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Patent 1059002 Summary

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(12) Patent: (11) CA 1059002
(21) Application Number: 243326
(54) English Title: DETERGENT COMPOSITIONS
(54) French Title: DETERSIFS
Status: Expired
Bibliographic Data
(52) Canadian Patent Classification (CPC):
  • 167/301
  • 8/53
  • 134/3.1
(51) International Patent Classification (IPC):
  • C11D 1/32 (2006.01)
  • A61K 8/64 (2006.01)
  • A61K 8/65 (2006.01)
  • C11D 1/22 (2006.01)
  • C11D 3/384 (2006.01)
(72) Inventors :
  • MARSH, ROBERT A. (Not Available)
  • MACKIE, GORDON J. (Not Available)
  • HALE, PETER (Not Available)
(73) Owners :
  • THE PROCTER AND GAMBLE COMPANY (Not Available)
(71) Applicants :
(74) Agent: NA
(74) Associate agent: NA
(45) Issued: 1979-07-24
(22) Filed Date:
Availability of licence: N/A
(25) Language of filing: English

Patent Cooperation Treaty (PCT): No

(30) Application Priority Data: None

Abstracts

English Abstract






DETERGENT COMPOSITIONS
R.A. Marsh, G.J. Mackie, P. Hale



ABSTRACT OF THE DISCLOSURE
Detergent Compositions having a protective effect on
keratinous material incorporate a proteinaceous material whose
primary amino or carboxylic acid side chain groups have been
modified by reaction with C1-C7 acyl- or alkyl- group-containing
materials respectively to give a modified protein of isoionic
point (pI) less than pH 6. Granular, bar and liquid detergent
formulations embodying the invention are disclosed.


Claims

Note: Claims are shown in the official language in which they were submitted.



The embodiments of the invention in which an ex-
clusive property or privilege is claimed are defined as follows:
1. A composition for protecting keratinous
material from the deleterious effects of detergents or from
adverse climatic conditions, said composition comprising:
(a) from 0.1 to 90% by weight of a foaming
non cationic detergent material; and
(b) from 0.1 to 20% by weight of a chemically
modified protein having an isoionic point
(pI) less than pH of 6, said chemically
modified protein being selected from the
group consisting of oxybutylated hydrolyzed
protein and acetylated hydrolyzed protein.
2. A composition as recited in Claim 1, in which
the chemically modified protein is present in an amount
between 2 and 6% by weight.
3. A composition as recited in Claim 2, in
which the chemically modified protein has a molecular
weight in the range from 2000 to 5000.
4. A composition as recited in Claim 3, in
which the chemically modified protein is oxybutylated base
hydrolyzed soy protein isolate.
5. A composition as recited in Claim 3, in
which the chemically modified protein is acetylated base
hydrolyzed soy protein isolate.
6. A composition as recited in Claim 3, in
which the chemically modified protein is acetylated base
hydrolyzed whey.
7. A composition as recited in Claim 3, in
which the chemically modified protein is acetylated base
hydrolyzed protein derived from yeast.



33


8. A composition as recited in Claim 3, in which
the chemically modified protein has a pI in the range of from
pH2.5 to pH5.5

34

Description

Note: Descriptions are shown in the official language in which they were submitted.


FIELD OF THE INVENTION
This invention relates to compositions which protect
keratinous material, such as skin or hair, from the deleterious
effects of detergents or other harsh materials such as
solvents, and from adverse climatic conditions.
The compositions of the invention accordingly help to
maintain the keratinous material in good condition. The
invention also relates to a method of treating keratin.
BACKGROUND OF THE INVENTION
The deleterious effects of compositions containing
surfactants upon keratin are well known. These effects are
caused, it is thought, by penetration of the surfactant into
the keratin surface leading to "leaching out" of oils and
moisturising components essential for good condition of the
keratin. This penetration by surfactant and "leaching out"
of essential oils also affects the ability of the keratin,
particularly in the case of skin, to retain water within the
tissue and this again leads to poor condition of the keratinous
material.
Many attempts have been made in the past to provide


-- 1 -- .

1059C~0Z
compositions for maintaining or improving the condition of
skin and hair. The application of protein to skin and hair as
cosmetic treatments probably antedates recorded history.
Casein, in the form of milk, has been used as a time-honoured
beautifier and more recently has been recommended for use in
toilet soaps. U.K. Patent 1,160,485 describes the inclusion
of partially degraded water soluble proteins having a gel
strength of zero Bloom grams in detergent compositions and
lotions for application to skin as dishwashing liquids.
German Offenleyungsschriften (Published Specifications)
2,151,739 and 2,151,740 describe certain fatty derivatives
of low-molecular-weight aminolysates suitable for use in
shampoos. U.K. Patent 1,122,076 describes the preparation of
low-molecular-weight, alcohol-soluble protein esters suitable
for use in hair-spray formulations. Various low-molecular-
weight polypeptides or modified po-lypeptides are commercially
available and recommended for use in cosmetic and shampoo
formulations, for instance "Hydro Pro 220"1 and "Hydro Pro
330~2 marketed by The Stepan Chemical Company; and "Wilson
X250",3 "Wilson X1000" and "Wilson Aqua Pro"5 marketed by the
Wilson Chemical Company. However, it has been found that none
of these compositions are especially effective in protecting
keratin from the action of harsh detergents, and this is
particularly true when the proteins are incorporated in the
detergent composition itself. The emolliency of these
compositions can often be improved by addition of fatty or
oily materials but, when used in dishwashing liquids, this
usually leads to loss of foaming power or aesthetic changes
which are generally considered undesirable by consumers.


1-5 inclusive. The terms bearing these numerals are all
trade marks.


lOS9~0Z

SU~lARY OF THE INVENTION
The present invention therefore provides protein-
containing compositions which are particularly effective in
protecting keratinous material, such as skin or hair, from the
deleterious effects of detergents and other harsh materials
and from adverse climatic conditions, which compositions are
effective even when applied to keratin in foaming detergent
solutions and which result in no loss of foaming or cleaning
power for detergent solutions containing them.
Accordingly, the present invention provides a composi-
tion for protecting keratinous material from the deleterious
effects of detergent and other harsh materials and from adverse
climatic conditions, the composition comprising a foaming,
non-cationic detergent material and a chemically modified
protein (as hereinafter defined) having an isoionic point
less than pH6 in which at least a portion of the precursor
protein carboxylic acid groups or primary amino groups
replaced by -(CO)Q and -NHYQ respectively, where Y is a direct
link, carbonyl or sulphonyl groups and Q represents R, SR, OR
or NHR, with R comprising alkyl, alkenyl, aryl, cycloalkyl
or heterocyclyl moieties and containing no more than seven
carbon atoms, the alkyl or alkenyl moieties optionally being
interrupted by heteroatoms or substituted with nonionic or
cationic radicals.
In a mor~ particular aspect, the present invention
resides in a composition for protecting keratinous material
from the deleterious effects of detergents or from adverse
climatic conditions, said composition comprising:
(a) from 0.1 to 90% by weight of a foaming non
cationic detergent material; and
(b) from 0.1 to 20~ by weight of a chemically

modified protein having an isoionic point

~s9ooz

(pI) less than pH of 6, said chemically
modified protein being selected from the group
consisting of oxybutylated hydrolyzed protein
and acetylated hydrolyzed protein.

DETAILED DESC~IPTION OF THE INVENTION




... . _ _
In this specification a modified protein means a
product, other than a derived protein, obtained in one or rnore
stages by chemical modification of a precursor protein, a
precursor protein being a non-enzymic protein chosen from
natural, derived, synthetic or biosynthetic proteins, and a
derived protein being the product of hydrolytic, ammoniolytic,
enzymic or thermal degradation of a protein material. Precur-
sor protein also covers low molecular weight materials which
may, more strictly, be termed polypeptides and peptides.
According to a further aspect of the invention, there
is provided a method of protecting keratinous material from the
deleterious effects of detergent and other harsh materials,
the method comprising treating keratin with an aqueous solution
or dispersion of the composition of the invention.
The precursor proteins suitable for use, after modifi-
cation, in the compositions of the invention, may be chosen
from natural, derived, synthetic or biosynthetic proteins.
Natural proteins may be of either animal or vegetable origin
and include simple and con~ugated protein.
Typical natural proteins include intracellular proteins
and globular proteins such as those present in blood plasma

and milk, as well as solubilized colla;gen and protein
isolates from nuts, cereals, etc. such as soybean isolate,
peanut protein, cotton seed protein, etc. Derived proteins
may be obtained from many sources, for instance by hydrolytic,
ammoniolytic, thermal or enzyme degradation of globular or
structural proteins such as keratin, collagen, fibrinogen,


lOS900Z

myosin, whey, egg white, casein or vegetable proteins such as
those obtained from cereals, nuts, soybean curd or the protein-
rich residues from seedoil manufacture. Preferred synthetic
proteins include polylysine and unicellular proteins obtained
from bacterial micro-organisms.
Protein primary amino group modification takes place
primarily at lysine groups and, desirably, the precursor
protein should have at least 4 gms., preferably at least 6 gms.
of lysine per 100 gms. of protein. Suitable precursor proteins
in this class include the milk proteins, casein and whey, and
egg white proteins (primarily ovalbumin), bacterially derived
unicellular protein and soy, or derived proteins prepared
therefrom. In addition, suitable precursor proteins should
comprise at least 20 gms. of aspartyl and glutamyl groups, in
total, per 100 gms. of protein. Amino acid contents for a wide
variety of proteins are given on page 105 of Amino Acids and
Proteins by D.M. Greenberg published by Charles Thomas in 1951.
Of the above-detailed modified proteins, preferred are
those proteins in which R has the formula:

CH2~(CHQ )p-(CH2)~-Q
in which Ql is Rl, -SRl, -ORl, or NHR in which R is
a hydrogen atom or an alkyl or alkenyl moiety, p is 0
or 1 and q is from 0 to (5-p).
Preferred classes of modified protein falling within
the above definitions are those in which R is represented by:
1) CH2-CH(OH) - (CH2)r-H in which r is from 0 to 4, and
2) CH2-(CH2)r-H in which r is from 0 to 3.
The modified proteins of the present invention are made
by modification of protein precursor side chains comprising
free carboxylic acid groups or free primary amino groups. In

particular, modification of acid groups preferably takes the



~ _ 5 _

1{~59~02

form of oxyalkylation and esterification of amidation.
Modification of the basic groups, on the other hand, pre-
ferably takes the form of acylation and alkylation.




- 5a -

lOS900Z
Methods of preparation of proteins having these func-
tional substituents are well known in the art and the neces-
sary preparative techniques are described in "The Chemical
Modification of Proteins" by G.E. Means and R.E. Feaney pub-
lished by Holden-Day Inc. in 1971.
Although the principal reactive centres are the protein
side-chains comprising carboxylic acid or primary amino
groups, simultaneous modification of other reactive centres
such as sulphydryl, aliphatic or phenolic hydroxy, imidazole
or guanidino groups, may also occur. An exemplary modified
protein has, as substituents, hydroxyalkyl ester groups
derived from the carboxylic acid groups of the unmodified sub-
strate and prepared by reaction of the protein with an epoxide,
for example but-l-ene oxide.
In preferred embodiments of the invention, the proteins
may be acylated or alkylated via primary amino groups. Acyla-
tion may be performed by using the appropriate acid anhydride
or N-carboxy anhydride. In the latter case, this results in
acylation predominantly at amino groups. In the former case,
if the acid anhydride is cyclic, the modification leads to
acidic substituents which should be neutralized, for
instance by esterification. Reactions analogous to acylation
may also be performed. Thus, primary amino groups may be
converted to unsymmetrical disubstituted ureas by treatment
with isocyanates. In addition, sulphonamide derivatives of
proteins may be prepared, for instance, by reaction of protein
primary amino groups with sulphonyl halides.
As stated above, exemplary modified proteins to be
used in the present invention include hydroxyalkylation products
of acid or base hydrolysed or ammonolysed soyprotein isdlates,
with molecular weights in the region from 1,000 to 10,000.
Such modified proteins have proportionately fewer carboxylic



-- 6 --

1059111 02
acid groups and more carboxylic ester groups than the un-
modified proteins. Lower alkyl or hydroxyalkyl ester
derivatives are preferred. They may be prepared simply by
treatment with an alkylene oxide, in which case esterification
may be accompanied by hydroxyalkylation of other reactive
species, for example, primary amino groups. The extent of
such N-hydroxyalkylation depends primarily on the pH
conditions employed. If the pH of the reaction medium is
held in the acid region during the course of the reaction,
then the degree of N-hydroxyalkylation is rather less than if
the pH is allowed to rise during the reaction.
Where it is intended to modify the carboxyl groups
of the proteins, reaction conditions are adjusted so that at
least 5%, preferably at least 20% and desirably at least 35%
of the free carboxylic acid groups are modified. Modification
of more than about 50% of the free carboxyl groups is difficult
and also undesirable for the purposes of the present invention.
Particularly highly preferred proteins are the N-acyl
and N-sulphonyl derivatives of degraded proteins, particularly
of degraded casein, soyprotein and collagen (gelatin). The acyl

group may be introduced by allowing an aqueous solution of the
protein to stand at a temperature of 10 - 20C for 1 - 2 hours
with the anhydride of the appropriate carboxylic acids, in partic-
ular acetic, propionic, n- and iso- butyric acids. The reaction

may be conducted at a pH of from 6 to 9, especially from 7 to 8,
using a suitable buffer to promote acylation rather than
hydrolysis of the anhydride which occurs as a side-reaction.
The degree of acylation of the protein will depend upon
the relative amounts of protein and anhydride used.l Generally
at least 20% of the protein primary amino groups will be

acylated, preferably at least 40% and especially at least 60%;
80% or more acylation is readily achievable using a large


lOS9~OZ

(20 to 30 fold) excess of anhydride.
Condensation products with sulphonic acid derivatives
are generally prepared via the corresponding sulphonyl chloride
compounds. The sulphonyl chloride compound is conveniently
obtained from the corresponding sulphonic acid by treatment with
phosphorus pentachloride and is treated with an alkaline
solution or dispersion of the protein at 50 - lOQ C for,
e.g. 4 - 5 hours, with constant addition of aqueous alkali
to maintain an alkaline pH.
Particularly preferred proteins for use in the composi-
tions of the invention have characteristic values of molecular
weight and isoionic-point pH and these will now be discussed in
some detail.
It will be appreciated that the molecules of a protein
vary widely in their size and complexity and that the molecular
weight of a protein is necessarily an imprecise quantity. The
molecular weight of a protein may be specified by defining the
molecular weight distribution of the molecules of the protein,
but it is usual to define, instead, the average molecular
weight of the protein sample because it is an average molecular
weight which is measured by most physical techniques. Such
an average is only an approximate guide, however, to the actual
molecular weight distribution of the sample. Also, it should
be appreciated that the average molecular weight as measured
may vary from one measuring technique to another although the
differences between the results of the various techniques
generally diminish towards lower molecular weights. In this
specification, one method employed for determining average
molecular weights of proteins (for molecular weights greater
than about 5000) makes use of viscometric measurements of
buffered protein solutions. The intrinsic viscosity of a

buffered protein solution is known to be primarily dependent


~os9ooz

upon the overall length of the protein coil and to be rela-
tively independent of the nature of the sidechain and end
groups of the protein. There is, therefore, a relationship
between intrinsic viscosity and the average molecular weight
of the protein, which may be expressed as

[~] = K . M a [Staudinger's Equation]
where X and a are constants for a particular source of protein.
It is thus straightforward to determine molecular weights from
viscosity measurements, knowing K and a, and this is fully
described in Macromolecular Chemistry of Gelatin, page 72,
by A. Veiss, and in Biochimica et Bisphysica Acta, 57, 222 ~ 9
(1961) by J. Bello, H.R. Bello, and J.R. Vinograd.
However, the viscosity method is not very accurate at
molecular weights of about 5000 and below and ultracentrifuge
techniques reveal only small differences in observed values
for molecular weights up to about 80,000.
When measured by the above methods, the precursor and
modified proteins of the present invention generally have
molecular weights in the range from 300 to 50,000, preferably
from 600 to 20,000, desirably from 1,000 to 10,000 and more
especially from 2,000 to 5,000.
The modified proteins may be present in the compositions
of the invention in an amount from 0.1% up to 20%, but gener-
ally in an amount between 1% and 10%, preferably between 2%
and 6%, by weight of the composition.
Protein molecules, having both acidic and basic side
chains, are charged in both acidic and basic solutions and thus
are amphoteric in nature. The pH at which equal concentrations
of protein anions and cations exist in solution is known as
the isoionic point, and in the present invention, the isoionic
point of the modified proteins must be less than 6, generally
in the range 2.5 to 5.5, and preferably in the range 2.5 to

~)59002

4Ø The isoionic point pH may be determined in the follow-
ing manner:-

"Amberlite" acid resin (IR 120) and base resin (IR400) are washed with several volumes of water, filtered and
mixed in the ratio 0.4:1. A solution (20 mls.) of protein
(3~) and urea (20% by weight) is prepared with minimum warming
and allowed to cool to constant temperature. The resin
mixture (8.4g.) is added, the solution is stirred for five
minutes, the mixture is filtered and the pH of the filtrate is
the isoionic point pH of the protein.
Specific preparative methods for modified proteins
useful in the present invention are as follows:
Oxyalkylation of Proteins
The following procedure is typical of methods which
may be used for oxyalkylation of proteins. In this instance,
the method is described with reference to the oxybutylation
of alkali-degraded soyprotein.
Promine F (50g), an edible grade soybean isolate
(Promine F being a Trade Mark) was added to vigorously stirred
warm water (150 mls.) to form a slurry. The mixture was
heated to a slurry temperature of 90-95C. and sodium hydroxide
pellets (5g) were added. After stirring for 4 hours, the
liquid was cooled to 30C. and treated with hydrogen peroxide
solution (2 mls. of 30~). The solution was stirred for 20
minutes at room temperature and the pH of the solution was
adjusted to 5-6. The hydrolysis solution was then diluted
with water (150 mls.), but-l-ene oxide (50 mls.) was added and
the solution was stirred at 40-60C. for a period of 24-31
hours. After cooling, excess epoxide was distilled off, the

* "Amberlite" is a trade mark of the Rohm and Haas Company

for a series of ion-exchange resins.


-- 10 --

l()S9~0~
solution was neutralised and the product isolated by freeze
drying.
Variations of the above method may, of course, be
employed. Thus the soyprotein may be degraded using a medium
strength, 1:5 ammonia/water solution, or may be degraded by
acid hydrolysis or by reductive cleavage with, for example,
sodium borohydride. Other types of modified proteins may
be used in place of soy derived-protein, for example casein,
gliadin, zein and serum or egg albumins. Other processes may
be employed to obtain oxyalkylated derivatives, for example,
reaction with anhydrous alkylene carbonates.
Acyl derivatives of proteins
Promine F (120g) was first hydrolysed in water
(360 mls.) containing sodium hydroxide (12g) as described
earlier. After cooling, acetic anhydride (60 mls.) was added
slowly to the solution over a period of about 1 hour, keeping
the pH of the solution at about 7 to 8, by the addition of
further sodium hydroxide, and maintaining the temperature
below 20. The solution was then stirred for a further hour,
and the protein was precipitated by acidifying to pH3 and
cooling. The precipitate was washed with cold acid and the
protein obtained by freeze drying. It had an isoionic point
pH of about 3, a molecular weight of about 3000 and contained
substantially no unacetylated ~ -amino groups.
A similar procedure was used to obtain higher acyl
derivatives, although somewhat longer reaction times were
required in these cases. The procedure was also applicable to
the acylation of whole protein, such as whole casein, whey,
serum albumin, etc.
The optimum choice of protein for any particular
composition depends to a certain extend upon the pH of the com-
position in use, i.e., the pH of the carrier upon application

-- 11 --

lOS9C~OZ
to keratin. This in-use pH may, depending upon the type of
application, be the pH of the composition itself, or be the
pH of an aeqeous solution or dispersion of the composition at
a concentration of use which may be as little as 0.01%.
In order to obtain the maximum occlusive benefit,
compositions of the invention should have an in-use pH as
different as possible from th~ pI of the modified protein.
For modified proteins having a pIc6, the in-use pH is

preferably greater than pH6 and desirably is greater than
(pI + 2).
The in-use pH of the compositions of the invention may
vary widely, of course, depending upon the purpose and manner
of use of the compositions. Liquid compositions designed for
shampoos are generally applied to hair in medium/high concentra-
tion aqueous solution, and the in-use pH is close to the pH of
the composition itself. This may be any pH in the range,
generally, from 4 to 9. Detergent compositions such as liquid
dishwashing compositions, bathing compositions and heavy-

duty granular or liquid detergents are usually 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 from 0.01~ to 2% by weight. Builder free detergent
compositions used, for instance, as light-duty detergents gener-
ally have an in-use pH of about 7; built heavy-duty detergents
generally have an in-use pH in the alkaline range up to a pH
of about ll. Soap bar compositions are applied to skin as an
aqueous solution or dispersion of the soap bar ingredients at
a concentration, generally in the range from 5 to 15 wt%. The
pH of the soap dispersion may vary, depending upon the type of

soap bar employed, from a pH of 5.5 to about 10.5.
Surfactant materials which may be used in the composi-
tions of the invention can be selected from foaming water-
soluble soap and synthetic anionic, nonionic, zwitterionic


_ 12 -
.

1059~30;2
and amphoteric detergents described as below. Cationic mate-
rials may be present but preferably only in the presence of
other types of detergent.
A. Anionic Soap and Non-Soap Synthetic Detergents
This class of detergents includes ordinary alkali
soaps such as the sodium, potassium, ammonium, alkyl ammonium
and alkylolammonium salts of higher fatty acids containing from
8 to 24 carbon atoms and preferably from 10 to 20 carbon atoms.
Suitable fatty acids can be obtained from natural sources, such
as plant or animal esters (e.g. palm oil, coconut oil, babassu
oil, soybean oil, castor oil, tallow, whale and fish oils,
grease, lard, and mixtures thereof). The fatty acids also
can be synthetically prepared (e.g. by the oxidation of
petroleum or by hydrogenation of carbon monoxide by the Fischer
Tropsch process). Resin acids are suitable, such as rosin
and those resin acids in tall oil. ~aphthenic acids are also
suitable. Sodium and potassium soaps can be made by direct
saponification of the fats and oils or by the neutralization
of the free fatty acids which are prepared in a separate
manufacturing process. Particularly useful are the sodium,
potassium, and triethanol-ammonium salts of the mixtures of
fatty acids derived from coconut oil and tallow, e.g. sodium
or potassium tallow and coconut soaps.
This class of detergents also includes water-soluble
salts, particularly the alkali metal salts, of organic sul-
phuric reaction products having in their molecular structure an
alkyl radical containing from 8 to 22 carbon atoms and a sul-
phonic acid or sluphuric acid ester radical. (Included in the
term alkyl is the alkyl portion of higher acyl radicals).
Examples of this group of synthetic detergents which form a
part of the preferred compositions of the present invention are
the alkali metal, e.g. sodium or potassium, alkyl sulphates,



- 13 -

105900Z
especially those obtained b~ sulphating the higher alcohols
(8 to 18 carbon atoms) produced by reducing the glycerides of
tallow or coconut oil; the alkali metal olefin sulphonates of
from 8 to 24 carbon atoms described, for example, in U.S.
Patent 3,332,880; and the alkali metal alkyl glyceryl ether-
sulphonates, especially those ethers of the higher alcohols
derived from tallow and coconut oil. Other anionic detergents
include the alkali metal alkylbenzene sulphonates, in which the
alkyl group contains from 9 to 15 carbon atoms, including
those of the types described in United Sta.es Patents Nos.
2,220,099 and 2,477,383 (the alkyl radical can be a straight
or branched aliphatic chain); sodium coconut oil fatty acid
monoglyceride sulphates and sulphonates; salts of alkyl
phenol ethylene oxide ether sulphates with 1 to 12 units of
ethylene oxide per molecule and in which the alkyl radicals
contain from 8 to 18 carbon atoms; the reaction product of
fatty acids esterified with isethionic and neutralized with
sodium hydroxide where, for example, the fatty acid is oleic
or derived from coconut oil; sodium or potassium salts of
fatty acid amides of a methyl tauride in which the fatty
acids, for example, are derived from coconut oil; sodium or
potassium ~-acetoxy- or ~-acetamido-alkanesulphonates where
the alkane has from 8 to 22 carbon atoms; and others known in
the art. A number are speciflcally set forth in United States
Patents Nos. 2,286,921; 2,486,922; and 2,396,278.
A further class of surfactants falling within this
category are water-soluble salts of the organic, sulphuric
acid reaction products of straight or branched~ saturated, ali-
phatic hydrocarbon radicals having from 8 to 24, preferably
from 12 to 18 carbon atoms, particularly hydrocarbon radicals
of the methane series, including iso-, neo-, meso-, and n-
paraffins. Water soluble salts of C14-C16 sulphonated paraffins



- 14 -


105900Z
are especially preferred.
Other synthetic anionic detergents useful herein are
alkyl ether sulphates. These materials have the formula
R 0(C2H4O)xSO3 wherein R is alkyl or alkenyl of about 8 to
24 carbon atoms, x is 1 to 30, and M is a salt-forming
cation selected from alkali metal, ammonium and dimethyl-,
trimethyl-, triethyl-, dimethanol-, diethanol-, trimethanol-
and triethanol- ammonium cations.
The alkyl ether sulphates are condensation products
of ethylene oxide and monohydric alcohols having about 8 to
24 carbon atoms. Preferably, R2 has 14 to 18 carbon atoms.
The alcohols can be derived from fats, e.g., coconut oil or
tallow, or can be synthetic. Lauryl alcohol and straight-
chain alcohols derived from tallow are preferred herein. Such
alcohols are reacted with from 1 to 12, especially 6, molar
proportions of ethylene oxide and the resulting mixture of
molecular species, having, for example an average of 6 moles
of ethylene oxide per mole of alcohol, is sulphated and
neutralized.
The alkyl ether sulphates are described in U.S. Patent
3,332,876.
B. Nonionic Synthetic Detergents
Nonionic synthetic detergents may be broadly defined as
compounds produced by the condensation of alkylene oxide
groups (hydrophilic in nature) with an organic hydrophobic
compound, which may be aliphatic or alkyl aromatic in nature.
One class of nonionic synthetic detergents is
commercially available under the trade mark of 'Pluronic'.
These compounds are formed by condensing ethylene oxide with a
hydrophobic base having a molecular weight in the range 1500 -
1800 and formed by the condensation of propylene oxide with
propylene glycol.



- 15 -

l~S9002

Other suitable nonionic synthetic detergents include
the following:
1. The polyethylene oxide condensates of alkyl phenol,
e.g. the condensation products of alkyl phenols
having an alkyl group containing from 6 to 12 carbon
atoms, in either a straight-chain or branched-
chain configuration, with ethylene oxide, the ethylene
oxide being present in amounts e~ual to 5 to 25 moles
of ethylene oxide per mole of alkyl phenol. The
alkyl substituent in such compounds may be derived,
for example, from polymerised propylene, diisobuty-
lene, octene or nonene. Specific examples include
nonyl phenol condensed with 20 moles of ethylene
oxide, dodecyl phenol condensed with 15 moles of
ethylene oxide and diiso-octyl phenol condensed with
15 moles of ethylene oxide.
2. Those derived from the condensation of ethylene oxide
with a hydrophobic base formed by the product result-
ing from the reaction of propylene oxide and ethylene
diamine. Bases having a molecular weight of the order
of 2,500 to 3,000 are satisfactory and typical com-
pounds contain from 40% to 80% polyoxyethylene by
weight and have a molecular weight of from 5,000 to
11, 000 -
3. The condensation product of aliphetic alcohols having
from 8 to 24 carbon atoms, in either straight-chain
or branched chain configuration with ethylene oxide,
e.g. a coconut alcohol-ethylene oxide condensate

having from 5 to 30 moles of ethylene oxide per mole
of coconut alcohol, the coconut alcohol fraction


having from 10 to 14 carbon atoms.
4. Other particularly preferred materials are synthetic


- 16 -

~OS9C~02

primary alcohol ethoxylates available from the Shell
Oil Company under the trade marks 'Dobanol' and
'Neodol', from Imperial Chemical Industries Ltd,
under the trade mark 'Synperonic', and from
Liquichimica SA under the trade mark 'Lial'.
Specific examples of these synthetic alcohol ethoxy-
lates include "Dobanol 45E7", a C14-C15 predominantly
linear alcohol containing up to 25% 2-methyl branch-
ing condensed with an average of seven moles ofi
ethylene oxide, "Dobanol 91E8", a Cg-Cll predomin-
antly linear alcohol condensed with an average of
eight moles of ethylene oxide, and "Synperonic E-3",
a condensation product of 3 moles of ethylene oxide
with one mole of an alcohol mixture comprising a 2:1
ratio of C13-C15 primary alcohols with 50~ 2-methyl
branching.
5. A detergent having the formula R R R5N-~0 (amine
oxide detergent) wherein R3 is an alkyl group contain-
ing from 10 to 28 carbon atoms, from 0 to 2 hydroxy
groups and from 0 to 5 ether linkages, there
being at least one moiety of R3 which is an alkyl
group containing from 10 to 18 carbon atoms and 0
ether linkages, and R4 and, R5 are each selected
from alkyl radicals and hydroxyalkyl radicals
containing from 1 to 3 carbon atoms.
Specific examples of amine oxide detergents include:
dimethyldodecylamine oxide, dimethyltetradecylamine
oxide, ethylmethyltetradecylamine oxide, cetyldime-
thylamine oxide, dimethylstearylamine oxide,
cetylethylpropylamine oxide, diethyldodecylamine
oxide, diethyltetradecylamine oxide, dipropyldode-

cylamine oxide, bis-(2-hydroxyethyl) dodecylamine


- 17 -

1059002

oxide, bis-(2-hydroxyethyl)-3-dodecoxy-1-hydroxy-
propylamine oxide, (2-hydroxypropyl)methyltetradè-
cylamine oxide, dimethyl~leylamine oxide, dimethyl-
(2-hydroxydodecyl) amine oxide, and the corresponding
decyl, hexadecyl and octadecyl homologues of the
above compounds. O
6. A detergent having the formula R -S-R wherein R
and R4 are as defined above. Specific examples of
sulphoxide detergents include dodecyl methyl
sulphoxide, tetradecyl methyl sulphoxide,
3-hydroxytridecyl methyl sulphoxide, 3-methoxy-
tridecyl methyl sulphoxide, 3-hydroxy-4-dodecoxy-
butyl methyl sulphoxide, octadecyl 2-hydroxyethyl
sulphoxide and dodecyleth~l sulphoxide.
7. The ammonia, monethanol and diethanol amides of
fatty acids having an acyl moiety of from 8 to 18
carbon atoms. These acyl moieties are normally
derived from naturally occurring glycerides, e.g.
coconut oil, palm oil, soybean oil and tallow
but can be derived synthetically, e.g. by the oxida-
tion of petroleum, or by hydrogenation of carbon
monoxide by the Fischer Tropsch process.
C. Ampholytic Synthetic Detergents
Ampholytic synthetic detergents can be broadly described
as derivatives of aliphatic or aliphatic derivatives of
heterocyclic secondary and tertiary amines, in which the
aliphatic radical may be straight-chain or branched and
wherein one of the aliphatic substituents contain from 8 to 18
carbon atoms and at least one contains an anionic water-
solubilizing group, e.g. carboxy, sulpho or sulphato. Examples
of compounds falling within this definition are sodium 3-

(dodecylamino)-propionate, sodium 3-(dodecylamino)propane-1-


- 18 -

~os9ooz
sulphonate, sodium 2-~dodecyl-amino)-ethylsulphate, sodium 2-
(dimethylamino)-octadecanoate, disodium octadecyl-iminodiaze-
tate, sodium l-carboxymethyl-2-undecyl imidazole, and sodium
N,N-bis-(2-hydroxyethyl)-2-sulphato 3-dodecoxypropylamine.
D. Zwitterionic Synthetic Detergents
Zwitterionic synthetic detergents can be broadly described
as derivatives of aliphatic quaternary ammonium and phosphonium
or tertiary sulphonium compounds in which the cationic atom
may be part of a heterocyclic ring, and in which the aliphatic
radical may be straight-chain or branched and wherein one
of the aliphatic substituents contains from 3 to 18 carbon
atoms, and at least one aliphatic substituent contains an
anionic water-solubilizing group, e.g. carboxy, sulpho or
sulphato.
Examples of compounds falling within this definition are
3-(N,N-dimethyl-N-hexadecyl-ammonio)-2-hydroxypropane-1-
sulphonate, 3-(N,N-dimethyl-N-hexadecylammonio)-propane-l-
sulphonate, 2-(N,N-dimethyl-N-dodecylammonio)acetate, 3-
~N,N-dimethyl-N-dodecylammonio) propionate, 2-N,N-dimethyl-
N-octadecylammonio)-ethyl sulphate, 2-(S-methyl-S-tert.hexa-
decyl-sulphonio)ethane-l- sulphonate, 3-(S-methyl-S-dodecyl-
sulphonio) propionate, 4-(S-methyl-S-tetradecylsulphonio)
butyrate, l-(2-hydroxy-ethyl) 2-undecyl imidazolium-l-
acetate, 2-(trimethylammonio) octadecanoate, and 3-(N,N-
bis-(2-hydroxyethyl)-N-octadecylammonio)-2-hydroxy propane-l-
sulphonate and 3-(N,N-dimethyl-N-l-methyl alkyl ammonio)-2-
hydroxy propane -l-sulphonate, wherein alkyl averages 13.5
to 14.5 carbon atoms in length. Some of these detergents
are described in U.S. Patents Nos. 2,129,264; 2,178,353;
2,774,786; 2,813,898 and 2,828,332.
The soap and non-soap anionic~ nonionic and zwitterionic
detergent surfactants mentioned above can be used as the sole

-- 19 --

1059002
surface-active agents, or the various examples may be mixed
when used in the practice of the invention. Expecially pre-
ferred are anionic and nonionic surface-active agents. The
amount of surface-active agent incorporated in the preparation
depends upon the intendea use of the particular formulation.
Thus it will relate to the weight of the preparation as a
whole, when it is applied directly to skin or hair, e.g. as
a shampoo, or the concentration at which it will be used as

a solution in, for example, dishwashing water or bath water.
In most cases a content within the range of 0.1% to 90% by

weight of the preparation is suitable. More particularly,
detergent compositions for cleaning purposes will generally
comprise between 5 and 50% by weight of surface-active agent,
preferably between 10 aXd 30% of surface active agent.
The invention is applicable to a variety of detergent
compositions which may come into contact with keratin in the
normal course of use, for example dishwashing liquids, hair
shampoos, bathing compositions, heavy-duty detergent composi-
tions, hard-surface-cleaning compositions and bar soaps. The

physical form of the composition may vary widely, from granular
solids, through gels and creams, to viscous or mobile liquid
compositions. Dishwashing compositions are generally liquid
and comprise mixtures of water and foaming detergents.
Granular detergent compositions on the other hand, may contain
little or no free water.
The preferred liquid or granular detergent compositions
for use, for instance, as heavy-duty detergents, dishwashing
compositions or shampoos, comprise between 5 and 50% by weight
of foaming detergent. More especially, the foaming detergent

is selected from:
a. From 0~ to 45% of a water-soluble hydrocarbon sulphate
of the general formula R O(C2H4O)nSO3M wherein R is a



- 20 -

1059~30Z
straight or branched/ saturated or unsaturated aliphatic,
hydrocarbon radical having from 8 to 24 carbon atoms, n
is from 1 to 12; and M is an alkali or alkali earth
metal, ammonium or dimethyl-, trimethyl-, triethyl-,
dimethanol-, diethanol-, trimethanol- or triethanol-
ammonium cation;
b. From 0% to 45% by weight of a water-soluble hydrocarbon
sulphonate of the general formula R SO3M; wherein R3 is
a straight or branched chain saturated or unsaturated C8-

C24 aliphatic hydrocarbon radical or a C8-C18 straight or
branched chain alkyl benzene radical and M is as defined
above;
c. From 0~ to 45% by weight of a water-soluble hydrocarbon
sulphate of the general formula R OSO3M; where M and R2
are as defined above;
d. From 0% to 10% by weight of an ammonia, monoethanol or
diethanol amide of a fatty acid having an acyl moiety
of from 8 to 18 carbon atoms;
e. Up to 40% by weight of the condensation product of from
3 to 25 moles of an alkylene oxide, preferably ethylene
or propylene oxide, and one mole of an organic, hydro-
phobic compound, aliphatic or alkyl aromatic in nature,
the latter having from 8 to 24 carbon atoms; and
f. From 0% to 10% of a trialkyl amine oxide of formula

R4R5R6N ->O
wherein R4 is an alkyl group containing from 10 to 28
carbon atoms and R5 and R6 are each selected from alkyl
radicals and hydroxyalkyl radicals containing from 1 to
3 carbon atoms.
Granular detergents conventionally contain from 5% to
about 20% by weight of the composition of foaming surfactant

normally a el0-C14 linear alkyl benzene sulphonate, alone or in


- 21 -

~0S9002
admixture with a h~gher alk~l sulp~ate such as a synthetic or
naturally der~ved C16-C18 al~y~l sulpha$e, e~g. tallow alkyl sul-
phate. Optional ingredients of such mixtures are also higher
alkyl ethoxysulphates such as those disclosed in German Laid Open
Applications DOS Nos. 2-355940 and 2355983. ~`~t~
Nonionic surfactants such as ethoxylated primary of
secondary alcohols and/or alkyl amides and ethanolamides may also
be present at levels up to 10% of the composition.
Dishwashing liquid products in accordance with the
invention can contain up to 45% surfactant by weight of the
composition. Typical formulations include 15~ - 30% of a linear
alkylbenzene sulphonate and 15% - 30% of a C10-C18 li~near alkyl
ethoxy sulphate containing an average of 1 - ~ éthoxy groups.
Another preferred formulation includes 5% - 15% of a C14-C16
paraffin sulphonate, 5 - 15% of C12 alkyl triethoxysulphate and
1% - 10% of each of C12 amine oxide, coconut alcohol hexaethoxylate
and lauric diethanolamide. Another dishwashing liquid having
mild properties to skin includes from about 15% to about 25~ of
a C12-C14 alkyl ether sulphate containing an average of from
about 3 to about 12 ethylene oxide groups, up to about 10% of a
C12-C14 alkyl sulphate, ~from about 1% to about 5% of a C12-C14
alkyl glyceryl e~her sulphonate and from about 2% to about 6
of a C12-C14 alkyl dilower alkyl amine oxide.
A further preferred liquid detergent compositior con-
tains from 10% - 25% by weight of a water-soluble saturated hydro-
carbon sulphonate, from 1~ - 10~ by weight of an alkyl ether
sulphate and from 1% - 15~ by weight of a water soluble solvent
such as a lower alkanol, in addition to the usual minor ingredients
such as perfume, colour, buffers, anti-tarnish agents etc.
The liquid detergent or gel compositions of the invention
generally comprise a carrier based upon water and/or a water-
soluble solvent. Suitable solvents include C2 8 mono and di-

alcohols, e.g. ethanol, butanol, methyl propanol-l and -2, amylol

1059~02

or pentanol, butanediol, toluol, benzyl carbinol, ethyleneglycol
monobutyl ether, propyleneglycol propyl ether and diethyleneglycol
dimethyl ether. They are generally present in amounts up to 15%
by weight of the composition. Additional components of liquid
detergent compositions include buffer materials, foam boosters,
such as higher alkyl (C12-C14) amine oxides and alkylolamides of
C10-C14 carboxylic acids, thickeners, preservatives, opacifiers,
perfumes, dyes, fluorescers, tarnish inhibitors, bactericides,
hydrophobic oily materials and hydrotropes. Commonly employed
hydrotropes include conventional lower alkylar ~ sulphonates such
as sodium and pottassium toluene sulphonate, ~xylene sulphonate,
benzene sulphonate and cume~e sulphonate at levels of up to 10%
normally in the range 2 - 6% by weight of the composition. Urea
and lower alkanol hydrotropes such as methanol, ethanol, propanol
and butanol may also be used ~at levels of 1 - 15~, normally
5 - 15~ by weight of the composition.
Hydrophobic oily materials suitable for use in the
present invention include animal, vegetable and mineral oils and
waxes, for example beeswax, spermaceti and carnauba wax; fatty
alcohols such as stearyl, myristyl and cetyl alcohols; fatty
esters and partial esters such as isopropyl myristate and glyceryl
monostearate; fatty acids such as stearic acid; lanolin and
cholesterol derivatives; and silicone oils. The compositions of
the invention may also comprise components designed to enhance
the moisturizing effectiveness of the compositions. Suitable
components include lower aliphatic alcohols having from 2 to 6
carbon atoms and 2 to 3 hydroxy groups, for example 1,4 butanediol,
1,2-propylene glycol and glycerine. Other suitable components
include urea or urea derivatives such as guanidine, pyrrolidone
or allantoin.
Solid granular detergent compositions may contain foam

enhancers, foam depressants, bleaches, anti-redeposition agents,



- 23

1059~302

enzymes, enzyme and bleach activators, fluorescers, builders and
other normal components of granular detergent compositions. Solid
compositions in bar fo~m may also contain additives such as fatty
acids, salts, skin creams and oils.
Skin Conditioning Tests
Conditioning performance was measured in both in-vit o
and in-vivo tests, a high degree of aorrelation between the two
test methods being found. The in-vitro test (called the calf-
skin occl-~sivity test) was based upon the rate of water tran-

spiration through a sample of calf-skin brought into contact
wlth a 0.15~ aqueous solution of a detergent composition (at 18~
ha~dness) containing the protein. The occlusivity of the protein
was measured as the percentage reduction in the rate of water
transpiration for the proteinaceous surfactant solution compared
with that for water.
One in-vivo test used was hand-immersion testing (HIT).
This test used a group of normal housewives in a multi-product
test; hands were balanced for right hand/left ha~d differences,
so that there were 32 ha~ds per product, 16 right and 16 left.
Ea~h person immersed left and right hands in different solutions
for three consecutive 10 minute periods in half an hour per day,
for 2 weeks, 5 days per wee~. Treatment solutions were re-
plenished every 10 minutes. Hands were withdrawn and ~eimmersed
in the solution every 2 minutes. Hands were graded on the
starting Monday (before iMmerSiOn) and on each Friday of the test.
HIT graded for protein/surfactant solutions were deter-
mined and are jquoted here, on a scale in which an 0.15% aqueous
solution of a standard detergent was assigned HIT grades of 0,
and a lmg/cm2 application of hand-care lotion was assigned HIT
grades of 100.

A second in-vivo test was also used which compares the
rate of water loss through skin, specifically human forearm skin,
- 24 -

1~)59002

under controlled conditions before and after treatment with a
test :solution. The lower the rate of water loss, the greater
the ability of the skin to bind moisture and hence the greater
the resistance to chapping, cra~king etc.
A test area of skin was treated with a compound
(Poldine methyl sulphate) that inhibits sweating and the treated
area was then swept with-dry nitrogen and the water content of
the gas assayed before and after passage over the skin. The
Test area was immersed in an 0.15% product solution for 10
minutes at 45C (Water hardness ~ 18~), dried and allowed to
equilibrate for one hour before a further reading was obtained
of the water content of a dry nitrogen stream passed over the
treated skin surface. The change in water loss before and after
treatment expressed as a percentage of the water loss before
treatment gives the relative skin conditioning power of the
particular protein.
Non-limitative embodiments of the invention are set
out in the following examples.
EXAMPLE I
A liquid detergent composition having the formulation shown below,
was prepared and compared for conditioning effectiveness against
a standard liquid dishwashing composition containing no protein.





~059002

CompositionExample I Standard

Ammonium linear
C12-C14 alkyl benzene
sulphonate 18.4 18.4

Sodium linear C12-C14-
alcohol sulphate including
3 ethylene oxide moieties18.4 1~.4

Lauric monoethanolamide 2.0 4.5

Industrial methylated spirits 11.0 11.0

Protein 4.0

Magnesium chloride 2.1

Water To 100 To 100

Performance
. _
In Vitro Occlusivity 9.4 -6.1
Hand lmmersion Testing 43 0
The protein used in the above example was obtained from soyprotein
isolate by hydrolysis with sodium hydroxide followed by hydroxy-
alkylation with butylene oxide, as described earlier. The protein
had a molecular weight of about 3000, an isoionic point pH of
5.9 and a degree of hydroxyalkylation of about 50% of free ;
carboxylic acid groups. Thb protein is thus seen to be particu-
larly effective in protecting skin from the deleter~ous effects
of detergent, both in-vivo and in-vitro.
EXAMPLE II

Two liquid detergent compositions identified as A & B were made
up and tested using the in-v-ivo test method set out previously
for assessing the water loss through skin.
Composition A was in accordance with the Standard in Example 1
and contained no modified protein.
Compositioni)B had the following ingredients:-



- 26 -

l~S9OOZ


12 14 linear alkyl
benzene sulphonate 18.4
Sodium C12-C14 linear trieth~xy alkyl sulphate 18.4
C12 monoethanolamide ~.0
Industrial Methylated Spirits 13.0
Single Cell Protein* acetylated alkaline
hydrolysate in which acetylation of the amino
groups was substantially complete.
Estimated pI = 3 - 4 3.6
Water To 100
~Toprina G"+, a protein derived from yeast cultured on purified
alkines and supplied by British Petroleum Ltd.
In the above-mentioned in-vivo test the two compositions performed
.
as follows:-

A + 20 ~ 10.5% i.e. an increase in
water loss as a result
of the treatment
B - 27 + 11%
It can be seen that composition B (acetylatéd, hydrolysed single
cell protein) is significantly better than composition A which
is a protein-free standard.
EXAMPLE III
Three liquid detergent compositions identified as C - E were made
up and tested using the in-vivo test method employed in Example
II. Each composition had the Base formulation of composition B
of Example II and contained 3% by weight protein as follows:-
Composition C `Alkali-hydrolysed Whey protein (pI = 5.0)
D Alkali-hydrolysed acetylated Whey protein;
estimated pI = 3 - 4, in which substantially
all of the amino groups were acetylated.
E Alkali-hydrolysed acetylated soybean protein
in which substantially all the amino groups
were acetylated.
In the in-vivo test, the compositions had the following per-
formance:-

* Trademark - 27 -

10~9002



C + 3 + 8%
-




D - 7.5 + 8%
E - 15.5 + 5%
It can be seen that compositions D and E containing proteins
modified in accordance with the invention provide an occlusive
benefit.
EXAMPLE IV
The composition of Example IV was the same as Example I except
that the protein was prepared by hydrolysis of soyprotein isolate
followed by acylation with acetic anhydride, as described above.
The N-acetylated protein had an isoionic point pH of 3, a
molecular weight of about 3000 and a degree of N-acylation o,f
about 100% of -amino acids. The hand immersion test value for
Example IV was 48.
EXAMPLES V to X
The following examples serve to illustrate, but not to limit,
liquid detergent compositions according to the present inve~tion
All percentages indicated are by weight:




- 28 -

~5900Z



EXA~LES
V VI VII VIII IX X
Dimethyldodecyl amine oxide 8% 4% 2% - 4% 2% 4%
Coconut alcohol ethylene
oxide (6) condensate 15 7 6 7 2 7
Diethanol C12_i6 fatty acid
amide 2~ - 3 - 2
Coconut alcohol ethylene oxide
(3) sulphate sodium salt- 10 9 14 10 12
C13_18 paraffin sulphonate,
sodium salt - 10 9 - 9 10
C12_14 alpha-olefin sulphonate,
ammonium salt - - - 12
Urea 8 6 - 10 8 6
Industrial Methylated Spirits 11 13 13 13 13 12
*Modified Soyprotein 2 4 4 4 5 3
Water Balance
* Modified soyprotein: hydroxybutyl derivative of NaOH
hydrolysed Promine F;'molecular weight 3000; isoionic point
5.9; percentage of 0-alkylated side chains 50.




_ ~9 _

~C~S9~02

The above compositions are mi.lder to skin and hair than the
corresponding compositions containing no modified protein and
there is substantially no diminution of the volume or the
stability of foam produced by the detergent. Substantially
similar cleaning and conditioning performance is obtained when
the modified protein in the above example is replaced by N-
acetyl whole casein, N-butyryl whey protein, N-hexanoyl
gelatin, N acetyl soyprotein, hydroxypropylated cottonseed
protein and the corresponding modified derived proteins in
which the derived protein has been obtained by acidic or basic
hydrolysis or by reduc~ion with, for example, sodium borohydride.
EXAMPLE XI
A dishwashing liquid which is mild to skin has the following
composition:-
Parts by wt.

Coconut alcohol-ethylene oxide (12)
sulfate ammonium salt 18.75
Coconut alcohol sulfate, ammonium salt 5.8

. Sodium alkyl glyceryl ether sulfonate
(where the alkyl is derived from "middle-cut"
coconut alcohols and has the following
approximate compositions

2% C10; 66% C12; 23% C14; ~% C16 4 0
Coconut alkyl dimethyl amine oxide
(wherein the coconut is middle cut) 5.0
Potassium toluene sulfate 0.5
Potassium chloride 2.5
Citric acid 0.1
Hydrogen chloride 0.81
Ammonium Xylene sulfate 5.0
Ethanol 8.75


Protein - N-acetylated alkali degraded
Promine F; isoionic point 3.0;
molecular weight 300n 4.0
Water To 100
- 30 -

~os~oz
Similar results are obtained when the protein is replaced by
N-acetylated whole casein.
EXAMPLE XII
A soap bar composition which is mild to skin has the following
composition:
Parts by wt.
Real soap (Tallow/coconut = 50/50) 78.5
Free fatty acid 7.6
Moisture 9.3
Skin Cream 0.5
Hydroxybutylated alkali degraded 4.0
Promine F; isoionic point 5.9;
Molecular weight 3000
EXAMPLES XIII - XVI
Granular detergent compositions were prepared with the following
compositions:-

Example Example Example Example
XIIIXIV XV XVI
Sodium linear dodecyl
sulphonate - 6 6
Sodium tallow alkyl sulphate -4 4
Sodium soap (90 Tallow/
10 Coconut) 0.5 2.5 2.5 0.5
Coconut monoethanolamide - 1.5 1.5
Tallow monoethanolamide 0.25 - - 0.25
3-(NrN-dimethyl-N-cl4 8-
alkylammonio)-2-hydroxy-
propane-l-sulphonate) 6 - - 6
"Tergitol 15-S-9"* 6 - - 6
Sodium tripolyphosphate 2 33 10 2
Sodium silicate 37.5 7 7 7
Sodium carboxymethyl cellulose 0.5 0.5 0.5 0.5
Sodium sulphate 34 8 31 30
Sodium perborate 25 25 8 25

Sodium chloride 1.5 - - 1.5
*Trademark of Union Carbide Corp. ~or a nonio3ic s ~ fahct~nt, it is
a polye~hylene glycol ether of a llnear secon ary a co o .

1~59~02

Example Example Example Example
XIII XIV XV XVI
Protease Present Present Present Present
Sodium EDTA 0.25 0.25 0.25 0.25
Perfune/brighteners -0.6 0.6 0.6 0.6
Inert impurities 3.9 0.65 0.65 3.9
Moisture 7 7 7 7
Protein 4 4 4 4
The protein was an N-acetylated alkali degraded soyprotein having
an isoionic poi~t of 3 and a molec~lar weight of about 3000.
EXAMPLE XVII
The following liquid detergent compositd~on was made up:-

Wt%
Sodium C14 alkane sulphonate 14.4
; Sodium coconut alkyl triethoxy sulphate 3.6
Ethyl Alcohol 5.0
Colour Perfume etc. 0.1
Water -To 100
Acetylated hydrolysed soyprotein of pI 3.0 was then added to
a sample of the formulation at a level of 4% of the composition
and both formulations were tested in-vivo for the rate of water
loss through forearm skin using the test described herein.
Results were as follows:-

Base formulation + 3 + 7%
Base formulation withacetylated soyprotein - 9 + 7%
The composition in accordance with the invention can be seen to
provide a reduction in water loss from the skin whilst the base
composition does not give the same benefit.




32

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Administrative Status

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Administrative Status

Title Date
Forecasted Issue Date 1979-07-24
(45) Issued 1979-07-24
Expired 1996-07-24

Abandonment History

There is no abandonment history.

Owners on Record

Note: Records showing the ownership history in alphabetical order.

Current Owners on Record
THE PROCTER AND GAMBLE COMPANY
Past Owners on Record
None
Past Owners that do not appear in the "Owners on Record" listing will appear in other documentation within the application.
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Document
Description 
Date
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Number of pages   Size of Image (KB) 
Description 1994-04-23 33 1,280
Drawings 1994-04-23 1 7
Claims 1994-04-23 2 44
Abstract 1994-04-23 1 14
Cover Page 1994-04-23 1 16