethyl oxide per mol phenl, dinonylphenbl condensed

with 15 mol of ethylene oxide per moles of phenol, dodecyl mercaptan condensed with lo moles of ethylene oxide per mol mercaptan, bis-(N-2-hydroxyethyl)-lauramide, nonylphenol condensed with 20 mol ethylene oxide per moles of nonylphenol, myristyl alcohol condensed with lo moles of ethylene oxide per mole of myristyl alcohol, lauramide condensed with 15 moles of ethylene oxide per moles of lauramide and di-iso-octylphenol condensed with. 15 moles of ethylene oxide. 5. A detergent with the formula R 3 R 4 R 5N 0 (amine oxide detergent) in which R 3 is an alkyl group containing lo - 28 carbon atoms, from 0 to 2 hydroxy groups and from 0 to 5 ether bonds, there is at least one R 3 -group which is an alkyl group containing lo - 18 carbon atoms and 4 5

0 ether bonds, and each of R and R comprises alkyl groups or hydroxyalkyl groups containing 1-3 carbon atoms.

Specific examples of amine oxide detergency compounds include dimethyldodecylamine oxide, dimethyltetradecylamineoxide, ethylmethyltetradecylamineoxide, cetyldimethylamineoxide, dimethylstearylamineoxide, cetylethylpropylamineoxide, diethyldodecylamineoxide, bis-(2-hydroxyethyl)-3-dodecoxy-1-hydroxypropylamineoxide, (2-hydroxypropyl)methyltetradecylamineoxide, dimethyloleylamine oxide and dimethyl-(2-hydroxydodecyl)amine oxide, as well as the corresponding decyl, hexadecyl and octadecyl homologues of the above-mentioned

connections.

6. A detergent-active compound with the formula

in which

R3 and R4 are as indicated above. Specific examples of sulfoxide detergents include: dodecyl methyl sulfoxide, tetradecyl methyl sulfoxide, 3-hydroxytridecyl methyl sulfoxide, 3-methoxytridecyl methyl sulfoxide, 3-hydroxy-4-dodecoxybutyl methyl sulfoxide, octadecyl 2-hydroxyethyl sulfoxide, and dodecyl ethyl sulfoxide. 7. Ammonium, monoethanol and diethanolamides of fatty acids with an acyl group of 8-18 carbon atoms. These acyl groups are normally derived from naturally occurring glycerides, for example coconut oil, palm oil, soybean oil and tallow oil, but can also be derived synthetically, for example by oxidizing petroleum or by hydrogenating carbon monoxide in the Fischer Tropsch process. C. Amphorolytic, synthetic detergent active agents. Ampholytic, synthetic detergents can be broadly described as derivatives of aliphatic or aliphatic derivatives of heterocyclic secondary and tertiary amines, in which the aliphatic group can be straight-chain or branched and in which one of the aliphatic substituents contains 8-18 carbon atoms and at least one e contains an anionic water-soluble group, for example carboxy, sulpho or sulphato group.

Examples of compounds that fall within the definition given above are sodium 3-(dodecylamino)-propionate, sodium 3-(dodecylamino)propane-1-sulfonate, sodium 2-(dodecylamino)ethyl-! sulfate, sodium 2-dimethyl)octadecanoate, disodium 3-(N-carboxymethyldodecylamino)propane-1-sulfonate, disodium octadecyl-imino-diacetate, sodium l-caroxymethyl-2-undecyl-imidazole and sodium N,N-bis -(2-Hydroxyethyl)-2-sulfato 3-dodecoxypropylamine.

D. Zwitterionic synthetic detergents

Zwitterionic synthetic detergents can be broadly described as derivatives of aliphatic quaternary ammonium and phosphonium or tertiary sulfonium compounds, in which the cationic atom may be part of a heterocyclic ring and in which the aliphatic group may be straight chain or branched and in which one of the aliphatic substituents contain 3-18 carbon atoms, and at least one of the aliphatic substituents contains an anionic, water-soluble group, for example a carboxy, sulpho or sulphate group. Examples of compounds that fall within-. for this definition are: 3-(N,N-dimethyl-N-hexadecyl-ammonio)-•2-hydroxypropane-1-sulfonate, 3-(N,N-dimethyl-N-hexadecylammonio)-propcine-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.hexadecyl-sulfonio)ethane-1-sulfonate, 3-(S-methyl-S-dedecylsulfonio)propionate, 4-(S-methyl-S-tetradecylsulfonio)butyrate, 1-(2-hydroxy -ethyl)2-undecyl-imidazolium-1-acetate, 2-(trimethylammonio)octadecanoate and 3-(N,N-bis-(2iuhydroxyethyl)-N-octadecylammonio)-2-hydroxy-propane-1-sulfonate and 3- (N,N dimethyl-N-1-methyl-alkyl-ammonio)-2-hydroxypropane-1-.sulfonate, in which the alkyl groups contain on average 13.5 - 14.5 carbon atoms. Some of these detergent-active compounds are described in the following US patents 2,129,264, 2,178,353, 2,774,786, 2,813,898 and 2,828,332.

E. Cationic detergents

Cationic, wax-active agents include those of the formula R 6 -N(R 7 )-.An in which R 6 is an alkyl group containing 8 - 20 carbon atoms, each R 7 includes alkyl and alkanol groups containing 1-4 carbon atoms, as well as benzyl groups, as it normally

• 1

is not more than 1 benzyl group and 2 R groups which may be connected by either carbon-carbon ether or amino bonds to form a ring structure, and An represents a halogen atom,

a sulfate group, nitrate group or other pseudohalogen group.

Specific examples are alkyltrimethylamine chloride, dodecyldimethylbenzylammonium bromide and dodecylmethylmorpholino chloride.

The soap and non-soap anionic, nonionic and zwitterionic detergent surfactants, mentioned above, may be used as the sole surfactant, or the various types may be mixed in the practice of the present invention. Particularly preferred are anionic and non-ionic surfactants. The amount of surface-active agent incorporated in the compositions depends on the intended use thereof; composition. It will thus be related to the weight of the composition as a whole, whether it is applied directly to the skin, for example as a cosmetic liquid, or the concentration at which it will be used as a solution, for example in dishwater or bathwater. In most cases, the content within the range of 0.1 - 90% by weight of the composition is suitable. More particularly, detergent compositions for cleaning purposes will generally contain 5 - 50% by weight of the surfactants, while cosmetic compositions will generally comprise 0.1 - 10% by weight of the surfactants.

The invention is applicable to a number of different compositions which may come into contact with keratin in its normal use, e.g. in liquid dishwashing detergents, skin and face creams, body lotions, hair shampoos, bath compositions, detergent compositions, cleaning compositions for hard surfaces, bar soaps, etc. The physical form of the composition can also vary widely, from granular solids to gels and creams, to viscous or mobile liquid compositions. Detergent compositions are generally a liquid and comprise a mixture of water and foaming detergents. Granular detergent compositions, on the other hand, may contain little or no free water. Cosmetic and related compositions will generally contain a basic composition comprising a mixture of water, emulsifier and oil and the physical composition of these compositions will either be an oil-in-water or water-in-oil emulsion. However, it is also envisaged that cosmetic-like compositions, according to the invention, can be in the form of gels comprising the modified protein and water, optionally containing a preservative such as methyl alcohol. Other cosmetic-like compositions may contain little or no free water, but comprise a mixture of the modified protein, oil and a foaming surfactant. Such compositions are particularly suitable for bathing compositions.

t

The preferred liquid or granular detergent compositions for use, for example, as coarse detergents, dishwashing detergent compositions or shampoos, comprise 5 - 50% by weight of foaming detergent agents. More particularly, the foaming surfactant is selected from:"a. Up to 45% by weight of water-soluble hydrocarbon sulfate of the general formula R 0 (C^H^O^SO^M wherein R"<*>is a straight-chain or branched saturated or unsaturated aliphatic hydrocarbon group with 8-24 carbon atoms, or a ^benzene group substituted with an aliphatic, straight-chain or branched hydrocarbon with 8-18 carbon atoms,

n is 1 - 12, and M is an alkali metal, ammonium, dimethyl, trimethyl, triethyl, dimethanol, diethanol, trimethanol and triethanol ammonium salt,

b. up to 45% by weight of a water-soluble hydrocarbon sulfonate 2

of the general formula R SO^M,

c. up to 45% by weight of a water-soluble hydrocarbon sulfate of the general formula R<2>OSO^M, d. up to 40% by weight of an ammonium, monoethanol and diethanolamides of a fatty acid with an aryl group of 8-18 carbon atoms ,

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

Another compound which can be included in the compositions according to the present invention is a water-soluble buffer material. The purpose of the buffer is to establish a pH range which optimizes the conditioning efficiency of these compositions.

In the event that the compositions comprise a precursor protein, the buffer establishes the necessary pH condition, namely that the pH of the aqueous solution or dispersion of the composition at the use concentration is less than (pl - o.7). When the protein has a pl of up to pH 8, for example type B gelatin, the optimum pH range for use is 5.5-7 and this necessitates the use of a weakly acidic buffer material. Suitable acidic buffers can be chosen from vinegar, lemon, malic, gluconic, maleic, lactic, tartaric, propionic, butyric, malic, polymaleic, polyitaconic, gluar, citroaconic, benzenepentacarboxylic and hexacarboxylic acids, succinic acid, ethylenediaminetetraacetic acid and nitrileacetic acid, and weakly acidic salts thereof. When the protein has a pl greater than approx. pH 9 is the optimal application pH range approx. 7 or higher and this may necessitate the use of basic buffer materials. These can be selected from the basic salts of the above-mentioned organic acids, or from the more traditional inorganic buffer materials such as alkali metal phosphates, polyphosphates, carbonates, silicates and borates. Acidic buffer materials are generally used in a ratio of up to 15% by weight, preferably up to 5% by weight of the composition. Alkaline buffer materials can be used in an amount of up to 40% by weight in a granular detergent composition or up to 5% by weight in a liquid detergent composition.

The liquid detergent or gel compositions according to the present invention generally comprise a carrier based on

water and/or water-soluble solvents. Suitable solvents include c2_q monohydric and dihydric alcohols, for example ethanol, butanol, methyl, 1-methylpropanol and 2-methylpropanol, amylol or pentaol, butanediol, toluene, benzyl carbynol, ethylene glycol, monobutyl ether, propylene glycol propyl ether, diethylene glycol dimethyl ether. These are generally present in amounts of up to 15% by weight of the composition. Additional components in liquid detergent compositions include foam enhancers such as higher alkylamine oxides and alkylolamides of C 10 -C 14 carboxylic acids, thickeners, preservatives, opacity promoters, perfumes, colors.

fluorescence promoters, corrosion inhibitors, bactericides, hydrophobic oily material and hydrotropes.

Commonly used hydrotropes conventionally include lower alkyl arylsulfonates such as sodium and potassium toluenesulfonate* xylenesulfonate, benzenesulfonate and cumenesulfonate. 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 invention include animal, vegetable and mineral oils, as well as waxes such as beeswax, spermacet 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, laolin and cholesterol derivatives, as well as silicone oils.

The compositions according to the present invention, especially cosmetic creams and lotions can also include components suitable for promoting the moisturizing efficiency of the compositions.

Suitable components include lower aliphatic alcohols

with 2-6 carbon atoms and with 2-3 hydroxy groups, for example 1,4 butanediol, 1,2-propylene glycol and_glycerol.

Other suitable components include urea or urea derivatives, such as guanidine, pyrrolidone or allantoin.

Solid, granular detergent compositions may also contain suds enhancers, suds suppressors, bleaching agents, anti-fouling agents, enzymes, enzyme and bleach activators, fluorescent agents, building salts and other components normally found in granular detergent compositions. Solid compositions in stick form can also contain additives such as fatty acids, salts, skin creams and oil.

Oxyalkylation of proteins.

The following procedure is typical of the methods that can be used for oxyalkylation of proteins. In the present case, the method is described with reference to the oxybutylation of gelatin. Gelatin (lo g), derived by basic hydrolysis, with a molecular weight of approx. 80,000 and isoionic pH of 5.35 was dissolved in water (500 ml) and the solution pH was adjusted to 7.5 with a sodium hydroxide solution. The solution was heated with stirring to a constant temperature of 27°C and but-1-ene oxide (65 ml) was added. The reaction was allowed to proceed for 26 hours during which time the pH was kept below 8.0 by the addition of sulfuric acid. At the end of this period, the isoionic pH of the hydroxybutylated gelatin was measured by mixed-site ion exchange to be 7.8. After evaporation of excess but-1-ene oxide, the solution was slowly dialyzed for 6 hours to remove salt and low molecular weight material and the modified gelatin was finally obtained by freeze drying. The product was washed with 1:1 methanol/ether, followed by ether and then dried to dryness. The hydroxybutylated gelatin had an intrinsic viscosity (measured in a 4.5 pH buffer solution comprising sodium chloride (0.15 mol), sodium acetate (0.1 mol)

and acetic acid (o.l mol)) of o.3ol, which, using the empirical ratio according to Staudinger and the values for the constants K and a according to Bello, Bello and Vinograd, corresponds to an average molecular weight of 73.ooo. The esterification percentage of the gelatin, measured by titration, was 43% and the percentage N-alkylation was 61%,

measured by Van Slyke's determination of primary amino groups.

The method given above, or variants thereof, can be used for . to produce modified gelatins by different substituents and physical properties. E.g. by holding

The pH of the reaction medium in the acidic range decreases the degree of N-hydroxyalkylation, which takes place during the reaction. Modified gelatins with higher molecular weight can be prepared using starting methods with correspondingly higher molecular weight. Ethylene or propylene oxide can be used instead of but-1-ene oxide to give the corresponding oxyalkylated derivatives. Other protein types can be used in a similar way instead of gelatin derived by basic hydrolysis, for example gelatin derived by acid hydrolysis, or proteins such as casein, gliadin, soybean protein, zein and serum or egg white. Other processes can also be used to obtain oxyalkylated derivatives, for example by reaction with anhydrous alkylene carbonates.

Protein esterinq

Protein derivatives in which only the carboxylate group has been modified can be produced according to the following procedure: Gelatin (log) with a gel strength of approx. 14o "Bloom g", isoionic point of approx. 5.3 and ground to 60mesh size was stirred at room temperature in a 0.036 N sulfuric acid solution consisting of concentrated sulfuric acid (1.76 g) in abs. methanol (l.ooo ml). After a delay of approx. After 20 hours with frequent shaking, the methanolic solution was decanted from the solid, which was washed with methanol, followed by ether and then dried in a desiccator at a pressure of o.1 mmHg. Acidic residues were removed from the product by stirring the gelatin with a quantity of water corresponding to 10 times the weight of the gelatin, while adding 5 N sodium hydroxide until a pH value of 6 was reached. The swollen granules were melted at 40°C to give a clear liquid which formed a gel at 4°C and which was dried in an air stream. Salts of low molecular weight were removed from the product by autodialysis, after which the product was dried as indicated previously.

The isoionic pH value of the methyl ester derivative of gelatin, measured by mixed ion exchange layer, was 7.8. Its intrinsic viscosity, measured in a buffer solution at pH 4.5, was 0.31, corresponding to an average molecular weight of 7o.ooo. The percentage methyl esterin was 44%.

Aminealkylamide derivatives of proteins.

Protein derivatives with high isoionic pH values can, for example, be prepared by modifying the protein's carboxylic acid groups to carboxylic acid aminoalkylamide groups in the following way: A solution of N,N-dimethylethyldiamine (10 ml) in water (80 ml) was prepared and the pH of the reading adjusted to 4.5 with sulfuric acid . Gelatin (2 g) with a gel strength of approx. 24o "Bloom" g was added along with N-cyclohexyl-N-(2-(4-B-morpholinyl)-ethyl)-carbodiimidemethyl-p-toluenesulfonate (4 g). The solution's pH value was adjusted to 4.8 and the solution was allowed to stand at approx. 25°C for 6.5 hours, after which the solution was diluted with water and

dialyzed slowly for approx. 14 hours, during which time the pH

rose to 7.5. Finally, the product was isolated by freeze drying followed by vacuum drying in a desiccator. The 2-(N,N-dimethylamino)-ethyl-amide derivative of the gelatin had the following properties:

Skin conditioning ionization trial

The conditioning effect was measured by both in-vitro and in-vivo tests and a high degree of correlation between the two test methods was found. The in-vitro test (referred to as calfskin resealing test) was based on the rate of water transpiration through a calfskin sample brought into contact with a 0.15% aqueous solution of the detergent composition (at 18° hardness) containing the protein. The sealing ability of the protein was measured by the reduction of the water transpiration rate of the proteinaceous surfactant solution compared to that of water. The in vivo experiment was a hand immersion test (HIT). This sample was based on 16 people (32 hands) per product in a multi-product sample, where the hands were balanced for the right hand/left hand difference, so that 32 hands were used per product, namely 16 right and 16 left. Each person dipped their right and left hands in different solutions for three consecutive lo min. periods of half an hour per day, for three weeks, five days per week. The treatment solutions were renewed every ten minutes. The hands were pulled up and down in the solution every two minutes.

On Monday at the beginning of the experiment, the hands were graded.. ( for immersion, and every Friday after the experiment. The hands were graded according to an o-lo (perfect) scale for the overall condition of the hand,

according to an o - lo (poor) skin peeling scale and according to an o - lo (perfect) nail grading scale. HIT ratings for protein/surfactant solutions were determined and reproduced therein

subsequently, on a scale in which a o.15% aqueous solution of the surfactant for standard II (see Table V) was given the HIT rating o, and a 1 mg/cm 2 application of a hand lotion was given the HIT rating loo .

EXAMPLES I - XIII

A number of oxybutylated gelatins, prepared by the previously described methods, were compared to provide the conditioning benefits of aqueous surfactant solutions.

The modified proteins were prepared with varying molecular weights, isoionic points, degrees of O-alkylation, N-alkylation etc. They were then incorporated into the various liquid detergent compositions according to examples I - XIII indicated in table

V.

Examples I - IV show the effect (see Table I) on the conditioning effect by changing the molecular weight of the oxybutylated gelatins. It can be seen that oxybutylated gelatins with molecular weights in the range 5ooo-2oo.ooo are all effective in that they provide conditioning benefits from aqueous, surface-active solutions, but that these are most beneficial for modified proteins in the high molecular weight range, i.e. over approx. 2o.ooo. However, lower molecular weight proteins exhibit

ie 5ooo or even less is still a useful conditioning level.

Examples VI - IX show the effect of changing the protein's isoionic pH value on the conditioning effect at a constant application pH value on the skin (nil 7). It can be seen that the conditioning effect is very sensitive to the modified proteins' isoionic pH value (pI), in that modified proteins with a pI above 8 and preferably above 8.5 are most effective for a given molecular weight value.

It can be seen that the effect diminishes to a certain extent for pl values on the pH value.

The effect of the amount of modified protein in the surfactant is shown by comparison between Examples I, X and XI.

The optimal protein level is approx. 4% by weight of the composition and

only minor benefits are achieved by raising the protein level to

5% by weight. however, at an application level of 2% by weight, the conditioning benefits were reduced by over 50%.

The conditioning effect according to examples I, II and III which

a function of pH upon application to keratin is indicated in Table IV. The optimal pH range for the conditioning efficiency obviously lies below the protein's isoionic pH value, as the conditioning efficiency generally decreases for pH values above the isoionic point. Compared to the surfactant control solution (standard II), however, it can be seen that the conditioning benefits are to some extent present even in the higher pH range.

The tp last rows in Table I, Examples XII and XIII demonstrate inclusion of the same modified protein used in Example I in a surfactant solution based on paraffin sulfonate and alkyl ether sulfonate. Although it can be seen that examples XII and XIII are less effective than most previous examples, it is obvious from the calf skin test that the composition according to examples XII and XIII will be milder than the same liquid detergent-active compositions (standard III) not containing modified protein.

Also included in Table I is hand immersion test data for Examples I - III and XI. These data show that modified proteins with a molecular weight greater than 15.ooo and an isoionic pH value greater than 8 are particularly effective with regard to

to protect keratin against damaging effects of detergent composition ions applied to the keratin above pH 7. More particularly, it has been shown that the composition according to Examples I - III from dilute aqueous surfactant solutions provides at least two thirds of the conditioning effect provided by a hand treatment lotion applied directly to the skin surface. Further, the composition of Example I resulted in five,

three-week hand immersion test significantly (95% condensation level) better condition for hands and nails than the composition according to standard II.

A further advantage of the protein-containing compositions shown above is that there is no significant reduction in volume or stability of the foam associated with the detergent composition itself. Furthermore, it has been found that the compositions shown above have excellent storage stability and in fact the surfactant has the effect of increasing the stability of the protein against hydrolysis, at pH-7 by a factor of up to 6 times.

EXAMPLES XIV - XIX

Table II compares the conditioning effect for different modified proteins, incorporated in the surfactant compositions as defined in Table V, it can again be seen that high molecular weight modified proteins with a high isoionic point, according to the present invention, are particularly effective in providing in vitro exclusion benefits from aqueous surfactant solutions.

The conditioning efficiency of the composition of Example XVII as a function of application pH and keratin is

shown in Table IV. This modified protein had a high isoionic pH (about 10.5) and was effective over a wide pH range below the isoionic pH and up to 2 pH units above its isoionic pH. Efficiency decreases for application pH values greater than (pl + 2). Different from most other examples where the conditioning efficiency at pH values below the modified protein's pl value was relatively insensitive to the hardness of the treatment solution, as the composition according to example XVII was somewhat more effective above this pH range in the absence of free water hardness. Thus at pH 9.3 - 9.5 the degree of calfskin sealing was 4.5 at o° hardness but only 1.5 at 18° hardness.

EXE MPLES XX - XXL

Examples XX and XXI, indicated in Table III, were two compositions according to the invention comprising two precursor proteins. The precursor protein according to Example XX was a type A gelatin with an isoionic pH value of 7.7 (corresponding to an isoelectric pH value of 8.4) and a molecular weight of approx. 75.ooo. According to the precursor protein

Example XXI was a synthetic polypeptide polylysine with an isoionic pH value. > 11 and a molecular weight of 7o.ooo and above. The composition comprising precursor proteins has been found to be effective over a pH range to the acidic side of the isoionic pH value for the precursor protein. Thus, a type A gelatin is used at an application pH in the range 5-7. Polylysines can be used at any pH in the range pH 5 - lo.

EXAMPLES XXII - XXVIII

The following examples serve to illustrate liquid detergent compositions according to the present invention. All percentages are percentages by weight.

The compositions shown above have a milder effect on skin and hair than corresponding compositions that do not contain any modified protein and there is essentially no reduction in volume or the stability of the foam obtained with the waxing agent. Essentially similar cleaning and conditioning effects are obtained when the modified protein in the examples shown above is replaced with the oxybutylated product of casein, which was purified using the Hammarsten method, and where the modified casein had a pI value of 8 .8, % O-alkylated side chains were

4o% and % N-alkylated side chains was 61%.

A substantially similar cleaning and conditioning effect is obtained when the modified protein is replaced with methyl, ethyl, propyl or butyl ester of gelatin with a molecular weight of approx. 80,000 and an isoionic pH in the range 8-9.5.

EXAMPLES XXXIV - XXXVI

Liquid detergent compositions suitable as shampoos or dishwashing detergents had the following compositions

Gelatin : Type A isoionic pH 7.8, molecular weight 80,000.

All the compositions shown above gave a pH in the range 5-7 when diluted with water. At a use concentration of o.2%, they gave a pH of approx. 6.

EXAMPLE X XXVIII

A foaming oil bath with foaming and skin conditioning properties had the following composition.

EXAMPLE XXXVIII

A bar soap composition which is gentle on the skin had the following composition.

EXAMPLE EL XXXIX

A moisturizing skin cream had the following composition

Modified gelatin: the hydroxypropyl derivative with a molecular weight of 80,000, isoinic pH 9.2, % O-alkylated side chains 35, % N-alkylated side chains 61.

EXAMPLE XL

A protein-containing hair cleansing cream had the following composition

"Tegamine S 13" is a dialkylaminoalkyl stearamide (Goldschmidt Chemical Company). Modified casein: oxybutyl derivative with an isoionic pH 8.8, % O-alkylated side chains 4o, % N-alkylated side chains 61. E XAMPLE XLI■ A face and hand cosmetic gel had the following composition

Modified gelatin: the oxybutyl derivative, isoinic pH 9.6, molecular weight 15.ooo, % O-alkylated side chains 24, % N-alkylated side chains 43.

Claims (1)

1. Composition for protecting keratin-containing materials from the damaging effects of detergents and other sharp materials, as well as harsh climate conditions, characterized in that the composition comprises an effective amount of a modified protein, with a molecular weight greater than 5ooo and an isoionic pH -value greater than 6, as the modified protein is incorporated into a compatible carrier which further comprises a surface-active agent or a cosmetic base material. 2. Composition according to claim 1, characterized in that the modified protein comprises functional types obtained as a result of the modification and selected from one or more of: -C-W-Q, -N-X-Q, -O-Y-Q, S-Z-Q, in which C, N, O and S respectively represent carbon, nitrogen, oxygen and sulphur, -Z- represents a direct bond or a carbonyl group, -Y- represents -Z-, sulfonyl or phosphonyl groups, -X- represents -Y- or C=NR -groups, -W- represents -X-, -NX-, -OY- or -SZ groups, and Q represents -R1-, -SR1, -OR <1> , -NR2, -& R2' -NR3 wherein R represents a . hydrogen atom or -R1 in which R comprises one or more alkyl, alkenyl, aryl, cycloalkyl or heterocyclic groups, wherein the alkyl or alkenyl groups are optionally interrupted by heterogeneous atoms or functional groups which cause colour, fluorescence etc. and which are optionally substituted with groups selected from Q and WQ, and in which R does not contain more than 20 contiguous carbon atoms in alkyl - or the alkenyl groups. 3. Composition according to NOK of 2, characterized in that R1 has the formula: wherein Q is a hydrogen atom or Q, p is 0 or 1 and q has the value o - (5-p).. 4. Composition according to claim 2 or 3, characterized in that R comprises up to 8 carbon atoms and up to 2 heteroatoms. 5. Composition according to claims 2-4, characterized in that R1 has the formula where r is 0 - 6. 6. Composition according to claims 2-4, characterized in that R1 has the formula where r* is 0 - 7. 7. Composition according to requirements 2-4, character sert v-: é d' that R <1> has the formula where r is 1 - 4 and s and t are 0 - 3. 8. Composition according to claims 1-7, characterized in that the modified protein has an average molecular weight greater than lo.ooo. 9. Composition- -• according to claims 1-8, characterized in that the modified protein has an average molecular weight greater than 15.ooo. I laughed. Composition according to claims 1-9, characterized in that the modified protein has an average molecular weight in the range 2o.ooo - 2oo.ooo. 11. Composition according to claims 1 - 1, characterized in that the precursor protein is gelatin, casein or soybean protein. 12. Composition according to claim 11, characterized in that the precursor protein is type B gelatin. 13. Composition according to claims 1-12, characterized in that at least 5o% of the average molecular weight of the modified protein is derived from the precursor protein. 14. Composition according to kcav 13, characterized , Note that 80 - 99% of the average molecular weight of the modified protein is derived from the precursor protein. 15. Composition according to claim 14, characterized in that 90 - 96% of the average molecular weight thereof. modified protein is derived from the precursor protein. 16. Composition according to claims 1 - 15, characterized in that at least one of the functional types of the modified protein is obtained by modifying a precursor protein side chain comprising carboxylic acid groups. 17. Composition according to claim 16, characterized in that WQ represents 18. Composition according to claim 17, characterized in that R<1> has the formula according to claim 5 and that the modified protein is obtained by oxyalkylation of the protein precursor with an alk-1-ene oxide. i19. Composition according to claim 18, characterized in that the alk-1-ene oxide is but-1-ene oxide. 20 . Composition according to claim 17, characterized in that R <1> has the formula according to claim 6 and the modified protein is obtained by esterification of the precursor protein with a primary alcohol. 21. Composition according to claim 16, characterized in that WQ represents 0, , . CNHR 22. Composition according to claim 21, characterized in that R<1> has the formula according to claim 7 and that the modified protein is obtained by amidation of the precursor protein with an alkylenediamine. 23. Composition according to claims 1-23, characterized in that at least one of the functional types of the modified protein is obtained by modification of precursor protein side chains comprising basic groups. 24. Composition according to claim 23, characterized in that the basic groups are primary amino groups. ; 25. Composition according to claim 23 or 24, characterized in that XQ represents -R<1>. 26. Composition according to requirement 23, grade! cert in that R <1> has the formula according to claim 5 and that the modified . protein is obtained by oxyalkylation of the precursor protein with an alk-1-ene oxide. 27. Composition according to claim 23, characterized in that R <1> has the formula according to claim 6 or 7 and that the modified protein is obtained by alkylation with R <1-> halogen. 28. Composition according to claims 1-27, characterized in that the modified protein has an isoionic point greater than pH 7.2. in 29. Composition according to claim 28, characterized in that the modified protein has an isoionic point greater than pH 8.0. 30 . Composition according to claims 1 - 29, characterized in that at least 5% of the acid side chains of the precursor protein are modified. 31. Composition according to claim 3o, characterized in that at least 2o% of the free acid side chains of the precursor protein are modified. 32. Composition according to claims 1 - 31, characterized in that the modified protein has a free basic side chain content, measured by titration against nitric acid solution, greater than the equivalent of o.1 mmol of acid per g. modified' protein. 33. Composition according to claims 1 - 32, characterized in that the modified protein has a free basic side chain content greater than the equivalent of o.5 mmol of acid per g modified protein. 34. Composition according to claim 33, characterized in that the modified protein has a free basic side chain greater than the equivalent of 0.8 mmol of acid per g modified protein. 35. Composition according to claims 1 - 34, characterized in that the modified protein has a free acid side chain content, measured by titration against sodium hydroxide solution, less than the equivalent of 1.5 mmol sodium hydroxide per g modified protein. 36. Composition according to claim 35, characterized in that the modified protein has a free acid side chain content less than the equivalent of 1.1 mmol of sodium hydroxide per g modified protein. 1 '37. Composition according to claim 36, characterized in that the modified protein has a free acid side chain content less than the equivalent of 0.8 mmol of sodium hydroxide per g. modified protein. 38. Composition according to claims 1-37, characterized in that the modified protein has a higher isoionic pH than the precursor protein. 39. Composition according to claims 1 - 38, characterized in that the modified protein is more hydrophobic than the precursor protein. 40 . Composition according to claims 1 - 39, characterized in that the pH of the composition or of an aqueous solution or dispersion of the composition in use concentration is less than (pI +2), where pI is the isoinic pH of the modified protein. 41. Composition according to claim 4o, characterized in that the modified protein has an isoionic point greater than pH 8.o. 42. Composition according to claim 4o, characterized in that the pH for. the composition or for an aqueous solution or dispersion of the composition in use concentration is less than (pl + o.5). 43. Composition according to claim 4o, characterized in that the pH of the composition or of an aqueous solution or dispersion of the composition in use concentration is less than (pl - o.7). 44. Composition according to claim 4o, characterized in that the pH of the composition or of an aqueous solution or dispersion of the composition in use concentration is less than (pl - 1.4). IN !45. Composition according to claims 1 - 44, characterized in that the pH of the composition or of an aqueous solution or dispersion of the composition in use concentration is approx. 7. 46. Composition for protecting keratin material from the damaging effects of detergents or other sharp materials as well as harsh climate conditions, characterized in that the composition comprises a liquid carrier that incorporates a foaming detergent and an effective amount of a natural, derived synthetic or biosynthetic proteinaceous material, said proteinaceous material has an average molecular weight greater than 5.ooo and an isoionic point greater than pH 6, the pH of the composition or of an aqueous solution or dispersion of the composition in use concentration is less than (pl - o.7) in which pl is the isoionic pH of the proteinaceous material. 47. Composition according to claim 46, characterized in that the pH of the composition-; or for an aqueous solution. or dispersion of the proteinaceous material in the use concentration traspn is less than (pl -1.4). 48. Composition according to claims 46 or 47, characterized in that it contains a buffer material such that the pH of the composition or of an aqueous solution or dispersion of the proteinaceous material in use concentration is between 5.5 and 6.9. 49. Composition according to claims 46 - 48, characterized in that the proteinaceous material has an average molecular weight greater than lo.ooo. 50 . Composition according to claim 49, characterized in that the proteinaceous material has an average molecular weight greater than 15.ooo. 51. Composition according to claims 46 - 5o, characterized in that the proteinaceous material is a type A gelatin which has an average molecular weight between 2o.ooo and 2oo.ooo. 52. Composition according to claims 46-5o, characterized in that the proteinaceous material is a synthetic polyamino acid. 53. Composition according to claims 1 - 52, characterized in that it comprises up to 5% by weight of modified, natural, derived, synthetic or biosynthetic proteinaceous material. 54. Composition according to claim 53, characterized in that it comprises between 1 - 10% by weight of the said proteinaceous material. 55. Composition according to claim 54, characterized in that it comprises between 2-6% by weight of the said proteinaceous material. 56. Composition according to claims 1 - 55, characterized in that it comprises between 0.1 - 90% by weight of surfactant.. 57. Composition according to claims 1 - 56, characterized in that the surface-active agent comprises an anionic or non-ionic, synthetic detergent active agent or a salt of a higher fatty acid. 58. Composition according to claims 1-57, characterized in that it is in the form of a liquid or gel in which the carrier comprises water and/or a water-soluble solvent. 59. Composition according to claim 58, characterized in that the solvent is a lower alkanol. 60 . Composition according to claims 1 - 59, characterized in that it further comprises a water-insoluble oil material.