Note: Descriptions are shown in the official language in which they were submitted.
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DETERGENT COMPOSITIONS COMPRISING ANTIBODY
CONTROLLED PROTEOLYTIC ACTIVITY
FIELD of the INVENTION
The present invention relates to laundry delerger)l compositions
comprising a protease and a protcasc di~ected antibody in order to provide
sxcelle.,l cleaning pe,rù""ence and fabric care pe,ru"nal)ce.
BACKGROUND of thc INVENTION
An important part of the system which protects vel lebrdles against
infections by ba-;teria and viruses is the humoral immune system. Speci~lised
cells present in bone " ~ar, u.~, Iymphoid tissues and blood, produce
immunoglobulins (antibody) which appear in response to the introduction of a
micro- or macromolecule) foreign to that body and bind the body-foreign structure
initiating its destruction. Such a body-foreign ",a'e~ule is called an antigen. The
ar,libody is dil~cted against the antigenic determinant ûr hapten of the antigene.g. an amino acid sequence, parts of oligosaccharides, polysaccharides,
lipopolys~c~;~arides, glycûprot~i.)s, lipoproteins, lipoteichoinic acids.
The specific antibodies ge"erdted in this manner can CGIlltiine with the
antigen which elicited their formation to form an antigen-antibody complex.
Antibody "~alecu'es have binding sites that are very specific for and
co",pl~mentary to the structural features of the antigen that induced their
fol",aliom
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This highly specific antigen-antibody recognition and binding has found
several applications such as recognition agent, binding agent or carrier agent in
various domains such as analytical chemistry, therapeutic treatment, health and
beauty care.
EP 479 600, EP 453 097 and EP 450 800 relate to the use of antibodies
or fragments thereof for the delivery of active ingredients to a target site. EP 48~
701 discloses l,eat"~ent compositions for topical application containing
microc~pSll'es which enclose a beneficial agent at a target location, the
microcarsules having an antibody or antibody fragment specific to the target
location or a lectin.
W092/04380 describes reshaped human antibody or reshaped human
allli6Ody fragments having specihcity for human poiymorphic epithelial mucin to
be used in the l~eat~ent or diagnosis of cancer. The use of Epstein-Barr virus
specific poiypeplides for the production of antibodies and the diagnostic and
I,edl,nent of said ~~ise~se is disclosed in W094/06470.
Oral compositions comprising antibodies as anti-carie or periodontal
dise~ses l,eal"~e"l have been extensively described in WO95/01155,
WO95/00110, WO95/10612, EP 140 498, GB 2 151 923, GB 2 176 400, GB 2
167 299, DE 4324859, US 5 401 723 and EP 280 576.
EP 673 683 and EP 542 309 disclose hair cosmetic compositions
co"laining an anti6O-ly to hair or hair extract, obtained from egg yolk or poultry
immunised with the hair or hair extract and a polymer emulsion to provide
reduce~ hair damage, sunl ~ess, moistened feel and smoothness, said
co",position being adsorbed only onto a specified part of the hair.
Compositions containi"g antagonists (ty"uho-~li-,s or anli6Odias) against
epidermal and l,ansforl,ling growth factors, suitable for use in treatment of acne
are described in W095/24896.
The use of a"li6Odies in the overall detergellcy CGI Itext has been
suggested in Unilever Researchprijs "Molecule zoekt partner" 1992 wherein
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3 _
modofied antibodies directed to specific stains are proposed to be used in
bleaching process.
The production of antibodies by hyperimmunisation of mammals such as a
cow with a vaccine derived from E. coli bacteria is described in EP 102 831. EP
400 569 discloses a ,netl,od for preparing vaccine compositiGIl for dental caries
in nasal drops co,nl rising an antigen produced by integrating a protein anliyen-
expressing gene into the chromosomal gene of a streptococcus mutants GS-5
strain. WO94125591 cliscloses the production of antibodies or functionalised
fragments thereof derived from heavy chain immunoglobulins of ca",e' d~?.
Detergent compositions include nowadays a complex combination of
active ingredients which fulfill certain specific needs: a surfactant system,
enzymes providing cleaning and fabric care benefits, bleaching agents, a buildersystem, suds suppressor~, soil-suspending agents, soil-releasc agents, optical
brighteners, softening agents, dispersants, dye transfer inhibition compounds,
abrasives, bactericides, perfumes, and their overall performance has indeed
improved over the years.
In particular, current laundry detergent formulations generally include
detergent enzymes and more specifically proteases.
However, overeYposu~e of the sub~l,dle to the proteolytic activity and/or
transfer of the proteolytic activity to the post mainwash part of the washing cycle
such as rinse, spinning and/or drying steps can lead to unwanted effects. It is
well- known that the cletergel-t proteolytic enzymes can under certain
circu,l,stal)ces lower the tensile strength of the wool constituants of fabrics. It
should be noted ho~e~,er, that tensile ~lreilylll loss of fabric is also an
unavoidable result of mechanical action due to use/wearing and may further
result from da",age by a bleachi"g co"~ onent in the laundry process, especiallyif the fabric is contaminated with metal compounds.
It has now been surprisingly found that the appliodlioll of antibodies raised
agai"~t the proteolytic enzyme prevents the occurrence of undesirable residual
proteolytic activity. The proteolytic activity can be fully controlled during the
clearii"g process so that the negative effects due to the overexposure of the
substrate to the proteolytic enzyme can now be avoided.
. .
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It is therefore an object of the present invention to provide a protease-
containing laundry detergent composition delivering eYcellent cleaning benefits
such as stain and/or soil removal dingy cleaning and fabric care benefits.
The above need has been met by specific laundry detergent compositions
comprising a protease and an antibody directed to said proteolytic enzyme.
SUMMARY of the INVENTION
The present invention relates to laundry detergent compositions
comprising a protease enzyme and an antibody raised against the proteolytic
enzyme in order to provide excellent cleaning peif~.i",ance and fabric care
pe, fi~r"~ance.
DETAILED DESCRIPTION of the INVENTION
ANTIBODY
An esse"tial ele.-,ent of the deteryellt cG",positions of the present
invention is an antibody.
The immunoglobulins are classified into 5 cl~sses respe~;ti-/ely: IgM IgG
IgA IgD and IgE. P~f~r,ed types of immunoglobulins are IgG and IgA. Secretory
slgA which are follnd into human excreted body fluids such as milk saliva
respiratory and inlesli"al fluids are especially designed to survive in said
sec,~liol,s they have enhanced bindillg characteristics and are resistant to
prot~olytic hydrolysis.
The antibody which may be monoclonal or polyclonal or an antibody
r,dgment may be generdted by techniques conventional in the art for example
by using ~cGn)binant DNA techniques allowing to produce alltiLodies variants
with new properties: reduced immunogenecity enhanced affinity altered size ...
Specific binding may also be used. Preferred for the purpose of the present
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invention is a monoclonal antibody, more preferred is a f~dyr"ent thereof. Thesefragments may be similarly generated by conventional techniques such as
enzymatic digestion by papain or pepsin, or using recombinant DNA techniques.
Antibody f,agmenl~ may also be generated by conventional recombinant DNA
techniques. Antihod e~ and antibodies' fragments may be humanised, such as
described in Meded. - Fac. Landbouwkd. Toegepast Biol. Wet. (Univ. Gent)
(1995), 60(4a, Forum forApplied Biotechnology, 1995, Part 1), 2057-63.
Heavy and light chains are indeed colnposed of constanl and variable
domains. In the organis-"s producing immunoglobulins in their natural state the
constant do",ains are very important for a number of fullclions, but for many
app'~,ntions in industrial processes and products their variable domains are
sufficient. Consequently many Ill~thods have been described to produce
antibody fragments.
Antibody f,ag,.,ellts which are used may be a Fab, a Fv, a scFv or any
other f,ay",ent having similar binding properties. rle~r,ed routes to antibodiesfragments are through recG"Iti.~ant DNA technology, so that the f,dyn~ent is
expressed by a ge"elically transfor")ed organism.
Antibodies and ar,lil,ody fragments produced by recombinant DNA
technology do not need to be idenlical to f,dyn,ent of anlil,odies produced in
vertebrates, having nevertheless the same binding properties ev~ ted by their
Km, Ki and Kcat. For i":,tance they may include sequences of amino acids and/or
glycosylations which differ from those found in antihodi~s produced in other
ways, eSpec~lly sequences at the ends of fragments. Somewhat analogously,
antibody r,ay",ents produced through reco,nbinal1t DNA technology may include
extra amino acid sequences at their termini which have no counterpart in
antibodies produced in other ways.
A related possibility is that a binding agent for use in this invention is a
natural or sy"ll,etic polymer which mimics the specific binding activity of a natural
antibody's comple~enlary region(s). Such a polymer is for example a
polypeptide or a polymer imprinting (Arigew. Chem. Int. Ed. Engl. 1995, 34,
181 2-1 832).
.
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The usual method for the production of antibodies may be adopted in
immunising ",amrllals or poultry with the corresponding anligens. As Illamri,als to
be immunised, mice, rabbits, goats, sheep, horses, cows, etc. may be used. The
antibody (immunoglobulin fraction) may be separated from the antiserum, the
milk or the eggs according to the ordinary antibody purification method including
salting-out Ill~:lhod, Polson exlldction, gel-fill,dtion chlo,nalography, ion-
exchange chromalography, affinity chrunlatogld~Jhy and the like, the salting-outmethod using a~mG~Iium sulfate to produce the precipitates, followed by
dialysing the precipit~'?~ against physiological saline to obtain the purified
precirit~tes as the antibody.
Plants are also capatle of synthesising and assembling every kind of
antibody ma'ec~le and allow a large scale of production of a"lil.ocJies as
described in Tibtech. Dec 1995, Vol 13, pp 522-527; Plant Mol. Biol., 26, pp
1701-1710, 1994 and Biotechnol. proj. 1991, 7, pp 455461 and in US patent 5,
202,422. Anlil,od;es can also be produced into
microorganisms such as E. coli or S. cerevisiae via biofer",el,tatioll process as
illu~,aled in the EP patent 667 394.
Techniques for the production of antibody r,ay",ents are well known in the
literature: Saiki et al. Science 230 1350-54 (1985); Orlandi et al. PNAS USA 86
3833-7 (1989); W089109825; EP 368 684; WO 91/08482 and WO94125591.
The drawbacks due to prolonged activity of the enzyme can be avoided by
an effective control of the enzymatic activity trough the introduction of the
specifically cor,espol-ding antibody. Such antibodies can be either polyclonal -directed to the whole enzyme structure - or ~I~Gnoclonal - directed to specific
epitopes of the enzyme activity controlling regions of the enzyme structure.
Antibodies raised against specific enzyme can effectively deactivate the enzyme
by the antibody-antigen binding in or very near the active site. The fo""alio" of
such complex leads to the enzyme deactivation and could be explained by the
distortion of the 3-dimensional structure and/or steric hindrance at the substrate
cleft. The deactivation of the enzyme can also be achieved by the precipitation of
the complex antibody-antigen from the washing solution. Due to very high
specificity and effficiency of the antibody-antigen interaction, no other detergent
active is thereby affected.
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The protease-directed antibodies are preferably included into the
detergent compositions of the present invention at a level of from 10E-6% to
10E+1% by weight of total composition. In some instances, antibodies raised
against specific proteases have the capability of binding other proteases of high
structural similarity, providing cross-reactivity. Typically, a ,nolecular ratio of
protease-directed antibody to protease will be of 100:1 or lower, preferably of
50:1 or lower. For ",onoclooal anlil,odies or fragments thereof, the molecular
ratio of protease-dir~cted antibody to protease will be generally of 50:1 or lower,
plc:~r~bly of 20:1 or lower.
The antibodies raised against the protease are releAced in the wash
solution after a lag-period allowing the protease to deliver exce"ent performance
benefits to be achieved by the end of the wash process.
Therefore, the antibodies are prererably il,cGr~.orated into a release agent
in order to control their r~,lease timing and rate in the wash solution. The physical
forrn of the antibody-containing release agent is adapted to the physical form of
the corresponding detergent or additive.
For granular and powder detergent and cleaning products, the antibodies
and release agents can be contained in a granulate. Said antibody granulate can
suitably cG"lain various granulation aids, binders, fillers, pla~(ici~ers, lubricants,
cores and the like. Examples ll~er~of include cellulose (e.g. cellulosic fibers or in
",i.~rocrystalline form), cellulose derivatives (CMC, MC, HPC, HPMC), gelatin,
starch, ~exl,i"s, sugars, polyvinylpy~olidone, PVA, PEG, salts (e.g. sodium
sulfate, calcium sulfate), titanium dioxide, talc, clays (kaolin or bentonit~)and
nonionic su- rdct~. lls. Other n)aterials of relevance for incorporation in the
granulate are described in EP 304 331.
The "_lease agent may be, for example, a cGdliny. Said coali,)g pr~,te~ts
said granulates in the wash environment for a certain period of time. The codti,-g
will n~l",ally be app!ied to said granulates in an amount in the range of 1% to
50% by weight (ca~c~ ted on the basis of the weight of the uncoated, dry
granulate), pleferdl~ly in the range of 5 % to 40 % by weight. The amount of
coating to be applied to said granulates will depend to a considerable extent on
.
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the nature and composition of the desired coali~g, and to the kind of protectionsaid coating should offer to said granulates. For example, the thickness of saidcoating or a multi-layered coaling applied onto any of the above granulates may
deterllline the period in which the content of said granulates is released. A
possible multi-layered coating may be a coating in which, for example, a fast
release coaling is applied over a slow release coali"g.
Also co-granulates can be constructed containing in the outer layer the
detergent enzyme and a fast releasing agent and in the inner core, the antibody
and a slow releasi,lg agent.
Suitable r~lease coatings are codlillgs which give rise to release of the
contents of antibody-containing granulates under the conditiGns prevailing during
the use II,er~of. Thus, for example, when a preparation of the invention is to be
introduced into a washi.)g liquor containing a washing deteryent (llor",al'y
comprising, e.g. one or more types of surfactants), the coali"g should be one
which ensures the lelease of the co"tel-ts of said granulates from the release
agent when it is introduced into the washing medium.
Preferred release codling are coatings which are substanLially insoluble in
water. Release codlillgs which are appn~ riate in washing media may suitably
co".plise subst~nces selevt,ad from the following: cellu'ose and cellulase
derivatives, PVA, PVP, tallow; hydrogenated tallow; partially hydrolyzed tallow;fatty acids and fatty alcohols of natural and synthetic origin; long-chain fatty acid
mono-, di- and l,iesters of glycerol (e.g. glycerol monosteardle); ethoxylated fatty
alcohols; I~I.exes; h~d~oca,Lons of Illeltill9 point in the range of 50-80~C; and
waxes. Melt-codtins~ agents are a ~refer,ed class of fast or slow release coating
agents which can be used without dilution with water. Reference may be made to
Controlled Rele~-se Systems: FablicaliGn Technology, Vol. I, CRC Press, 1988,
forfurther i,.fol",dlion on slow release coaling.
Coati.,gs may suitably further cG",prise subst~nces such as clays (e.g. kaolin),titanium dioxide, pigments, salts (such as calcium carLonale) and the like. Th
person skilled in the art will be aware of further coaling constituents of relevance
in the present invention.
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In liquid detergent compositions, the antibody can be incorporated as a
dispersion of particies containing in addition to the antibody, a release agent. The
antibody can be present in a liquid or solid form. Suitable pa,tic'es consist of a
porous hydrophobic material (e.g., silica with an average pore diameter of 500
Ang~l,o,ll or higher) containing into the pores a solution of antibodies and a
surfactant as described in EP 583 512 of Surutzidis A. et al.
The release agent might be a coating which protects said particles in the wash
cycle for a certain period of time. The coali"g is preferdbly a hydrophobic coating
i"dte,ial such as a hydrophibic liquid polymer. Said polymer can be an organo
polysiloxane oil, alternatively a high olecula weight hydrocarbon or water
insoluble but water permeable polymeric "~alerial such as
carboxymethylcellulose, PVA, PVP. The polymer p~upel lies are selected to
achie~e a suitable release profile of the antibody in the wash solution.
THE PROTEASE ENZYME
The proteolytic enzymes are incGr,uGrdtecl in the deleryent compositions of
the present invention at a level of from 0.0001% to 2%, pr~rer~bly from 0.001%
to 0.2%, more preferably from 0.005% to 0.1% pure enzyme by weight of the
composition.
The proteolytic enzyme can be of various origin, e.g. produced by
m~l"l"als, plants, mic,uGrgal,i,,-"s. Origin can further be mesophilic or
exl.emophilic (psychropl)ilic, psychrotrophic, thermophilic, barophilic, alkalophilic,
~cidophilic, halophilic, etc.). Microorganisms are prerer.ed producers of
proteolytic-enzymes. Very preferred are serine proteases of bacterial origin.
Purified or non-purified forms of these enzymes may be used. Also included by
definition, are mutants of native enzymes. Mutants can be obtained e.g. by
protein and/or ge,-~tic enyineeri"g, chemical and/or physical modiricbliGns of
native enzymes. Co",r,ol- practice as well is the expression of the enzyme via
host organism in which the genetic material responsible for the production of the
enzyme has been cloned.
Suitable prote~ses are the sublil;sins which are obtained from particular
strains of B. sLlbtilis and B. Iicheniforrnis (subtilisin BPN and BPN'). One suitable
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protease is obtained from a strain of Bacillus, having maximum activity
throughout the pH range of 8-12, developed and sold as ESPERASE~ by Novo
Industries A~S of Denmark, hereinafter "Novo". The preparation of this enzyme
and analogous enzymes is described in GB 1,243,784 to Novo. Other suitable
proteases include ALCALASE~g), DURAZYMa~ and SAVINASE~ from Novo and
MAXATASE~19, MAXACAL~), PROPERASE~) and MAXAPEM~ (protein
engineered MaY~cal) from Gist-Broc~es. Proteolytic enzymes also encompass
modified bacterial serine prot~-ses, such as those described in European Patent
Application Serial Number 87 303761.8, filed April 28, 1987 (particularly pages
17, 24 and 98), and which is called herein "P~otease B", and in European Patent
APPIjC~ljGn 199,404, Venegas, published October 29, 1986, which refers to a
modified bacterial serine protealytic enzyme which is called "Protease A" herein.
Suitable is the protease called herein "Protease C", which is a variant of an
alkaline serine protease from Bacillus in which Iysine re~l~ced arginine at
position 27, tyrosine ,eplaced valine at position 104, serine ~eplaced asparagine
at position 123, and alanine repl~ced threonine at position 274. Protease C is
described in EP 90915958:4, cor,esponding to WO 91/06637, Published May 16,
1g91. Genetically modified variants, particularly of Plotease C, are also included
herein.
A preferred protease refened to as "P~otease D" is a carbonyl hydrolase variant
having an amino acid sequence not found in nature, which is derived from a
precursor catbonyl hydrolase by sl~bstitl.lting a different amino acid for a plurality
of amino acid residues at a position in said carbonyl hydrolase equivalent to
position +76, preferably also in combination with one or more amino acid residuepOsitiol~s equivalent to those selevled from the group cGIlsisli~lg of +99, +101,
+103, +104, +107, +123, +27, +105, +109, +126, +128, +135, +156, +166, +195,
+197, +204, +206, +210, +216, +217, +218, +222, +260, +265, and/or +274
according to the numbering of Bac~llus amyloliquefaciens subtilisin, as described
in WO95110591 and in the patent application of C. Ghosh, et al, "Bleaching
Compositions Co"" risi~g Protease Enzymes" having US Serial No. 08/322,677,
filed October 13, 1994.
Also suitable for the present invention are p~oleases described in patent
applications EP 251 446 and WO 91/06637, plutea5e BLAP~ described in
WO91/02792 and their vdria"l:, described in WO 95/23221.
See also a high ptl protease from R~cil~vs sp. NCIMB 40338 described in WO
93/18140 A to Novo. Enzymatic de~rge"ls comprising protease, one or more
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WO 98106811 11 PCT/US97/14288
other enzymes and a reversible protease inhibitor are described in WO
92/03529 A to Novo. When desired. a protease having decreased adsorption
and increased hydrolysis is available as described in WO 95/07791 to Procter ~
Gamble. A recombinant trypsin-like protease for detergents suitable herein is
described in WO 94/25583 to Novo. Other suitable proteases are described in
EP 516 200 by Unilever.
The cor,~osition of the present invention can also includes protease
enzymes which are non-naturally-occurring carbonyl hydrolase variants having a
different proteolytic activity stability subal,dle specificity pH profile and/orperforrnance cha~acteri~lic as co~ .Jr~d to the precursor carbonyl hydrolase
from which the amino acid sequence of the variant is derived. As stated earlier
the protease enzymes are designed to have trypsin-like specificity and preferably
also be bleach stable. The precursor carbonyl hyd~olase may be a naturally-
occurring carbonyl hydrolase or ~tcon,binant hydrolase. Specifically such
carbonyl hydrolase v~riar~ts have an amino acid sequence not found in nature
which is derived by repl-ce",ent of a plurality of amino acid residlles of a
precursor carbollyl hydrulase with different amino acids. The plurality of aminoacid residues of the precursor enzyme correspond to position +210 in
combination with one or more of the following residlJes +33 +62 +67 +76
+100 +101 +103 +104 +107 +128 ~129 +130 +132 +135, +156 +158
+164 +166 +167 +170 +209 +215 +217 +218 and +222 where the
numbered position corresponds to naturally-occurring subtilisin from Bacillus
amyloliquefaci~ns or to equivalent amino acid residues in other carbonyl
hydrolases or subtilisins such as Bacillus lentus subtilisin.
The carL,o"yl hydrolase variants which are protease enzymes useful in the
present invention co",posilions comprise r~lace",el,t of amino acid residue
+210 in coin~ination with one or more additional ,nodifi~liGns. While any
combination of the above listed amino acid substit~Jtions may be employed the
preferred variant p,otease enzymes useful for the present invention comprise thesl Ihstitution deletion or inse, lion of amino acid residues in the following
combinations: 210/156; 210/166; 210/76; 210/103; 210/104; 210/217;
210/156/166; 210/156/217; 210/166/217; 210/76/156; 210/76/166; 210176/217;
210/76/156/166; 210/76/156/217; 210/76/166/217; 210/76/103/156;
210/76/103/166; 210/76/103/217; 210/76/104/156; 210/76/104/166;
210/76/104/217; 210/76/103/104/156; 210/76/103/104/166; 210/76/103/104/217;
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WO 98/0~11 12 PCT~S97/14288
210~6/1031104/156/166; 210~6/103/104/156/217; 210~6/103/104/166/217
and/or 210176/103/104/156/166/217; 210~6/103/104/166/222;
210/67~6/103/104/166/222; 210/67~6/103/104/166/218/222 Most preferably
the variant enzymes useful for the present invention comprise the substitution
deletion or insertion of an amino acid residue in the following combination of
residues: 210/156; 210/166; 210/217; 210/156/166; 210/156/217; 210/166/217;
210~6/156/166; 210/76/103/156/166 and 210~6/103/104/156/166 of B. Ientus
subtilisin with 210/76/103/104/156/166 being the most pr~r~:r,ed.
Variant DNA sequences encoding such carbonyl hydrolase or subtilisin
variants are derived from a precursor DNA sequence which encodes a naturally-
occurring or recombinant precursor enzyme. The variant ~)NA sequences are
derived by modifying the precursor DNA sequence to encode the substitution of
one or more specific amino acid residlles encoded by the precursor DNA
sequence cor,~s~onding to positions +210, +33, +62, +67, +76, +100, +101,
+103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166,
+167, +170, +209, +215, +217, +218, and +222 in Bacillus lentus or any
combination ll,ert:or. Although the amino acid residues identified for modific~lion
herein are ide"lified accorcJi"g to the numbering arpli~hle to B.
amyloliquefaciens (which has become the conventional method for identifying
residue positions in all subtilisins) the pref~r,t:d precursor DNA sequence useful
for the present invention is the DNA sequence of Bacillus lentus. These
recGmbinant DNA sequences encode carbonyl hydrolase variants having a novel
amino acid sequence and in general at least one prDpe,ly which is sllbst~ntiallydirrer~nt from the same property of the enzyme encoded by the precursor
carbonyl hydrolase DNA sequence. Such properties include proteolytic activity
substrate specificity stability altered pH profile and/or enhanced perforrnance
characterislics.
The protease enzymes useful herein encor"pass the substitution of any of
the nineteen naturally occurring L-amino acids at the desig"ated amino acid
residue positions. Such suhstitutions can be made in any precursor subtilisin
(procaryotic eucaryotic ma"""alian etc.). Throughoutthisapplicationreference
is made to various amino acids by way of co,n~on one- and three-letter codes.
Such codes are identified in Dale M.W. (1989) Molecul~r Genetics of Bacteria
John VVIley & Sons Ltd. Appendix B.
Preferably the substitution to be made at each of the identified amino acid
residue positions include but are not limited to substitutions at position +210
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13 _
including 1, V, L, and A, substitutions at positions +33, +62, +76, +100, +101,
+103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166,
+167, +170, +209, +215, +217, and +218 of D or E, substitutions at position 76
including D, H, E, G, F, K, P and N; substitutions at position 103 including Q, T,
D, E, Y, K, G, R and S; and substitutions at position 104 including S, Y, I, L, M,
At W, D, T, G and V; and substitutions at position 222 including S, C, A. The
specifically preferred amino acid(s) to be substituted at each such position aredesig"atecl below in Table 1. Although specific amino acids are shown in Table 1,
it should be under~tood that any amino acid may be substituted at the identifiedresidues.
Table I
Amino Acid residue Preferred Amino Acid to
be Substituted/lnselled
+210 I,V, L,A
+33, +62, +100, +101, +107 D, E
+128, +129, +130, +135
+156, +158, +164, +166
+167, +170, +209, +215
+217 and +218
+76 D, H
+ 103 A,Q,T,D,E,Y,K,G,R
+ 104 I,Y,S,L,A,T,G
+222 S,C,A
A comparison of the preferred amino acid residues iclenlified herein for
substitution versus the preferred suhstitution for each such position is provided in
Table ll.
Table ll
+210+156 +166 +217 +76 +103 +104
B. amyloliquefaciens P E G Y N Q Y
(wild-type)
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14
B. Ientus (wild-type) P S S L N S V
Most Preferred I E/D E/D E/D D A l/Y
Substitution
Detergent components
The detergent compositions of the invention may also contain additional
detergent components. The preci~e nature of these additional components, and
levels of incorporation thereof will depend on the physical forrn of the
composition, and the nature of the cleaning operation for which it is to be used.
The detergent compositions acconJing to the invention can be liquid,
paste, gels, bars, tablets, powder or granular forrns. Granular compositions canalso be in "cG",pact form, the liquid coi"positions can also be in a
"concentrated" form.
The compositions of the invention may be formulated as hand and
machine laundry detergent compositions including laundry additive compositions
and compositions suitable for use in the soaking and/or prel~:dl"~ent of stainedfabrics, rinse added fabric softener co,n~ositions. Such compositions can provide
fabric cleaning, stain removal, whiteness maintenance, softening, color
appearance and dye transfer inhibition.
When formulated as compositiG,)s suitable for use in a laundry machine
washing rt~t:t~,od, the cGn"~ositions of the invention preferably contain both asurfactant and a builder c~""~ound and aclJilionally one or more detergent
cG~"pGI~ents p~srera~ly selected from organic polymeric compounds, bleaching
agents, additional enzymes, suds suppressors, disper~allls, lime-soap
dispersants, soil suspension and anti-redeposition agents and corrosion
inhibitors. Laundry compositions can also contain softening agents, as additional
detergent components.
The compositions of the invention can also be used as detergent additive
products comprising a protease-directed antibody and will be added to a
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._
conventional detergent protease-containing compositions. The detergent
additives can also comprise the protease and the protease-directed antibody.
Such additive products are intended to supplement or boost the performance of
conventional detergent compositions and preferably comprise up to 50%
antibodies by weight of totai composition.
If needed the density of the laundry detergent compositions herein ranges
from 400 to 1200 gllitre, preferably 600 to 950 gllitre of composition measured at
20~C.
The "compact" form of the compositions herein is best reflected by density and,
in terms of co"~position, by the amount of inorganic filler salt; inorganic filler salts
are conventional ing~dients of detergent compositions in powder form; in
conventional detergent compositions, the filler salts are present in substdl,lial
amounts, typically 17-35% by weight of the total composition.
In the compact compositions, the filler salt is present in amounts not
exceeding 15% of the total composition, preferably not exceeding 10%, most
preferably not exceeding 5% by weight of the composition.
The inorganic filler salts, such as meant in the present co",positions are
selected from the alkali and alkaline-earth-metal salts of sulphates and chlorides.
A preferred filler salt is sodium sulphate.
Liquid detergenl compositions acconJing to the present invention can also
be in a "concent,dted form", in such case, the liquid detergent compositions
according the present invention will contain a lower amount of water, compared
to convel,liol)al liquid deterye"ls.
Typically the water content of the concel,LIdted liquid detergent is
preferably less than 40%, more preferably less than 30%, most pr~reldbly less
than 20% by weight of the deteryent composition.
Surfactant system
The detergent cornpositions according to the present invention comprise a
surfactant system wherein the surfactant can be selected from nonionic and/or
anionic and/or cdlion.~ and/or ampholytic and/or zwitterionic and/or semi-polar
surfactants.
,. . . .. . .
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16
The surfactant is typically present at a level of from 0.1% to 60% by weight.
More preferred levels of incorporation are 1% to 35% by weight, most preferably
from 1% to 30% by weight of detergent compositions in accord with the invention.
The surfactant is preferably formulated to be compatible with enzyme
components present in the composition. In liquid or gel compositions the
surfactant is most preferably formulated such that it pr~,notes, or at least does
not degrade, the stability of any enzyme in these compositions.
Preferred surfactant systems to be used according to the present invention
comprise as a surfactant one or more of the nonio"ic and/or anionic surfactants
described herein.
Polyethylene, polypropylene, and polybutylene oxide condensa~es of alkyl
phenols are suitable for use as the nonionic sulractant of the surfactant systems
of the present inventionl with the polyethylene oxide condensates being
preferred. These compounds include the condens~tion products of alkyl phenols
having an alkyl group containing from about 6 to about 14 carbon atoms,
preferably from about 8 to about 14 carbon atoms, in either a straight-chain or
branched-chain configuration with the alkylene oxide. In a p~fer,ed embodi.nenl,the ethylene oxide is present in an amount equal to from about 2 to about 25
moles, more preferably from about 3 to about 15 moles, of ethylene oxide per
mole of alkyl phenol. Commercially available nonionic s~"ractal-ts of this type
include IgepalTM C0-630, marketed by the GAF Corporation; and TritonTM X-
45, X-114, X-100 and X-102, all marketed bythe Rohm & Haas Co,opany. These
surfactants are co""-,only referred to as alkylphenol alkoxylates (e.g., alkyl
phenol ethoxylates).
The condensdlion products of primary and secondary aliphatic alcohols with
from about 1 to about 25 moles of ethylene oxide are suitable for use as the
nonionic surfactant of the nonionic surfactant systems of the present invention.The alkyl chain of the aliphatic alcohol can either be straight or b(ar,ched, primary
or secondary, and generally contains from about 8 to about 22 carbon atoms.
P~efer,ed are the condensation products of alcohols having an alkyl group
containing from about ~ to about 20 carbon atoms, more preferably from about
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17 ~_
10 to about 18 carbon atoms, with from about 2 to about 10 moles of ethylene
oxide per mole of alcohol. About 2 to about 7 moles of ethylene oxide and most
preferably from 2 to 5 moles of ethylene oxide per mole of alcohol are present in
said condensation products. Ex~rnples of commercially available nonionic
surfactants of this type include TergitolTM 15-S-9 (the condensation product of
C11-C1s linear alcohol with 9 moles ethylene oxide), TergitolTM 24-L-6 NMW
(the cG"densalion product of C12-C14 primary alcohol with 6 moles ethylene
oxide with a narrow molecular weight distribution), both marketed by Union
Carbide Corporation; NeodolTM 45-9 (the concJensalion product of C14-C1s
linear alcohol with 9 moles of ethylene oxide), NeodolTM 23-3 (the condensation
product of C12-C13 linear alcohol with 3.0 moles of ethylene oxide), NeodolTM
45-7 (the concJensation product of C14-C1s linear alcohol with 7 moles of
ethylene oxide), NeodolTM 45-5 (the condensation product of C14-C1s linear
alcohol with 5 moles of ethylene oxide) marketed by Shell Chemical Company,
KyroTM EOB (the condensation product of C1 3-C15 alcohol with 9 moles
ethylene oxide), marketed by The Procter & Gamble Company, and Genapol LA
030 or 050 (the condcr,sa~ion product of C12-C14 alcohol with 3 or 5 moles of
ethylene oxide) marketed by Hoechst. Pr~fer~ed range of H~B in these products
is from 8-11 and most preferred from 8-10.
Also useful as the nonionic surfactant of the surfactant systems of the present
invention are the alkylpolysaccharides disclosed in U.S. Patent 4,565,647,
Llenado, issued January 21, 1986, having a hydrophobic group containing from
about 6 to about 30 carbon atoms, l~referably from about 10 to about 16 carbon
atoms and a polysaccharide, e.g. a polyglycoside, hydrophilic group containing
from about 1.3 to about 10, preferably from about 1.3 to about 3, most preferably
from about 1.3 to about 2.7 saccharide units. Any reducing saccharide containing5 or 6 carbon atoms can be used, e.g., glucose, g~laGtose and g~l~ctosyl
moieties can be sul~stihJted for the glucosyl moieties (opliGn011y the hydrophobic
group is attached at the 2-, 3-, 4-, etc. positions thus giving a glucose or
g~'-ctose as opposed to a glucoside or g~l~ctoside). The intersaccha,ide bonds
can be, e.g., betvlecn the one position of the additional saccharide units and the
2-, 3-, 4-, and/or 6- positions on the preceding saccharide units.
The preferred alkylpolyglycosides have the formula
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W O 98/06811 18 PC~AUS97/14288
R20(CnH2nO)t(9lycosyl)x
wherein R2 is selected from the group consisting of alkyl, alkylphenyl,
hydroxyalkyl, hydroxyalkylphenyl. and mixtures thereof in which the alkyl groupscontain from about 10 to about 18, preferably from about 12 to about 14, carbon
atoms; n is 2 or 3, prererably 2; t is from 0 to about 10, preferably 0; and x is from
about 1.3 to about 10, pref~rdbly from about 1.3 to about 3, most preferably from
about 1.3 to about 2.7. The glycosyl is pr~fer;ably derived from glucose. To
prepare these compounds, the alcohol or alkylpolyethoxy alcohol is formed first
and then reacted with glucose, or a source of glucose, to form the glucoside
(attachl),en~ at the 1-position). The adcJitiG"al glycosyl units can then be attached
between their 1-positioll and the preceding glycosyl units 2-, 3-, 4- and/or 6-
position, preferably predominately the 2-position.
The condensalion products of ethylene oxide with a hydrophobic base forrned
by the condensdlion of propylene oxide with propylene glycol are also suitable for
use as the additional nonionic sulrdctdllt systems of the present invention. Thehydrophobic portion of these compounds will prererably have a molecular weight
of from about 1500 to about 1800 and will exhibit water insolubility. The addition
of polyoxyethylene moieties to this hydrophobic portion tends to increase the
water solubility of the ",~!ec~'e as a whole, and the liquid character of the
product is re~dined up to the point where the polyoxyethylene content is about
50% of the total weight of the condensdlion product, which cor,esponds to
condensation with up to about 40 moles of ethylene oxide. Examples of
cGI"pounds of this type include certain of the cGr"r"er~ially-available PlurafacTM
LF404 and PluronicTM su, rdctants, marketed by BASF.
Also suitable for use as the nonionic surfactant of the nonionic surfactant
system of the present invention, are the condensation products of ethylene oxidewith the product resulting from the rea~;tion of propylene oxide and
ethylenediamine. The hydrophobic moiety of these products consists of the
reaction product of ethylenediamine and excess propylene oxide, and generally
has a molecular weight of from about 2500 to about 3000. This hydrophobic
moiety is condensed with ethylene oxide to the extent that the condensation
product contains from about 40% to about 80% by weight of polyoxyethylene and
has a molecula~ weight of from about 5,000 to about 11,000. Examples of this
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19
type of nonionic surfactant include certain of the comr"ercially available
TetronicTM compounds, marketed by BASF.
Preferred for use as the nonionic surfactant of the surfactant systems of the
present invention are polyethylene oxide condensales of alkyl phenols,
condensation products of primary and secondary aliphatic alcohols with from
about 1 to about 25 moles of ethylene oxide, alkylpolysaccl,arides, and mixturesthereof. Most preferred are Cg-C14 alkyl phenol ethoxylates having from 3 to 15
ethoxy groups and Cg-C1g alcohol ethoxylates (p~ft:rably C10 avg.) having from
2 to 10 ethoxy groups, and mixtures thereof.
Highly preferred nonionic su, rd~,ta"ts are polyhydroxy fatty acid amide
surfactants of the formula.
R2 C-N-Z,
Il I
o R1
wherein R1 is H, or p~1 is C14 hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl ora mixture thereof, R2 is Cs 31 hydrocar~yl, and Z is a polyhydroxyhydrocarbyl
having a linear hydrocarbyl chain with at least 3 hydroxyls directly connected to
the chain, or an alkoxylated derivative thereof. Preferably, R1 is methyl, R2 is a
straight C11 15 alkyl Ot C16 18 alkyl or alkenyl chain such as coconut alkyl or
mixtures thereof, and Z is derived from a reducing sugar such as glucose,
fructose, maltose, l~ose, in a reductive a",inalion reaction.
Suitable anionic surfactants to be used are linear alkyl benzene sulfonate,
alkyl ester sulfonate surfactants including linear esters of Cg-C20 carboxylic
acids (i.e., fatty acids) which are sulfonated with g~seous SO3 according to "The
Journal of the American Oil Cl,el"isls Society", 52 (1975), pp. 323-329. SuitabJe
starting materials would include natural fatty subst~nces as derived from tallow,
palm oil, etc.
The preferred alkyl ester sulfonate surfactant, especi~ly for laundry applicatiGns,
comprise alkyl ester sulfonate surfactants of the structural formula:
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WO 98/06811 PCT/US97/14288
_
R3 - CH - C - oR4
I
SO3M
wherein R3 is a Cg-C20 hyd~cari,yl, prefeldbly an alkyl, or combination thereof,R4 is a C1-C6 hydrocarbyl, pr~fer~bly an alkyl, or combination thereof, and M isa cation which forms a water soluble salt with the alkyl ester sulronale. Suitable
salt-forming caliGns include metals such as sodium, potassium, and lithium, and
substituted or unsubstituted ammonium cations, such as monoelllanolar"il,e,
diethanolamine, and triethanolamine. Preferably, R3 is C10-c16 alkyl, and R4 is
methyl, ethyl or isopropyl. Especially ,ureferled are the methyl ester sulfonates
wherein R3 is C10-C16 alkyl.
Other sl~it~hle anionic surfactants include the alkyl sulfate surfactants which
are water soluble salts or acids of the formula ROSO3M wherein R preferably is
a C10-C24 hydrocarbyl, pl~rerably an alkyl or hydroxyalkyl having a C10-C20
alkyl component, more preferably a C12-C1g alkyl or hydroxyalkyl, and M is H or
a cation, e.g., an alkali metal cation (e.g. sodium, potassium, lithium), or
a",r"o"ium or substit(lted ~ o~ium (e.g. methyl-, di.l,etl,yl-, and trimethyl
ammonium cdtions and quaternary a,n,nonium cations such as tetramethyl-
ammonium and di,llelllyl p.,er~i"ium cations and quaternary anln,onium cations
derived from alkylamines such as ethylamine, diethylamine, triethylamine, and
mixtures thereof, and the like). Typically, alkyl chains of C12-C16 are preferred
for lower wash te"~pelal.lres (e.g. below about 50~C) and C16 18 alkyl chains
are prefe"ed for higher wash temperatures (e.g. above about 50~C).
Other anionic sl" racta"l~ useful for detersive purposes can also be included inthe detergent co"~ositions of the present invention. These can include salts
(including, for e3(~",ple, sodium, potassium, a"""onium, and sl~bstitllted
ammonium salts such as mono-, di- and triethanolamine salts) of soap, Cg-C22
primary of secondary alkanesulfonates, Cg-C24 olefinsulfonates, sulfonated
polycarboxylic acids prepared by sulfonation of the pyrolyzed product of alkaline
earth metal citldtes, e.g., as described in British patent specification No.
1,082,179, Cg-C24 alkylpolyglycolethersulfates (conlai,ling up to 10 moles of
ethylene oxide); alkyl glycerol sulfonates, fatty acyl glycerol sulfonates, fatty oleyl
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glycerol sulfates, alkyl phenol ethylene oxide ether sulfates, paraffin sulfonates,
alkyl phosphates, isethionates such as the acyl isethionates, N-acyl taurates,
alkyl succinamates and sulfosuccinates, monoesters of sulfosuccinates
(especially saturated and unsaturated C12-C1g monoesters) and diesters of
sulfosuccinates (especially saturated and unsaturated C6-C12 diesters), acyl
sarcosinates, sulfates of alkylpolysaccharides such as the sulfates of
alkylpolyglllcoside (the nonionic nonsulfated compounds being described below),
branched primary alkyl sulfates, and alkyl polyethoxy carboxylates such as thoseof the formula RO(CH2CH2O)k-CH2COO-M+ wherein R is a Cg-C22 alkyl, k is
an integer from 1 to 10, and M is a soluble salt-forming cation. Resin acids andhydrogenated resin acids are also suitable, such as rosin, hyd,ogenaled rosin,
and resin acids and hydrogenated resin acids present in or derived from tall oil.
Further examples are described in "Surface Active Agents and Detergents"
(Vol. I and ll by Schwartz, Perry and Berch). A variety of such surfactants are
also generally disclosed in U.S. Patent 3,929,678, issued December 30, 1975 to
Laughlin, et al. at Column 23, line 58 through Column 29, line 23 (herein
incorporated by reference).
When included therein, the laundry detergent compositions of the present
invention typically co",prise from about 1% to about 40%, preferably from about
3% to about 20% by weight of such anionic surfactants.
Highly p,~fer,ecl anionic sl"ractanls include alkyl alkoxylated sulfate
su,rdcla"b. hereof are water soluble salts or acids of the formula RO(A)mSO3M
wherein R is an unsuhstituted C10-C24 alkyl or hydroxyalkyl group having a C10-
C24 alkyl component, pr~ferdbly a C12-C20 alkyl or hydroxyalkyl, more
preferably C12-C1g alkyl or hydroxyalkyl, A is an ethoxy or propoxy unit, m is
greater than zero, typically be~ween about 0.5 and about 6, more preferably
between about 0.5 and about 3, and M is H or a cation which can be, for
example, a metal cation (e.g., sodium, potassium, lithium, calcium, magnesium,
etc.), a"""onium or substituted-a"""onium cation. Alkyl ethoxylated sul~tes as
well as alkyl propoxylated sulfates are contemplated herein. Specific examples
of s~bstihlte~ ammonium cdlions include methyl-, di",etl,yl, l~i"~elhyl-ammoniumcalions and quaternary ammonium cations such as tetramethyl-am",ollium and
dilllelllyl piperdinium cations and those derived from alkyla",.nes such as
ethylamine, diethylamine, triethylamine, mixtures thereof, and the like. Exemplary
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surfactants are C12-C1g alkyl polyethoxylate (1.0) sulfate (C12-C1gE(1.0)M),
C12-C1g alkyl polyethoxylate (2.25) sulfate (C12-C1gE(2.25)M), C12-C1g alkyl
polyethoxylate (3.0) sulfate (c12-c18E(3.o)M)~ and C12-C1g alkyl polyethoxylate
(4.0) sulfate (C12-C1gE(4.0)M). wherein M is conveniently selected from sodium
and potassium.
The cletergent compositions of the present invention may also contain cationic,
ampholytic, zwitterionic, and semi-polar su,rdctant~, as well as the nonionic
and/or anionic surfactants other than those aiready described herein.
Cationic detersive surfactants suitable for use in the detergent compositions ofthe present invention are those having one long-chain hydrocarbyl group.
Examples of such cationic surfactants include the ammonium surfactants such as
alkyll, i" ,ethyla, r,r"onium halogenides, and those surfactants having the formula:
[R2(oR3)y][R4(0R3)y]2R5N+X-
wherein R2 is an alkyl or alkyl benzyl group having from about 8 to about 18
carbon atoms in the alkyl chain, each R3 is selected from the group cGI~sislill~ of
-CH2CH2-, -CH2CH(CH3)-, -CH2CH(CH2OH)-, -CH2CH2CH2-, and mixtures
thereof; each R4 is selected from the group consisting of C1-C4 alkyl, C1-C4
hydroxyalkyl, benzyl ring structures formed by joining the two R4 groups, -
CH2CHOH-CHOHCOR6CHOHCH20H wherein R6 is any hexose or hexose
polymer having a ",Dlecu4r weight less than about 1000, and hydrogen when y
is not 0; R5 is the same as R4 or is an alkyl chain wherein the total number of
carbon atoms of R2 plus R5 is not more than about 18; each y is from 0 to about
10 and the sum of the y values is from 0 to about 15; and X is any compatible
anion.
Quaternary ammonium surfactant suitable for the present invention has
the formula (I):
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R ~ ~ ~
Formula I
whereby R1 is a short chainlength alkyl (C6-C10) or alkylamidoalkyl of the
formula (Il):
C6~D~N~
Formula ll
y is 2-4, preferably 3.
whereby R2 is H or a C1-C3 alkyl,
whereby x is 04, preferably 0-2, most preferably 0,
whereby R3, R4 and R5 are either the same or different and can be either a shortchain alkyl (C1-C3) or alkoxylated alkyl of the formula lll,
whereby X~ is a counterion, preferably a halide, e.g. chloride or methylsulfate.
R6
~o7H
Formula lll
R6 is C1-C4 and z is 1 or 2.
r~et~r,ed quat a,~")~on.um surfactants are those as defined in formula I
whereby
R1 is Cg, C10 or mixtures thereof, x=o,
R3, R4 = CH3 and R5 = CH2CH2~H
Highly prefer,ed calio"ic surfactants are the water-sDlub!e quaternary
ammonium compounds useful in the present composition having the formula:
R1 R2R3R4N+X- (i)
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24
wherein R1 is Cg-C16 alkyl, each of R2, R3 and R4 is independently C1-C4
alkyl, C1-C4 hydroxy alkyl, benzyl, and -(C2H40)xH where x has a value from 2
to 5, and X is an anion. Not more than one of R2, R3 or R4 should be benzyl.
The preferred alkyl chain length for R1 is C12-C1s particularly where the alkyl
group is a mixture of chain lengths derived from coconut or palm kernel fat or is
derived sy~ll)etically by olefin build up or OXO alcohols synthesis. Preferred
groups for R2R3 and R4 are methyl and hydroxyethyl groups and the anion X
may be selected from halide, methosulphate, acetate and phosphate ions.
Examples of suitable quaternary ammonium compounds of formulae (i) for use
herein are:
coconut trimethyl ammonium chloride or bromide;
coconut methyl dihydroxyethyl al~""G"ium chloride or bromide;
decyl triethyl ammonium chloride;
decyl dimethyl hydroxyethyl a""),onium chloride or bromide;
C12 15 dimethyl hydroxyethyl ammonium chloride or bromide;
coconut dimethyl hydroxyethyl ammonium chloride or bromide;
myristyl llilll~thyl ammonium methyl sulphate;
lauryl di"lelhyl benzyl ammonium chloride or bromide;
- lauryl dimethyl (ethenoxy)4 ammonium chloride or bromide;
choline esters (compounds of formula (i) wherein R1 is
CH2-CH2-O-C-C12 14 alkyl and R2R3R4 are methyl).
Il
o
di-alkyl imida oli.,es [co""~ounds of formula (i)].
Other calionic su,rd-;lanls useful herein are also described in U.S. Patent
4,228,044, Cambre, issued October 14, 1980 and in European Patent
Application EP 000,224.
When included therein, the deter~aent compositions of the present invention
typically con,prise from 0.2% to about 25%, pr~rably from about 1% to about
8% by weight of such cationic surfactants.
Ampholytic surfactants are also suitable for use in the detergent compositions
of the present invention. These surfactants can be broadly described as aliphatic
derivatives of secondary or tertiary amines, or aliphatic derivatives of heterocyclic
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WO 98/06811 25 PCT~US97/14288
secondary and tertiary amines in which the aliphatic radical can be straight- orbranched-chain. One of the aliphatic substituents contains at least about 8
carbon atoms typically from about 8 to about 18 carbon atoms and at least one
contains an anionic water-solubilizing group e.g. carboxy sulfonate sulfate. SeeU.S. Patent No. 3 929678 to Laughlin et al issued Dece~ber 30 1975 at
column 19 lines 18-35 for examples of ampholytic surfactants.
When included therein the deteryc.~t co,t,l~ositions of the pr~sent invention
typically comprise from 0.2% to about 15% ~)ref~:r~bly from about 1% to about
10% by weight of such ampholytic surfactants.
Zwitterionic su"dcla,lts are also suitable for use in detergent c~.,.po~itiGns.
These sulf~cta.lt~ can be br~,adly described as derivatives of secondary and
tertiary a,ni.les derivatives of heterocyclic secondary and tertiary amines or
derivatives of quaterna y ammonium quater"d~ phosphol)ium or tertiary
sulfonium compounds. See U.S. Patent No. 3 929 678 to Laughlin et al. issued
December 30 1975 at column 19 line 38 through column 22 line 48 for
exel",ples of ~itleriGnic su,rdctants.
Wllen included therein the detergent composili~"s of the present invention
typically cbr"pri~e from 0.2% to about 15% preferably from about 1% to about
10% by weight of such zw;tl_.ibni~ surfactants.
Semi-polar nonionic surfactants are a special category of non.onic SUIr~Ct3.llS
wh~ch include water-soluhlQ amine oxides containing one alkyl moiety of from
about 10 to about 18 carbon atoms and 2 moieties selected from the group
cbnsisti"g of alkyl groups and hydroxyalkyl groups containing from about 1 to
about 3 carbon atoms; water-soluble phosphine oxides containing one alkyl
moiety of from about 10 to about 18 carbon atoms and 2 moieties sele~d from
the group c~nsisti,-g of alkyl groups and hydroxyalkyl groups containing from
about 1 to about 3 carbon atoms; and water-so'uhle sulfoxides c~ntaining one
alkyl moiety of from about 10 to about 18 carbon atoms and a moiety selected
from the group cbnsi~ling of alkyl and hydroxyalkyl moieties of from about 1 to
about 3 carbon atoms.
Semi-polar nonionic detergent su, ractanl~ include the amine oxide surfactants
having the formula
. .
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W O98/06811 26 PCT~US97/14288
R3(oR4)xN(RS)2
wherein R3 is an alkyl, hydroxyalkyl, or alkyl phenyi group or mixtures therof
containing from about 8 to about 22 carbon atoms; R4 is an alkylene or
hydroxyalkylene group containing from about 2 to about 3 carbon atoms or
mixtures thereof; x is from 0 to about 3; and each R5 is an alkyl or hydroxyalkyl
group containing from about 1 to about 3 carbon atoms or a polyethylene oxide
group cont~3.-ing from about 1 to about 3 ethylene oxide groups. The R5 groups
can be attached to each other, e.g., through an oxygen or nitrogen atom, to forrn
a ring structure.
These amine oxide surfactants in particular include C10-c18 alkyl di,ne~
amine oxides and Cg-C12 alkoxy ethyl dihydroxy ethyl amine oxides.
When inchlded therein, the d&ter~ent co-"positiGns of the present invention
typically comprise from 0.2% to about 15%, prer~rably from about 1% to about
10% by weight of such semi-polar nonionic su, ra-;t.,. ~ts.
The deteryen~ con,rosition of the present invention may further con,prise
a cos~,- rdctdl ~t selec~d from the group of primary or tertiary amines.
Suitable primary amines for use herein include amines according to the formula
R1NH2 wherein R1 is a C6-C12, preferably C6-C10 alkyl chain or R4X(CH2)n, X
is -O-,-C(O)NH- or-NH-, R4 is a C6-C12 alkyl chain n is belvleen 1 to 5,
preferably 3. R1 alkyl chains may be 5l~ ht or bra. ~ched and may be
interrupted with up to 12, pr~rably less than 5 ethylene oxide r ,~.eties.
r,efer,ed amines ac~ordi.,y to the formula herein above are n-alkyl amines.
Suitable amines for use herein may be selected from 1-hexylamine, 1-
octylamine, 1-decylamine and laurylamine. Other pr~f~nt:d primary am;nes
include C8-C10 oxypropylamine, octyloxypropylam.ne, 2-ethylhexyl-
oxypropylamine, lauryl amido propylamine and amido propylamine.
Suitable tertiary arnil)es for use herein include tertiary ar"ines having the
formula R1 R2R3N wherein R1 and R2 are C1-Cg alkylchains or
--( CH2--CH--~)XH
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W O98/06811 27 PCT~US97/14288
Rs
--( CH2--CH--O )~CH
R3is either a C6-C12, preferably C6-C10 alkyl chain, or R3 is R4X(CH2)n,
whereby X is -0-, -C(O)NH- or -NH-,R4 is a C4-C12, n is between 1 to 5,
preferably 2-3.R5is H or C1-C2 alkyl and x is between 1 to 6.
R3 and R4 may be linear or branched; R3 alkyl chains may be interrupted with
up to 12, preferably less than 5, ethylene oxide moieties.
Preferred tertiary amines are R1R2R3N where R1is a C6-C12 alkyl chain,
R2 and R3 are C1-C3 alkyl or
R5
--( CH2--CH--O )xH
where R5is H or CH3 and x = 1-2.
Also preferred are the amidoamines of the formula:
Rl - C- NH -(C~2)- N -(R2)
wherein R1 is C6-C12 alkyl; n is 2~,
preferably n is 3; R2 and R3 isC1-C4
Most preferred amines of the present invention include 1-octylamine, 1-
hexylamine, 1-decylamine, 1-dodecylamine,C8-100xypropylamine, N coco 1-
3dia",inopr~pa"e, coconutalkyldimethylamine, lauryldimethylamine, lauryl
bis(hydroxyethyl)amine, coco bis(hydroxyehtyl)amine, lauryl amine 2 moles
propoxylated, octyl amine 2 moles propoxylated, lauryl
amidopropyldi"~etl,yla"line, C8-10 amidopropyldimethylamine and C10
amidopropylcJ;"~etl ,ylami"e.
The most preferl~d amines for use in the composilions herein are 1-hexylamine,
1-octylamine, 1-decylamine, 1-dodecylamine. Especially desirable are n-
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dodecyldimethylamine and bishydroxyethylcoconutalkylamine and oleylamine 7
times ethoxylated, lauryl amido propylamine and cocoamido propylamine.
Co~ .,f;ona/ detergent enzymes
The detergent compositions can further comprise one or more enzymes
which provide detergent performance and/or fabric care benefits.
Said enzymes include enzymes selected from hem.cellul~ses, per"xidAses,
gluco-amylases, amylases, xylanases, lipases, phosphol;r~se, es~erdses,
cutinases, pectinases, keratanases, reduct~ses, oxidases, phenoloxidases,
lipoxygenases, ligninases, pullulanases, tan,lases, pentosanases, malanases, ~-
glucanases, arabinosid~ses, hyaluronidase, chondroitinase, laccase or mixtures
thereof.
A pl~Ft:nt:d c~i"bi"ation is a deter~enl c~l"position having cocktail of
conventional applicable enzymes like protease, amylase, lipase, cutinase and/or
cellulase in conjunction with one or more plant cell wall degrading enzymes.
The cellu~~ses usable in the present invention include both bacterial or
fungal cellul~-se. r,~r~r;ably, they will have a pH optimum of between 5 and 9.5.
Suitable cellulases are disclosed in U.S. Patent 4,435,307, Barbesgoard et al,
which discloses fungal cellulase produced from Humicola insolens. Suitable
cellul~ses are also disclosed in GB-A-2.075.028; GB-A-2.095.275 and DE-OS-
2.247.832.
Examples of such celM~-ses are cellulases produced by a strain of
Humicola insolens (Humicola grisea var. thermoidea), particularly the Humicola
strain DSM 1800.
Other $uitable cellul~,es are cellulases originated from Humicola insolens having
a n.Qlecul-r weight of about 50KDa, an isoelectric point of 5.5 and containing 415
amino acids and a -43kD endoglucanase derived from Humicola insolens, DSM
1800, exhibiting cellulase activity; a preferred endoglucanase cGIoponent has the
amino acid sequence disclosed in PCT Patent Applicalion No. WO 91/17243.
Also suitable cellula-ses are the EGIII ce"ul~es from Trichoderma
IG1l9ibrdCIIidlUm described in WO94/21801, Genencor. published September 29,
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1994. Especially suitable cell~ ses are the cellulases having color care benefits.
Examples of such cellulases are cellulases described in European patent
application No. 91202879.2, filed November 6, 1991 (Novo).
Peroxida-se enzymes are used in combination with oxygen sources, e.g.
percarbonate, perborate, persulfate, hydrogen peroxide, etc. They are used for
"solution bleaching", i.e. to prevent transfer of dyes or pi~"lenl~ removed fromsubsl,dtes during wash operations to other subsl,dtes in the wash solution.
Peroxidase enzymes are known in the art, and include, for example, horseradish
peroxid~se, ligninase, and haloperoxidase such as chloro- and bromo-
peroxidase.
Peroxidase-containing detergent compositions are disclosed, for example,
in PCT Inte",dtional Application WO 89/099813 and in European Patent
appl ~tion EP No. 91202882.6, filed on November 6, 1991.
Other suitable oxid~se enzymes is the l~cc~se enzyme using hydrogen
peroxide, oxygen as primary subsl,dles.
Said cellu~ases and/or perlJxid~ses are normally incorporated in the
detergent composition at levels from 0.0001% to 2% of active enzyme by weight
of the detergent composition.
Other pr~:fened enzymes that can be included in the detergent
compositions of the present invention include lipases. Suitable lipase enzymes
for del~ryen~ usage include those produced by microorganisms of the
Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclQsed
in British Patent 1,372,034. Suitable lipases include those which show a positive
immunological cross~ aclion with the a"li6Ody of the lipase, produced by the
microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from
Amano Pha.",~ceutic~l Co. Ltd., Nagoya, Japan, under the trade name Lipase P
"Amano," hereind~ler lefer,ed to as "Amano-P". Other suitable corn")ercial
lipases include Amano-CES, lipases ex Chromobacter viscosum, e.g.
Chromobacter viscosum var. Iipo/yticum NRRLB 3673 from Toyo Jozo Co.,
Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp.,
U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas
gladioli. Fsperi~lly suitable lipases are lipases such as M1 LipaseR and
LipomaxR (Gist-Brocades) and LipolaseR and Lipolase UltraR(Novo) which have
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found to be very effective when used in combination with the compositions of thepresent invention.
Also suitable are cutinases lEC 3.1.1.50] which can be considered as a special
kind of lipase, namely lipases which do not require interfacial activation. Addition
of cutinases to detergent compositions have been described in e.g. WO-A-
88/09367 (Genencor).
The ~ip~ses and/or cutinases are normally incorporated in the detergent
composition at levels from 0.0001% to 2% of active enzyme by weight of the
detergent composition.
Amylases (a and/or ~) can be included for removal of carbohydrate-based
stains. W094/02597, Novo Nordisk A/S published February 03, 1994, describes
detergent CGm posilio,)s which incorporate mutant amylases. See also
WO94/18314, Genencor, published August 18, 1994 and W095/10603, Novo
Nordisk A/S, published April 20, 1995. Other amylases known for use in
detergent compositions include both a- and ~-amylases. a-Amylases are known
in the art and include those disclQsed in US Pat. no. 5,003,257; EP 252,666;
WO/91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341; and British
Patent specilicalion no. 1,296,839 (Novo). Other suitable amylase are stability-enhanced amylases including Purafact Ox AmR described in WO 94/18314,
published August 18, 1994; W096105295, Genencor, published February 22,
1996 and amylase varia,lt~ having additional ~odi~cation in the immediate
parent available from Novo Nor.lisk A/S, disclose~l in WO 95/10603, published
April 95. Examples of con,r"ercial a-amylases products
are Termamyl~), Ban~ ,Fungamyl~) and Duramyl~, all available from Novo
Nordisk A/S De~ ark. W095/26397 describes other s~lit~hle amylases: a-
amylases chard.;terised by having a specific activity at least 25% higher than the
specific activity of Termamyl~ at a temperature range of 25~C to 55~C and at a
pH value in the range of 8 to 10, measured by the Phadeb~s~3~ a-amylase activityassay. Other amylolytic enzymes with improved pro~ellies with respect to the
activity level and the combination of thermostability and a higher activity level are
described in W095/35382.
The above-mentioned enzymes may be of any suitable origin, such as
vegetable, animal, bacterial, fungal and yeast origin. Said enzymes are normallyincorporated in the detergent composition at levels from 0.000~% to 2% of active
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3 1 ._
enzyme by weight of the detergent composition. The enzymes can be added as
separate single ingredients (prills, granulates, stabilized liquids, etc., containing
one enzyme ) or as mixtures of two or more enzymes ( e.g. cogranulates ).
Other suit~hlc detergent ingredients that can be added are enzyme
oxiddlion scavengers which are described in Co-pending European Patent
application 92870018.6 filed on January 31, 1992. Examples of such enzyme
oxidation scavengers are ethoxylated tetraethylene polyamines.
A range of enzyme materials and means for their i.,cGr,uoration into
sy"ll,~lic detergenl compositions is also disslosecl in WO 9307263 A and WO
9307260 A to Genencor International, WO 8908694 A to Novo, and U.S.
3,553,139, Janualy 5, 1971 to McCarty et al. Enzymes are further disclosed in
U.S. 4,101,457, Place et al, July 18, 1978, and in U.S. 4,507,219, Hughes,
March 26, 1985. Enzyme materials useful for liquid detergent formulations, and
their incorporation into such formulations, are disclQsed in U.S. 4,261,868, Hora
et al, April 14, 1981. Enzymes for use in detergents can be stabilised by various
techniques. Enzyme stabilisation techniques are disclosed and exemplified in
U.S. 3,600,319, August 17, 1971, Gedge et al, EP 199,405 and EP 200,586,
October 29, 1986, Venegas. Enzyme stabilisation systems are also described,
for example, in U.S. 3,519,570. A useful Bacillus, sp. AC13 giving p,oteases,
xylanases and cellulases, is described in WO 9401532 A to Novo.
Color care benefts
Techno'ogies which provide a type of color care benefit can also be
included. Exar"~ les of these technologies are metallo catalysts for color
maintenance. Such metallo catalysts are described in co-pending European
PatentApplicaliGIl No. 92870181.2.
The Bleaching agent
The detergent compositions of the present invention can further include
bleaching agents such as hydrogen peroxide, PB1, PB4 and percarbonate with a
particle size of 400-800 "~icro"s. These bleaching agent components can
include one or more oxygen bleaching agents and, depending upon the
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32 _
bleaching agent chosen. one or more bleach activators. When present oxygen
bleaching compounds will typically be present at levels of from about 1% to about
25%.
The bleaching agent component for use herein can be any of the
bleaching agents useful for deter~ent compositions including oxygen bleaches as
well as others known in the art. The bleaching agent suitable for the present
invention can be an activated or non-activated bleaching agent.
One category of oxygen bleaching agent that can be used encomp~sses
percarboxylic acid bleaching agents and salts ~hereof. Suitable examples of thisclass of agents include magnesium monoperoxyphthalate hexahydrate, the
magnesium salt of meta-chloro perbenzoic acid, 4-nonylamino4-
oxoperoxybutyric acid and diperoxydodecanedioic acid. Such bleaching agents
are disclosed in U.S. Patent 4,483,781, U.S. Patent Application 740,446,
European Patent Applic~tion 0,133,354 and U.S. Patent 4,412,934. Highly
pre~r,ecl bleaching agents also include 6-nonyla",ino-6-oxoperoxycaproic acid
as descriLed in U.S. Patent 4,634,551.
Another category of bleaching agents that can be used encomp~sses the
halogen bleaching agents. Examples of hypohalite bleaching agents, for
example, include Ll ichlGro isocyanuric acid and the sodium and potassium
dichlGroisocyanurates and N-chloro and N-bromo alkane sulphonamides. Such
materials are normally added at 0.~-10% by weight of the finished product,
preferably 1-5% by weight.
The hydrogen peroxide releasing agents can be used in combination with
bleach activators such as le:l~dacetylethylenediamine (TAED),
nonanoyloxyL,en~. ,e-sulf~" ,ate (NOBS, described in US 4,412,934), 3,5,-
I,i"~ell"~lhexanoloxyben~enesulro"ate (ISONOBS, descrii~ed in EP 120,591) or
pentaacetylglucose (PAG)or Phenolsulfonate ester of N-nonanoyl-6-
aminocaproic acid (NACA-OBS, described in WO94/28106), which are
perhydrolyzed to form a peracid as the active bleaching species, leading to
improved bleaching effect. Also suitable activators are acylated citrate esters
such as disclosed in Co-pending European Patent Al-plir~iGn No. 91870207.7.
Useful bleaching agents, including peroxyacids and bleaching systems
cG."~.rising bleach activators and peroxygen bleaching compounds for use in
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detergent compositions according to the invention are described in our co-
pending applications USSN 08/136,626, PCT/US95/07823, W095/27772,
W095/27773, W095/27774 and W095/27775.
The hydrogen peroxide may also be present by adding an enzymatic
system (i.e., an enzyme and a substrate therefore) which is capable of
generating hydrogen peroxide at the beginning or during the washing and/or
rinsing process. Such enzymatic systems are disclosed in EP Patent Application
91202655.6 filed October 9, 1991.
Metal-containing catalysts for use in bleach compositions, include cobalt-
containing catalysts such as Pentaamine acetate cobalt(lll) salts and
manganese-containing catalysts such as those described in EPA 549 271; EPA
549 272; EPA 458 397; US 5,246,621; EPA 458 398; US 5,194,416 and US
5,114,611. Bleaching composition comprising a peroxy compound, a
manganese-containing bleach catalyst and a chelating agent is described in the
patent application No 94870206.3.
Bleaching agents other than oxygen bleaching agents are also known in
the art and can be utilized herein. One type of non-oxygen bleaching agent of
particular interest includes photoactivated bleaching agents such as the
sulronaled zinc and/or aluminum phthalocyanines. These materials can be
deposited upon the subsl,dle during the washing process. Upon irradiation with
light, in the p,esel)ce of oxygen, such as by hanging clothes out to dry in the
daylight, the sulr~nated zinc phthalocyanine is activated and, consequently, thesubsl,dte is bleached. Preferred zinc phthalocyanine and a photoactivated
bleaching process are described in U.S. Patent 4,033,718. Typically, deteryen~
co,l~positions will contain about 0.025% to about 1.25%, by weight, of sulfonated
zinc phthalocyanine.
Builder system
The compositions according to the present invention may further comprise a
builder system. Any conventional builder system is suitable for use herein
including aluminosilicale materials, silicates, polycarboxylates, alkyl- or alkenyl-
succinic acid and fatty acids, materials such as ethylenediamine tetraacetate,
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34 _
diethylene triamine pentamethyleneacetate, metal ion sequestrants such as
aminopolyphosphonates, particularly ethylenediamine tetramethylene
phosphonic acid and diethylene triamine pentamethylenephosphonic acid.
Phosphate builders can also be used herein.
Suit~hle builders can be an inorganic ion exchange material, con~n,only an
inorganic hydrated aluminosilicate material, more particularly a hydrated
sylllll~tic zeolite such as hydrated zeolite A, X, B, HS or MAP.
Another suitable inorganic builder material is layered silicate, e.g. SKS-6
(Hoechst). SKS-6 is a crystalline layered silicate consisting of sodium silicate
(Na2Si2~5)
Suitable polycarLoxylates containing one carboxy group include lac~tic
acid, glycolic acid and ether derivatives thereof as disclosed in Belgian PatentNos. 831,368, 821,369 and 821,370. Polycarboxylates containing two carboxy
groups include the water-soluble salts of succinic acid, malonic acid,
(ethylenedioxy) diacelic acid, maleic acid, diglycollic acid, tartaric acid, tartronic
acid and fumaric acid, as well as the ether carboxylates described in German
Offenlegenschrift 2,446,686, and 2,446,687 and U.S. Patent No. 3,935,257 and
the sulfinyl carboxylates desc~ ibed in Belgian Patent No. 840,623.
Polycarboxylates containing three carboxy groups include, in particular, water-
soluble ~;itlales, aconitrates and cit-dconates as well as succinate derivativessuch as the car~oxymethyloxysuccinates described in British Patent No.
1,379,241, lactoxysucc;"ales described in Netherlands Application 7205873, and
the oxypolycarL,oxylate n~terials such as 2-oxa-1,1,3-propane tricarboxylates
descril~ecl in British Patent No. 1,387,447.
Polyca.boxylates containing four carboxy groups include oxydisuccinates
;,closed in British Patent No. 1,261,829, 1,1,2,2-ethane tetracarboxylates,
1,1,3,3-propane tet,dca,Loxylates and 1,1,2,3-propane tetracarboxylates.
Polycarboxylates containing sulfo substituents include the sulfosucci"ate
derivatives disclQsed in British Patent Nos. 1,398,421 and 1,398,422 and in U.S.Patent No. 3,936,448, and the sulru"ateJ pyrolysed cil,dtes described in BritishPatent No. 1,082,179, while polycarboxylates containing phosphone suhstituents
are disclosed in British Patent No. 1,439,000.
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Alicyclic and heterocyclic poiycarboxylates include cyciopentane-
cis,cis,cis-tetracarboxylates, cyclopentadienide pentacarboxylates, 2,3,4,5-
tetrahydro-furan - cis, cis, cis-tetracarboxylates, 2,5-tetrahydro-furan -cis -
dicarboxylates, 2,2,5,5-tetrahydrofuran - tetracarboxylates, 1,2,3,4,5,6-hexane -
hexacar-boxylateS and and carboxymethyl derivatives of polyhydric alcohols
such as sorbitol, mannitol and xylitol. Al~"nalic poly-carboxylates include mellitic
acid, pyromellitic acid and the phthalic acid derivatives clisclosed in British Patent
No. 1,425,343.
Of the above, the prertr,ed poiycarboxylates are hydroxycarboxylates
cGntaining up to three carboxy groups per molecule, more particularly cillates.
Preferred builder systems for use in the present con,posiliol,s include a
mixture of a water-insoluble aluminosi' ~te builder such as zeolite A or of a
layered silicate (SKS-6), and a water-soluble carboxylate chelating agent such as
citric acid. P,aferr~d builder systems for use in liquid detergent cor ,posilions of
the present inveulions are soaps and polycar60~ylates.
A sl ~it~lc chelant for inclusion in the detergent compositions in
accordance with the invention is ethylenediamine-N,N'-disuccinic acid (EDDS) or
the alkali metal, alkaline earth metal, ammo"ium, or s!~hstih~ted ammonium saltsthereof, or mixtures thereof. Pref~ned EDDS compounds are the free acid form
and the sodium or magnesium salt lhereof. Examples of such pre~t:r"ad sodium
salts of EDDS include Na2EDDS and Na4EDDS. Examples of such preferred
magnesium salts of EDDS include MgEDDS and Mg2EDDS. The ",agnesium
salts are the most p~efer~d for inclusion in compositions in accordance with theinvention.
r~eftr,~:d builder systems include a mixture of a water-insoluble
aluminosilicate builder such as zeolite A, and a water~cluble carboxylate
chelating agent such as citric acid.
Other builder materials that can form part of the builder system for use in
granular cori,positions include inorganic malerials such as alkali metal
carbonates, bicarbollates, siliG~tes, and organic "~aterials such as the organicphosphonates, amino polyalkylene phosphonates and amino polycarboxylates.
.
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Other suitable water-soluble organic salts are the homo- or co-polymeric
acids or their salts in which the polycarboxylic acid comprises at least two
carboxyl radicals separated from each other by not more than two carbon atoms.
Polymers of this type are disclosed in GB-A-1 596 756 Examples of such salts
are polyaclylates of MW 2000-5000 and their copolymers with maleic anhydride
such copolymers having a molecular weight of from 20 000 to 70 000 especially
about 40 000.
Detergency builder salts are normally included in amounts of from 5% to
80% by weight of the composition preferably from 10% to 70% and most usually
from 30% to 60% by weight.
Suds suppressor
Another optional ingredient is a suds suppressor exemplified by silicones
and silica-silicone mixtures. Silicones can be generally repr~sented by alkylated
polysiloxane materials whiJe silica is normally used in finely divided forms
exemplified by silica aerogels and xerogels and hydrophobic silicas of various
types. These ~"aterials can be incorporated as particulat~s in which the suds
suppressor is advant~geo~sly releas~hly incGr,uGrated in a water-soluble or
water-dispersible sul-st~nlially non-surface-active detergent impermeable
càrrier. Alternatively the suds suppressor can be dissolvcd or dispersed in a
liquid carrier and applied by spraying on to one or more of the other components.
A preferled silicone suds controlling agent is disclosed in Bartollota et al.
U.S. Patent 3 933 672. Other particularly useful suds suppressors are the self-
emulsifying silicone suds sup~ ressors described in German Patent Application
DTOS 2 646 126 pu~lisl,ed April 28 1977. An example of such a compound is
DC-544 cG~ ercially available from Dow Corning which is a siloxane-glycol
copolymer. Es,l~eci&lly p,ererr~d suds controlling agent are the suds suppressorsystem comprising a mixture of sil;cone oils and 2-alkyl-alcanols. Suitable 2-alkyl-
alkanols are 2-butyl-octanol which are con""ercially avdilable under the trade
name Isofol 12 R.
Such suds su~.~,r~ssor system are desc~ibed in Co-pending European Patent
applirqtion N 92870174.7 filed 10 November 1992.
Especially preferred silicone suds controlling agents are described in Co-
pending European Patent application N~92201649.8. Said compositions can
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comprise a silicone/silica mixture in combination with fumed nonporous silica
such as AerosilR.
The suds suppressors described above are normally employed at levels of
from 0.001% to 2% by weight of the composition, p~ererably from 0.01% to 1% by
weight.
Others
Other cGn)poilents used in detergent compositions may be employed,
such as soil-suspending agents, soil-release agentsl optical brighteners,
abrasives, bactericides, tarnish inhibitors, coloring agents, and/or encarsul~d
or non-encarsulated perfumes.
Especially suitable encapsulating materials are water soluble c~rsu'~s
which co"si:jl of a matrix of polysaccharide and polyhydroxy compounds such as
described in GB 1,464,616.
Other suitable water soluble encapsulating materials comprise dextrins
derived from ungelatinized starch acid-esters of substituted dicarboxylic acids
such as described in US 3,455,838. These acid-ester dexl,i"s are, preferably,
prepared from such starches as waxy maize, waxy sorghum, sago, tapioca and
potato. Suitable examples of said encarsn4ting materials include N-Lok
manufactured by National Starch. The N-Lok encarsul~ting ~"alerial consists of amodified maize starch and glucose. The starch is modified by adding
monofunctional substituted groups such as octenyl succinic acid anhydride.
Antiredeposition and soil suspension agents suitable herein include
cellulose derivatives such as methylcellulose, carboxymethylcellulose and
hydroxyethylcellulose, and homo- or co-polymeric polycarboxylic acids or their
salts. Polymers of this type include the polyacrylates and maleic anhydride-
acrylic acid copolymers previously mentioned as builders, as well as copolymers
of maleic anhydride with ethylene, methylvinyl ether or methacrylic acid, the
maleic anhydride constituting at least 20 mole percent of the copolymer. These
materials are normally used at levels of from 0.5% to 10% by weight, more
. . .
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preferably from 0.75% to 8%, most preferably from 1% to 6% by weight of the
composition.
Preferred optical brighteners are anionic in character, examples of which
are disodium 4,4'-bis-(2-diethanolamino-4-anilino -s- triazin-6-ylamino)stilbene-
2:2' disulphonate, disodium 4, - 4'-bis-(2-morpholino4-anilino-s-triazin 6 ylamino-
stilbene-2:2' - disulphonate, disodium 4,4' - bis-(2,4-dianilino-s-triazin-6-
ylamino)slilbene-2:2' - disulphonate, monosodium 4',4" -bis-(2,4-dianilino-s-tri-
azin-6 ylamino)stilbene-2-sulphonate. disodium 4,4' -bis-(2-anilino-4-(N-methyl-N-
2-hydroxyethylamino)-s-triazin-6-ylamino)stilbene-2.2' - disulphonate, di-sodium4,4' -bis-(4-phenyl-2, 1 ,3-triazol-2-yl)-stilbene-2,2' disulphonate, di-so-dium4,4'bis(2-anilino~-(1-methyl-2-hydroxyethylamino)-s-triazin-6- ylami-no)stilbene-
2,2'disulphonate, sodium 2(stilbyl-4"-(naphtho-1',2':4,5)-1,2,3 - triazole-2"-
sulphonate and 4,4'-bis(2-sulphostyryl)biphenyl. Highly preferred brighte"ers are
the specific brighteners of co-,l~e"dins; European Patent application No.
95201 943.8.
Other useful polymeric materials are the polyethylene glycols, particularly
those of "~olerular weight 1000-10000, more particularly 2000 to 8000 and most
preferably about 4000. These are used at levels of from 0.20% to 5% more
pref~rdbly from 0.25% to 2.5% by weight. These polymers and the previously
mentioned homo- or co-polymeric polycarboxylate salts are valuable for
improving whiteness maintenance, fabric ash deposition, and cleaning
pe"or-l,al)ce on clay, protein~ceous and oxidizable soils in the presence of
transition metal impurities.
Soil r~lease agents useful in compositions of the present invention are
conventionally copolymers or terpolymers of terephthalic acid with ethylene
glycol and/or propylene glycol units in various arrangel"ellt~. Examples of suchpolymers are disclQsed in the co"~monly assigne.J US Patent Nos. 4116885 and
4711730 and European Published Patent Application No. 0 272 033. A particular
preferred polymer in accordance with EP-A-0 272 033 has the formula
(cH3(pEG)43)o.75(poH)o.25[T-po)2.8(T-pEG)o 4l~(
H)0.25((PEG)43CH3)0.75
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where PEG is -(OC2H4)O-,PO is (OC3H6O) and T is (pcOC6H4CO).
Also very useful are modihed polyesters as random copolymers of
dimethyl terephlhalate, dimethyl sulfoisophthalate, ethylene glycol and 1-2
propane diol, the end groups consisting primarily of sulphobenzoate and
secondarily of mono esters of ethylene glycol and/or propane-diol. The target isto obtain a polymer capped at both end by sulphobenzoate groups, "primarily", inthe present context most of said copolymers herein will be end-capped by
sulphobenzoate groups. However, some copolymers will be less than fully
capped, and lherefore their end groups may consist of monoester of ethylene
glycol and/or propane 1-2 diol, thereof consist "secondar;ly" of such species.
The selected polyesters herein contain about 46% by weight of .Ji~ hyl
teleplltl,alic acid, about 16% by weight of propane -1.2 diol, about 10% by weight
ethylene glycol about 13% by weight of dilot:lhyl sulroben,oic acid and about
15% by weight of sulfoisophthalic acid, and have a molecular weight of about
3.000. The polyesters and their method of preparation are described in detail inEPA 311 342.
Is is well known in the art that free chlorine in tap water rapidly deactivates
the enzymes comprised in detergent compositions. Therefore, using chlorine
scavenger such as perbGrale, ai"r"onium sulfate, sodium sulphite or
polyethyleneimine at a level above 0.1% by weight of total cor"position, in the
formulas will provide improved through the wash stability of the detergent
enzymes. Compositions comprising chlorine scavenger are described in the
EurupeJn patent arp'i~~tion 92870018.6 filed January 31, 1992.
Alkoxylated polycarboxylates such as those prepared from polyacrylates
are useful herein to provide additional grease removal perfo~"ance. Such
"aterials are described in WO 91/08281 and PCT 90/01815 at p. 4 et seq.,
incorporated herein by reference. Chemically, these materials comprise
polyacrylates having one ethoxy side-chain per every 7-8 acrylate units. The
side-chains are of the forrnula -(CH2CH2O)m(CH2)nCH3 wherein m is 2-3 and n
is 6-12. The side-chains are ester-linked to the polyacrylate "backbone" to
provide a "comb" polymer type structure. The molecular weight can vary, but is
typically in the range of about 2000 to about 50,000. Such alkoxytated
,
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._
polycarboxylates can comprise from about 0.05% to about 10%, by weight, of the
compositions herein.
Sorh.,i"g agents
Fabric softening agents can also be incorporated into laundry detergent
compositions in accordance with the present invention. These agents may be
inorganic or organic in type. Inorganic softening agents are exemplified by the
smectite clays disçlosed in GB-A-1 400 898 and in USP 5,019,292. Organic
fabric softening agents include the water i-,saluhle tertiary a,.lb~es as disclosed in
GB-A1 514 276 and E~-B0 011 340 and their co"lLi.,ation with mono C12-C14
quaternary ammonium salts are disclosed in EP-B-0 026 527 and EP-B-0 026
528 and di-long-chain amides as disclosed in EP-B-0 242 919. Other useful
organic ingredients of fabric softening systems include high ,-,c'e..ula~ weightpolyethylene oxide ~.~aterials as disclQsed in EP-A-0 299 575 and 0 313 146.
Levels of smectite clay are normally in the range from 2% to 20%, more
preferably from 5% to 15% by weight, with the material being added as a dry
mixed compone;lt to the remainder of the formulation. Organic fabric softening
agents such as the water-insoluble tertiary amines or dilong chain amide
materials are incorporated at levels of from 0.5% to 5% by weight, normally from1% to 3% by weight whilst the high i"clecu~ar weight polyethylene oxide
materials and the water soluble cationic materials are added at levels of from
0.1% to 2%, normally from 0.15% to 1.5% by weight. These materials are
normally added to the spray dried portion of the composition, although in some
instances it may be more convenient to add them as a dry mixed particulate, or
spray them as molten liquid on to other solid components of the composition.
Dispc. ~Jt~
The detergent composition of the present invention can also contain
dispersants: Suitable water-soluble organic salts are the homo- or co-polymeric
acids or their salts, in which the polycarboxylic acid comprises at least two
carboxyl P~ic~ls separated from each other by not more than two carbon atoms.
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41 _
Polymers of this type are disclosed in GB-A-1,596,756. Examples of such salts
are polyacrylates of MW 2000-5000 and their copolymers with maleic anhydride,
such copolymers having a molecular weight of from 1,000 to 100,000.
FSpec~ yt copolymer of acrylate and methylacrylate such as the 480N
having a molecular weight of 4000, at a level from 0.5-20% by weight of
composition can be added in the detergent compositions of the present
invention.
The cGn,positions of the invention may colll. ;.l a lime soap peptiser
compound, which has a lime soap dispersing power (LSDP), as defined
her_i.,drler of no more than 8, p~ferably no more than 7, most preferably no
more than 6. The lime soap peptiser compound is preferably present at a level
from 0% to 20% by weight.
A nu",erical measure of the effectiveness of a lime soap peptiser is given
by the lime soap dispersant power (LSDP) which is dete""ined using the lime
soap disper~ant test as desc,il,ed in an article by H.C. Borghetty and C.A.
Bergman, J. Am. Oil. Chem. Soc., volume 27, pages 88-90, (1950). This lime
soap dispersion test ",ell,ocl is widely used by practitioners in this art field being
rer~r,ed to, for example, in the follDw;n~ review articles; W.N. Linfield, Su,ractant
science Series, Volume 7, page 3; W.N. Linfield, Tenside surf. det., volume 27,
pages 159-163, (1990); and M.K. Nagarajan, W.F. Masler, Cosmetics and
Toiletries, volume 104, pages 71-73, (1989). The LSDP is the % weight ratio of
disper~ing agent to sodium oleate required to disperse the lime soap deposits
formed by 0.025g of sodium oleate in 30ml of water of 333ppm CaCo3
(Ca:Mg=3:2) equivalent hardness.
Surfactants having good lime soap peptiser capability will include certain
amine oxides, betaines, sulfobetaines, alkyl ethoxysulfates and ethoxylated
alcohols.
Exemplary surfactants having a LSDP of no more than 8 for use in accord
with the present invention include C16-C1g di",ell,yl amine oxide, C12-C1g alkylethoxysulfates with an average degree of ethoxylation of from 1-5, particularly
C12-C1s alkyl ethoxysulfate surfactant with a degree of ethoxylation of amount 3
.
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42
(LSDP=4), and the C14-C1s ethoxylated alcohols with an average degree of
ethoxylation of either 12 (LSDP=6) or 30, sold under the tradenames Lutensol
A012 and Lutensol A030 respectively, by BASF GmbH
Polymeric lime soap pepliser~ suitable for use herein are described in the
article by M.K. Nagarajan, W.F. Masler, to be found in Cos,l,etics and Toiletries,
volume 104, pages 71-73, (1989).
Hydrophobic bleaches such as 4-[N-octanoyl-6-aminohexanoyl]benzene
sulro"ale, 4-[N-nonanoyl-6-aminohexanoyl]benzene sulrondla, 4-[N-decanoyl-6-
aminohexanoyl]benzene sulfonate and mixtures thereof; and nonanoyloxy
benzene sulfonate together with hydrophilic / hydrophobic bleach formulations
can also be used as lime soap peptisers compounds.
Dye h...,~f~rinhibition
The detergent colll,l~osiliol)s of the present invention can also include
compounds for inhibiting dye transfer from one fabric to another of solubilized
and suspended dyes encountered during fabric laundering operations involving
colored fabrics.
Po/y". eric dye transferi"h~iti,~g agents
The detary~nt compositions according to the present invention also
comprise from 0.001% to 10 %, preferably from 0.01% to 2%, more pr~ferably
from 0.05% to 1% by weight of polymeric dye transfer inhibiting agents. Said
polymeric dye transfer inhibiting agents are norrnally incor,uordtad into detergent
col"positions in order to inhibit the transfer of dyes from colored fabrics ontofabrics washed therewith. These polymers have the ability to complex or adsorb
the fugitive dyes washed out of dyed fabrics before the dyes have the opportunity
to become all~cl,ed to other articles in the wash.
Especially suitable polymeric dye transfer inhibiting agents are polyamine N-
oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimid~-ole,
polyvinylpyrrolidone polymers, polyvinyloxazolidones and polyvinylimidazoles or
mixtures thereof.
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Addition of such polymers also enhances the performance of the enzymesaccording the invention.
a) Polyamine N-oxide polymers
The polyamine N-oxide polymers suitable for use contain units having the
following structure forrnula:
p
I
(I) Ax
I
R
wherein P is a polymerisable unit ~,vl,er~to the R-N-O group can be atldched to
or wherein the R-N-O group forrns part of the poly",eri -a~le unit or a
combination of both.
O O O
Il 11 11
A is NC CO C -O- -S- -N-; x is O or 1;
R are ali~)hdtic ethoxylated aliphatics aru,nalic hetero.;~clic or alicyclic
groups or any combination thereof whereto the nitrogen of the N-O
group can be dtlacl,ed or wherein the r,ibuge" of the N-O group is part
of these groups.
The N-O group can be ~prt:sented by the following general structures:
O O
(R1)x -N- (R2)y =N- (R1)x
I
(R3)z
wherein R1 R2 and R3 are aliphaticgroups aromatic heterocyclicoralicyclic
groups or combinaliGns thereof x or/and y orland z is O or 1 and
wherein the nitrogen of the N-O group can be attached or wherein the
r,il,ogen of the N-O group forms part of these groups.
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44 _
The N-O group can be part of the polymerisable unit (P) or can be
attached to the polymeric backbone or a combination of both.
Suitable polyamine N-oxides wherein the N-O group forms part of the
polymerisa~le unit comprise polyamine N-oxides wherein R is selected from
aliphatic, aromdlic, alicyclic or heterocyclic ~roups.
One class of said polyamine N-oxides colnl~ri~es the group of polyamine N-
oxides wherein the nitrogen of the N-O group forms part of the R-group.
Preferred polyamine N-oxides are those wherein R is a heterocyclic group such
as pyrridine, pyrrole, imidazole, pyrrolidine, piperidine, quinoline, acridine and
derivatives thereof.
Another class of said polyamine N-oxides co,,,,urises the group of polyamine N-
oxides wherein the nil,o~ell of the N-O group is attached to the R-group.
Other suitable polyamine N-oxides are the polyamine oxides whereto the
N-O group is attached to the polymerisable unit.
Preferred class of these polyamine N-oxides are the polyamine N-oxides having
the general formula (I) wherein R is an aromatic, heterocyclic or alicyclic groups
wherein the nitrogen of the N-0 functional group is part of said R group.
Examples of these cla~ses are polyamine oxides wherein R is a heterocyclic
compound such as pyrridine, pyrrole, imidazole and derivatives thereof.
Another pleftr,.2d class of polyamine N-oxides are the polyamine oxides having
the general formula (I) wherein R are aro,r,~lic, heterocyclic or alicyclic groups
wherein the r,it.oge" of the N-0 functional group is attached to said R groups.
Examples of these cla ,ses are polyamine oxides wherein R groups can be
aromatic such as phenyl.
Any polymer l~ckhone can be used as long as the amine oxide polymer
formed is water-soluble and has dye transfer inhibiting properties. Examples of
suitable polymeric backbones are polyvinyls, polyalkylenes, polyesters,
polyethers, polyamide, polyimides, polyacrylates and mixtures thereof.
The amine N-oxide polymers of the present invention typically have a ratio
of amine to the amine N-oxide of 10:1 to 1:1000000. However the amount of
amine oxide groups present in the polyamine oxide polymer can be varied by
appropriate copolymeli~ation or by appropriate degree of N-oxidation. I~leferably,
the ratio of amine to amine N-oxide is from 2:3 to 1:1000000. More preferably
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WO 98/06811 PCT/US97/14288
from 1:4 to 1:1000000, most preferably from 1:7 to 1:1000000. The polymers of
the present invention actually encompass random or block copolymers where
one monomer type is an amine N-oxide and the other monomer type is either an
amine N-oxide or not. The amine oxide unit of the polyamine N-oxides has a PKa
~ 10, preferably PKa c 7, more preferred PKa < 6.
The polyamine oxides can be obtained in almost any degree of polymerisation.
The degree of polymerisation is not critical provided the material has the desired
water-solubility and dye-suspending power.
Typically, the average molecular weight is within the range of 500 to 1000,000;
preferably from 1,000 to 50,000, more preferably from 2,000 to 30,000, most
preferably from 3,000 to 20,000.
b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole
The N-vinylimidazole N-vinylpyrrolidone polymers used in the present
invention have an average molecular weight range from 5,000-1,000,000,
preferably from 5,000-200,000.
Highly plef~r,ed polymers for use in detergent co".ro6itions according to
the present invention comprise a polymer selecl~sd from N-vinylimid~-~le N-
vinylpyrrolidone copolymers wherein said polymer has an average n,o'ecul~r
weight range from 5,000 to 50,000 more p,t:reraLly from 8,000 to 30,000, most
preferably from 10,000 to 20,000.
The average molecular weight range was determined by light scattering as
descri62d in Barth H.G. and Mays J.W. Chemical Analysis Vol 113,"Modern
Methods of Polymer Chara-,~, i~dtiOI ,".
Highly preferled N-vinylimidazole N-vinylpyrrolidone copolymers have an
average mcl~cu'-r weight range from 5,000 to 50,000; more preferably from
8,000 to 30,000; most p,eferdbly from 10,000 to 20,000.
The N-vinylimidazole N-vinylpyrrolidone copolymers characterized by
having said average ,nole.,ul~r weight range provide excel'ent dye transfer
inhibiting properties while not adversely affecting the cleaning performance of
detergent con-positions formulated therewith.
The N-vinylimid~-sle N-vinylpyrrolidone copolymer of the present invention has amolar ratio of N-vinylimidazole to N-vinylpy~olidone from 1 to 0.2, more
preferably from 0.8 to 0.3, most preferably from 0.6 to 0.4 .
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46 _
c) Polyvinylpyrrolidone
The detergent compositions of the present invention may also utilize
polyvinylpyrrolidone ("PVP") having an average molecular weight of from about
2 500 to about 400 000 preferably from about 5 000 to about 200 000 more
preferably from about 5 000 to about 50 000 and most preferably from about
5 000 to about 15 000. Suitable polyvinyipyrrolidones are co""nen ially vailablefrom ISP Cor~oralion. New York NY and Mo"t~eal Canada under the product
names PVP K-15 (viscosity mo'ecul~r weight of 10 000~ PVP K-30 (average
mc'ecu~r weight of 40 000) PVP K-60 (average ",oleculqr weight of 160,000),
and PVP K-90 (average molecular weight of 360 000). Other suitable
polyvinylpyrrolidones which are co"~"~ercially available from BASF Cooperation
include Sokalan HP 165 and Sokalan HP 12; polyvinylpyrrolidones known to
persons skilled in the detergent field (see for example EP-A-262,897 and EP-A-
256 696).
d) Polyvinyloxazolidone:
The detergent composilions of the present invention may also utilize
polyvinylox~cl done as a polymeric dye transfer inhibiting agent. Said
polyvinylo~~-,l.dones have an average l"~'ecu'~r weight of from about 2,500 to
about 400 000 prere~bly from about 5 000 to about 200 000 more p~ferably
from about 5 000 to about 50 000 and most preferably from about 5,000 to about
15 000.
e) Polyvinylimidazole:
The detergent compositions of the present invention may also utilize
polyvinylimii~ ole as polymeric dye l~an:jfer inhibiting agent. Said
polyvinylimidazoles have an average about 2 500 to about 400 000 preferably
from about 5 000 to about 200 000 more preferably from about 5,000 to about
50 000 and most preferably from about 5,000 to about 16 000.
f) Cross-linked polymers:
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47
Cross-linked polymers are polymers whose backbone are interconnected to a
certain degree; these links can be of chemical or physical nature, possibly withactive groups n the backbone or on branches; cross-linked polymers have been
described in the Journal of Polymer Science, volume 22, pages 1035-1039.
In one embodill,ent. the cross-linked polymers are made in such a way that
they form a three-dimensional rigid structure, which can entrap dyes in the pores
furl~led by the three-dimensional structure. In another embodiment, the cross-
linked polymers entrap the dyes by swelli~
Such cross-linked polymers are described in the co-pending patent application
9487021 3.9
Method of washing
The compositions of the invention may be used in essentially any washing
or claaning methods, including soaking methods, p~tledlllle,,~ methods and
methods with rinsing steps for which a separate rinse aid composition may be
added.
The process described herein comprises contacting fabrics with a
laundering solution in the usual manner and exemplified hereunder.
The process of the invention is conveniently carried out in the course of
the claaning process. The method of cleaning is preferably carried out at 5~C to95~C, especially betv~een 10~C and 60~C. The pH of the treatment solution is
preferably from 7 to 11.
The following examples are meant to exemplify compositions of the
present invention, but are not necessarily meant to limit or otherwise define the
scope of the invention.
In the detergent comro~itions, the enzymes levels are expressed by pure
enzyme by weight of the total composition and unless otherwise specified, the
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W O 98106811 48 PCT~US97/14288
detergent ingredients are expressed by weight of the total compositions. The
abbreviated component idel,liricalions therein have the following meanings:
LAS : Sodium linear C12 alkyl benzene sulphonate
TAS : Sodium tallow alkyl sulphate
CXYAS : Sodium C1X - C1y alkyl sulfate
25EY : A C12 C1s predominantly linear primary alcohol
condensed with an average of Y moles of ethylene
oxide
CXYEZ : A C1X - C1y predominantly linear primary alcohol
cond~nsed with an average of Z moles of ethylen
oxide
XYEZS : C1X - C1y sodium alkyl sulfate conde,lsed with an
average of Z moles of ethylene oxide per mole
QAS : R2.N+(CH3)2(C2H4OH) with R2 = C12-C14
Soap : Sodium linear alkyl car~oxylate derived from a 80/20
mixture of tallow and coconut oils.
TFM : C16-C1g alkyl N-methyl glucamide.
TPKFA : C12-C14 tOp~l ed whole cut fatty acids.
DEQA : Di-(tallow-oxy-ethyl) dillletllyl ammonium chloride.
SDASA : 1:2 ratio of stearyldin)ell,yl amine:triple-pressed stearic
acid.
Necdol 45-13 : C14-C15 linear primary alcohol ethoxylate, sold by
Shell Chemical CO.
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Silicate : Amorphous Sodium Siiicate (SiO2:Na2O ratio = 2.0)
NaSKS-6 : Crystalline layered silicate of formula ~-Na2Si2Os
Carbonate : Anhydrous sodium carbonate with a particle size
between 200 ~lm and 900~1m.
Bicarbonate : Anhydrous sodium bicarbonate with a particle size
between 400 ~lm and 1200~Lm.
STPP : Anhydrous sodium tripolyphosphate
MA/M : Copolymer of 1:4 maleic/acrylic acid, average
molec~ weight about 80,000
Polyacrylate : Polyacrylate homopolymer with an average molecular
weight of 8,000 sold under the tradename PA30 by
BASF GmbH
Zeolite A : Hydrated Sodium Aluminosi~;c~te of formula
Na12(A1O2SiO2)12. 27H20 having a primary particle
size in the range from 0.1 to 10 micror"eter~
Citrate : Tri-sodium citrate dihydrate of activity 86,4% with a
pallicle size distribution between 425 )lm and 850 ,um.
Citric : Anhydrous citric acid
PB1 : Anhydrous sodium perL,ora~ monohydrate bleach,
empirical formula NaB~2 H2~2
PB4 : Anhydrous sodium perboratetetrahydrate
Percarbonate : Anhydrous sodium percarbonate bleach of empirical
formula 2Na2CO3.3H2O2
., ~,
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TAED : Tetraacetyl ethylenediamine.
NOBS : Nonanoyloxybenzene sulfonate in the form of the
sodium salt.
Photoactivated : Sulfonated zincphtlocyanineencars~ ted in dextrin
Bleach soluble polymer.
Antibody : Rabbit anti /\lc~se provided by Novo Nordisk A/S at
a dilution of 1:1000 (anti-Alca'~se PPA 1619),
Reference 28-901-03; anti-Savinase antibody PPA
1897, available from Novo Nordisk A/S and Anti-
Protease B provided by Genencor.
Prolease : Proteolytic enzyme sold under the tradename
Savinase and AIC-I-SQ by Novo Nordisk A/S,
M~Yarem, I\/I~Y~C~I and Maxatase by Gist-Broc~des
and proteases desc,ibed in patenls WO91/06637
and/orWO95/10591 and/orEP251 446.
Amylase : Amylolytic enzyme sold under the tradename Purafact
Ox AmR described in WO 94118314, W096/05295
sold by Genencor; Termamyl(~), Fungamyl(~ and
Duramyl~), all available from Novo Nordisk AIS and
those described in W095/26397.
Lipase : Lipolytic enzyme sold under the tradename Lipolase,
Lipolase Ultra by Novo Nordisk A/S
Cellulase : Cellulytic enzyme sold under the tradename
Carezyme, Celluzyme and/or Endolase by Novo
Nordisk A/S.
CMC : Sodium carboxymethyl cellulose.
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W098tO6811 51 PCT/US97/14288
HEDP ~ hydroxyethane diphosphonic acid.
DETPMP Diethylene triamine penta (methylene phosphonic
acid), marketed by Monsanto under the Trade name
Dequest 2060.
PVNO : Poly(4-vinylpyridine)-N-Oxide.
PVPVI : Poly (4-vinylpyridine)-N-oxide/copolymer of vinyl-
imidazole and vinyl-pyrrolidone.
B,ighte"er 1 : Disodium 4,4'-bis(2-sulphostyryl)biphenyl.
Brightel)er 2 : Disodium 4,4'-bis(4-anilino-6-~Gr~holino-1 .3.5-triazin-
2-yl) stilbene-2:2'-disulro,)ate.
Silicone anliroa,ll : Polydi",ethylsiloxane foam controller with siloxane-
oxyalkylene copolymer as dispersing agent with a ratio
of said foam controller to said dispersing agent of 10:1
to 100:1.
Granular Suds : 12% Silicone/silica, 18% stearyl alcohol,70% starch in
Suppressor granular form
SRP 1 : Sulfobenzoyl end carped esters with oxyethylene oxy
and terephtaloyl backbone.
SRP 2 : Diethoxylated poly (1,2 propylene le~ephlalate) short
block polymer.
Sulphate : Anhydroussodium sulphate.
HMWPEO : High molecular weight polyethylene oxide
PEG : Polyethylene glycol.
. . .
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Encapsulated: Insoluble fragrance deliver,v technology utilising zeolite
perfume particles 13x, perfume and a dextrose/glycerin agglomerating
binder.
ExamPle 1:
Ant~bodies' production:
Chickens were in,ected in the breast muscle with 1 ml of a 1 mg/ml Savinase~) orAlc~l~se~) emulsion. The ploteolytic emulsion was prepared with a Freunds
completed adjuvants (Freund and McDe,llloll, 1942; Freund 1956) by intensively
mixing an equal amount of Savinase~) or Alc~ e~9 solution (2 mg/ml) and
Freunds complete adjuvant.
The immunisation scheme was completed with injections using a Freunds
uncomplete adjuvant and after a 4 weeks period, the eggs were collected during
one week. The extraction of the antibodies from the eggs yolks was done
according to the Polson extraction method as described in Immunological
Investigation 19, 1990, pp 253-258.
Protease enzymatic inactivation:
A Savinase~ or Alc~ stock solution was prepared in a Tris Buffer (5x1 o-2M
Tris, 25 mM NaCI, pH=8) at a concel,l,dlion of 0.05% active enzyme. A
rl,osphate Buffer (0.05M KH2PO4, pH 6.8)conlained the antibody (0.18 mg/ml).
The interaction proteolytic enzyme (Final concenl,dlion 0.004%) / antibody was
achieved in cGmn)ercially available detergent solutions co~"prisi"g Ariel liquid(0.8% in cit,v water, pH 8.5) and Ariel Color Futur(0.8% in city water, pH 9.5)
during 15 minutes at 40~C.
The proteolytic residual activit,v was measured accordi"g the method described
in Delmar et al.(1979) Anal. Biochem. 99, pp316-320. Within 5 minutes the
enzymatic activity of the prutease was successfully blocked as shown in the table
below.
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W O98/06811 PCTAUS97/14288
Residual proteolytic activity
(in % after 5 minutes)
ProteasQ Ariel liquid Ariel ColorFutur
Savinase~g) 19 20
' AIC~IASe~) 1 1
Exa,,,Ple 2
The following laundry detergent con,positions were prepared in accord with the
invention:
11 111 lV V Vl
LJ~S 8.0 8.0 8.0 8.0 8.0 8.0
C25E3 3.4 3.4 3.4 3 4 3 4 3 4
Q A S - 0.8 0.8 - 0.8 0.8
Zeolite A 18.1 18.1 18.1 18.1 18.1 18.1
Carbonate 13.0 13.0 13.0 27.0 27.0 27.0
Silicate 1.4 1.4 1.4 3.0 3.0 3.0
Sulfate 26.1 26.1 26.1 26.1 26.1 26.1
PB4 9.0 90 90 90 9.0 9.0
TAED 1.5 1.5. 1.5 1.5 1.5 1.5
DETPMP 0.25 0.25 0.25 0.25 0.25 0.25
HEDP 0.3 03 03 03 03 03
Amylase O.OOOg 0.0009 0 0009 0.0009 0.0009 0.0009
P,otease 0.15 0.005 0.004 0.002 0.001 0.1
Antibody 0.5 0.01 0.1 0.01 0.001 1.0
MA/M 0.3 0.3 0.3 0.3 03 03
CMC 0.2 0.2 0.2 0.2 0.2 0.2
rl ,otoactivated 15 15 15 15 15 15
bleach (ppm)
Brightener 1 0.09 0.09 0.09 0.09 0.09 0.09
Perfume 0.3 0.3 0 3 0 3 0 3 0 3
Silicone a,lliroa." 0.5 0.5 0.5 0.5 0.5 0.5
Misc/minors to 100%
. .
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Density in g/litre 850 850 850 850 850 850
Example 3
The following granular laundry detergent compositions of bulk density 750 g/litre
were prepared in accord with the invention:
11
LAS 5.25 5.61 4.76
TAS 1.25 1.86 1.57
C45AS - 2.24 3.89
C25AE3S - 0.76 1.18
C45E7 3.25 - 5.0
C25E3 ~ 5-5
QAS 0.8 2.0 2.0
STPP 19.7 - -
Zeolite A - 19.5 19.5
NaSKS-6/citric acid (79:21) - 10.6 10.6
Carbonate 6.1 21.4 21.4
Bicarbonate - 2.0 2.0
Silicate 6.8
Sodium sulfate 39.8 - 14.3
PB4 5.0 12.7
TAED 0.5 3.1
DETPMP 0.25 0.2 0.2
HEDP - 0.3 0.3
Antibody 0.01 0.1 1.0
P~otease 0.0026 0.0085 0.08
Lipase 0.003 0.003 0.003
Cellu'-~ 0.00064 0.00064 0.00064
Amylase 0.0009 0.0009 0.0009
MA/M 0.8 1.6 1.6
CMC 0.2 0.4 0.4
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Photoactivated bleach 15 ppm27 ppm 27 ppm
(ppm)
Brightener 1 0.08 0.19 0.19
Brightener 2 - 0.04 o 04
Enc~pslJI~ted perfume 0.3 0.3 0.3
particles
Silicone anliroarll0.5 2.4 2.4
Minors/misc to 100%
ExarnplE 4
The following detergenl formulations, according to the present invention were
prepared, where I is a phosphorus-containing detergent coi"posilion, Il is a
zeolite-containing detergent composition and lll is a compact detergenl
composition:
l~
Blown Powder
STPP 24.0 - 24.0
Zeolite A - 24.0
C45AS 9.0 6.0 13.0
MA/M 2.0 4.0 2.0
IAS 6.0 8.0 11.0
TAS 2.0
Silicate 7.0 3.0 3.0
CMC 1.0 1.0 0.5
Briy~llener 2 0.2 0.2 0.2
Soap 1.0 1.0 1.0
DETPMP 0.4 0.4 0.2
Spray On
C45E7 2.5 2.5 2.0
C25E3 2.5 2.5 2.0
Silicone anliroa"- 0.3 0.3 o 3
Perfume 0.3 0.3 03
Dry additives
.. . . . . . .. . ....
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Carbonate 6.0 13.0 15.0
PB4 18.0 18.0 10.0
PB1 4.0 4.0 0
TAED 3.0 3.0 1.0
Photoactivated bleach 0.02 0.02 0.02
Plotease 0.01 0.002 0.05
Lipase 0.009 0.009 0.009
Amylase 0.002 0.003 0.001
Antibody 0.03 0.03 0 5
Dry mixed sodium sulfate 3.0 3.0 5.0
Balance (Moisture & 100.0 100.0 100.0
Miscellaneous)
Density (g/litre) 630 670 670
ExamPle 5
The following nil bleach-containing detergent forrnulations of particular use in the
washing of colored clothing, accGrJing to the present invention were prepared:
ll lll
Blown Powder
Zeolite A 15.0 15.0
Sodium sulfate 0.0 5.0
LAS 3.0 3.0
DETPMP 0.4 0.5
CMC 0.4 0.4
MA/M 4.0 4.0
Agglomerates
C45AS - - 11.0
LAS 6.0 5.0
TAS 3.0 2.0
Silicate 4.0 4.0
Zeolite A 10.0 15.0 13.0
CMC - - 0.5
MA/M - - 2.0
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W O 98/06811 PCT~US97/14288
Carbonate 9.0 7.0 7 0
Spray On
Perfume 0.3 0.3 0.5
C45E7 4.0 4.0 4.0
C25E3 2.0 2.0 2.0
Dry additives
MAJM - - 3.0
NaSKS-6 - - 12.0
Citrate 10.0 - 8.0
Bicarbonate 7.0 3.0 5.0
Carbonate 8.0 5.0 7.0
PVPVI/PVNO 0.5 0.5 0.5
Lipase 0.009 0.009 0.009
Amylase 0.005 0.005 0.005
Cellulase 0.0014 0.0014 0.0014
Protease 0.05 0.03 0.007
Antibody 0.8 0.1 0.2
Silicone anli~", 5.0 5.0 5.0
Dry additives
Sodium sulfate 0.0 9.0 0.0
Balance (Moisture and 100.0 100.0 100.0
Misce"arleous)
Density(g/litre) 700 700 700
ExamDle 6
The following deteryent formulations, according to the present invention were
prepared:
11 111 lV
LAS 20.0 14.0 24.0 22.0
QAS 0.7 1.0 - 0.7
TFM - 1.0
C25E5/C45E7 - 2.0 - 0.5
C45E3S - 2.5
. . .
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STPP 30.0 18.0 30.0 22.0
Silicate 9.0 5.0 10.0 8.0
Carbonate 13.0 7.5 - 5.0
Bicarbonate - 7.5
DETPMP 0.7 1.0
SRP 1 0.3 0.2 - 0.1
MAIM 2.0 1.5 2.0 1.0
CMC 0.8 0.4 0.4 0.2
Protease 0.08 0.002 0.02 0.005
Amylase 0.007 0.004 - 0.002
Lipase 0.004 0.002 0.004 0.002
Cellulase 0.0004 0.0001
Antibody 0.3 0.16 0.2 0.01
Photoactivated 70ppm 45ppm - 1 Oppm
bleach (ppm)
Brightener1 0.2 0.2 0.08 0.2
PB1 6.0 2.0
NOBS 2.0 1.0
Balance (Moisture 100 100 100 100
and l\l sc~"~neous)
Exam~le 7
The following detergent formulations, according to the present invention were
prepared:
11 111 lV
Blown Powder
Zeolite A 30.0 22.0 6.0 6.7
Na SkS-6 - - - 3.3
Polycarboxylate - - - 7.1
Sodium sulfate 19.0 5.0 7.0
MA/M 3.0 3.0 6.0
LAS 14.0 12.0 22.0 21.5
C45AS 8.0 7.0 7.0 5.5
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Cationic - - - 1.0
Silicate - 1.0 5.0 11.4
Soap - - 2.0
Brightener 1 0.2 0.2 0.2
Carbonate 8.0 16.0 20.0 10.0
DETPMP - 0.4 0.4
Spray On
C45E7 1.0 1.0 1.0 3.2
Dry additives
PVPVI/PVNO 0.5 0.5 0.5
Antibody 0.2 0.09 0.15 0.05
Pn~tease 0.053 0.01 0.005 0.01
Lipase 0.009 0.009 0.009 0.009
Amylase 0.0008 0.0008 0.0008 0.0008
Cellulase 0.0002 0.0002 0.0002 0.0002
NOBS - 6.1 4.5 3.2
PB1 1.0 5.0 6.0 3.9
Sodium sulfate - 6.0 - tobalance
Balance (Moisture and 100 100 100
Miscellaneous)
Exa,-,Ple 8
The following high density and bleach-col)ta;ning detergent formulations,
according to the present invention were prepared:
ll lll
Blown Powder
Zeolite A 15.0 15.0 15.0
Sodium sulfate 0.0 5.0 0.0LAS 3.0 3.0 3.0
QAS - 1.5 1.5
DETPMP 0.4 0.4 0.4
CMC 0.4 0.4 0 4
MA/M 4.0 2.0 2.0
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Agglomerates
LAS 5.0 5.0 5.0
TAS 2.0 2.0 1.0
.Si~i~te 3.0 3.0 4.0
Zeolite A 8.0 8.0 8.0
Carl,~"ate 8.0 8.0 4.0
Spray On
Perfume 0.3 0.3 0.3
C45E7 2.0 2.0 2.0
C25E3 2.0 -
Dry additives
Citrate 5.0 - 2.0
Bica.Lonat_ - 3.0
Ca,L,o"ate 8.0 15.0 10.0
TAED 6.0 2.0 5.0
PB1 14.0 7.0 10.0
Polyethylene oxide of MW - - 0.2
5,000,000
Bentonite clay - - 10.0
Antibody 1.0 0.05 0.01
Protease 0.1 0.01 0.007
Lipase 0.009 0.009 0 009
Amylase 0.005 0.005 0.005
Cellulase 0.0014 0.0014 0.0014
Silicone a"t;i~&n, 5.0 5.0 5.0
Dry additives
Sodium sul~ate 0.0 3.0 0.0
Balance (Moisture and 100.0 100.0 100.0
Misc~ ,eous)
Density(g/litre) 850 850 850
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Example 9
The following high density detergent formulations, according to the present
invention were prepared:
ll
Ag~lo,nerate
C45AS 11.0 14.0
Zeolite A 15.0 6.0
C~lLG~Idt~ 4.0 8.0
MAIM 4.0 2.0
CMC 0.5 0.5
DETPMP 0.4 0.4
Spray On
C25E5 5.0 5.0
Perfume 0.5 0.5
Dry Adds
HEDP 0.5 0.3
SKS 6 13.0 10.0
Citrate 3.0 1.0
TAED . 5.0 7.0
rer~a,LGI-~t~3 20.0 20.0
SRP 1 0.3 0.3
AlllilJGJy 0.05 0.015
rtot~asc 0.014 0.005
Lipase 0.009 0.009
Cellulase 0.0014 0.0014
Amylase 0.005 0.005
Silicone autif~a.-, 5.0 5.0
Brightener 1 Q.2 0.2
B~iyhteller 2 0.2
Balance (1~1~isture and 100 100
Miscellaneous)
Density(g/litre) 850 850
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Example 10
The following granular detergent formulations, according to the present invention
were prepared:
11 111 lV V
LAS 21.0 25.0 18.0 18.0
Coco C12-14 AS - - - - 21.9
AE3S - - 1.5 1.5 2.3
Decyldimethyl hydroxyethyl - 0.4 0.7 0.7 0.8
NH4+CI
Nonionic 1.2 - 0.9 0.5
Coco C12-14 Fatty Alcohol - - 1.0
STPP 44.0 25.0 22.5 22.5 22.5
Zeolite A 7.0 10.0 - - 8.0
MAIM - - 0.9 0.9
SRP1 0.3 0.15 0.2 0.1 0.2
CMC 0.3 2.0 0.75 0.4 1.0
Carbonate 17.5 29.3 5.0 13.0 15.0
Silicate 2.0 - 7.6 7.9
Antibody 0.16 0.5 0.1 0.9 10.0
F'luteasc 0.005 0.04 0.007 0.09 0.15
Amylase - 0.004 0.004 - .004
Lipase 0.003 0.003 0.003
Cellulase - 0.001 0.001 .001 .001
NOBS - - - 1.2 1.0
PB1 - - - 2.4 1.2
Diethylene triamine penta - - - 0.7 1.0
acetic acid
Diethylene triamine penta - - 0.6
methyl phosphonic acid
Mg Sulfate - - 0.8
Pl ,otoactivated bleach 45 50 ppm 15 45 ppm 42
ppm ppm ppm
B-iyhte"er 1 0.05 - 0.04 0.04 0.04
Brightener 2 0.1 0.3 0.05 0.13 0.13
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Water and Minors up to 100%
Example 12
The follc~r;ng liquid detergent formulations, according to the present inventionwere prepared:
11 111 lV V Vl Vll Vlll
LAS 10.0 13.0 9.0 - 25.0
C25AS 4.0 1.0 2.0 10.0 - 13.0 18.0 15.0
C25E3S 1.0 - - 3.0 - 2.0 2.0 4.0
C25E7 6.0 8.0 13.0 2.5 - - 4.0 4.0
TFM - - - 4.5 - 6.0 8.0 8.0
QAS - - - - 3.0 1.0
TPKFA 2.0 - 13.0 2.0 - 15.0 7.0 7.0
Rapeseed fatty - - - 5.0 - - 4.0 4.0
acids
Citric 2.0 3.0 1.0 1.5 1.0 1.0 1.0 1.0
Dodecenyl/ 12.0 10.0 - - 15.0
tetradecenyl
succinic acid
Oleic acid 4.0 2.0 1.0 - 1.0
Ethanol 4.0 4.0 7.0 2.0 7.0 2.0 3.0 2.0
1,2 Plupanediol 4.0 4.0 2.0 7.0 6.0 8.0 10.0 13.-
Mono Ethanol - - - 5.0 - - 9.0 9.0
Amine
Tri Ethanol - - 8
Amine
NaOH (pH) 8.0 8.0 7.6 7.7 8.0 7.5 8.0 8.2
Ethoxylated 0.5 - 0.5 0.2 - - 0.4 0.3
tetraethylene
pentamine
DETPMP 1.0 1.0 0.5 1.0 2.0 1.2 1.0
SRP 2 0.3 - 0.3 0.1 - - 0.2 0.1
PVNO - - - - - - - 0.10
.,
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Antibody 0.1 0.01 10E- 0.1 .001 10.0 0.01 .001
Protease 0.16 .002 .005 0.08 .008 0.1 0.01 .006
Lipase - .002 - .0002 - - .003 .003
Amylase .002 .002 - .004 .002 - .005 .005
Cellulase - - - .001 - - .002 .001
Boric acid 0.1 0.2 - 2.0 1.0 1.5 2.5 2.5
Na fo~ dte - - 1.0
Ca chloride - 0.015 - 0.01
Bentonite clay - - - - 4.0 4.0
Suspending clay - - - - 0.6 0.3
SD3
Balance Moisture 100 100 100 100 100 100 100 100
and
Miscell~neou
Example 12
Granular fabric cleaning co,-~positions which provide surtening through the
wash" capability were prt:pdr~d in accord with the present invention:
45AS - 10.0
LAS 7.6
68AS 1 3
45E7 4.0
25E3 5.0
Coco-alkyl cli."ethyl hydroxy- 1.4 1.0
ethyl a"""onium chloride
Citrate 5.0 3.0
Na-SKS-6 - 11.0
Zeolite A 15.0 15.0
MA/AA 4.0 4.0
DETPMP 0.4 0.4
PB1 15.0
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Percarbonate - 15.0
TAED 5.0 5.0
Smectite clay 10.0 10.0
HMWPEO - 0.1
Antibody 0.075 0.1
Protease 0.02 0.006
Lipase 0.02 0.01
Amylase 0.03 0.005
CelhJI~se 0.001
Silicate 3.0 5.0
Carbonate 10.0 10.0
Granular suds suppressor 1.0 4.0
CMC 0.2 0.1
Water/minors Up to 100%
ExamDle 13
The following rinse added fabric softener cor"position was prepared in
accord with the present invention:
Softener active 20.0
Antibody 0.01
P~otease 0-005
Cellulase 0.001
HCL 0 03
Antifoar" agent 0.01
Blue dye 25ppm
CaCI2 0.20
Perfume 0 90
Water / minors Up to 100%
.. .. .
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Example 14
The following fabric softener composition was prepared in accord with the
present invention:
ll lll
DEQA 2.60 19.00
SDASA - 70 o
Stearic acid of IV=0 0.30
Neodol 45-13 - - 13.0
Hydrochloride acid 0.02 0.02
Ethanol - - 1.0
PEG - 0.60
Antibody 0.1 0.1 1.0
Protease 0.01 0.008 0.05
Perfume 1.00 1.00 0.75
Digeranyl Succindte - - 0.38
Silicone anlirod") 0.01 0.01
Electrolyte - 600ppm
Dye 100ppm 50ppm 0.01
Water and minors 100% 100%
ExamDle 15
Syndet bar fabric cleaning c~""~ositions were prepared in accord with the
present invention:
11 111 lV
C26 AS 20.00 20.00 20.00 20.00
CFM 5.0 5.0 5.0 ~.0
LAS (C11-13) 10.0 10.0 10.0 10.0
Sodium carbonate 25.0 25.0 25.0 25.0
Sodium pyrophosphate 7.0 7.0 7.0 7.0
STPP 7.0 7.0 7.0 7.0
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ZeoliteA 50 50 50 50
CMC 0.2 0.2 0.2 0.2
Polyacrylate (MW 1400)0.2 0.2 0.2 0.2
Coconut monethanolamide 5.0 5.0 5.0 5.0
Antibody 0.1 0.1 0.01 0.001
Amylase 0.01 - 0.01
P~olease 0.08 0.01 0.005 0.001
B,iyl,tener, perfume 0.2 0.2 0.2 0.
CaS04 1.0 1.0 1.0 1.0
MgSO4 1.0 1.0 1.0 1.0
Water 4.0 4.0 4.0 4.0
Filler~: balance to 100%
~Can be selecl~d from convenient materials such as CaC03, talc, clay (Kaolinite,S",e~;tite), silicates, and the like.
Example 16
Deteryel)~ additives were prepared in accord with the present invention:
ll lll
LAS - - 5
STPP 30 30
Zeolite A - - 35
PB1 20 20 15
TAED 10 10 8
r~ot~ase 0-3 - 0-3
Amylase 0. 1
Antibody 10 10 1.0
