DE2434063A1 - COMPOSITION FOR THE PROTECTION OF KERATINIC MATERIAL - Google Patents

Description

The present invention relates to compositions the keratinous material, such as skin or hair, against the harmful effects of detergents or others sharp materials, such as solvents, etc., and against adverse ones protect climatic conditions.

■ r "

The compositions according to the invention accordingly provide help to keep keratinous materials in good condition. The invention also relates to a Method of treating keratin.

The adverse effects of surfactants compositions containing keratin are known. These effects are believed to be caused by that the surfactant is in the keratin surface penetrates, which leads to leaching of oils and moisturizing components / which for good condition of keratin are borrowed. This surface penetration

409886/145 «!

active agent and essential oil leaching also the ability of keratin, especially in the case of skin, to retain water in the tissue and thereby arise again a bad condition of the keratinous material.

Many attempts have been made to create compositions which improve the condition of the skin and hair. The use of protein in skin and hair as a cosmetic treatment is probably \ older than recorded history. Casein in the form of milk 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 having a gel strength of full bloom grams in detergent compositions and lotions for use on the skin, as dishwashing liquids, etc.

DT-OS Kr. 2 151 759 and Kr. 2 151 74-0 describe certain fat derivatives of aminolysates of low molecular weight which are suitable for use in shampoos. In the GB-FS Kr. 1,122,076 the production of alcohol-soluble Described low molecular weight protein esters suitable for use in hairspray approaches, are. Various low molecular weight polypeptides or modified polypeptides are commercially available as well are recommended for use in cosmetic and shampoo formulations, e.g. Hydro Pro 220, Hydro Pro 530, Maypon 4C (marketed by Stepan Chemical Company); Wilson X250, Wilson X1000 and Wilson Aqua Pro {manufactured by V / iIson Chemical Company on the Market). It was found that none these compositions for the protection of keratin against the Effect of harsh detergents is particularly effective, and this is particularly true when the proteins of the section composition are incorporated into themselves. The soften-

409886 / U51

de effect of these compositions can often through. Encore can be improved by greasy or oily materials, but this results in 'use in dishwashing liquids to a loss of foam power or to aesthetic changes, which are generally considered by the consumer be viewed undesirably.

The present invention therefore provides protein-containing compositions which are particularly suitable for the protection of keratinous materials, such as skin or hair, against the harmful effects of detergents and others sharp materials, as well as against adverse climatic conditions are effective, which exert their effect even when applied to keratin in foaming detergent solutions and which do not result in any loss of foam or detergency in detergent solutions containing them.

According to one aspect of the present invention, a composition for protecting contains keratinous material an effective amount of a modified protein against the harmful effects of detergents and other harsh environments, as defined below, which has a molecular weight of "more than pOOO and a pH value of isoionic Point greater than 6, wherein the modified protein is incorporated into a compatible carrier that additionally contains a surfactant or cosmetic base.

In the context of the present invention, a modified Protein refers to a product that, unlike a derived protein, occurs in one or more stages is obtained by chemical or biological modification of a precursor protein, "where a precursor protein non-enzymatic «s protein, which is among natural derived, synthetic or biosynthetic proteins is selected, and a derived protein is the product of the

4098867 UB 1

hydrolytic, ammoniolytic, enzymatic ^ η or thermal Degradation of a protein material is.

In another aspect of the invention, a composition for protecting keratinous material against the deleterious effects of "detergents and other harsh environments" contains an effective amount of a precursor protein as defined above which has an average molecular weight of more than 50000 and "egg" The pH value of the "isöiönlschen" point (also sometimes referred to as "pT'b'ezeiciine't) has more than 6," whereby the ir'ec'ursorprbt'ein 'is incorporated into a compatible carrier i 'st ühd "zusäifziich a"schäumenies' detergent '' includes, ^, and ^'r of pH'ier't ■' ^ the total weight ämmense estimation "öäer" a "aqueous Losling"o'der dispersion of the composition at Gebrauchskon-

ch ^a; ¥¥ n ^ m ^ ifeeien ^ iliikt ^£ de ^: r ^! ° E

rustic-Hrorr Üeterg Films ¹ and ^: ~ others ^; ~ schäife'S 'Wati'Sriaixen ""'

Overriding ¹ and ^: ~ other ^; ~ schäife'S 'Wati'Sriaixen made available which procedure essentially "* consists in keratin with a composition or with' e * i'n ^; er ^: watery-eii 'iosiing" - or' dispers ioi! "oTi

The preferred teodi ^ i ^ z-r & rtgn proteins "for use the compositions and the method according to the above

which as a result

are selected from one or more of the following: - '''ioyanaIiioS 8 v-.La ii ^^ Udo in. H bil * n & ü lessen L i &

-Z- means a direct bond -Y- means -Z-, sulfonyl or phosphonyl groups,

b-Ji- .ieuuebed \\ sxd O ■ - ί fixiov? _f H-_. _T (^ HO) - ^ HD = S

~ ⁴ "^ ORIGINAL" INSPECTED

U 0 9 8 8 6 / UB Ϊ ^C "■

-W- stands for -X-, -NX-, -OY- "or -SZ groups and · Q represents

111 θ e

-R, -SR, -OR, -KR ₂ , -SR ₂ , -NR ₃ , wherein

1 R denotes a hydrogen atom or -R and in which

R one or more alkyl, alkenyl, aryl, cycloalkyl or Heterocyclyl radicals, the alkyl or alkenyl radicals optionally being replaced by heteroatoms or functional residues, such as dyes,. Fluorescent substances, etc., interrupted and if desired by residues Q. 'or WQ are interrupted, • where R does not contain more than 20 interconnected carbon has atoms in the alkyl or alkenyl radical.

In a given modified protein, these groupings need not all be identical. Also can the different R groups may be the same or different.

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

GH ₂ - (CHQ ¹ ) _p - (GH ₂ ) _q -YQ ¹

where Q is a hydrogen atom or Q is ρ for 0 or 1 and q symbolizes 0 to (5-p).

In general, R will contain no more than 8 carbon atoms and up to 2 heteroatoms, which can be the same or different. Preferred classes of modified protein falling under the above definitions are those in which _r R is denoted by; , "

1. CH ₂ -CH 0H- (CH ₂ ) _r -H, where r = 0 to 6,

2. CH ₂ - (CH ₂ ) _r -H, where r = 0 to 7, and

409886/1451.

(CHp) -H
3 · (CH ₂ ) 3 ^-ii C 'where r = 1 to 4 and

( ^C3s 2 ^ t ~ ^H s and t stand for 0 to 3, is represented.

Protein modification can be carried out using the normal methods used in the preparation of proteins with functional substituents. In general, the reactive centers at 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 (xuanidino groups, or which contain a reactive aromatic ring A preferred modified protein has as substituents carboxylic acid ester or amide groups which are derived from the carboxylic acid groups of the unmodified substrate. The ester can be derived from the protein and the corresponding alcohol by suspending the protein in the anhydrous alcohol at a temperature between '' See 0 and 25 C and at an acid concentration of 0.02 to 0.10 molar for several days. Alternatively, hydroxyalkyl esters can be prepared by reacting the protein with an epoxide, for example 1-butene oxide 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 at the same time lead to ° / ^ζ 3.® ^Γ Ψο% phenolic groups of the tyrosine or sulfhydryl groups of the cyste in, whereby O-arylisoureas or SA lkyli-thioureas are obtained.

According to another embodiment of the invention can the proteins via amino, hydroxy or sulfhydryl groups. acylated or alkylated. Acylation can take place under Use of the appropriate acid anhydride or li-carboxy

409886/1461.

anhydrides are effected. In the latter case it leads ^; this leads to acylation which mainly attacks amino groups. In the former case, the modification results if the acid ^anhydride: is cyclic to acidic substituent, - which are to be neutralized, for example by esterification. " Reactions analogous to acylation can also be carried out. So'können e-Aminogrüppen 'a Behändlung selectively a & al replaced by the more basic of proteins ^{Öuanidinogruppen:} is made with east-llkylisöharnstoff or S-urea. '■ " ^: ■ - '

Sulfate esters or sulfonamide derivatives of- 'P can be prepared, for example, by reacting the hydroxyl or amino groups of the protein with sulfonyl halides ^; ■ 'are provided. These modified proteins können.wieder used to obtain further modifications by cleavage of the 'alkyl / Sauerstörf-Siiidttng of suif onats, "AuIL- be .. Thus, by X könnenifereispielsweise- hydroxy groups: ./ i. S-alkyl groups'-ers-etiffi ^ be. ^ir e ^:: ■ -..--. · ....-:;. - ■; ', b & u O Λβχί;

"'- ■ -" · "■■''' = ■■ JI '-'ίίτ θ '"-Γ-'λ". · ■. ·" ·: Ί - "ΤΓ: ν._. J. ; ...... ■ - "' ^: "'" ^: '-.:r\iOi:I~Gf ^v O ■': i

To the. Education · -alky / läLeiFter ·: odercafy ^ ier.teni ^ otoejimejisMhen also other ¥ eJge ^; z ^ r -: ^ iriügungv - SoikSnnHeinel: S ^ db3, ^ yMs ^ j or N-Alkylation vomc SuLfhydry3f-Moder- -Amilnegr ^ ppeA. nucleophthia: Substituita-on;. bei ^ aalogenae & ta £ en-ry; .0o acetamides or through-AdditiOnf)
bindings, for example
or with one. Imidogratppe ','^; like ^; · Ϊιϊ]
are to be effected. Ε ^: ίη ^: ν.Κτ ^
Sodium borohydride reduction can be derived from the condensation of proteinamine groups with aldehydes or ketones. An arylation of sulfhydryl, amino, or hydroxyl groups at ^ 4U, H9- &, phile. Substitution of halogen,
fourth ha, logenbenz.olderivaten

"^; .. · .-. - - \: 'y.. ■■ - ■. ■ ■■■ -ivine ae.5 ^ The proteins of the compositions according to the invention

- 7 -

S f \

/ V4

ο pr. ORIGINAL jNSPECTEO

can be modified in numerous other ways. For example, proteins are responsible for electrophilic substitution reactions sensitive and thus allow the modification of Cysteines to cystines by reaction with a Joldonor and then by an alkyl mercaptan. The substitution of the aromatic ring of tyrosine by nitro groups using tetranitromethane as a nitrating agent or by pi azoniutn.gr up pe η is also possible. Also can the guanidino groups of arginine by reaction with 1,2-dicarbonyl derivatives, v / ie cyclohexanedione or phenyl glyoxal, be modified.

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

Typical natural proteins include intracellular proteins and globular proteins, v / ie those found in blood plasma and are present in milk. Derived proteins can be obtained from many sources, for example through hydrolytic, ammoniolytic, thermal or enzymatisc'hen Breakdown of globular or structural proteins, such as keratin, collagen, fibrinogen, myosin, whey egg, casein or vegetable proteins, v / ie those obtained from cereals.

(soybean curd)

de, low-soybean silag / or the residues submitted for samples can be obtained from seed oil production. A particularly suitable derived protein is gelatin, which the product the (usually acid or base catalyzed) hydrolysis of collagen from skin or bones and which can have an average molecular weight ranging from 5000 to 200,000 and even higher varied. Other highly useful precursor proteins include whole casein and soybean protein; synthetic proteins, v / ie polylysine, and proteins, obtained from unicellular microorganisms such as bacteria. Jens precursor proteins, the pH-V. "Erte of the iso-

- 8 4 0 9 8 8 6 / U 5 1 ^C0PY

Ionic point, holier than 6 cry, are also for the immediate use, i.e. without modification, in certain compositions according to the invention suitable. In particular such precursor proteins contain acidic hydrolysis products of, for example, collagen. These contain the so-called type Λ gelatins. Other suitable samples include

"from micro-

sen polyamino acids, such as polylysine and certain / unicellular /

received ^. ^ _n . · Ν. · -Ι '-u -ι ι _r7

orgiomenx proteins. In general, however, si.ch has such compositions according to the invention, which contain precursor proteins, proven considerably less effective than compositions which contain modified probeins. The latter become therefore highly preferred. Particularly preferred proteins for use in the compositions according to of the invention have characteristic values of molecular weight and pH word of the isoionic point and these become explained in more detail below.

The molecules of a protein vary greatly in terms of size The size and complexity and the molecular weight of a protein is therefore inevitably only inaccurate Measure. The molecular weight of a protein can be specified by defining the molecular weight distribution of the protein molecule , however, it is customary to indicate the average molecular weight of the protein sample in its place, 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 measured average molecular weight vary from one measuring method to another. Usually, so-called, the numerical value averaged molecule ar ge v / ich te by measurement the osmotic pressure, the diffusion speeds usv /. get- while averaged in terms of weight Molakulargev.'ichbe examplev / eir-e by ultracentrifuge testicles be goin. Within the scope of the present invention becomes average for determination in general

- 9 409886 / U5 1

COPY

Protein molecular weights applied method, from viscose

Protein measurements of buffered \ solutions are used. the

Intrinsic viscosity of a buffered protein

As is well known, the solution is primarily based on the overall length

(coil)
of the protein wad / dependent and relatively independent of the type of side chains and end groups of the protein. There is therefore a relationship between intrinsic viscosity and mean molecular weight, M, of the protein, which can be expressed as follows according to the Staudinger equation

= KM ^a ,

where K and a for a specific protein source, e.g. for gelatin derived from calf skin (see Macromolecular Chemistry of Gelatin, page? 2, by A. Veiss), are constants. The inherent viscosity is the reduced specific viscosity at infinite dilution of the protein solution and is measured in terms of the actual, in a viscometer Viscosities defined as follows:

measured viscosity of the protein

Relative viscosity K ₁ - = ^ J ^ S ^^^^ JäSWL ·, - ^ _

measured viscosity of the buffered solution

Specific viscosity i \ sp = \\ ^^ -1

Reduced specific viscosity = - £

Concentration (c) of the protein solution

Inherent viscosity -

c> ο

The constants K and a used in determining molecular weights modified from calf skin

- 10 -

409886 / UE1

Gelatin can be used. v / earth as follows (according to J. Bello, H.E. Bello and J.R. Vinograd, Biochiraxca Et Biophysica.Acta, 57, 222-229; 1962) used:

K = 2.9 χ 10 " ⁴ a = 0.62 .

The precursor and modified proteins as used according to the present invention have molecular weights of more than 300 and suitably more than 2000, and more suitably more than 500C. In particular, should whose molecular weights are preferably more than about 10,000, more preferably more than 15-000, and im generally they will range from 20,000 to 200,000.

In connection with the total molecular weight of the modified protein, it is preferred that at least the larger fraction originates 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 are both acidic and basic Have side chains are charged in both acidic and basic solutions and are therefore of amphoteric nature. The number of such acidic and basic residues in a protein molecule can be determined by titration with a monobasic, strong Acid (e.g. dilute nitric acid) or base (e.g. I sodium hydroxide solution) are measured and the results are recorded zv; e ckmä ßi gerweise in mmol / g, where it is the number of millimoles of acid or base that is required are to neutralize 1 g of the protein, Modified proteins of the type used in the invention have one Content of basic side chains, which is preferably greater than 0.1 mmol / g, in particular greater than 0.5 mmol / g and

- 11 -

409886 / U51

moderately greater than 0.8 mmol / g. You have a salary on acidic side chains, which is preferably less than 1.5 mmol / g, especially less than 1.1 mmol / g, and desirably is less than 0.8 mmol / g.

The modified proteins according to the invention are used, preferably have proportionally fewer anionic side chains and more non-polar or cationic Side chains as 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 ρΗτ value of the isoionic Point, the pH value at which the same concentrations of protein anions and cations exist in solution.

Preferably the modified or precursor proteins for use in the compositions according to According to the invention, an isoionic point pH of greater than 6.5, especially greater than 7 »2, and desirably greater than 8.0.

The pH of the isoionic point of the above protein can be somewhat different from the pH of the isoelectric point of the protein, although usually the differences are small. The isoelectric point is given by the Anion / cation equilibrium of all ions in the measured sample determined, including weight protein ions; the isoionic point, on the other hand, is determined by the anion / cation equilibrium of the protein ion alone is determined. The pH of the isoionic point can be determined in the following way.

Acid amberlite resin (IR 120) and basic amberlite resin (IR 4-00) are washed with several parts by volume of water, filtered and mixed in a ratio of 0.4: 1. Under minimal A 1 1/2% by weight protein solution (20 ml) is heated

- 12 -

409886/1451

prepared, allowed to cool to constant temperature and treated 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 composition depends to some extent on the in-use pH of the composition, that is, the pH of the carrier when applied to keratin. This in-use pH, depending on the type of application, may be the pH of the composition itself, or the pH of an aqueous solution or dispersion of the composition at a use concentration which can be as low as 0.01 % .

With regard to such compositions containing modified proteins, it is preferred if the pH of the composition or an aqueous solution or dispersion of the composition at use concentration is lower than (pi + 2), where pi is the pH of the isoionic point of the modified protein. More preferably, this in-use pH is less than (pi + 0.5) _5, desirably less than (pi-0.7), and even more desirably less than (pi-1.4). In addition, modified proteins having a pi greater than 9.6 can be used satisfactorily at a pH between (pi + 2) and pi.

In connection with such compositions according to of the invention containing precursor proteins has been indicated above that the pH of the composition or a aqueous solution or dispersion of the composition at use concentration must be less than (pi - 0.7). This use pH is thus preferably less than (pi - 1.4) and generally less than pH 7,

The use pH of the compositions according to Invention may vary depending on the purpose and nature of the

- 13 -

409886 / US1

Uses of the compositions will vary widely. Liquid or creamy compositions intended for shampoos, hand creams or cosmetic lotions are generally applied directly to the skin or hair and the pH in use is the pH of the composition itself. This can be any pH in the range of generally 4 to 9. Detergent compositions such as liquid dishwashing compositions, bath compositions and granular or heavy duty liquid detergents are generally used in a large excess of water and the in-use pH is the pH of an aqueous solution of the composition at a concentration generally in the range of 0. 01 wt .-% to 2 wt -.% is. Unbuilder detergent compositions, used, for example, as liquid mild detergents, will have a in-use pH of about 7; High-performance detergents containing builders generally have a usage pH value in the alkaline range "up to a pH value of about 11. Soap compositions are applied to the skin as an" aqueous solution or dispersion of the ingredients of the soap bar in a concentration that corresponds to generally ranges from 5 to 15 percent by weight. The pH of the soap dispersion can vary, depending on the type of soap bar used, from a pH of 5 »5 to 9 _} 5.

The preferred compositions according to the present invention have a use pH value in the range from 4 to 11, in particular in the range from 5 to 9.5 _7, particularly preferably in the range from 5-5 to 7 * 5. Precursor proteins are generally used liquid detergent compositions in the pH range from 5 »5 to 6.9 incorporated.

The modified proteins according to the present invention are preferably obtained by modifying the protein precursor side chains, the free carboxyl groups or free

- 14- -

409886/1461

-IS-

basic, in particular containing primary amino groups. In particular, the modification of acid groups is preferably done by oxyalkylation and esterification (corresponding to a substitution of ^ _οπ 1 instead of WQ) or amidation (corresponding to the substitution of Amro ^ instead of WQ). On the other hand, the basic groups are preferably modified in the form of alkylation (corresponding to the substitution of -R instead of 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 of 4.5 to 5 »5. N-acylation is therefore preferably not used as a type of modification, unless there is another compensating modification which increases the pi of the IT-acylated protein to more than 6.

Particularly preferred modified proteins for use within the scope of the invention include esterification or hydroxyalkylation products of gelatins with high "molecular weight, which arise during 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 used preferred. They can easily be made by acid-catalyzed esterification with the appropriate alcohol, in which case the reaction primarily attacks the protein · carboxylic acid functions, or alternatively they can by treatment with an alkylene oxide, in which case esterification by hydroxyalkylation of others reactive groups, for example primary amino groups, may be accompanied. The extent of such ET hydroxyalkylation depends primarily on the pH conditions used. If the pH of the reaction medium during

- 15 -40988B / U61

- fC-the reaction is kept in the acidic range, the extent of IT-hydroxyalkylation is rather lower than if the pH is allowed to rise during the reaction. The effect of the N-hydroxyalkylation is to increase the hydrophobicity of the protein, but to decrease the isoionic point of the protein. The benefit in terms of co-conditioning effectiveness. is therefore relatively small compared to the effect of esterification on 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 used in the inventive compositions in an amount up to 50 wt .-%, but generally in an amount between 1 wt .- ^ and 10 wt .-%, preferably between 2 wt .-% to 6 wt. - % of the composition are present. Thus, they are effective keratin conditioning agents even at relatively low concentrations.

Surfactant materials that can be used in the compositions according to the invention among the water-soluble soaps and synthetic, anionic, nonionic, cationic, zwitterionic and amphoteric detergents as described below can be selected. Preferably those are surface-active Medium 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 higher fatty acid alkylolammonium salts containing about 8 to 24 carbon atoms, and preferably from about 10 to about 20 Contain carbon atoms. Suitable fatty acids can be obtained from natural sources, such as from vegetable or animal esters (e.g. palm oil, coconut oil, babassu oil, soy

- 16 -

409886/1451

bean oil, castor oil, tallow, whale and fish oils, fat, lard and mixtures thereof). The fatty acids can also synthetic (e.g. by oxidation of petroleum or by hydrogenation of carbon monoxide according to the Fischer-Tropsch process) produced v / earth. 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 produced by direct saponification of fats and oils or by neutralization of the free fatty acids, which are obtained in a separate manufacturing process. Particularly the sodium, potassium and triethanolium salts are useful 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, in particular the alkali metal salts of organic sulfuric acid reaction products, which in their molecular structure _{contain an alkyl radical (} with about 8 to about 22 carbon atoms and a sulfonic acid or sulfuric acid ester radical. (The term "alkyl" also refers to the alkyl segment of higher acyl radicals 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) , which latter ¹ are formed by reducing the glycerides of tallow or coconut oil; the Alkalimetallolefinsulfonate having 8 to 24 carbon atoms are, for example, in US Patent No. 3,332,880 described and Alkalimetallalkylglyceryläthersulfonate, especially those ethers of the higher alcohols d i. e are derived from sebum 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 of the types described in U.S. Patents No. 2,220,099 and No. 2,4-77,383 (the alkyl group can be any

- 17 -

409886 / U61

straight or branched aliphatic chain); Sodium Coconut Oil Fatty Acid Monoglyceride Sulphates and sulfonates; Salts of alkyl phenol ethylene oxide ether sulfate with about 1 to about 12 Units of ethylene oxide per molecule and in which the alkyl radicals are 8 Ms contain about 18 carbon atoms; the reaction product of fatty acids that are esterified with isethionic acid and with sodium hydroxide are neutralized, where for example the fatty acid is oleic acid or is derived from coconut oil; Sodium- or potassium salts of fatty acid amide, a methyl tauride, wherein the fatty acids are, for example, derived from coconut oil; Sodium or potassium ß-acetoxy- or -ß-acetamidoalkanesulfonate, wherein the alkane has 8 to 22 carbon atoms and others as are known per se, a number of which in particular in US Pat. Nos. 2,286,921, No. 2,486,922 and No. 2,? 96.2? 8, respectively.

Other synthetic anionic detergents useful in the context of the invention are the alkyl ether

sulfates. These materials have the formula R 0 (CoHf ₁ O) SO ^ M, 2 έ. ** ■ X 3

wherein R is alkyl or alkenyl of about 8 to about 24 carbon atoms, χ = 1 to 30 and M selects a sala-forming cation

salts salts of the group of alkali metals, ammonium, dimethyl, triethyl, Triethyl, dirnethanpl, diethanoi, trimethanol and Triethanol ammonium salts mean.

The alkyl ether sulfates according to the present invention are condensate! ons products of ethylene oxide and monovalent ones Alcohols having from about 8 to about 24 carbon atoms. Preferential

p
The radical R has from 14 to 18 carbon atoms. The alcohols can be derived from fats, for example coconut oil or tallow, 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 proportions of ethylene oxide and the resulting mixture of molecular species containing, for example, an average of 6 moles of ethylene oxide per mole of alcohol.

- 18 -

4Q9886 / U61-

show, is sulfated and neutralized.

Specific examples of alkyl ether sulfates according to the present invention Invention are sodium coconut alkyl ethylene glycol ether sulfate, Lithium tallow alkyl triethylene glycol ether sulphate and sodium tallow alkyl hexaoxyethylene sulphate.

Preferred for reasons of excellent cleaning properties and more readily available are the alkali metal coconut and tallow alkyloxyethylene ether sulfates, which on average contain about 1 to about 10 oxyethylene radicals. 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 are produced by condensation of alkylene oxide groups (hydrophilic nature) with an organic hydrophobic compound, which is more aliphatic or alkyl aromatic in nature. The length of the hydrophilic or polyoxyalkylene, which with any special hydrophobic group is condensed, can be easily adjusted to create a water-soluble compound provide the desired degree of equilibrium between having hydrophilic and hydrophobic elements.

For example, one known class of nonionic synthetic detergents is on the market under the trade name "Pluronic" available. 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 section leads to an increase in the water solubility of the molecule as a whole and its liquid character of the product is retained to the point where the

- 19 -

4098-867 U.S. 1

Polyoxyethylene content makes up about 50 % of the total weight of the condensation product.

Other suitable nonionic synthetic detergents include:

1. The polyethylene oxide condensates of alkylphenol, e.g. the condensation products of alkylphenols containing an alkyl group having about 6 "to 12 carbon atoms either straight-chain or branched-chain configuration, with ethylene oxide, the ethylene oxide being present in amounts equal to 5 Ms 25 moles of ethylene oxide per mole of alkylphenol correspond. The alkyl substituent in such compounds can, for example, be polymerized Derive propylene, diisobutylene, octene or hair dryer.

2. Those resulting from the condensation of ethylene oxide with the product obtained from the reaction of propylene oxide with ethylenediamine is formed. For example, compounds that contain about 4-0 wt% to about 80 wt% polyoxyethylene and have a molecular weight of about 5000 to about 11,000 on v / iron and in the reaction of ethylene oxide groups are formed with a hydrophobic base, which is the reaction product of ethylenediamine and excess Represents propylene oxide, the base having a molecular weight in the range of 2500 to 3000, satisfactory.

3 The condensation product of aliphatic alcohols, the 8th up to 24 carbon atoms in either straight chain or have 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, where the coconut alcohol fraction has 10 to 14 carbon atoms having.

4. Mchtionic detergents, including HOnylphenol,

- 20 -

4Q9886 / U51

that with either about 10 or about 30 moles of ethylene oxide per mole of phenol is condensed, and the condensation products of coconut alcohol with an average of 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, the one with 12 moles Ethylene oxide is condensed per mole of phenol; Dinonylphenol, which is condensed with 15 moles of ethylene oxide per mole of phenol; Dodecyl mercaptan, which contains 10 moles of ethylene oxide per mole of mercaptan is condensed; bis (N-2-hydroxyethyl) lauramide; Nonylphenol, which contains 20 moles of ethylene oxide per mole of nonylphenol is condensed; Myristyl alcohol, which condenses with 10 moles of ethylene oxide per mole of myristyl alcohol is; Lauramide condensed with 15 moles of ethylene oxide per mole of lauramide; and diisooctylphenol, the is condensed with 15 moles of ethylene oxide.

3 4 5

A detergent with the general formula RR R ^ U -> 0

(Amine oxide detergent) where R is an alkyl group of about 10 to about 28 carbon atoms, 0 to about 2 hydroxy groups and represents 0 to about 5 ether bonds, where

• 3

at least one of the radicals R, which represents an alkyl group, about 10 to about 18 carbon atoms and 0 ether

Ll c.

contains bonds and each of the radicals R and Ό / 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: dimethyldodecylamine oxide, dimethyltetradecylamine oxide,
Ethyl methyl tetradecylamine oxide, cetyldimethylamine oxide,
DimethyIstearylaminoxid, Cetyläthylpropylaminoxid, Diethyldodecylaminoxid, Diethyltetradecylaminoxid, Dipropyldodecylaminoxid, bis- (2-Hydroxyäthyl) -dodecylaminoxid, bis- (2-Hydroxyäthyl) -3-dodecoxy-i-hydroxypropylaminoxid, (2-Hydroxyäthyl) -hydroxylaminoxid, (2-Hydroxyäthyl) -3-dodecoxy-i-hydroxypropyl-hydroxypropyl)

- 21 -

409886/1451

amine oxide, dimeth.yl- (2-hydroxydoaecyl) -amine oxide and the corresponding decyl, hexadecyl and oetadecyl homologues of the above compounds.

• 3 » H.

6. A detergent having the general formula R-S-R, wherein

-% a.
R 'and R have the meaning given above.

Specific examples of sulfoxide detergents include: Dodecyl, tetradecyl, 3-hydroxytridecyl methyl sulfoxide, 3-ßIethoxytridecylmethylsulfoxid, 3-hydroxy ^z ^ -dodecoxybutylmethylsulfoxid, octadecyl-2-hydroxyäthylsulfoxid and Dodecyläthylsulfoxid.

7 · The ammonia, monoethanol and diethanoiamides of fatty acids with an acyl radical containing from about 8 to about 18 carbon atoms. These acyl residues usually derive of naturally occurring glycerides, e.g. coconut oil, Palm oil, soybean oil and tallow, but can also be of synthetic origin, e.g. from oxidation of petroleum or the hydrogenation of carbon monoxide by the Fischer-Tropsch process.

C. Ampholytic synthetic detergents.

Ampholytic synthetic detergents can generally be used as derivatives of aliphatic or aliphatic derivatives of heterocyclic secondary and tertiary amines in which the aliphatic radical is straight-chain or branched can and wherein one of the aliphatic substituents is about 8 up to 18 carbon atoms and at least one anionic water-solubilizing group, e.g. Carboxy, SuIfο or SuIfato, contains. Examples of compounds that fall under this definition are sodium 3- (dodecylamino) propionate, sodium 3- (dodecylamino) propane-1-sulfonate, Sodium 2- (dodecylamino) ethyl sulfate, sodium 2-6-imethylamino) octadecanoate, Disodium 3- (ϊΓ-car b oxymethyldode cylamino) -pr opane-1 -sulfonate, Disodium octadecyliminodiacetate, urodium-1-carboxymethyl-2-

- 22 409886 / U51

undecylimidazole and sodium-N, N-Ms- (2-hydroxyethyl) -2-sulfato-3-cLodecoxypropylamine.

D. Zwitterionic Synthetic Detergents.

Zwitterionic synthetic detergents can be broadly referred to as derivatives of aliphatic quaternary ammonium and phosphonium or tertiary sulfonium compounds wherein the cationic atom can be part of a heterocyclic ring and wherein the aliphatic radical can be straight or branched and one of the aliphatic substituents can be from about 3 to 18 carbon atoms contains, at least one aliphatic substituent having an anionic water-solubilizing group, for example carboxy, sulfo or sulfato. Examples of compounds falling under this definition are 3r (N, N-dimethyl-N-hexadecylammonio) -2-hydroxypropane-1-sulfonate, 3- (N, N-dimethyl-N-hexadecylammonio) -propane-1- 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-1-sulfonate, 3- (S-methyl-S- & odecylsulfonio) -propionate, 4- (S-methyl-S-tetradecylsulfonio) -butyrate, 1 - (2-Hydroxyethyl) -2-undecylimidazolium-1-acetate, 2- (trimethylammonio) octadecanoate, 3- / N, N-bis- (2-hydroxyethyl) -N-octadecylammonio_7-2-hydroxypropane-1-sulfonate and 3- (N, N-dimethyl-N-1-methylalkylammonio) -2-hydroxypropane-1-sulfonate, v / orin alkyl has an average length of 13.5 to 14.5 carbon atoms. Some of these detergents are η disclosed in U.S. Patent No. 2,129,264 ^1. 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

exhibit,

R ⁶ -N (R ⁷ ) ₅ ⁺ An "

- 23 -

409 886/1451

wherein R is an alkyl chain of from about 8 to about

7th
atoms, each R is selected from the group consisting of alkyl and alkanol groups having 1 to 4 carbon atoms and benzyl groups, with normally no more than one benzyl group being present, and two R 'groups either by a carbon-carbon ether or , may be linked through an imino bond to form a ring structure, and An. represents a halogen atom., a sulfate group, fitrate group or other pseudohalogen group. Specific examples are coconut alkyl trimethylamine chloride, dodecyldimethylbenzyl bromide, and dodecylmethylmorpholino chloride.

The soap and non-soap anionic, nonionic and zwitterionic surfactant detergents mentioned above can be used as the sole surfactants or the various examples can be mixed together in the practice of the invention. Particularly preferred are anionic and nonionic surfactants. The amount of surfactant that is incorporated into the preparations depends on the intended use of the particular formulation. Thus, it is in relationship zura weight of the preparation _t as a whole when it is applied directly to the skin, for example, applied as a cosmetic lotion, or, are at the concentration at which it is used as a solution in, for example, tableware washing water or bath water. In most cases a content in the range from 0.1% by weight to 90% by weight of the preparation is suitable. In particular, detergent compositions for cleaning purposes will generally contain between about 5% and 50% by weight of the surfactant, while cosmetic compositions will generally contain between 0.1% and 10% by weight of the surfactant.

The invention is applicable to various compositions

- 24- -

4Q9886 / U51

applicable in the normal course of use with keratin come into contact, e.g. dishwashing liquids, hand or face creams, body lotions, hair shampoos, Bath compositions, heavy duty detergent compositions, Hard surface cleaning compositions, Soap bars, etc. The physical form of the composition can also vary widely, from granular solids to gels and creams to viscous, viscous or mobile liquid compositions. Dish washing compositions are generally liquid and comprise mixtures of water and foaming detergents. Granular detergent compositions, on the other hand, can do something Contain water or be anhydrous. Cosmetic and related compositions generally become one Based on a mixture of water and emulsifying agents and oil, and the physical state of these compositions will be that of oil-in-water or water-in-oil emulsions. However, it is also considered that cosmetic-like compositions according to the invention can be in the form of gels which contain the modified protein and water and optionally a protective agent. such as methyl alcohol. However, other cosmetic-like compositions can be somewhat watery contained or anhydrous, but a mixture of modified protein, oil and foaming surfactant Funds included. Such compositions are useful as bath compositions particularly suitable.

The preferred liquid or granular detergent " compositions for use as, for example, high-performance detergents1, Dishwashing detergent compositions or shampoos contain between 5% by weight and 50% by weight foaming detergent. In particular, the foaming detergent is selected from:

- 25 -

409886 / UBi

COAL WATER

a. up to 45% by weight of a water-soluble one

Sulphate of the general formula RO (C ₂ H ₄ O) _n SO ^ M, where R is a straight or branched, saturated or unsaturated aliphatic hydrocarbon radical having 8 to 24 carbon atoms or a substituted by an aliphatic, straight-chain or branched hydrocarbon group having 8 to 18 carbon atoms Benzene residue is:

saiz '

η represents 1 to 12; and M for an alkali metal /, ammo salt '

nium ', dimethyl, trimethyl, triethyl, dimethanol, diethanoi, Trimethanol or triethanolammonium salt;

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

2 sulfonate of the general formula R SO ^ Mj

c. up to 45% by weight of a water-soluble hydrocarbon is only exposed

ρ sulfate of the general formula R

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

e. up to 40 wt .-? 6 of the condensation product from 3 to 25 Moles of an alkylene oxide, preferably ethylene or propylene oxide, and one mole of an organic, hydrophobic, compound of aliphatic or alkylarpmatic temperature, the latter having from 8 to 24 carbon atoms.

Another component included in the compositions of the invention can be incorporated is a water-soluble buffer material. The purpose of the buffer is to adjust the pH range that the conditioning effectiveness brings these compositions to an optimum. In the case of compositions containing precursor protein, the buffer sets the essential pH condition, namely that the pH of an aqueous solution or dispersion of the composition is at the use concentration

- 26 409886 / U51

is less than (pi - 0.7) - If the protein has a pi up to about pH 8, for example type B gelatin, the optimal pH range of use is about 5i5 to 7 and this makes the use of a mild acidic buffer material required. 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 optimum in-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. Acid buffer materials are generally used in proportions of up to 15% by weight , preferably up to 5% by weight, of a composition. Alkaline buffer materials may contain up to about 40 wt -.% In a granular V / aschmittelzusammensetzung be used, or up to about 5 wt .- £ in a liquid detergent composition?.

The liquid detergent or gel compositions according to the invention generally contain a carrier based on water and / or water-soluble solvents. Butanediol, toluene, benzyl carbinol, ethylene glycol monobutyl ether, propylene glycol propyl ether and diethylene glycol dimethyl ether. They are generally present in amounts up to 15 % by weight of the composition. Additional components of liquid detergent compositions include foam-

- 27 -

409886/1451

enhancers, such as the higher alkylamine oxides, and alkylolamides of carboxylic acids with 10 to 14 carbon atoms, Thickeners, protective substances / ^ opacifiers, perfumes, Dyes, fluorescent substances, opacifying substances, bactericides, hydrophobic oily materials and hydrotropes.

Commonly used hydrotropes include common lower alkyl aryl sulfonates, such as sodium and potassium toluene sulfonate, 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 invention include animal, vegetable and mineral oils and waxes, e.g. B. beeswax, spermaceti and carnauba wax; Fatty alcohols, such as stearyl, myristyl and cetyl alcohol; Fatty and Partial esters such as isepropyl myristate, glyceryl monostearate; Fatty acids such as stearic acid; Lanolin and cholesterol derivatives; and silicone oils.

The compositions according to the invention and in particular the cosmetic creams or lotions can also contain components intended to increase the moisturizing effectiveness of the compositions. Suitable components include lower aliphatic alcohols which have about 2 to about 6 carbon atoms and 2 to 1> hydroxyl groups, for example 1, ^ -. Butanediol, 1,2-propylene glycol, glycerol. Other suitable components include urea or urea derivatives such as guanidine, pyrrolidone or allantoin.

Solid granular detergent compositions can add foam boosters, Foam suppressants, bleaches, anti-redeposition agents, enzymes, enzyme and bleach activators, fluorescent

- 28 409 88 6/1451

contain detergents, builders and other normal components of granular detergent compositions. Fixed compositions Bars can also contain additives such as fatty acids, salts, skin creams and oils.

Oxyalkylation of proteins.

The following procedure is a typical method that can be used to oxyalkylate proteins. In
in this case the method is described with reference to the oxybutylation of gelatin. 10 g gelatin obtained by base hydrolysis with a molecule ar ge v / i cht of approx
80,000 and a pH of the isoionic point of about
5> 35 are dissolved in 500 ml v / water and the pH value of the solution is adjusted to 71 with sodium hydroxide solution. The solution is heated to a constant temperature of 27 C and with stirring
adds 65 ml of 1-butene oxide. The reaction is allowed to proceed for 26 hours, during which time the pH drops below
Addition of sulfuric acid is kept below 8.0. 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. After evaporation of the
Excess but-1-enoxide, the solution is dialyzed slowly for 6 hours in order to add salts and low molecular weight material
remove, and the modified gelatin will eventually
obtained by freeze drying. The product then comes with
Methanol / ether 1: 1 and then washed with ether, ^ whereupon it is brought to dryness. The hydroxybutylated
Gelatin has an inherent viscosity (measured in a buffer solution of pH 4.5, which contains 0.15 mol of sodium chloride, 0.1 mol of sodium acetate and 0.1 mol of acetic acid) of 0.301, which corresponds to Staudinger's empirical equation and the values the constants K and a according to BelIo, Bello and Vinograd one
corresponds to an average molecular weight of 73,000 '.

The percentage of esterification of the gelatin, measured by titration, was 4-3%, while the percentage
of N-alkylation, measured by Van Slyke determination primarily

- 29 -

409886/1451

rer amino groups, was 61 % .

The above method or variations thereof can be used to make modified gelatins that contain have different substituents and physical characteristics. For example, the maintenance diminishes of the pH value of the reaction medium in the acidic range, the extent of the ^ -hydroxyalkylation that occurs during the reaction he follows. Modified gelatins of higher molecular weight. can be prepared by using starting materials accordingly higher molecular weight can be used. Ethylene or propylene oxides can be used instead of 1-butene oxide can be used to prepare the corresponding oxyalkylated derivatives. Other types of proteins can as well can be used in place of base-hydrolyzed gelatin; gelatin obtained, for example, by acid hydrolysis, or proteins such as casein, Güadin, soybean protein, Zein and serum or egg albums. Other procedures can also be used to oxyalkylated Produce derivatives, e.g. the reaction with anhydrous alkylene carbonates.

Protein esterification.

Protein derivatives in which only the carboxylate groups modified; can be prepared using the following procedure. 10 g gelatin with a gel / strength of about 14-0 Bloom g and an isoionic point of about 5> 3, which is a size corresponding to a mesh size 60 mesh screen is ground at room temperature Sulfur concentrated in an O, O36N solution 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 whereupon it is dried in a desiccator at a pressure of 0.1 mm Hg. Acid residues become out of the product

409886 / US1

by stirring the gelatin in ten times the weight of water with the addition of 5N sodium hydroxide solution until a pH value is reached from 6 away. The swollen grains are brought to melt at A-O C, whereby a clear liquid is obtained which solidifies to a gel at 4 σ and becomes in is dried in a stream of air. Salts and low molecular weight Material is removed from the product by autodialysis, whereupon 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. "Their inherent 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 %.

Amine alkyl amide derivatives of proteins.

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

A solution of 10 ml of ΪΓ, ΪΓ-dimethylethylenediamine in 80 ml of water is prepared and its pH is adjusted to 4-5 with sulfuric acid. 2 g gelatin, the one Has a gel strength of about 240 Bloom g is used together with 4 g of if-cyclohexyl-II / ~ 2- (4-B-morpholinyl) -äthyl_7-carbodiimidmethyl-p-toluenesulfonate added. The pH of the solution is adjusted to 4.8 and the solution is left then stand at about 25.G for 6 1/2 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 made through and then freeze drying Vacuum drying isolated in a desiccator. The 2 - ('N, N-dimethylamino) ethylamide derivative of gelatin has the following characteristics:

4098867U61

pH of the isoionic

Point = 10.5

Inherent viscosity = 0.49

Average molecular weight = 162,000

Percentage of modified carboxylic acid groups = 42 % .

Skin conditioning tests.

Conditioning performance was measured by both in vitro and in vivo tests, with a high degree of. Agreement found between the two test methods'. The in vitro test (called calf skin occlusivity test) is based on the rate of perspiration of water through a sample of calf skin which has been treated with a 0.15% aqueous solution of a detergent composition (at 18 hardness) that contains the protein in Is brought into contact. The occlusiveness of the protoin was

speed reduction of water transpiration / for proteinaceous surface-active solution compared to that measured for water.

The in vivo test used was a hand immersion test (HIT). This test was carried out on the basis of 16 people (32nd Hands) per product carried out in a multi-product test, with the hands balanced in terms of the differences between the right hand and the left hand, so that pro Product 52 hands, namely 16 right and 16 left hands, have been tested. Each person dipped their left and right hands into different solutions for three consecutive times 10 minute periods within half an hour per day, u.zw. during 3 weeks, 5 days each "week. The treatment solutions were replenished every 10 minutes. The hands are removed from the solution every 2 minutes and submerged again.

The hands were assessed on the first Monday (before immersion) and every Friday of the test. the

- 3? _
409886/1451

. '.JV. 2A3A063

Assessment was based on a score from 0 to 10 (perfect) ranging scale, regarding the overall condition of the hand, on the basis of a scale from 0 to 10 (bad), regarding skin flaking, and one from 0 to 10 (perfect) ranging scale, regarding the nail assessment. HIT grades for protein / surfactant solutions were determined and plotted on a scale at which. a 0.15% aqueous solution of the surfactant from Standard II (see Table V) received HIT grade 0 and

a hand care lotion applied in an amount of 1 mg / cm was assigned the HIT grade 100.

Examples 1- 15:

A number of oxybutylated gelatins made by the methods described above have been tested for their conditioning benefits exhibited in aqueous surfactant-containing solutions. The modified proteins were with varying molecular weights, isoionic points, degrees of O-alkylation, N-degrees of alkylation, etc. produced. they were various liquid detergent compositions of Examples 1-13 given in Table V, incorporated. Examples 1 through 4 illustrate the effect (see Table I) of changing molecular weight on Conditioning of oxybutylated gelatins. It can it will be seen that oxybutylated gelatins have molecular weights are all effective in the range from 5000 to 200,000, however, when they provide conditioning benefits in aqueous surfactant solutions, these benefits are most severe with modified proteins in the higher molecular weight range, i.e. above about 20,000. Proteins, however, which have lower molecular weights of about 5000 or less still give useful ones Conditioning benefits.

Examples 6 through 9 illustrate the effect of

409886/1451

Change of the pH value of the isoionic point on the conditioning performance "at a constant pH of application to skin (pH 7). It can be seen that the conditioning performance with respect to the pH of the isoionic point (pi) is very sensitive, with modified proteins that have a pI above 8, and preferably above 8.5, are most effective for a given molecular weight value are.

It can also be seen that the performance to some extent at pi values below the pH of the Application is decreased.

The effect of the concentration of the modified protein in the surfactant is demonstrated by comparing Examples 1, 10 and 11. The optimum protein concentration is about 4 wt -.% Of the composition, little advantage in increasing the protein proportion of 5 wt -.% Are obtained. With an incorporation amount of 2% by weight, however, the conditioning advantages are reduced by over 50 ° ß>.

The conditioning performance of Examples 1, 2 and 3 as a function of the pH of the application to keratin is off Table IV can be seen. The optimal pH range for conditioning effectiveness is apparently below the pH of the isoionic point of the protein, where the conditioning effectiveness is generally reduced for pH values above the isoionic point. In comparison for the solution of the surfactant used as a control (Standard II), however, result Conditioning benefits at a slightly lower value even above the higher pH range.

The last two entries in Table I, Examples 12 and 15, illustrate the incorporation

409886/1451

of the same modified. Protein as in Example 1 has been used in a solution of the surfactant based on paraffin sulfonate and alkyl ether sulfate. Although Examples 12 and 13 show less effectiveness than most of the previous examples, it shows in the calf skin test found that the compositions of Examples 12 and 13 were more mild than the same liquid detergent compositions (Standard III) that do not contain modified protein.

Also in Table I are the hand immersion test data for Examples 1 to 3 and 11 were added. These data show that such modified proteins, having a molecular weight greater than about 1500 and an isoionic point pH greater than about 8 while protecting Keratin against the harmful effects of detergent solutions applied to keratin at pH values of around 7 are particularly effective. In particular, the compositions showed of Examples 1 to 3, from dilute aqueous solutions of surface-active agents at least 2/3 the conditioning benefits obtained with a hand care lotion applied directly to the skin surface is applied. In addition, the composition of the example remained in five three week hand immersion tests 1 hands and nails in significantly better condition with 95% reliability than with the composition from Standard II.

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

- 35 -

409886/1451

Examples 14-19:

In Table II is the conditioning performance of various modified proteins that are used in surfactants containing compositions as defined in Table V are incorporated. This can be done again It will be seen that the modified proteins according to the present invention have high molecular weight and high isoionic point are particularly effective in order to gain occlusivity to deliver in vitro the aqueous solutions of surfactants.

The conditioning performance of the composition of Example 17 as a function of 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 point v / ineffective. The effectiveness decreases at application pH values that are higher than (pi + 2). In contrast to most of the other examples, where the conditioning performance at pH values below the pi of the modified protein is relatively insensitive to the hardness of the treatment solution, the composition of Example 17 is somewhat more effective above this pH value in the absence of free water hardness. For example, at pH values of 9 »3 to 9.5, the calfskin occlus is:
Hardness.

Degree of occlusion 4.5 at 0 ° hardness, but only 1.5 at 18 °

Examples 20 and 21:

Examples 20 and 21 given in Table III represent two compositions according to the invention, which Contain precursor proteins. The precursor protein of Example 20 is a type A gelatin, which has a pH the isoionic point of 7 »7 (corresponding to a pH value of the isoelectric point of 8.4) and a molecular weight

- 56 409886 / U51

of etv; a has 75,000. The precursor protein of the example 21 is a synthetic polypeptide - polylysine with a pH of the isoionic point of > 11 and a molecular weight of 70,000 and above. Compositions, which contain precursor proteins have become within a pH range up to the acidic side of the pH value of the isoionic point of the precursor protein proved to be effective. Thus, type A gelatins are preferably used at an application pH of about pH 5 "to 7. Polylysines can be used at any pH in the range from 5 to 10 can be used.

Examples 22 to 28:

The following examples are intended to illustrate, but not limit, liquid detergent compositions according to the present invention. All percentages are percentages by weight.

Examples:

22 23 24 25 26 27 28

Dirnethyldodecyl

amine oxide 8% 4% 2% W / o 2P / o WA

Coconut alcohol

lenoxide (6) condensate 15 7 6 7 2 7

Diethanol -C _{1 9} _ _{Λ (} - ~ fat-

acid amide 2 3 2

Coconut alcohol ethylene oxide (3) sulfate, Sodium al ζ

C * -z ^ Q-paraffin sulfonate, Sodium salt

10 9 14th 10 12th 14th 10 9 9 10 12th

Ammonium saltζ 12

Urea -86 10 8 6 10

technical alcohol denatured with methanol 11 13 13 13 13 12 13 Modified gelatine * 2 4 4 4 5 3 4 water remainder

- 37 -409886 / U51

= Modified gelatin: hydroxybutyl derivative; Molecular weight 25,000; pH of the isoionic point 9j1; Percentage of O-alkylated side chains 48; percent set of N-alkylated side chains 20.

The above compositions are milder to the skin and hair than the corresponding compositions which do not contain modified protein and there is essentially no reduction in the volume or stability of the lather formed by the detergent. Substantially the same cleaning and conditioning performance is obtained. when the modified protein in the above example is replaced by the oxybutylated product of casein purified by the Hammarsten method, the modified casein having a pi of 8.8, a percentage of O-alkylated side chains of 40 % and a percentage of F-alkylated side chains of 61 % .

Examples 29-34:

Examples:

- 29 30th 1 31 32 33 34 Coconut alcohol ethylene
oxide (3) sulfate, ammonium
salt 16 18th 18th 12th Coconut alcohol ethylene
oxide (9) sulfate, sodium salt 22nd 14th C ^ * ζλ o-Paraf f insulphonate,
Sodium salt 10 8th 14th 10 5 8th C _{12 1} ^ -a-olefin sulfonate,
Ammonium salt 8th 10 ^G 10-14 ~ ^Alkylbeilzo1 '
Sodium salt 5 14th Modified gelatin 4th 3 4th 2 5 ' 3 technical, with methanol
denatured alcohol • 10 11 13th 10
) ao + - 13th 8th 11 CLO O CX
- 38 - lüto Xl 409886 / 145

* = Modified gelatin: hydroxyethyl derivative; Molecular weight 80,000; pH of the isoionic point 8.3; Percentage of O-alkylated side chains 47; percentage N-alkylated side chains 40.

Essentially the same cleaning and conditioning performance is obtained when the modified protein is replaced by a methyl, ethyl, propyl or butyl ester of gelatin which has a molecular weight of about 80,000 and an isoionic point pH of 8 to 9.5.

Examples 35-37:

Liquid detergent compositions useful as shampoos or dishwashing products are composed as follows.

Examples: 35 36; 37

Coconut alkyl ethoxylate (3) sulfate, Sodium salt 25.0 15 18

Coconut alkyldimethyl

amine oxide 3.5 4

Coconut alkyl sulfates,

Ammonium salt 15.0 14

C _{/] 0} _ ₁ ^ alkyl benzene, sodium salt

acetic acid
Citric acid

technical spirit denatured with methanol

Cetyl alcohol gelatin

water

* = Gelatin: type A; pH of the isoionic point 7.8;

Molecular weight 80,000.

- 39 - ' 409886/1451

5 18th 3.2 8.0 10 10.0 12.0 13th 3.0 4.0 4.0

All of the above compositions, when diluted with water, give a pH in the range of 5 to 7 · When used a concentration of about 0.2 % they give a pH of about 6. '

Example 38:

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

Parts by weight;

Hexadecyl dimethyl amine oxide 40

Mineral oil 56

Water 1 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 39:

A soap bar composition that is opposite to that of the Skin is mild, has the following composition:

Parts by weight:

Real side (sebum / coconut

in a ratio of 50:50) 78.5

free fatty acid 7.6

Humidity 9.3

Skin cream 0.5

N, N-dimethylethylenedi amine ivat of gelatin:

pH of the isoionic
Point 10.5;
Molecular weight 100,000;
Percentage of 0-alkylated

Side chains 42 4.0

- 40 409886 / U51

Example 40:

A moisturizing hand cream has the following composition.

Parts by weight:

Stearic acid Rest on 12th mineral oil 2 Cetyl alcohol 0.6 Glycerin 6.0 Triethanolamine 1.5 borax 0.9 Glyceryl monostearate 2.0 Methyl p-hydroxybenzoate 0.25 Modified gelatin * 5.0 water 100.00

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

Example 41:

A proteinized hair cream dish detergent has the föl-. low composition.

Parts by weight:

Tegamin S-13 ⁺ Rest on 4th Phosphoric acid (85%) 0.6 Methyl p-hydroxybenzoate 0.2 Glyceryl monostearate 1.5 Modified Casein * 8.0 water 100.00

= Tegamin S-13 is a dialkylaminoalkylstearamide that is marketed by Goldschmidt Chemical Company.

- 41 -409 886/1451

* = Modified casein: oxybutyl derivative; pH of the isoionic Point 8.8; Percentage of O-alkylated Side chains 4-0; Percentage of N-alkylated side chains 61. -

Example 4-2:

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

Parts by weight: Ethyl alcohol 10 Methyl p-hydroxybenzoate 0.5 Modified gelatin * 15th water Remainder to 100.00

* = Modified gelatin: oxybutyl derivative; pH of the isoionic Point 9.6; Molecular weight 15,000; Percentage of 0-alkylated side chains 24 ·; Percentage of F-alkylated side chains 4-3

Tab. I - V: ./.

- 4-2 409886 / U51

Table I: Conditioning performance of oxybutylated gelatins at pH'7

at
game: Weight %
of the pro
teins in
the to
together
setting: percent
sentence of
0-alky
lation: percent
sentence of
N-alky-
lation: PH value
of the iso
ionic
Point: Molecu
lar
weight : in vitro
Occlusi-
vity: Hand immersion test: Dandruff
p-
condition: ISJ 1 4th - 45 40 8.8 190,000 8.2 total
condition: 44 CO 2 4th 44 39 9.0 80,000 7.7 64 53 σ
cn 3 4th 48 20th 9.1 25-000 6.4 61 42 0 ^ω 4th 4th 24 43 9.6 15,000 4.6 68 - -12 VJl 4th - 17th 9.1 9. coo 3.1 - - 6th 4th 47 30th 8.9 80,000 8.3 - - 7th 4th 49 59 7.9 100,000 5.9 - - 8th' 4th 39 - 6.9 80,000 4.7 - - 9 6th 56 52 6.2 80,000 <1 - - 10 5 45. 40 8.8 190,000 7.8 - - 11 2 45 40 8.8 190,000 5.3 - 33 12th 4th 45 40 8.8 190,000 2.3 31 13th 4th 45 40 8.8 190,000 2.5 - default
I. _ 0 - II - - - - - -6.1 III - - - - - -3.6 0 0

Table II: Conditioning performance of various modified proteins at pH 7

at
game: Modified
Reagent / protein:
(a) Weight %
protein
in the
Together
setting:
Cb) percent
sentence of
O-alky-
lation:
(C) percent
sentence of
N-alky-
lation:
CD) pH value
of the iso
ionic
Point:
Ce) Molecu
lar
weight:
Cf) in vitro
Occlusi-
vity:
CeO 14th Ethylene oxide /
gelatin 4th 47 40 8.3 80,000 6.4 15th Pr opy1enoxi d /
gelatin 4th 35 61 9.2 80,000 4.4 2 1-butene oxide /
gelatin 4th 44 39 9.0 80,000 , 7.7 16 Methanol /
gelatin 4th 35 9.0 100,000 2.7 17th Ν, ΕΓ-dimethyl
ethylene diamine /
gelatin 4th 42 7th 10.5 ' 100,000 3.0 18th 1-butene oxide /
Casein 4th 40 61 8.8 _ 3.2 19th 1-butene oxide /
Soybean. N-
protein 4th - - 8.5 - 6.0 ^

Continued Tab. II: Cb) CO - Ce) Ci) Cs) Default: Ca) 6th - 5-6 1,000 <-7 IV Superpro 16 C 6th - - 6.5 300 +0.1 V Hydropro 230 6th - - 5 - 5.5 10,000 -6.1 VI Grotein SPG 6th - - 5 - 5.5 2,000 -1.2 VII Orotein SPO 6th - 6th 1,000 -3.4 VIII Wilson X 250 6th - 5 10,000 -6.7 IX Wilson X 1000

O CD OO OO

Table III:
Conditioning of various precursor proteins

at
game: % Protein by weight
in the together
setting: Utility
PH value: pH of the
isoionic
Point: Molecular
weight: in vitro
Occlusi-
vity: 20th
21 4th
4th 6th
7th 7.7
cationic
at all
pH values 75-000
> 70,000 5.3
13.5 Stan
dard: 4th -6.1 X 7th 4.5 140,000

Table IV: Conditioning performance as puncture of the application pH.

α co co οο cn

To whom-
dung pH: Standard II: Example 1: Example 2: Example 3: Example 17: Standard X: Example 20: -4.1 4.0 - - - - - - 5.2 - 4.5 - - - - - - - - 5.0 -8.5 • 2.5 - 1.3 - -5.0 - - 5.5 - - - - - - - - 6.0 -5.3 5.7 - - - - 5.3 6.5 - - - ■ - - - - 7.0 -6.1 8.2 7.7 6.4 3.0 6.1 - CaJ '7.5 - - - - - - -3.4 ^ j. _O
CD
«_A> 8.0 -6.2 - - - - - Ύ 8.5 - -1.5 1.5 - 1.5 - 9.0 -6.5 - - -2.7 1.4 - 9.3 -7.3 -6.2 -1.3 - 1.5 - 10.0 - -6.0 -3.7 - 1.0. - 10.5 - - - - - - 11.0 -5.2 - - " - 3.5 - 11.5 - - - - 3.8 - 12.0 - - - - 12.5 -1.1 -, - - -1.2 -

Table V:

Together-
setting: 15,
18
19: By S 6.7,
14,
16,
17,
21: 2: 3.5: ρ i e 1: 8th: 9: 10: 11: 12: 13: I: Default: Ill: IV
IX: X: Cb) Cc) CD) • Ce) 20: Cs) Ch) Ci) CD) Ck) Ci) Cm) II: Co) Cp) Cq) Ca) 18.4 18.4 18.4 18.4 Cf) 18.4 18.4 18.4 18.4 Cn) 18.4 18.4 Ammonium-
linear-
^G 12-i4 " ^Alk -
ylbenzene
sulfonate 18.4 18.4 - Sodium li
ne ar-C | 2_ / i4 ~ 18.4 18.4 18.4 18.4 18.4 18.4 18.4 18.4 13.5 18.4 13.5 18.4 18.4 alcoholic
fat, a
in the end
3 ethylene
oxide residues - - - - 18.4 - - - - 27.0 18.4 - 18.4 27.0 - IN)
_ -P-
Gp Sodium-
O ₁ ^ -paraf
fins ulf onate - -

O C7> CO

Continued act>.

(a). W. (C) W. (e) 2.0 Ce) (H) (i) U) (k) (D - (n) (O) (P) (q) Lauric acid
rethanol
amide 2.0 • 2.0 2.0. 2.0 10.0 4.5 4.5 4.5 2.0 *, 5 · 2.0 2.0 urea 10.0 - 6.0 10.0 11.4 - - - 8.0 6.0 12.0 - - - - 10.0, technical,
with metha-
nol denatured
the spirit 13.0 13.0 13.0 15.0 4.0 13.0 13.0 13.0 13.0 7.0 10.0 100 13.0 7.0 13.0 13.0 Protein * 4.0 4.0 4.0 4.0 100 4.0 6.0 5.0 2.0 4.0 4.0 - - 6.0 4.0 Water,
Rest on 100 Ί00 100 100 · 100 100 100 100 100 100 100 100 100 100

* = Protein incorporated as grains containing about 10 % water.

-!> ■ CO -P-CD CD CO

Claims (1)

Patent claims: Composition for protecting keratinous material against harmful effects of detergents and other sharp materials and against adverse climatic influences, characterized in that it contains an effective amount of a modified protein as defined above which is a Molecular weight greater than 5000 and a pH of isoionic Having a point greater than 6, wherein the modified protein is incorporated into an acceptable carrier which also contains a surfactant or cosmetic base. 2. Composition according to claim 1, characterized in that that the modified protein contains functional groupings formed as a result of the modification, selected from one or more of the following: -C-W-Q; -N-X-Q; -O-Y-Q; -S-Z-Q, where C, N, O and S carbon, nitrogen, oxygen and represent sulfur atoms, respectively; -Z- means a direct bond or carbonyl, -Y- stands for -Z-, sulfonyl or phosphonyl groups, Represents -X- -Y- or C = NR groups, -W- -X-, -NX-, -OY- or -SZ groups symbolizes and Q means -R ¹ -, -SR ¹ -, -OR ¹ -, -KR ₂ , - ^ R ₂ , -NR ^, whereby R represents a hydrogen atom or -R and R one or more alkyl, alkenyl, aryl, cycloalkyl or contains heterocyclyl radicals, the alkyl or Alkenyl radicals, optionally through heteroatoms or functional radicals, such as dyes, fluorescent substances etc., are interrupted and are optionally substituted by radicals which represent q and / or WQ, where R has no more than 20 interconnected carbon atoms in the alkyl or alkenyl radical. - 50 409886/1451 3. Composition according to claim 2, characterized draws that R is the formula -CH ₂ - (CHQ ¹ ) _p - (GH ₂ ) ^ - YQ ¹ '' 1
where Q is a hydrogen atom or Q, ρ = O or 1 means and symbolizes q = O his (5 - Ρ). 4. Composition according to claim 2 or 3, characterized 1 shows that R Contains 2 heteroatoms. characterized in that R has up to 8 carbon atoms and up to 5 · Composition according to any one of claims 2 to characterized in that R has the formula -CH ₂ -CHOH- (CH ₂ ) _r -H, where r = 0 to 6. 6. Composition according to any one of claims 2 to characterized in that R has the formula -CH ₂ - (CH ₂ ) _r -H, where r = 0 to 7. 7. Composition according to any one of claims 2 to characterized in that R has the formula (CH ₂ ) -H ^ where r = 1 to 4 and s and t = 0 to 3. 8. Composition according to any one of claims 1 to characterized in that the modified protein has an average molecular weight of more than 10,000. - .51 40 98 86/14 9. Composition according to one of Claims 1 to 8, characterized in that the modified protein is a has an average molecular weight of more than 15,000. 10. The composition according to any one of claims 1 to 9, characterized in that the modified protein is a has an average molecular weight between 20,000 and 200,000. 11. Composition according to one of claims 1 to 10, characterized in that the precursor protein is gelatin, casein or soybean protein. 12. Composition according to claim 11, characterized in that that the precursor protein is a type B gelatin. 13. Composition according to one of Claims 1 to 12, characterized in that at least 50 % of the average molecular weight of the modified protein comes from the precursor protein. 14. Composition according to claim 13, characterized in that that 80 to 99% of the average molecular weight derive the modified protein from the precursor protein. 15 · Composition according to claim 14, characterized in that. Derive 90 to 96 % of the mean molecular weight of the modified protein from the precursor protein. 16. Composition according to one of claims 1 to 15 » characterized in that at least one of the functional groupings of the modified protein by. modification the precursor protein side chains are formed which contain carboxylic acid groups. - 52 - 409886 / U51 sy 17. The composition of claim. 16, thus identified Il Λ draws that WQ has the meaning COR. 18. ' Composition according to claim 17, characterized indicates that R has the formula given in claim 5 and the modified protein by oxyalkylation of the Precursors formed with an alk-1-enoxide “is. 19. Composition according to Claim 18, characterized in that the 1-alkene oxide is 1-butene oxide. 20. Composition according to claim 17, characterized in that that R has the formula given in claim 6 and the modified protein by esterification of the precursor protein is formed with a primary alcohol. 21. Composition according to claim 16, characterized in that WQ denotes the radical "" "1. 22. Composition according to claim 21, characterized in that that R has the formula given in claim 7, and that the modified protein is obtained by amidation of the precursor protein is formed with an alkylenediamine. 23 Composition according to one of Claims 1 to 22, characterized in that at least one of the functional groups of the modified protein by modification of precursor protein side chains containing basic groups is formed. 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 characterized in that XQ stands for -R. - 53 -409886 / U51 26. Composition according to claim 23, characterized in that that R has the formula given in claim 5 and the modified protein by oxyalkylation of the precursor protein is formed with an alk-1-enoxide. 27. Composition according to claim 23, characterized in that that R has the formula given in claim 6 or 7 and the modified protein by alkylation with R is halogen is formed. 28. Composition according to one of claims 1 to 27, characterized in that the modified protein has a pH of the isoionic point which is greater than 7.2 is. 29 · Composition according to claim 28, characterized in that that the modified protein has a pH of the isoionic point which is greater than 8.0. 30. Composition according to one of claims 1 to 29, characterized in that at least 5 % of the acidic side chains of the precursor protein are modified. ■ 31. Composition according to claim 30, characterized in that that at least 20% of the free acidic side chains of the precursor protein are modified. 32. Composition according to one of claims 1 to 31, characterized in that the modified protein is a Has content of free basic side chains, which, measured by titration against nitric acid solution, is greater as the equivalent of 0.1 mmol acid / g modified protein. 33 Composition according to one of Claims 1 to 32, characterized in that the modified protein has a 409886 / U5i Has content of free basic side chains that is greater is modified as the equivalent of 0.5 mmol acid / g Protein. Composition according to Claim 33, characterized in that that the modified protein has a content of free "basic side chains that is greater than that Equivalent of 0.8 mmol acid / g modified protein. 35 · Composition according to any one of claims 1 to 34-, characterized in that the modified protein has a content of free acidic side chains, measured modified by titration against sodium hydroxide solution which is less than the equivalent of 1.5 mmol sodium hydroxide / g Protein. 36. Composition according to claim 35 »characterized in that that the modified protein has a content of free acidic side chains which is less than that Equivalent of 1.1 mmol sodium hydroxide / g modified protein. 37 Composition according to Claim 36, characterized in that that the modified protein has a content of free acidic side chains which is less than that Equivalent of 0.8 mmol sodium hydroxide / g modified protein. 38. Composition according to one of claims 1 to 37t characterized in that the modified protein has a higher pH of the isoionic point than that Precursor protein. 39 Composition according to one of Claims 1 to 38, characterized in that the modified protein is more hydrophobic than the precursor protein. - 55 A09886 / U51 40. Composition according to one of Claims 1 to 39. characterized in that the pH of the composition or an aqueous solution or dispersion of the composition "at use concentration is less than (pi 4- 2), where pi is the pH of the isoionic point of the modified protein. 41. Composition according to claim 40, characterized in that that the modified protein has a pH fourth of the isoionic point which is greater than 8.0. 42. Composition according to claim 40, characterized in that that the pH of the composition or an aqueous solution or dispersion of the composition contributes Use concentration is less than (pi + 0.5) 43. Composition according to claim 40, characterized in that that the pH of the composition or an aqueous solution or dispersion of the composition contributes Use concentration is less than (pi - 0.7). 44. Composition according to claim 40, characterized in that that the pH of the composition or an aqueous solution or dispersion of the composition contributes Use concentration is less than (pi · - 1.4). 45. Composition according to one of claims 1 to 44, characterized in that the pH of the composition or an aqueous solution or dispersion of the composition at use concentration is about 7 ". 46. Composition for protecting keratinous material against harmful effects of detergents and other harsh substances and against adverse climatic influences, characterized in that the composition contains a liquid carrier to which a foaming detergent - 56 .- "409886 / U51 gene and a ν / effective set of a natural derived, synthetic or biosynthetic proteinaceous material is incorporated, the protein art if. ' material an average molecular weight of more than 5000 and has a pH value of the isoionic point of more than 6, and the pH of the composition or of an aqueous solution or dispersion of the composition at use concentration is less than (pi - 0.7), where pi is the pH of the isoionic point of the proteinaceous Material is. 4-7 · Composition according to claim 46, characterized in, that the pH of the composition or of an aqueous solution or dispersion of the proteinaceous material at use concentration is less than (pl-1,4-) 48. Composition according to claim 46 or 47, characterized characterized in that it contains such a buffer material that the pH of the composition or an aqueous Solution or dispersion of the proteinaceous material Use concentration is between 5 * 5 and .6.9. 49. Composition according to one of claims 46 to 48, characterized in that the protein.like material is a has an average molecular weight greater than 10,000. . 50. Composition according to claim 49, characterized in that that the proteinaceous material has an average molecular weight which is greater than 15,000. 51. Composition according to one of claims 46 to 50, characterized in that the proteinaceous - material is a gelatin of type A, which has an average molecular weight has between 20,000 and 200,000. - 57 -409886 / U51 52. Composition according to one of claims MG to 50> characterized in that the proteinaceous material is a synthetic polyamino acid. 53 · The composition of any of claims 46 to 52, characterized in that it contains up to 50 wt -% .modifiziertes, natural. derived, synthetic or biosynthetic proteinaceous. Contains material. Composition according to Claim 53, characterized in that it comprises between 1 and 10 % by weight of the proteinaceous. containing material. 55 Composition according to Claim 54, characterized in that they are between 2 and 6% by weight of the proteinaceous Contains materials. 56. Composition according to one of the preceding claims characterized in that it contains 0.1 to 90% by weight of surfactant Contains funds. 57 · Composition according to one of the preceding claims characterized in that the surfactant is an anionic or nonionic synthetic detergent or contains a salt of a higher fatty acid. 58. Composition according to one of the preceding claims in the form of a liquid or a gel, characterized in that that the carrier contains water and / or a water-soluble solvent. 59 · Composition according to claim 58 »characterized in that that the solvent is a lower alkanol » 60. Composition according to one of the preceding claims characterized in that it also contains a water-insoluble, Contains oily material. - 58 - 409886 / .U 51 61. Liquid detergent composition according to one of claims 57 to 60, characterized in that it contains between 5 and 50 % foaming detergent. 62. Liquid composition according to one of the claims 57 to 61, characterized in that they (A) up to 45 wt .- ^ of a water-soluble hydrocarbon sulfate of the general formula HO (O ₂ H ^ p) SOiM _)% wherein R is a straight or branched, saturated'or unsaturated aliphatic hydrocarbon radical with 8 to 24 carbon atoms or a through , an aliphatic, straight-chain or branched hydrocarbon group having 8 to 18 carbon atoms substituted. Is benzene residue η means 1 to 12 and salt ■ salt ·. M for an alkali metal /, ammonium /, dimethyl, trimethyl, Triethyl, dimethanol, diethanol, trimethanol or triethanolammonium salt, · (b) up to 45% by weight of a water-soluble hydrocarbon ' 2 su-lfonats of the general formula R SO-zM and (c) up to 45% by weight of a water-soluble hydrocarbon 2 ■ 'sulfate of the general formula R OSOJM contains. 63 · Substantially builder free dishwashing composition according to one of claims 58 to 62. 64 .. Shampoo composition according to one of the claims 58 to 62. 65 · Composition according to one of claims 58 to & \ - in the form of a lotion or a gel, characterized in that « - 59 - A09886 / U51 that they between. Contains 0.1 and 10 % of an emulsifying agent. -66. Composition according to any one of Claims 1 "to 57 in the form of a soap bar. 67 · Method of protection, keratinous material against harmful effects of detergents or others sharp materials or against adverse climatic influences for other than medical purposes, characterized in that the material is mixed with a composition or with an aqueous solution or dispersion of the composition according to any one of the preceding claims treated. For: The Procter & Gamble Company Li "'' ' Dr.H.J.WoIff Lawyer - 60 -409886/1451