CA2396974C - Liquid laundry detergent compositions having enhanced clay removal benefits - Google Patents

Abstract

The present invention relates to liquid laundry detergent compositions which provide enhance hydrophilic soil cleaning benefits, said compositions comprising: a) from about 0.01 to about 20 % by weight, of a zwitterionic polymer which comprises a polyamine backbone, said backbone comprising two or more amino units where in at least one of said amino units is quaternized end wherein at least one amino unit is substituted by one or more moieties capable of having an anionic charge wherein further the number of amino unit substitutions which comprise an anionic moiety is less than or equal to the number of quaternized backbone amino units; b) from about 0.1 % to about 7 % by weight, of a polyamine dispersant; c) from about 0.01% to about 80 % by weight, of a surfactant system comprising one or more surfactants selected from the group consisting of nonionic, anionic, cationic, zwitterionic, ampholytic surfactants, and mixtures thereof; and d) the balance carriers an d adjunct ingredients.

Description

LIQUID LAUNDRY DETERGENT COMPOSITIONS
HAVING ENHANCED CLAY REMOVAL BENEFITS
FIELD OF THE INyENTTON
The present invention relates to nil bleach liquid laundry,detergent compositions which provide enhanced hydrophilic soil, inter olio, clay, r~wval benefits. The laundry detergent compositions of the present invention combine zwitterionic polyamines, a polya'tkyleneimine dispersant, and a surfactant system which comprises mid-chain branched s~urfactat~ts inter olio mid-chain branched alkyl sulphates and provides hydrophobic soil removal in the absence of a bleaching system. The present invention fiuther relates to methods for cleaning fabric having heavy clay soil deposits.
BACKGROUND OF THE IIWENT'ION
Fabric, especially clothing, can become soiled with a variety of foreign substances ranging from hydrophobic stains (grease, oil) to hydrophilic stains (cla ). The level of cleaning which is necessary to remove said foreign substances depends to a large degree upon the amount of stain present and the degree to which the foreign substance has contacted the fabric fibers. Grass stains usually involve direct abrasive contact with vegetative matter thereby producing highly penetrating stains. Clay soil stains, although in some instances contacting the fabric fibers with less force, nevertheless provide a different type of soil removal problem due to the high degree of charge associated with the clay itself. This high surface charge density may act to repel some laundry adjunct ingredients, inter alto, clay dispersants, thereby resisting any appreciable removing or carrying away of the clay into the laundry liquor.
A s~ per se is not all that is necessary to remove unwanted clay soils and stains. In fact, not all suW work equally well on alI types of stains. In addition to surfactants, polyamine hydrophilic soil dispersants are added to laundry detergent compositions to "carry away" clay soils from the fabric surface and to reduce or lower the possibility that the clay soil. wi71 be re-deposited upon the fabric. However, unless the clay can be initially removed frown the fabric fiber, especially in the case of hydrophilic fibers, inter olio, cotton, there will be nothing in solution for the added dispersants to remove. Therefore, there is a long felt need for a detergent system which will ensure that the soils will be removed from fabric so that the surfactants and dispersants can effectively remove the soils and prevent redeposition.
There is a long felt need in the art for liquid laundry detergent compositions which can effectively remove embedded clay and other hydrophilic soils from fabric. The desired laundry , detergent compositions will effectively remove the embedded soils and prevent the soils from being xe-deposited onto the fabric surface.
SUMMARY OF THE INVENTION
The present invention meets the aforementioned needs in that it has been surprisingly discovered that certain zwitterionic polyamines in combination with one or more polyamine dispersants provides enhanced removal of clay and other hydrophilic soils from fabric.
The first aspect of the present invention relates to a liquid laundry detergent composition comprising:
a) from about 0.01 %, preferably from about 0.05 %, more preferably from 0.1 %
to about 20%, preferably to about 10%, more preferably to about 3% by weight, of a zwitterionic polymer which comprises a polyamine backbone, said backbone comprising two or more amino units wherein at least one of said amino units is quaternized and wherein at least one amino unit is substituted by one or more moieties capable of having an anionic charge wherein fixrther the number of amino unit substitutions wluch comprise an anionic moiety is less than or equal to the number of quaternized backbone amino units;
b) from about 0.1%, preferably from about 0.5%, more preferably from about 1%
to about 7%, preferably to about 5%, more preferably to about 3% by weight, of a polyamine dispersant;
c) from about 0.01%, preferably from about 0.1% more preferably from about 1%
to about 100%, preferably to about 80% by weight, preferably to about 60%, most preferably to about 30% by weight, of a surfactant system comprising one or more surfactants selected from the group consisting of nonionic, anionic, cationic, zwitterionic, ampholytic surfactants, and mixtures thereof; and d) the balance carriers and adjunct ingredients.
A further aspect of the present invention relates to compositions which comprise:

a) from about 0.01%, preferably from about 0.05%, more preferably frown 0.1%
to about 20%, preferably to about 10%, more preferably to about 3% by weight, of a zwitterianic polyamine according to the present invention;
b) from about 0.1 %, preferably from about 0.5%, more preferably from about 1 % to about 7%, preferably to about 5%, more preferably to about 3 % by weight, of a polyamine dispersaat;
c) from about 0,01%, preferably from about 0.1% more preferably from about 1%
to about 100%, preferably to about 80% by weight, preferably to about 60%, most preferably to about 30% by weight, of a surfactant system comprising:
i) from 0.01 % by weight, of a mid-chain branched alkyl sulfate su~ant, a mid-chain branched alkyl alkoxy sulfate surfactant, and mixtures thereof;
ii) from 0.01 % by weight, of a surfactant selected from the group comsistmg of anionic, nonionic, and mixtures thereof;
c) from about 0.001% by weight, of a detersive enzyme, said enzyme selected from the group consisting of protease, amylases, lipases, cellulases, peroxidases, hydrolases, cutinases, mannanases, xyloglucanases, and mixtures thereof; and , d) the balance carriers and adjunct ingredients.
The present invention also relates to a method for removing hydrophilic stains from fabric by cornacting fabric in need of cleaning with a composition according to the present invention.
These and other objects, features and adva~ges will become apparent to dose of ordinary skill in the art from a reading of the following detailed description and the appended claims. All percentages, ratios and proportions herein are by weight, unless otherwise specified. AlI
temperatures are in degrees Celsius (o C) unless otherwise specified.
DETAILED DESCRIPTION OF THE INVENTION
The present invention relates to the surprising discovery that the combination of a zwitterio~nic polyamine and an ethoxylate polyamine dispersant provides enhanced benefits for removal of clay soil from fabric, especially clothing, in a liquid laundry detergent matrix. In addition, the present invention relaxes to a zwitterionic polymer/polyamine dispersant system which is compatible with one or more enzymes.

It has been surprisingly discovered that the formulator, by selecting the relative degree of quaternization of the polyamine backbone, the type and relative degree of incorporation of anionic units which substitute the polyamine backbone, and the nature of the amine backbone itself, is able to foam a zwitterionic polymer which can be tailored for optimization depending upon the desired execution. Preferably, as described herein below, the zwitterionic polymers which are incorporated into liquid laundry detergent compositions have an excess number of quaternized backbone nitrogens relative to the number of anionic units which are present.
For the purposes of the present invention the term "charge ratio", Qr, is defined herein as "the quotient derived from dividing the sum of the number of anionic units present excluding counter ions by the sum of the number of quaternary ammonium backbone units".
The charge ratio is defined by the expression:
Q - ~ q~~o r ~ q~a~o~o wherein qa"lo~~ is an anionic unit, inter alia, -S03M, as defined herein below and q~atlo"~~ represents a quaternized backbone nitrogen.
Those of skill in the art will realize that the greater the number of amine units which comprise the polyamine backbones of the present invention the greater the number of potential cationic units will be contained therein. For the purposes of the present invention the term "degree of quaternization" is defined herein as "the number of backbone units which are quaternized divided by the number of backbone units which comprise the polyamine backbone". The degree of quaternization, Q(+), is defined by the expression:
Q(+) - ~ quaternized backbone nitrogens ~ quaternizable backbone nitrogens wherein a polyamine having all of the quaternizable backbone nitrogens quaternized will have a Q(+) equal to 1. For the purposes of the present invention the term "quaternizable nitrogen" refers to nitrogen atoms in the polyamine backbone which are capable of forming quaternary ammoilium ions. This excludes nitrogens not capable of ammonium ion formation, ihter° alia, amides.
For the purposes of the present invention the term "anionic character", 4Q, is defined herein as "the sum ofthe number of anionic units which comprise the zwitterionic polymer minus the number of quaternary ammonium backbone units". The greater the excess number of anionic units, the greater the anionic character ofthe zwitterionic polymer. It will be recogiuzed by the formulator that some anionic units may have more than one unit which has a negative charge. For the purposes of the present invention units having more than one negatively charged moiety, -CHzCH(S03M)CHZS03M, ihter alia, will have each moiety capable of having a negative charge counted toward the sum of anionic units. The anionic character is defined by the expression:
~Q = ~ qznionic " ~ qca$oruc wherein q~,lo,~~ and q~a~;oru~ are the same as defined herein above.
As described herein below, a key aspect of the present invention is the finding that the formulator, by adjusting the parameters Qr, ~Q, and Q(+), will be capable of customizing a polymer to formulate liquid laundry detergent compositions having enhanced particulate soil removal benefits throughout a wide variety of settings, for example as a function of (1) the nature of the polymeric structure itself (e.g., EO level, MW, length and HLB of the amine backbone, etc.), (2) the detergent matrix (e.g., pH, type of surfactant), (3) the particular embodiment (e.g., liquids, gel, structured liquid, non-aqueous, etc.), and (4) desired benefit (e.g., clay stain removal, whiteness, dingy cleaning, etc.). Therefore, in one desired embodiment the zwitterionic polymers of the present invention may have a Qr of from about 1 to about 2, whereas another embodiment will employ zwitterionic polymers having a Qr greater than 2. Specific embodiments, as described herein below, may require a Qr significantly less than 1 or even zero.
Liquid laundry detergent compositions may comprise clay soil dispersants which adsorb on the anionic surfaces of dislodged clay particles and form a stabilized suspension of the particles and hold the particles in solution until they are removed during the rinsing process thus preventing the particles from re-depositing upon the fabric surface. An example of preferred hydrophilic dispersants which are further described herein below, is a dispersant which comprises a polyethyleneimine backbone having an average molecular weight of about 189 daltons and in which each nitrogen which comprises said backbone has the appended hydrogen atom replaced by an ethyleneoxy unit having from 15 to 18 residues on average. This preferred ethoxylated polyethyleneimine dispersant is herein after referred to as PEI 189 E15-18.
This dispersant is highly effective in dispersing clay soils once the clay soils are removed from fabric.
Subtle changes to the structure of polyalkyleneimines can provide profound changes to the properties thereof. For example, a preferred hydrophobic dispersant capable of dispersing soot, grime, oils, carbonaceous material, comprises a polyethyleneimine having a backbone with an average molecular weight of about 1800 daltons and i11 which each nitrogen which comprises said backbone has the appended hydrogen atom replaced by an ethyleneoxy unit having from about 0.5 to about 10 residues on average, preferably an average of 7 residues, for example, PEI 1800 E7.
The ability to affect profound changes in the properties of polyamines by making small changes to the structure of said polyamines is known and appreciated throughout the laundry art.
Knowing the propensity of these polyamines to exhibit activity in the aqueous laundry liquor, it is therefore surprising and highly unexpected that zwitterionic polyamines having hydrophilic backbone components would act synergistically with certain ethoxylated polyalkyleneimines to enhance the removal of clay and other hydrophilic soils directly from fabric fiber itself. Without wishing to be bound by theory it is believed the zwitterionic polyamines of the present inve~ion interact with ethoxylated polyalkyleneimines in a manner which makes clay and other soils easier to remove foam fabric surfaces. It is believed this system absorbs the clay or other particles from the fiber surface and the inherent agitation associated with the laundry process (for example, the agitation provided by an automatic washing machine) acts to break the once formed complexes loose from the fabric surface and disperse them into solution.
The following is a detailed description of the require elements of the preseat invention.
Zwitterionic Polvamines The zwitterionic polyamines of the present invention comprise from about 0.01%, preferably from about 0.05%, more preferably from 0.1% to about 20%, preferably to about 10%, more preferably to about 3 % by weight, of the final laundry detergent composition. The zwitterionic polymers ofthe present invention are suitable for use in liquid laundry detergent compositions, inter olio, gels, thixotropic liquids, and pourable liquids (i.e., dispersions, isotropic solutions).
The zwitterionic polymers of the present invention are comprised of a polyamine backbone wherein the backbone units which connect the amino units can be modified by the fomaulxtor to achieve varying levels of product enhancement, inter olio, boosting of clay soil removal by surfactants, greater effectiveness in high soil loading usage. In addition to modification of flue backbone compositions, the formulator may preferably substitute ome or more of the backbone amino unit hydrogens by other units, inter olio, alkyleneoxy units having a terminal anionic moiety.
In addition, the nitrogens of the backbone may be oxidized to the N-oxide.
Preferably at least two of the nitrogens of the polyamine backbones are quaternized.
For the purposes of the present invention "cationic units" are defined as 'nits which are capable of having a positive charge". For the purposes of the zwitrerionic polyamines of the present invention the cationic units are the quaternary ammonium nitrog~s of the polyamine backbones. For the purposes of the present invention "aiuonic units" are defined as "units which are capable of having a negative charge". For the purposes of the zwitterionic polyamines of the present invention the anionic units are "units which alone, or as a part of another unit, substitute for hydrogen atoms of the backbone nitrogens along the polyamine backbone" a non-limiting example of which is a -(CHZCHZO)zoS03Na which is capable of replacing a backbone hydrogen on a nitrogen atom.
The zwitterionic polyamines of the present invention have the formula:
[J-R]n-J
wherein the [J-R] units represent the amino units which comprise the main backbone and any branching chains. Preferably the zwitterionic polyamines prior to modification, i~ter° alia, quaternization, substitution of a backbone unit hydrogen with an alkyleneoxy unit, have backbones which comprise from 2 to about 100 amino units. The index n which describes the number of backbone units present is further described herein below.
J units are the backbone amino units, said units are selected from the group consisting of i) primary amino units having the formula:
~Rl)zN.
ii) secondary amino units having the formula:
- R1N.
iii) tertiary amino units having the formula:
B
-N.
iv) primary quaternary amino units having the formula:
(Ri)ZN
Q;
v) secondary quaternary amino units having the formula:

I
Q;
vi) tertiary quaternary amino units having the formula:
B
I
Q;

vii) primary N-oxide amino units having the formula:
~Ri)z viii) secondary N-oxide amino units having the formula:

O
ix) tertiary N-oxide amino units having the formula:
B
-N
0.
x) and mixtures thereof.
B units which have the formula:
[J-R]-represent a continuation of the zwitterionic polyamine backbone by branching.
The number of B
units present, as well as, any further amino units which comprise the branches are reflected in the total value of the index n.
The backbone amino units of the zwitterionic polymers are connected by one or more R
units, said R units are selected from the group consisting of i) CZ-C12 linear allcylene, C3-Clz branched alkylene, or mixtures thereof;
preferably C3-C6 alkylene. When two adjacent iutrogens of the polyamine backbone are N-oxides, preferably the allcylene backbone unit which separates said units are units or greater.
ii) alkyleneoxyalkylene units having the formula:
-(R20)~,(R3)-wherein RZ is selected from the group consisting of ethylene, 1,2-propylene, 1,3-propylene, 1,2-butylene, 1,4-butylene, and mixtures thereof; R3 is CZ-C$
linear alkylene, C3-C$ branched alkylene, phenylene, substituted phenylene, and mixtures thereof; the index w is from 0 to about 25. R2 and R3 units may also comprise other backbone units. When comprising alkyleneoxyallcylene units RZ and R3 units are preferably mixtures of ethylene, propylene and butylene and the index w is from l, preferably from about 2 to about 10, preferably to about 6.

iii) hydroxyalkylene units having the formula:

I
-(CH~~(CH)y(CHZ)Z
wherein R4 is hydrogen, Cl-C4 alkyl, -(R20)tY, and mixtures thereof. When R
units comprise hydroxyalkylene units, R4 is preferably hydrogen or -(R20)tY
wherein the index t is greater than 0, preferably from 10 to 30, and Y is hydrogen or an anionic unit, preferably -S03M. The indices x, y, and z are each independently from 1 to 6, preferably the indices are each equal to 1 and R4 is hydrogen (2-hydroxypropylene unit) or (R20)tY, or for polyhydroxy units y is preferably 2 or 3. A preferred hydroxyalkylene unit is the 2-hydroxypropylene unit which can, for example, be suitably formed from glycidyl ether forming reagents, inter alia, epihalohydrin.
iv) hydroxyalkylene/oxyalkylene units having the formula:

(CH2)x(C~y(CHz)z~r (Rz0)w (CHz)~CH)y(CH~z~r j k wherein R2, R4, and the indices w, x, y, and z are the same as defined herein above.
X is oxygen or the amino unit -NR4-, the index r is 0 or 1. The indices j and k are each independently from 1 to 20. When alkyleneoxy units are absent the index w is 0. Non-limiting examples of preferred hydroxyallcyleneloxyalkylene units have the formula:
OH OH
-CHZCHCHzO-(CHzCH2CHz0)z-CHZCHCHz-.
OH OH OH
-CHZCHCHzO-(CHZCH20)3 CHZCHCHzO CHZCHCHz OH OH
CHZCHCHZO-(CH2CH20) CH2CHCH2-OH OH
CH2CHCH20-(CHZCHZCH20)4 CH2CHCH2-z v) carboxyalkyleneoxy units having the formula:
O O
-(R30)w(R3)w~r-C-(~r-R3' ~r-C-(X)r(R3)w(OR3)w-.
wherein Rz, R3, X, r, and w are the same as defined herein above. Non-limiting examples of preferred carboxyalkyleneoxy units include:

II II
- Via- C- 0- ~~~z~2- 0- C- ~-.

-~-C-~ ~ ~ ~-C-(CH2CHZCH20)4-C ~ ~ C-(OCHZCH2CH~4-vi) backbone branching units having the formula:
Rø R4 (CH2)x(C)v(CH2)z(~r (R20)w (CH2)x(C)Y(CH2)z(~r j k wherein R4 is hydrogen, Cl-C6 alkyl, -(CHz)u(Rz0)c(CHz)"Y, and mixtures thereof.
When R units comprise backbone branching units, R4 is preferably hydrogen or -(CHz)u(Rz0)t-(CHz)"Y wherein the index t is greater than 0, preferably from 10 to 30; the index a is from 0 to 6; and Y is hydrogen, Cl-C4 linear allcyl, -N(Rl)z, an anionic unit, and mixtures thereof; preferably Y is hydrogen, or - N(Rl)2. A
preferred embodiment of backbone branching units comprises R4 equal to -(R20)tH. The indices x, y, and z are each independently from 0 to 6.
vii) The formulator may suitably combine any of the above described R units to make a zwitterionic polyamine having a greater or lesser degree of hydrophilic character.
Ri units are the units wluch are attached to the backbone nitrogens. R1 units are selected from the group consisting of:
i) hydrogen; which is the unit typically present prior to any backbone modification.
ii) Cl-C2~ alkyl, preferably Cl-C4 alkyl, more preferably methyl or ethyl, most preferably methyl. A preferred embodiment of the present invention in the instance wherein Rl units are attached to quaternary units (iv) or (v), R' is the same unit as quaternizing uiut Q. For example a J unit having the formula:
(CHs)aN

iii) C~-C22 arylallcyl, preferably benzyl.
iv) -[CHZCH(OR4)CH20]5(R20)tY; wherein R2 and R4 are the same as defined herein above, preferably when Rl units comprise Rz units, RZ is preferably ethylene.
The value of the index s is from 0 to 5. For the purposes of the present invention the index t is expressed as an average value, said average value from about 0.5 to about 100. The formulator may lightly alkyleneoxylate the backbone nitrogens in a manner wherein not every nitrogen atom comprises an Rl unit which is an alkyleneoxy unit thereby rendering the value of the index t less than 1.
v) Anionic units as described herein below.
vi) The formulator may suitably combine one or more of the above described Rl units when substituting the backbone of the zwitterionic polymers of the present invention.
Q is a quaternizing unit selected from the group consisting of Cl-C4 linear alkyl, benzyl, and mixtures thereof, preferably methyl. As described herein above, preferably Q is the same as Rl when Rl comprises an alkyl unit. For each backbone N+ unit (quaternary nitrogen) there will be an anion to provide charge neutrality. The anionic groups of the present invention include both units which are covalently attached to the polymer, as well as, external anions which are present to achieve charge neutrality. Non-limiting examples of anions suitable for use include halogen, inter' alia, chloride; methyl sulfate; hydrogen sulfate, and sulfate. The formulator will recognize by the herein described examples that the anion will typically be a unit which is part of the quaternizing reagent, inter alia, methyl chloride, dimethyl sulfate, benzyl bromide.
X is oxygen, -NR4-, and mixtures thereof, preferably oxygen.
Y is hydrogen, or an anionic unit. Anionic units are defined herein as "units or moieties which are capable of having a negative charge". For example, a carboxylic acid unit, -COZH, is neutral, however upon de-protonation the unit becomes an anionic unit, -COi , the unit is therefore, "capable of having a negative charge. Non-limiting examples of anionic Y units include -(CHa)tCOzM, -C(0)(CHZ)tCOaM, -(CHZ)fP03M, -(CHZ)fOP03M, -(CHZ)~S031VI, -(CHZ)tOS03M, _ CHZ(CHS03M)(CHZ)~S03M, -CHZ(CHS02M)(CHZ)~S03M, -CHZ(CHOS03M)(CHZ)fOS03M, -CH~(CHSOzM)(CH2)~S03M, -C(O)CHZCH(S03M)-COZM, -C(0)CHZCH(COZM)NHCH(COzM)CH2COZM, -C(0)CHZCH(COZM)NHCHZCOZM, -CHZCH(OZ)CH20(R10)tZ, -(CH2)fCH[0(R20)tZ]-CHtO(R20)tZ, and mixtures thereof, whereili Z
is hydrogen or an anionic unit non-limiting examples of which include -(CHZ)tC02M, -C(0)(CHz)~COzIVI, -(CHZ)fP03M, -(CHZ)fOP03M, -(CHZ)~S031VI, -CHZ(CHS03M)(CHZ)fS03M, _ CHZ(CHSOZM)(CHZ)~S03M, -C(0)CHZCH(S03M)COZM, -(CHZ)fOS03M, -CHz(CHOS03M)(CHZ)tOS03M, -CHZ(CHOSOzM)(CHZ)tOS03M, -C(O)CHZCH(COZM)NHCH(COZM)CHZCO~M, and mixtures thereof, M is a cation which provides charge neutrality.
Y units may also be oligomeric or polymeric, for example, the anionic Y unit having the formula:
OH S03Na -CH2CHCH20-CH2CHCHZS03Na may be oligomerized or polymerized to form units having the general formula:

S03Na CHZCHCHZO-CH2CHCH2S03Na n wherein the index n represents a number greater than 1.
Further non-limiting examples of Y units which can be suitably oligomerized or polymerized include:

OH SOZNa -CHZCHCH20-CH2CHCH2S03Na and OH
CHZCHCH20-CHZCH2CHZS03Na and OS03Na - CHzCHCH20- CHz,CHzCHzOS03Na As described herein above that a variety of factors, inter alia, the overall polymer structure, the nature of the formulation, the wash conditions, and the intended target cleaning benefit, all can influence the formulator's optimal values for Qr, tlQ, and Q(+). For liquid laundry detergent compositions preferably less than about 90%, more preferably less than 75%, yet more preferably less than 50%, most preferably less than 40% of said Y units comprise an anionic moiety, ihte~ alia, -S03M comprising units. The number of Y uiuts which comprise an anionic unit will vary from embodiment to embodiment. M is hydrogen, a water soluble cation, and mixtures thereof; the index f is from 0 to 6 The index n represents the number of backbone units wherein the number of amino units in the backbone is equal to n + 1. For the purposes of the present invention the index n is from 1 to about 99. Branching units B axe included in the total number of backbone units. For example, a backbone having the formula:
_NHz O
H N . N~O'~O~N ~z O H
has an index n equal to 4. The following is a non-limiting example of a polyamine backbone which is fully quaternized.
N(CH3)a O
(CH3~N +C ~ O~~ O~ N 3 N(CH3)s ~O CH3 The following is a non-limiting example of a zwitterionic polyarnine according to the preseat invention.
~I(~aa~hoho~
o~
+N~O O~N ~I(C~H20hos i ~ i CH3 I(Cho~~la O I(Mh Preferred zwitterionic polymers of the present invention have the formula:
Ri [Y(OR~ N-R N-R N-[(R~O~Yja Q Q Q
m wherein R~ are C~ alkylaie units, Rl ishyd~a~, Q, ~R~O~Y, o~'n~.ues thaeo~ R2 is ethylene, Y is selecbad from the gnup oaa>s~ting ofhy~g~, a~nic units selecbad frnmthe ~
of~c~'c~~~(oX~~-(-(-(s ~(CHSO,~(CEI2-CH~(CH~OzMxCHz~SO~IVl; ar~drrs ti~eo~ M is hydwg~, awa~ersohablec~ion, orm~G.uesiha~eo~ thei~fisf oanObo about 10;
Qisselecbadfrornthe g~vup coring of C, ~'ali~r alkyl, ba~zyl, arxlrrrahues thaeo~ the it~ex t is fin 15 to 25; the inrle~cmisfiio~nOb~20,p~efeablyfrnanObo l0,xrr.~eprefaablyfnxnObo4,yetmarep~ablyfiuan 0~ 3, rrnst~yfivmOb~ 2.
The present invention affords the formulator with the ability to optimize the zwitterionic polymer fnr a particular nse or embodimeatt. Not wishing to be limited by theorp, it is believed that the backbone quaternization (positive charge carriers) interact with the hydrophobic soils, Enter alia, clay, and the amomic capping units of the Rl nuns asncliarate the ability of surla~d molecules to interact, and therefore occupy, the cationic sites of the zwitterionic polymers. It is surprisingly found that the liquid laundry detergent compositions (ILL) which encompass the present invention are more effective in releasing hydrophilic soils when the backbones which comprise R units have a greater degree of alkylene unit character and which comprise an excess of backbone quaternary units with respell to the number of anioa~ic amts prese~xt.
The zwitterionic polymers of the present invention preferably comprise polyamine backbone which are derivatives of two types of backbone units:
normal oligomers which comprise R units of type (i), which are preferably polyamines having the fanmula:

H2N-(CH2~~n+1-~-(CH2)~iri ~-(CH2)~ri NH2 wherein B is a continuation of the polyamine chain by branching, n is preferably 0, m is from 0 to 3, x is 2 to 8, preferably from 3 to 6; and ii) hydrophilic oligomers which comprise R units of type (ii), which are preferably polyamines having the formula:
HaN-L(CH2)xO~Y(CH2)x~-lNH L(cHz)~ly(cH~J~lm NH2 wherein m is from 0 to 3; each x is independently from 2 to 8, preferably from 2 to 6; y is preferably from 1 to 8.
Preferred backbone units are the units from (i). Further preferred embodiments are polyamines which comprise units from (i) which are combined with R units of types (iii), (iv), and (v), an non-limiting example of which includes the epihalohydrin condensate having the formula:
H H OH H H
I I I I I
HEN-(CHZ)6-N--(CH~)6 N-CHZCHCHz N-(CHZ)6 N-(CH~6 NHZ.
As described herein before, the formulator may form zwitterionic polymers which have an excess of charge or an equivalent amount of charge type. An example of a preferred zwitterionic polyamine according to the present invention which has an excess of backbone quaten>ized units, has the formula:
(CHZCH20~oH ~CHzCH20)ZOH CH CH O off -~-N ~ 2 2 )2 H3C-N CH +N-CH3 (CHZCHZO)zoSOsM 3 (CHZCH2O)aoS03M
wherein R is a 1,5-hexamethylene, w is 2; R' is -(R20)tY, wherein Rz is ethylene, Y is hydrogen or -S03M, Q is methyl, m is 1, t is 20. For zwitterionic polyamines of the present invention, it will be recognized by the formulator that not every Rl unit will have a -S03 moiety capping said Rl unit.
For the above example, the final zwitterionic polyamine mixture comprises at least about 40% Y
units which are -S03 units.

Preparation of bis(hexamethylene)triamine, ethoxylated to average E20 per NH, quaternized to 90%, and sulfated to approximately 35% - 40%.
Ethoxylation of bis(hexamethyleneltriamine The ethoxylation is conducted in a 2 gallon stirred stainless steel autoclave equipped for temperature measurement and control, pressure measurement, vacuum and inert gas purging, sampling, and for introduction of ethylene oxide as a liquid. A ~20 1b. net cylinder of ethylene oxide is set up to deliver ethylene oxide as a liquid by a pump to the autoclave with the cylinder placed on a scale so that the weight change of the cylinder could be monitored.
A 200 g portion of bis(hexamethylene)triamine (BHMT) (M.W. 215.39, high purity 0.93 moles, 2.8 moles N, 4.65 moles ethoxylatable (N~1) sites) is added to the autoclave. The autoclave is then sealed and purged of air (by applying vacuum to minus 28" Hg followed by pressurization with nitrogen to 250 Asia, then venting to atmospheric pressure). The autoclave contents axe heated to 80 °C while applying vacuum. After about one hour, the autoclave is charged with nitrogen to about 250 psia while cooling the autoclave to about 105 °C. Ethylene oxide is then added to the autoclave incrementally over time while closely monitoring the autoclave pressure, temperature, and ethylene oxide flow rate. The ethylene oxide pump is turned on and off and cooling is applied to limit any temperature increase resulting from any reaction exotherm. The temperature is maintained between 100 and 110 °C while the total pressure is allowed to gradually increase during the course of the reaction. After a total of 205 grams of ethylene oxide (4.65 moles) has been charged to the autoclave, the temperature is increased to 110 °C and the autoclave is allowed to stir for an additional 2 hours. At this point, vacuum is applied to remove any residual unreacted ethylene oxide.
Vacuum is continuously applied while the autoclave is cooled to about 50 °C while introducing 60.5 g of a 25% sodium methoxide in methanol solution (0.28 moles, to achieve a 10%
catalyst loading based upon BHMT nitrogen functions). The methanol from the methoxide solution is removed from the autoclave under vacuum and then the autoclave temperature controller setpoint is increased to 100 °C. A device is used to monitor the power consumed by the agitator. The agitator power is monitored along with the temperature and pressure. Agitator power and temperature values gradually increase as methanol is removed from the autoclave and the viscosity of the mixture increases and stabilizes in about 1.5 hours indicating that most of the methanol has been removed. The mixture is fiuther heated and agitated under vacuum for an additional 30 minutes.
Vacuum is removed and the autoclave is cooled to 105 °C while it is being charged with nitrogen to 250 psia and then vented to ambient pressure. The autoclave is charged to 200 psia with nitrogen. Ethylene oxide is again added to the autoclave incrementally as before while closely monitoring the autoclave pressure, temperature, and ethylene oxide flow rate while maintaining the temperature between 100 and 110 °C and limiting any temperature increases due to reaction exotherm. After the addition of 3887 g of ethylene oxide (88.4mo1, resulting in a total of 20 moles of ethylene oxide per mol of ethoxylatable sites on BHMT), the temperature is increased to 110 °C
and the mixture stirred for an additional 2 hours.
The reaction mixture is then collected into a 22 L three neck round bottomed flask purged with nitrogen. The strong alkali catalyst is neutralized by slow addition of 27.2 g methanesulfonic acid (0.28 moles) with heating (100 °C) and mechanical stirring. The reaction mixture is then purged of residual ethylene oxide and deodorized by sparging an inert gas (argon or nitrogen) into the mixture through a gas dispersion frit while agitating and heating the mixture to 120 °C for 1 hour. The final reaction product is cooled slightly, and poured ilito a glass container purged with nitrogen for storage.
Quaternization of bis(hexamethylene)triamine which is ethoxylated to an average of 20 ethoxylations per backbone NH unit Into a weighed, SOOmI, 3 neck round bottom flask fitted with argon inlet, condenser, addition funnel, thermometer, mechanical stirring and argon outlet (connected to a bubbler) is added BHMT E020 (150g, 0.032mo1, 0.096mo1 N, 98%
active, m.w.-4615) and methylene chloride (300g) under argon. The mixture is stirred at room temperature until the polymer has dissolved. The mixture is then cooled to SoC using an ice bath. Dimethyl sulfate (12.8g, O.lmol, 99%, m.w.-126.13) is slowly added using an addition funnel over a period of 5 minutes. The ice bath is removed and the reaction is allowed to rise to room temperature. After 48 hrs. the reaction is complete.
Sulfation of bis(hexamethylene)triamine which is quaternized to about 90% of the backbone nitro~ens of the product admixture and which is ethoxylated to an average of 20 ethoxylations per backbone NH unit Under argon, the reaction mixture from the quaternization step is cooled to SoC using an ice bath (BHMT E020, 90+mol% quat, 0.16 mol OIL.
Chlorosulfonic acid (7.53g, 0.064 mol, 99%, mw-116.52) is slowly added using an addition funnel.
The temperature of the reaction mixture is not allowed to rise above lOoC. The ice bath is removed and the reaction is allowed to rise to room temperature. After 6 hrs. the reaction is complete. The reaction is again cooled to 5°C and sodium methoxide (28. 1g, 0.13 mol, Aldrich, 25% in methanol, m.w.-54.02) is slowly added to the rapidly stirred mixture. The temperature of the reaction mixture is not allowed to rise above lOoC. The reaction mixture is transferred to a single neck round bottom flask. Purified water (500m1) is added to the reaction mixture and the methylene chloride, methanol and some water is stripped off on a rotary evaporator at 50°C.
The clear, light yellow solution is transferred to a bottle for storage. The final product pH is checked and adjusted to ~9 using 1N NaOH or 1N HCl as needed. Final weight, 5308.
Ethoxvlated Polyalkvleneimine Dis~ersants The liquid laundry detergent compositions ofthe present invention comprise from about 0.1%, preferably from about 0.5%, more preferably from about 1% to about 7%, preferably to about 5%, more preferably to about 3% by weight, of a polyamine dispersant having a greater degree of average ethoxylation that typical hydrophobic dispersants, inter alia, the dispersants described in U.S. 5,565,145 Watson et al., issued October 15, 1996, however, having a larger molecular weight backbone that suitable cationic soil, clay, inter ulia, dispersauts which are suitably described in U.S. 4,597,898 Vander Meer, issued July 1, 1986 .
The ethoxylated polyalkyleneimines, which are preferably combined with one or more hydrophilic or hydrophobic dispersants as further described herein below, have the formula:
E B
I
~2N-R]w~'-R]x~N-R]yNE2 R is C2-C6 lineaa alkylene, C3-C6 branched alkylene, and mixtures thereof preferably R is ethylene, 1,3 propylene, and 1,6-hexylene, more preferred is ethylene. The indices w, ?t, and y are such that the molecular weight of said polyamines does not exceed about 2000 daltons, the backbone molecular weight is preferably about 600 daltoms.~ For example, for an entirely linear polyethyleneimine having a molecular weight of about 600 daltans, the index w =1, x =13, and y = 0. For an entirely branched polyethyleneimine having a molecular weight of approximately 600 dattons, w = 8, x = 0 and y =7. (This combination of indices results in a material having an average molecular weight of about 646 daltons, which, for the purposes ofthe present invention is a low molecular weight polyalkyleneimine.) The index w typically has the value of y + 1.
E is an ethyleneoxy unit having the formula:
-(CHZCHZO~H
wherein the index n is from about 12 to about 3 0, preferably the number of ethoxylations averages about 20 per backbone nitrogen hydrogen atom which is replaced. A preferred ethoxylated polyethyleneimine dispersant is PEI 600 B20.
SURFACTANT SYSTEM

The laundry detergent compositions of the present invention comprise a siufactant system.
The surfactant systems of the present invention may comprise any type of detersive surfactant, non-limiting examples of which include one or more mid-chain branched alkyl sulfate surfactants, one or more mid-chain branched alkyl allcoxy sulfate surfactants, ome ar more mid-chain branched aryl sulfonate surfactants, one or more non mid-chain branched sulphonates, sulphates, cationic surfactants, zwitterionic surfactants, ampholytic surfacta>rts, and mixtures thereof.
The total amount of surfactant present in the compositions of the present invention is from about 0.01 % by weight, preferably from about 0.1 % more preferably from about 1 % to about 60%, preferably to about 30% by weight, of said cazciposition.
Nonlimiting examples of surfactants useful herein include:
a) Cll-Cls alkyl benzene sulfonates (hAS);
b) C~-Cls mid-chain branched aryl sulfc~nates (BLAS);
c) Clo-Czo primary, a or au branched, and random alkyl sulfates (AS);
d) C14-C~ mid-chain branched alkyl sulfates (BAS);
e) Clo-Cps secondary (2,3) alkyl sulfates as descn'bed in U.S. 3,234,258 Morris, issued February 8, 1966; U.S. 5,075,041 Lutz, issued December 24, 1991; U.S.

5,349,101 Lutz et al., issued September 20, 1994; and U.S. 5,389,277 Prieto, issued February 14, 1995 .
Cio-Cis alkyl allcoxy sulfaxes (AExS) wherein Preferably x is from 1-7;
g) Ga-Czo ~d-chain branched alkyl alkoxy sulfates (BAExS);
h) Clo-C,s alkyl allcoxy carboxylates preferably comprising 1-5 ethoxy units;
i) C,z-Cis alkyl ethoxylates, C~-Clz alkyl phenol alkoxylates wherein the alkoxylate units are a mi~dure of ethyleneoxy and propyleneoxy units, Clz-Cps alcohol and C6-C~
alkyl phenol condensates with ethylene oxidelpropylene oxide block polymers inter alia Pluronic~ ex BASF which are disclosed in U.S. 3,929,678 Laughlin et al., issued December 30, 1975 .
j) C14-Czz mid-chain branched alkyl alkoxylates, BAEx;
k) Allcylpolysaccharides as disclosed in U.S. 4,565,647 Llenado, issued January 26, 1986 1) Polyhydroxy fatty acid amides having the fom~ula:

R~-C-N-Q
whereinR~ is CS-C31 allcyl; R8 is selected from the group consisting ofhydrogen, C1-C4 alkyl, C 1-C4 hydroxyalkyl, Q is a polyhydroxyalkyl moiety having a linear alkyl chain with at least 3 hydroxyls directly cc~mected to the chain, or an alkoxylated derivative thereof; preferred alkoxy is ethoxy or propoxy, and mixtures thereof; preferred Q is derived from a reducing sugar in a reductive amination reaction, more preferably Q is a glycityl moiety; Q is more preferably selected from the group consisting of -CH2(CHOH~CH20H, -CH(CH20H)(CHOH~_1CH20H, -CH2(CHOH)2-(CHOR')(CHOH)CH20H, and alkoxylaxed derivatives thereof, wherein n is an integer from 3 to 5, inclusive, and R' is hydrogen or a cyclic or aliphatic monosaccharide, which are described in U.S. 5,489,393 Connor et al., issued February 6, 1996; and U.S.
5,45,982 Munch et al., issued October 3, 1995 .
A non-limning example of a nonionic siufactant suitable for use in the present ikon has the formula:
O
R-C-N-[(Rl0~Rz0)yR~J~, ~~n wherein R is C~-C21 linear alkyl, C7-C21 branched alkyl, C~-C21 linear alkenyl, C~-C21 branched alkenyl, and mixtures thereof.
R1 is ethylene; R2 is C3-C4 linear alkyl, Cg-C4 branched alkyl, and mixtures thereof;
preferably R2 is 1,2 propylene. Nonionic suzfactants which comprise a mixture of Rl and R2 units preferably comprise from about 4 to about 12 ethylene units in combination with from about 1 to about 4 1,2-propylene units. The units may be aZtemating, or grouped together in any combination suitable to the formulator. Preferably the ratio of Rl units to R2 units is frarn about 4 1 to about 8 : 1. Preferably an R2 units (i.e. 1,2 propylene) is attached to the nitrogen atom followed by the balance of the chain comprising from 4 to 8 ethylene units.
R3 is hydrogen, Cl-C4 linear alkyl, Cg-C4 branched alkyl, and mixtures thereof;
preferably hydrogen or methyl, more preferably hydrogen.

R4 is hydrogen, C1-C4 linear alkyl, C3-C4 branched alkyl, and mixtures thereof;
preferably hydrogen. When the index m is equal to 2 the index n must be equal to 0 and the R4 unit is absent and is instead replaced by a -[(R10)x(R20)yR3] unit.
The index m is 1 or 2, the index n is 0 or l, provided that when m is equal to l, n is equal to 1; and when m is 2 n is 0; preferably m is equal to 1 and n is equal to one, resulting in one -[(R10)x(R20)yR3] unit and R4 being present on the nitrogen. The index x is from 0 to about 50, preferably from about 3 to about 25, more preferably from about 3 to about 10.
The index y is from 0 to about 10, preferably 0, however when the index y is not equal to 0, y is from 1 to about 4. Preferably all of the alkyleneoxy units are ethyleneoxy units. Those skilled in the art of ethoxylated polyoxyalkylene allcyl amide surface active agents will recognized that the values for the indices x and y are average values and the true values may range over several values depending upon the process used to alkoxylate the amides.
The mid-chain branched alkyl sulfate surfactants of the present invention have the formula:

CH3CH2(CH2)~,CH(CH2)~H(CHZ)yCH(CH2)ZOS03M
the alkyl alkoxy sulfates have the formula:

CH3CH2(CHZ)~,CH(CH2)XCH(CHZ)yCH(CHZ)~(OR3),nOS03M.
the alkyl alkoxylates have the formula:

CH3CH2(CH2)~,,,CH(CH~xCH(CH2)yCH(CH~Z(OR3),I,OH
wherein R, Rl, and RZ are each independently hydrogen, Cl-C3 alkyl, and mixtures thereof;
provided at least one of R, R', and RZ is not hydrogen; preferably R, Rl, and RZ are methyl;
preferably one of R, Rl, and RZ is methyl and the other units are hydrogen.
The total number of carbon atoms in the mid-chain branched allcyl sulfate and allcyl alkoxy sulfate surfactants is from 14 to 20; the index w is an integer from 0 to 13; x is an integer from 0 to 13; y is an integer from 0 to 13; z is an iliteger of at least l; provided w + x + y + z is from 8 to 14 and the total number of carbon atoms in a surfactant is from 14 to 20; R3 is Cl-C4 linear or branched alkylene, preferably e?hylene, 1,2 propylene, 1,3 propylene, 1,2 butyleue,1,4~rutylea~e, and mi~~res thereof. However, a preferred embodiment of the present invention comprises from 1 to 3 units wherein R3 is 1,2-Pmp3'1~, 1,3 propylene, or mixtures thereof followed by the balance of the R3 units connprising ethylene units. Another preferred embodime~ comprises R3 units which are randomly ethylene and 1,2 propylene units. The average value of the index m is at least about 0.01.
Whm the index m has low values, the surfactant system comprises mostly alkyl sulfates with a small amount of alkyl allcoxy sulfate surfactant. Some tertiary carbon atoms may be present in the alkyl chain, hovrever, this embodiment is not desired.
M denotes a ration, preferably hydrogen, a wainr soluble ration, and miartares thereof.
Non-limiting examples of water soluble rations include sodium, potassium, lithium, ammonium, alkyl ammonium, and mixtures thereof.
FORMInATIONS
As described herein above the compositiaais of the present invention may be in any liquid form inter aha pourable liquid, paste. Depending upon the specific form of the laundry coanposition, as well as, the eked use thereof the formulator may will use different zwittcrionic polyamine%thoxylated polyalkyleneimine combinations.
Preferably the Heavy Duty Liquid (ILL) compositions according to the present invention comprise:
a) from about 0.01%, preferably from about 0.05%, more preferably from 0.1% to about 20%, preferably to about 10%, more preferably to about 3% by weight, of a zwitterionic polyamine wherein said polyamine comprises more anionic substituents than the number of backbone quaternary nidrogen units; and b) franabout0.1%,fco~nabat0.5%,mo~epn~aablyf~enabout 1%mabout 7%,pn~abty~abouk5%,mocep~e~ablytoaba~3%byweig~,ofapoly~nr~ne c) fioarn about 0.01°/ by weight, preferably fiom about 0.1% more preferably fraan about 1 % to about 60%, prefeaably to abrnrt 30% by weight, of said conopositiam, of a surfactant systan, said ~ systean comprising:
r) from 0.01%, p~rably fiarn about 0.1% nuore preE~ably fiom. about 1%
to about 100%, preferably to about 80% by weight, prefarably to about 60%, most pre~ably to about 30% by weft, of a sarfadaat sdpcted fra~m the g~ consisting of mid-chain branched alkyl sulfate sums, mid-chain branched alkoxy sulfate surfactants, mid-chain branched aryl sulfonate surfactants, and mixtures thereof;
ii) optionally, but preferably, from 0.01 %, preferably from about 0.1 % more preferably from about 1% to about 100%, preferably to about 80% by weight, preferably to about 60%, most preferably to about 30% by weight, of one or more nonionic surfactants.
HDL laundry detergent compositions will typically comprise more of anionic detersive surfactants in addition to the preferred use of nonionic surfactants to augment the mid-chain branched surfactants. Therefore, the formulator will generally employ a zwitterionic polyamine having a greater number of cationic charged backbone quaternary units than the number of Rl unit anionic moieties. This net charge balance, taken together with the preferably greater degree of hydrophobicity of backbone R units, ihter alia, hexamethylene units, boosts the interaction of the surfactant molecules with the hydrophilic soil active zwitterionic polymers and thereby provides increased effectiveness. The lower net anionic charge of HDL's is surprisingly compatible with the relatively hydrophobic backbones of the more preferred zwitterionic polymers described herein.
However, depending upon the composition of the surfactant system, the formulator may desire to either boost or reduce the hydrophilic character of the R units by the use of, inter alia, allcyleneoxy units in combination with alkylene units.
Preferably the Heavy Duty Liquid (HDL) compositions according to the present invention comprise:
a) from about 0.01 %, preferably from about 0. OS %, more preferably from 0.1 % to about 20%, preferably to about 10%, more preferably to about 3% by weight, of a zwitterionic polyamine wherein said polyamine comprises less than or equal number of anionic substituents than the number of backbone quaternary nitrogen units;
b) from about 0.1%, preferably from about 0.5%, more preferably from about 1%
to about 7%, preferably to about 5%, more preferably to about 3% by weight, of a polyamine dispersant;
c) from about 0.01% by weight, preferably from about 0.1% more preferably from about 1% to about 60%, preferably to about 30% by weight, of said composition, of a surfactant system, said surfactant system comprising:

i) from 0.01 %, preferably from about 0.1 % more preferably from about 1 to about 100%, preferably to about 80% by weight, preferably to about 60%, most preferably to about 30% by weight, of a surfactant selected from the group consisting of mid-chain branched alkyl sulfate surfactants, mid-chain branched allcoxy sulfate surfactants, mid-chain branched aryl sulfonate surfactants, and mixtures thereof;
ii) from 0.01 %, preferably from about 0.1 % more preferably from about 1 to about 100%, preferably to about 80% by weight, preferably to about 60%, most preferably to about 30% by weight, of one or more nonionic surfactants, said nonionic surfactants selected form the group consisting of alcohols, alcohol ethoxylates, polyoxyalkylene alkylamides, and mixtures thereof;
iii) from 0.01 %, preferably from about 0.1 % more preferably from about 1 to about 100%, preferably to about 80% by weight, preferably to about 60%, most preferably to about 30% by weight, of one or more anionic surfactants.
d) the balance carriers and adjunct ingredients.
Another example of a preferred embodiment comprises:
a) from about 0.01%, preferably from about 0.05%, more preferably from 0.1% to about 20%, preferably to about 10%, more preferably to about 3% by weight, of a zwitterionic polyamine wherein said polyamine comprises less than or equal number of anionic substituents than the number of backbone quaternary nitrogen units;
b) from about 0.1%, preferably from about 0.5%, more preferably from about 1%
to about 7%, preferably to about 5%, more preferably to about 3 % by weight, of a polyamine dispersant;
c) from about 0.01 % by weight, preferably from about 0.1 % more preferably from about 1 % to about 60%, preferably to about 30% by weight, of said composition, of a surfactant system, said surfactant system comprising:
i) from 0.01 %, preferably from about 0.1 % more preferably from about 1 to about 100%, preferably to about 80% by weight, preferably to about 60%, most preferably to about 30% by weight, of one or more nonionic surfactants, said nonionic surfactants selected form the group consisting of alcohols, alcohol ethoxylates, polyoxyalkylene alkylamides, and mixtures thereof;
ii) optionally, from 0.01 %, preferably from about 0.1 % more preferably from about 1 % to about 100%, preferably to about 80% by weight, preferably to about 60%, most preferably to about 30% by weight, of one or more anionic surfactants; and d) from 0.001% (10 ppm) by weight, of an enzyme, preferably said enzyme is selected from the group consisting of proteases, cellulases, lipases, amylases, peroxidases, mannanases, xyloglucanases, and mixtures thereof.
ADJUNCT INGREDIENTS
The following are non-limiting examples of adjunct ingredients useful in the liquid laundry compositions of the present invention, said adjunct ingredients include enzymes, enzyme stabilizers, builders, optical brighteners, soil release polymers, dye transfer agents, dispersents, suds suppressers, dyes, perfumes, colorants, filler salts, hydrotropes, photoactivators, fluorescers, fabric conditioners, hydrolyzable surfactants, preservatives, anti-oxidants, chelants, stabilizers, anti-shrinkage agents, anti-wrinkle agents, germicides, fungicides, anti corrosion agents, and mixtures thereof.
Enzymes Enzymes are a preferred adjunct ingredient of the present invention. The selection of enzymes is left to the formulator, however, the examples herein below illustrate the use of enzymes in the liquid laundry detergents of the present invention.
"Detersive enzyme", as used herein, means any enzyme having a cleaning, stain removing or otherwise beneficial effect in a liquid laundry, hard surface cleaning or personal care detergent composition. Preferred detersive enzymes are hydrolases such as proteases, amylases and lipases.
Preferred enzymes for liquid laundry purposes include, but are not limited to, inter alia proteases, cellulases, lipases and peroxidases.
Protease Enzymes The preferred liquid laundry detergent compositions according to the present invention further comprise at least 0.001 % by weight, of a protease enzyme. However,.
an effective amount of protease enzyme is sufficient for use in the liquid laundry detergent compositions described herein. The term "an effective amount" refers to any amount capable of producing a cleaning, stain rarnoval, soil resnaval, whitening, deodorizing, or freshness improving cLfECt an substrates such as fabrics. In practical terms for current commercial preparations, typical amounts are up to about 5 mg by weight, more typically 0.01 mg to 3 mg, of active enzyme per gram of the detergent composition. Stated othezwise, the c~npositions herein will typically comprise fimn 0.001% to 5%, preferably 0.01°/rl% by weight of a commercial enzyme preparation.
The protease enzymes of the preseixk invention are usually present in sack commercial preparations at levels su~cient to provide from 0.005 to 0.1 Arson units (AU) of activity per gram of composition.
Preferred liquid laundry detergent compositions of the present invention comprise modified protease enzymes derioed from Bacillus a»ryloliquefaciens or Bacillus lentos.
For the purposes of the present invention, pzotease enzymes derived from B. amyloliquefaciens are fuzther referred to as "subtilisin BPN" also referred to as "Protease A" and protease enzymes derived froma B. Lentos are fiuther rel~red to as "subtilisin 309". For the purposes of the prese,~
inventiam, the numbering of Bacillus amyloliquefaciens subtilisin, as descn'bed in the patent of A
Baecds, et al, entitled "Protease-Cog Cleaning Compositions" having US Patent No. 5,679,630, serves as the amino acid sequence numbering system for both subtilisin BPN' and subtilisin 309.
Derivatives of Bacillus am Iy oliguefaciens subtilisin -BPN
A preferred protease ea~zyme for use in the present inve~iom is a variant of Protease A
(BPN~ which is a non-naturally occurring carbonyl hydrolase variant having a differart protcolytic activity, stability, substrate specificity, pH Profile andlor ~ characteristic as to the precursor carbonyl hydrolase frcan which the amino acid sequence of the variant is derived.
This variant of BPN is disclosed in EP 130,756 A, January 9, 1985.
Specifically Protease A-BSV
is BPN' wherein the Gly at positia~n 166 is replaced wig Asn, Sea, Lys, Arg, His, Gln, Ala, or C~u;
the Gly at position 169 is replaced with Ser; the Met at position 222 is replaced with Gln, Phe, Cys, His, Asn, Gh~, Ala or Thr; or altematwely the Gly at position 166 is replaced with Lys, and the Met at position 222 is replaced with Cys; or actively the Gly at position 169 is replaced with Ala, and the Met at position 222 is replaced with Ala.
A preferred protease enzyme far use in the present invention is Protease B.
Protease B is a non-natiually occun~g carbonyl hydrolase variant having a different proteolytic adiv~ty, stab~ity, substraxe specificity, pH profile and/or perFommance characteristic as caanpared to the precursoz carbonyl hydrolase from which the amino acid sequence of the variant is derived. Protease B is a variant of BPN' in which tyrosine is replaced with leucine at position +217 and as further disclosed in EP 303,761 A, April 28, 1987 and EP 130,756 A, January 9, 1985.
Bleach Stable Variants of Protease B (Protease B-BSV) A preferred protease enzyme for use in the present invention are bleach stable variants of Protease B. Specifically Protease B-BSV are variants wherein the Gly at position 166 is replaced with Asn, Ser, Lys, Arg, His, Gln, Ala, or Glu; the Gly at position 169 is replaced with Ser; the Met at position 222 is replaced with Gln, Phe, Cys, His, Asn, Glu, Ala or Thr;
or alternatively the Gly at position 166 is replaced with Lys, and the Met at position 222 is replaced with Cys; or alternatively the Gly at position 169 is replaced with Ala and the Met at position 222 is replaced with Ala.
Surface Active Variants of Protease B
Preferred Surface Active Variants of Protease B comprise BPN' wild-type amino acid sequence iii which tyrosine is replaced with leucine at position +217, wherein the wild-type amino acid sequence at one or more of positions 199, 200, 201, 202, 203, 204, 205, 206, 207, 208, 209, 210, 211, 212, 213, 214, 215, 216, 218, 219 or 220 is substituted; wherein the BPN' variant has decreased adsorption to, and increased hydrolysis of, an insoluble substrate as compared to the wild-type subtilisin BPN'. Preferably, the positions having a substituted amino acid are 199, 200, 201, 202, 205, 207, 208, 209, 210, 211, 212, or 215; more preferably, 200, 201, 202, 205 or 207.
Also preferred proteases derived from Bacillus amyloliquefaciehs subtilisin are subtilisin BPN' enzymes that have been modified by mutating the various nucleotide sequences that code for the enzyme, thereby modifying the amino acid sequence of the enzyme. These modified subtilisin enzymes have decreased adsorption to and increased hydrolysis of an insoluble substrate as compared to the wild type subtilisin. Also suitable are mutant genes encoding for such BPN' variants.
Derivatives of subtilisin 309 Further preferred protease enzymes for use according to the present invention also include the "subtilisin 309" variants. These protease enzymes include several classes of subtilisin 309 variants described herein below.
Protease C
A preferred protease enzyme for use in the compositions of the present invention Protease C. Protease C is a variant of an alkaline serine protease from Bacillus in which lysine replaced arginine at position 27, tyrosine replaced valine at position 104, serine replaced asparagine at position 123, and alanine replaced threonine at position 274. Protease C is described in WO 9I/06637, Published May 16, 1991. Genetically modified variants, particularly of Protease C, are also included .
Protease D
A preferred protease enzyme for use in the present invention is Protease D.
Protease D is a carbonyl hydrolase variant derived from Bacillus lentos subtilisin having an amino acid sequence not found in nature, which is derived from a precursor carbonyl hydrolase by substituting a different amino acid for a plurality of amino acid residues at a position in said carbanyl hydrolase equivalent to position +76, preferably also in cambinatian with one or more amino acid residue positions equivalent to those selected from the group consisting 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 Bacillus amyloliquefaciens subtilisin, as described in WO 95/10615 published April 20, 1995 by Geneucor International.
A. Loap Region 6 Substitution Variants - These subtilision 309-type variants have a modified amino acid sequence of subtilisin 309 wild-type amino acid sequence, wherein the modified amino acid sequence comprises a substitution at one or more of positions 193, 194, 195, 196, 197, 199, Z00, 201, 202, 203, 204, ZOS, 206, 207, 208, 209, 210, 211, 212, 213 or 214;
whereby the subtilisin 3 09 variant has decreased adsorption to, and increased hydrolysis of, an insoluble substrate as compared to the wild-type subtilisin 309. Preferably these proteases have amino acids substituted at 193, 194, 195, 196, 199, 201, 202, 203, 204, 205, 206 or 209; more preferably 194, 195, 196, 199 or 200.
B. Multi-Look Regions Substitution Variants - These subtilisin 309 variants may also be a modified amino acid sequence of subtilisin 309 wild-type amino acid sequence, wherein the modified amino acid sequence comprises a substitution at one or more positions in one ar more of the first, second, third, fourth, or fifth loop regions; whereby the subtilisin 309 variant has decreased adsorption to, and increased hydrolysis ~of; an insoluble substrate as compared to the wild-type subtilisin 309.
C. Substitutions at positions other than the loop re~,'o~ns - In addition, one or more substitution of wild-type subtilisin 309 may be made at positions other than positions in the loop regions, for example, at position 74. If the additional substitution to the subt~7isin 309 is mad at position 74 alone, the substitution is preferably with Asp, Asp, Glu, Gly, His, Lys, Phe or Pro, preferably His or Asp. However modifications can be made to one or more loop positions as well as position 74, for example residues 97, 99, 101, 102, 105 and 121.
Subtilisin BPN' variants and subtilisin 309 varianks are further descn'bed in WO 95/29979, WO 95/30010 and WO 95/30011, all of which were published November 9, 1995 .
A further preferred protease enzyme for use in combination with the modified polyamines of the preset invention is ALCALASE~ from Novo. Another suitable protease is obtained from a strain of Bacillus, having maa~imum activity throughout the pH range of 8-12, developed and sold as ESPERASE~ by Novo Industries A/S of Demnark, hereinafter "Novo". The preparation of this enzyme and analogous enzymes is described in GB 1,243,784 to Novo. Other suitable proteases include SAVINASE~ from Novo and MAXATASE~ from International Bio-Synthetics, Inc., The Netherlands. See also a high pH protease from Bacillus sp. NCI1VVIB 40338 described in WO
9318140 A to Novo. Enzymatic detergents comprising protease, one or more other enzymes, and a reversible protease inhibitor are described in WO 9203529 A to Novo. Other preferred proteases include those of WO 9510591 A to Procter & Gamble . When desired, a protease having decreased adsorption and increased hydrolysis is available as described in WO 9507791 to Procter &
Gamble. A recombinant trypsin-like protease for deterge~s suitable herein is described in WO
9425583 to Novo.
Other particularly useful proteases are multiply-substituted protease variants comprising a substitution of an annino acid residue with another naturally occurring amino acid residue at an amino acid residue position corresponding to position 103 of Bacillus amylolfquefacierls subtilisin in combination with a substitution of an amino acid residue with another naturally occurring amino acid residue at one or more amino acid residue positions corresponding to positions 1, 3, 4, 8, 9, 10, 12, 13, 16, 17, 18, 19, 20, 21, 22, 24, 27, 33, 37, 38, 42, 43, 48, 55, 57, 58, 61, 62, 68, 72, 75, 76, 77, 78, 79, 86, 87, 89, 97, 98, 99, 101, 102, 104, 106, 107, 109, 111, 114, 116, 117, I19, 121, 123, 126, 128, 130, 131, 133, 134, 137, 140, 141, 142, 146, 147, 158, 159, 160, 166, 167, 170, 173, 174, 177, 181, 182, 183, 184, 185, 188, 192, 194, 198, 203, 204, 205, 206, 209, 210, 211, 212, 213, 214, 215, 216, 217, 218, 222, 224, 227, 228, 230, 232, 236, 237, 238, 240, 242, 243, 244, 245, 246, 247, 248, 249, 251, 252, 253, 254, 255, 256, 257, 258, 259, 260, 261, 262, 263, 265, 268, 269, 270, 271, 272, 274 and 275 of Bacillus amyloliquefaciens subtilisin; wherein when said protease variant includes a substitution of amino acid residues at positions corresponding to positions 103 and ?6, there is also a substitution of an amino acid residue at one or more amino acid residue positions other than amino acid residue positions corresponding to positions 27, 99, 101, 104, 107, 109, 123, 128, 166, 204, 206, 210, 216, 217, 218, 222, 260, 265 or 274 of Bacillus amyloliquefaciens subtilisin and/or multiply substituted protease variants comprising a substitution of an amino acid residue with a~th~ naturally occurring amino acid residue at aa~e or more amino acid residue positions corresponding to positions 62, 212, 230, 232, 252 and 257 of Bacillus amyloliquefaclens subtilisin as descn'bed in CA 2,306,794; CA
2,306,894 and CA 2,308,206 from The Procter & Gamble Company.
Also suitable for the present invention are professes described in patea~t applicatzams EP
251446 sad WO 91/06637, protease BLAP~ descn'bed in W091/02792 and their varia~s described in WO 95/23221.
See also a high pH protease frarn Bacillus sp. NCI1VV1B 40338 described in W0 A to Novo. Enzymatic detergents comprising protease, one or more 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 deterge~s suitable herein is descn'bed in WO 94!25583 to Novo. Other suitable prateeses are described in BP 516 200 by Unilever.
Commercially available professes useful in the presartt ~ are lrnown as ESPERASE~, ALCALASE~, DU~F;AZYM~, SAVINASE~, EVERLASE~ and KANNASE~
all from Novo Nardisk A/S of Decmnark, and as MAXATASE~, MAXACAL~, PROPERASB~
and MAXAPEM~ all from Genencor hiternational (formerly Gist-Brocades of the Netherlands).
In addition to the above-descn"bed protease enzymes, other enzymes suitable for use in the liquid laundry detergent compositions of the present invention are further described herein below.
Other Euzr,~mes Enzymes in addition to the protease enzyme can be included in the present deDe~rg~t compositions for a variety of purposes, including removal of protein based, carbohydrate-based, or triglyceride-based slams from surfaces sash as textiles, for the prevention a~f refugx dye transfer, for example in laundering, and for fabric restoration. Suitable enzyrues include amylases, lipases, cellulases, peroxidases, and miJrtures thereof of any suitable origin, sack as vegetable, animal, bac6erial, fangs! and yeast origin. Preferred selections are influenced by factors such as pH
activity and/or stability optima, thermostability, and stability to active detergents, builders and the like. In this respect bacterial or fungal enzymes are preferred, such as bacterial amylases and proteases, and fungal cellulases.
Enzymes are normally incorporated into detergent or detergent additive compositions at levels sufficient to provide a "cleaning-effective amount". The term "cleaning effective amount"
refers to any amount capable of producing a cleaning, stain removal, soil removal, whitening, deodorizing, or freshness improving effect on substrates such as fabrics. In practical terms for current commercial preparations, typical amounts are up to about 5 mg by weight, more typically 0.01 mg to 3 mg, of active enzyme per grasp of the detergent composition.
Stated otherwise, the compositions herein will typically comprise from about 0.001%, preferably from about 0.01% to about 5%, preferably to about 1% by weight of a commercial enzyme preparation.
Protease enzymes are usually present in such commercial preparations at levels sufficient to provide from 0.005 to 0.1 Anson units (A~ of activity per gram of composition. For certain detergents, it may be desirable to increase the active enzyme content of the commercial preparation in order to minimize the total amount of non-catalytically active materials and thereby improve spotting/filming or other end-results. Higher active levels may also be desirable in highly concentrated detergent formulations.
Amylases suitable herein include, for example, a-amylases described in GB
1,296,839 to Novo; RAPIDASE~, International Bio-Synthetics, Inc. and TES~, Novo.
FLTNGAM~rL~ from Novo is especially useful. Engineering of enzymes for improved stability, e.g., oxidative stability, is known. See, for example J. Biological Chem., Vol. 260, No. 11, June 1985, pp 6518-6521. Certain preferred embodiments of the present compositions can make use of amylases having improved stability in detergents, especially improved oxidative stability as measured against a reference-point of TERMAMYLD in commercial use in 1993.
These preferred amylases herein share the characteristic of being "stability-enhanced"
amylases, characterized, at a minimum, by a measurable improvement in one or more of oxidative stability, e.g., to hydrogen peroxide / tetraacetylethylenediamine in buffered solution at pH 9-10; thermal stability, e.g.,. at common wash temperatures such as about 60°C; or alkaline stability, e.g., at a pH from about 8 to about 11, measured versus the above-identified reference-point amylase.
Stability can be measured using any of the art-disclosed technical tests. See, for example, references disclosed in WO
9402597. Stability-enhanced amylases can be obtained from Novo or from Genencor International.
One class of highly preferred amylases herein have the commonality of being derived using site-directed mutagenesis from one or more of the Baccillus amylases, especially the Bacillus oc-amylases, regardless of whether one, two or multiple amylase strains are the immediate precursors.
Oxidative stability-enhanced amylases vs. the above-identified reference amylase are preferred for use, especially in bleaching, more preferably oxygen bleaching, as distinct from chlorine bleaching, detergent compositions herein. Such preferred amylases include (a) an amylase according to the hereinbefore incorporated WO 9402597, Novo, Feb. 3, 1994, as further illustrated by a mutant in which substitution is made, using alanine or threonine, preferably threonine, of the methionine residue located in position 197 of the B. licheniformis alpha-amylase, known as TERMAMYL~, or the homologous position variation of a similar parent amylase, such as B.
amyloliquefaeiens, B.
subtilis, or B. stearothermophilus; (b) stability-enhanced amylases as described by Genencor International in a paper entitled "Oxidatively Resistant alpha-Amylases"
presented at the 207th American Chemical Society National Meeting, March 13-17 1994, by C.
Mitchinson. Thereili it was noted that bleaches in automatic dishwashing detergents inactivate alpha-amylases but that improved oxidative stability amylases have been made by Genencor from B.
lichenifo~mis NCIB8061. Methionine (Met) was identified as the most likely residue to be modified. Met was substituted, one at a time, in positions 8, 15, 197, 256, 304, 366 and 438 leading to specific mutants, particularly important being M197L and M197T with the M197T variant being the most stable expressed variant. Stability was measured in CASCADE~ and SUNLIGHT~;
(c) particularly preferred amylases herein include amylase variants having additional modification in the immediate parent as described in WO 9510603 A and are available from the assignee, Novo, as DURAMYL~. Other particularly preferred oxidative stability enhanced amylase include those described in WO 9418314 to Genencor International and WO 9402597 to Novo. Any other oxidative stability-enhanced amylase can be used, for example as derived by site-directed mutagenesis from known chimeric, hybrid or simple mutant parent forms of available amylases.
Other preferred enzyme modifications are accessible. See WO 9509909 A to Novo.
Cellulases usable herein include both bacterial and fungal types, preferably having a pH
optimum between 5 and 9.5. U.S. 4,435,307, Barbesgoard et al, March 6, 1984, discloses suitable fungal cellulases fromHunaicola insolens orHumicola strain DSM1800 or a cellulase 212-producing fungus belonging to the genus Aef~omonas, and cellulase extracted from the hepatopancreas of a marine mollusk, Dolabella Auricula Solandet~. Suitable cellulases are also disclosed in GB-A-2.075.028; GB-A-2.095.275 and DE-OS-2.247.832. CAREZYME~
(Novo) is especially useful. See also WO 9117243 to Novo.

Suitable lipase enzymes fair detergent usage include tbose produced by microoarga~ts of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in GB 1,372,034.
See also )ipases in Japanese Patent Applicatiart 53,20487, laid open Feb.
24,1978. This lipase is available from Amano Pharmaceutical Co. Ltd, Nagoya, Japan, under the trade mark Lipase P
"Amano," or °Amano-P." Other suitable carmnercial lipases include Amano-CES, Iipases ex Chromobacter viscosum, e.g. Chromobacter viscosum var. lipolyticum NRRLB 3673 from Toyo Jozo Co., Tagaxa, Japan; Chromobacter viscosum lipases fiom U.S. Biochemical Corp., U.S.A.
and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli.
LIPOLASE~ enzyme derived from Humicola lanuginosa and carnn~scially available fraan Novo, see also EP 341,947, is a preferred lipase for use herein. Lipase and amylase variants stabilized against peroxidase enzymes are desarbed in WO 9414951 A to Novo. See also WO 9205249 and ItD
94359044.
Cutinase enzymes suitable far use herein are described in WO 8809367 A to Genencor.
Peroxidase enzymes may be used in ca~tnbinatioa with oxygen sources, e.g., percarbomate, perborate, hydrogen peroxide, etc., for "solution bleaching" or prevention of transfer of dyes or pignnents removed frown substrates during the wash to other substrates present in the wash solution.
Known peroxidases includo horseradish peroxidase, ligninase, and haloperoxidases such as chloro-or bromo~eraxidase. Peroxidase-contanring detergent casnpositioa~s aze disclosed in WO
89099813 A, October 19, 1989 to Novo and WO 8909813 A to Novo.
A range of enzyme materials and means for their incorporation info synth~ic detecgeut compositions is also disclosed in WO 9307263 A and WO 9307260 A to Genencor Internatioa~al, WO 8908694 A to Novo, and U.S. 3,553,139 McCasty et al., issued January 5, 1971. Bnzymes are fiuther disclosed in U.S. 4,101,457 Place ct al, issued July 18, 1978, and U.S. 4,507,219 Hughes, issued March 26,1985. Fa~zyme materials useful for liquid detergent fotmailatio~s, and their incorporation info such formulations, are disclosed in U.S. 4,261,868 Hora et al., issued April 14, 1981. l3nzymes for rise in deterg~s can be stabilized by various tedmiques. Enzyme stabilization techniques are disclosed and exemplified in U.S. 3,600,319 Gedge et al., issued August I7, 1971; EP 199,405 and BP 200,586, October 29, 1986, Venegas. Enzyme stabili~icn systems are also described, for example, in U.S. 3,519,570. A useful Bacillus, sp. AC13 giving proteases, xylanases and cellulases, is described in WO 9401532 A to Novo.
A fuxther preferred enzyme according to the present inve~ion are mannanase enzymes.
When present maananase enzymes comprise frarn about 0.0001%, preferably from 0.0005%, more preferably from about 0.001 % to about 2%, preferably to about 0.1 % more preferably to about 0.02% by weight, of said composition.
Preferably, the following three mannans-degrading enzymes : EC 3.2.1.25 : (3-mannosidase, EC 3.2.1.78 : Endo-1,4-(3-mannosidase, referred therein after as "mannanase" and EC 3.2.1.100 : 1,4-(3-mannobiosidase (IUPAC Classification- Enzyme nomenclature, 1992 ISBN
0-12-227165-3 Academic Press) are useful in the compositions of the present invention.
More preferably, the detergent compositions of the present invention comprise a /3-1,4-Mannosidase (E.C. 3.2.1.78) referred to as Mannanase. The term "mannanase" or "galactomannanase" denotes a mannanase enzyme defined according to the art as officially being named mannan endo-1,4-beta-mannosidase and having the alternative names beta-mannanase and endo-1,4-mannanase and catalysing the reaction: random hydrolysis of 1,4-beta-D- mannosidic linkages in mannans, galactomannans, glucomannans, and galactoglucomannans.
In particular, Mannanases (EC 3.2.1.78) constitute a group of polysaccharases which degrade mannans and denote enzymes which are capable of cleaving polyose chains containing mannose units, i.e. are capable of cleaving glycosidic bonds in mannans, glucomannans, galactommnans and galactogluco-mannans. Mannans are polysaccharides having a backbone composed of (3-1,4- linked mannose; glucomannans are polysaccharides having a backbone or more or less regularly alternating (3-1,4 linked mannose and glucose;
galactomannans and galactoglucomannans are mannans and glucomannans with oc-1,6 linked galactose sidebranches.
These compounds may be acetylated.
The degradation of galactomannans and galactoglucomannans is facilitated by full or partial removal of the galactose sidebranches. Further the degradation of the acetylated mannans, glucomannans, galactomannans and galactogluco-mannans is facilitated by full or partial deacetylation. Acetyl groups can be removed by alkali or by mannan acetylesterases. The oligomers which are released from the mannanases or by a combination of mannanases and a-galactosidase andlor mannan acetyl esterases can be further degraded to release free maltose by ~i-maamosidase and/or ~3-glucosidase.
Mannanases have been identified in several Bacillus organisms. For example, Talbot et al., Appl. Ehviroh. Microbiol., Vo1.56, No. 11, pp. 3505-3510 (1990) describes a beta-mannanase derived from Bacillus steat~othermophilus in dimer form having molecular weight of 162 kDa and an optimum pH of 5.5-7.5. Mendoza et al., World J. Microbiol. Biotech., Vol.
10, No. 5, pp. 551-555 (1994) describes a beta-mannanase derived from Bacillus subtilis having a molecular weight of 38 kDa, an optimum activity at pH 5.0 and 55C and a pI of 4.8. JP-03047076 discloses a beta-mannaaase derived from Bacillus sp., having a molecular weight of 373 kDa measured by gel filtration, an optimum pH of 8-10 and a pI of 5.3-5.4. JP-63056289 describes the production of an alkaline, thermostable beta; mannanase which hydrolyses beta-1,4-D-manuopyranoside bonds of e.g. mannans and produces merino-oligosacchatides..JP-63036774 relates to the Bacillus microorganism FERM P-8856 which produces beta mannanase arLd beta-maanosidase at an alkaline pH. JP-08051975 discloses alkaline beta-mannanases from alkalophilic Bacillus sp. AM-001. A purified mannanase from Bacillus amyloliquefaciens useful in the bleaching of pulp and paper and a method of preparation thereof is disclosed in WO 97111164. WO
91/18974 descn'bes a hemicellulase such as a ghtcanase, xylanase or mannanase active at an extreme pH and temperature. WO 94/25576 discloses an enzyme fromAspergillus aculeatus, CBS
101.43, exhibiting mannanase activity which may be useful for degradation or modification of pleat or algae cell wall material. WO 93/24622 discloses a mannanase isolated frarn Trlchoderma reseei useful for bleaching lignocellulosic pulps. An hemicellulase capable of degrading merman containing hemicellulose is described m W091/18974 and a purified maananase finrn Bacillus amyloliquefaciens is described in W097/11164.
Preferably, the mannanase enzyme w;)1 be an alkaline mannanase as defined below, more preferably, a mannanase originating from a bacterial source. Especially, the laundry detergent composition of the pzesent invention will prise an alkaline matnuuiase selected frown ~e mannanase from the strain Bacillus agaradherens NICMB 40482; the maxmanase fra~n Bacillus strain 168, gene yght; the mannanase from Bacillus sp. I633 and/or the maananase framBacillus sp. AAI12. Most preferred mazmanase for the inclusion in the detergent compositions of the present invention is the mannanase enzyme oziginatmg from Bacillus sp. I633 as described in EP 1086211.
The terms "alkaline mannanase enzyme°' is meant to encoanpass as e'uzyme having as enzymatic activity of at least 10%, preferably at least 25%, more preferably at least 40% of its maximum activity at a given pH ranging froma 7 to 12, preferably 7.5 to 10.5.
The allcaline mannanase from Bacillus agaradherens NICMB 40482 is descn'bed in U.S. patent No. 6,566,114. More specifically, this mannanase is:
i) a polypeptide produced by Bacillus agaradherens, NCIN~ 40482; or ii) a polypeptide comprising an amino acid sequence as shown in positia~ns 32-343 of SEQ m N0:2 as shown in U.S, patent No. 6,566,114; or iii) an analogue ofthe polypeptide defined in l) or ii) which is at least 70%
homologous with said polypeptide, or is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polyclonal a~body raised against said polypeptide in purified foma.
Also encompassed is the corresponding isolated polypeptide having mannanase activity selected from the group consisting of a) polynucleotide molecules encoding a polypeptide having mannanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO: 1 from nucleotide 97 to nucleotide 1029 as shown in U.S. pateat No. 6,566,114;
b) species ho~nologs of (a);
c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 70% identical to the amino acid sequence of SEQ m NO: 2 from amino acid residue 32 to amino acid residue 343 as shown in U.S. patent No. 6,566,114;
d) molecules complementary to (a), (b) or (c); and e) degenerate nucleotide sequences of (a), (b), (c) or (d).
The plasmid pSJ1678 comprising the polynucleotide molecule (the DNA sequence) encoding said mannanase has been transformed into a strain of the Escherichia cola which was deposited by the inventors according to the Budapest Treaty on the W
temational Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mikzoorganismen and Zellkulturen GmbH, Mascheroder Weg lb, D-38124 Braunschweig, Federal Republic of Germany, on 18 May 1998 under the deposition number DSM 12180.
A second more preferred enzyme is the mannanase from the Bacillus subt~lis strain 168, which is described in U.S. patent No. 6,060,299. More specifically, this mannanase is:
l) is encoded by the coding part of the DNA sequence shown in SED m No. 5 shown in U.S. patent No. 6,060,299 or an analogue of said sequence; and/or ii) a polypeptide comprising an amino acid sequence as shown SEQ m N0:6 shown in U.S. patent No. 6,060,299; or iii) au analogue of the polypeptide defined in ii) which is at least 70%
homologous with said polypeptide, or is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polyclonal antibody raised against said polypeptide in purified form.
Also encompassed in the corresponding isolated polypeptide having mannanase activity selected from the group consisting op a) polynucleotide molecules encoding a polypeptide having mannanase activity and comprising a sequence of nucleotides as shown in SEQ 1D NO:S as shown in U.S. patent No. 6,060,299;
b) species honwlogs of (a);
c) polynucleotide molecules that encode a polypeptide having mamiauase activity that is at least 70% identical to the amino acid~sequence of SEQ ID N0: 6 as shown in U.S. patent No. 6,060,299;
d) molecules complementmy to (a), (b) or (c); and e) degenerate nucleotide sequences of (a), (b), (c) or (d).
A third more preferred mannanase is described in EP 1086211. Mae spa~lly, this mamarr~e is:
i) a polypeptide produced by Bacillus sp. I633;
ii) a polypeptide comprising an amino acid sequ~ce as shown in positions 33-340 of SEQ ID N0:2 as shown in EP 1086211; or iii) an analogue of the polypeptide defined in i) or ii) which is at least 65 homologous with said polypeptide, is derived frarn said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polycla~nal antibody raised against said polypeptide in purified form.
Also encompassed is the corresponding isolated polynucleotide molecule selected from the group cauosisting of a) polynucleatide molecules encoding a polypeptide having mannanase activity and comprising a sequence of nucleotides as shown in SEQ ID NO: 1 frarn nucleotide 317 to nucleotide 1243 in EP 108621 l;
b) species homologs of (a);

c) polynucleotide molecules that encode a polypeptide having mannanase activity that is at least 65% identical to the amino acid sequence of SBQ 1D N0: 2 from amino acid residue 33 to amino acid residue 340 in EP 1086211;
d) molecules complementary to (a), (b) or (c); and e) degenerate nucleotide sequences of (a), (b), (c) ar (d).
The plasmid pBXM3 comprising the polynucleotide molecule (the DNA sequence) encoding a mamianase of the present invention has been transformed into a strain of the Escherichia coli which was deposited by the inventors according to the Budapest Treaty on the International Recognition of the Deposit of Microorganisms for the Purposes of Patent Procediue at the Deutsche Sammlung von MilQOOrganismen and Zell>mhuren GinbH, Mascheroder Weg 1b, D-38124 Braunschweig, Federal Republic of Gezmany, on 29 May 1998 under the deposition cumber DSM 12197.
A fourth more preferred mannanase is described in EP 1086211.
More specifically, this mannanase is:
i) a polypeptide produced by Bacillus sp. AAI 12;
ii) a polypeptide comprising an amino acid sequence as shown in positions 25-362 of SEQ ID N0:2as shown in EP 1086211; or iii) an analogue of the polypeptide defined in i) or ii) which is at least 65%
homologous with said polypeptide, is derived from said polypeptide by substitution, deletion or addition of one or several amino acids, or is immunologically reactive with a polyclanal antibody raised against said polypeptide in purified form.
Also encompassed is the corresponding isolated polynucleotide molecule selected from the group consisting of a) ~ polynucleotide molecules encoding a polypeptide having mannanase activity and camprising a sequence of nucleotides as shown in SBQ 1D NO: 1 from nucleotide 225 to nucleotide 1236 as shown in EP 1086211;
b) species homologs of (a);
c) polynucleotide molecules that encode a polypeptide having mamianase activity that is at least 65% identical to the amino acid sequence of SEQ 1D N0: 2 from amino acid residue 25 to amino acid residue 362 as shown in EP 108621 l;
d) molecules comple~ary to (a), (b) or (c); and e) degenerate nucleotide sequences of (a), (b), (c) or (d).
The plasmid pBXMI comprising the polynucleotide molecule (the DNA sequence) encoding a mannanase of the present invention has been transformed into a strain of the Escherichia coli which was deposited by the inve~rs accardi~ to the Budapest Treaty an the I~rnafianal Recognition of the Deposit of Microorganisms for the Purposes of Patent Procedure at the Deutsche Sammlung von Mihoarganismen and Zellkulturen GmbH, Mascheroder Weg 1b, D-38124 Braunschweig, Federal Republic of y, on 7 October 1998 under the deposition member DSM 12433.
The compositions of the preseart invention may also comprise a xyloglucanase enzyme.
Suitable xyloglucanases for the purpose of the present ion are enzymes exhibiting endQglucanase activity specific for xyioglucan. The xyloglucanase is incorporated into the compositions of the inventia~n. preferably at a lcvel of firm 0.0001%, more preferably from 0.0005%, most preferably from 0.001% to 2%, preferably to 0.1%, more preferably to 0.02% by weight, of pure enzyme.
As used herein, the term "endoglucanase activity" means the capability of the enzyme to hydrolyze 1,4-(3 D-glycosidic linlpresent in any cellulosic meal, sacb. as ~ulosc, cellulose derivatives, lichenin, p D-glucan, or xyloglucan. The ardoglucanase activity may be determined in accordance with methods lmown in the art, examples of which are described in WO
94J14953 and hereinafter. One unit of endoglucanase activity (e.g. CMCU, AVIU, XGU or BGU) is defined as the production of 1 Enrol reducing sugarfmin freer a glucan substrate, the ghuan ~rM
substrate being, e.g., CMC (CMCU), acid swoll~ Avicell (AYItn, xyloghuan (XGU) or cereal ~-glucan (HGU). The reducing sugars are das described in WO 94/14953 and hereinafter.
The specific activity of an endoglucanase towards a substrate is defined as units/mg of protein.
More specifically, as used herein the team "specific far xyloghzcan" means that the ea~doglucanase enzyme extnbits its highest endoglucemase activity am a xyloglucan substrate, and preferably less than 75% a~,~tivity, more preferably less than 50% activity, most preferably less than about 25% activity, on other cellulose-coaitaining substrates such as carboxymethyl cellulose, cellulose, or other glucans.

Preferably, the specificity of an endoglucanase towards xyloglucan is further defined as a relative activity determined as the release of reducing sugars at optimal conditions obtained by incubation of the enzyme with xyloglucan and the other substrate to be tested, respectively. For instance, the specificity may be defined as the xyloglucan to (3-glucan activity (XGUBGU), xyloglucan to carboxy methyl cellulose activity (XGU/CMCU), or xyloglucan to acid swollen Avicell activity (XGU/AVIU), which is preferably greater than about 50, such as 75, 90 or 100.
The term "derived from" as used herein refers not only to an endoglucanase produced by strain CBS 101.43, but also an endoglucanase encoded by a DNA sequence isolated from strain CBS 101.43 and produced in a host organism transformed with said DNA sequence.
The term "homologue" as used herein indicates a polypeptide encoded by DNA which hybridizes to the same probe as the DNA coding for an endoglucanase enzyme specific for xyloglucan under certain specified conditions (such as presoaking in SxSSC and pre-hybridizing for 1 h at -40°C in a solution of SxSSC, SxDenhardt's solution, and 50 ~.g of denatured sonicated calf thymus DNA, followed by hybridization in the same solution supplemented with 50 ~.Ci 32-P-dCTP labeled probe for 18 h at -40°C and washing three times in 2xSSC, 0.2% SDS at 40°C for 30 minutes). More specifically, the term is intended to refer to a DNA sequence which is at least 70% homologous to any of the sequences shown above encoding an endoglucanase specific for xyloglucan, including at least 75%, at least 80%, at least 85%, at least 90% or even at least 95% with any ofthe sequences shown above. The term is intended to include modifications of any of the DNA
sequences shown above, such as nucleotide substitutions wluch do not give rise to another amino acid sequence ofthe polypeptide encoded by the sequence, but which correspond to the codon usage of the host organism into which a DNA construct comprising any of the DNA sequences is introduced or nucleotide substitutions which do give rise to a different amino acid sequence and therefore, possibly, a different amino acid sequence and therefore, possibly, a different protein structure which might give rise to an endoglucanase mutant with different properties than the native enzyme.
Other examples of possible modifications are insertion of one or more nucleotides into the sequence, addition of one or more nucleotides at either end of the sequence, or deletion of one or more nucleotides at either end or within the sequence.
Endoglucanase specific for xyloglucan useful in the present invention preferably is one which has a XGUBGU, XGU/CMU and/or XGU/AVIU ratio (as defined above) of more than 50, such as 75, 90 or I00.

Furthermore, the endoglucanase specific for xyloglucan is preferably substantially devoid of activity towaxds (3-glucan and/or exhibits at the most 25 % such as at the most 10% or about 5 %, activity towards carboxymethyl cellulose and/or Avicell when the activity towards xyloglucan is 100%. In addition, endoglucanase specific for xyloglucan of the invention is preferably substantially devoid of transferase activity, an activity which has been observed for most endoglucanases specific for xyloglucan of plant origin.
Endoglucanase specific for xyloglucan may be obtained from the fungal species A.
aeuleatus, as described in WO 94/14953. Microbial endoglucanases specific for xyloglucan has also been described in WO 94/14953. Endoglucanases specific for xyloglucan from plants have been described, but these enzymes have transferase activity and therefore must be considered inferior to microbial endoglucanases specific for xyloglucan whenever extensive degradation of xyloglucan is desirable. An additional advantage of a microbial enzyme is that it, in general, may be produced in higher amounts in a microbial host, than enzymes of other origins.
Enz~ne Stabilizing S, stem Enzyme-containing, including but not limited to, liquid compositions, herein may comprise from about 0.001%, preferably from about 0.005%, more preferably from about 0.01% to about 10%, preferably to about 8%, more preferably to about 6% by weight, of an enzyme stabilizing system. The enzyme stabilizing system can be any stabilizing system which is compatible with the detersive enzyme. Such a system may be inherently provided by other formulation actives, or be added separately, e.g., by the formulator or by a manufacturer of detergent-ready enzymes. Such stabilizing systems can, for example, comprise calcium ion, boric acid, propylene glycol, short chain carboxylic acids, boronic acids, and mixtures thereof, and are designed to address different stabilization problems depending on the type and physical form of the detergent composition.
One stabilizing approach is the use of water-soluble sources of calcium and/or magnesium ions in the fuushed compositions which provide such ions to the enzymes.
Calcium ions axe generally more effective than magnesium ions and are preferred herein if only one type of cation is being used. Typical detergent compositions, especially liquids, will comprise from about 1 to about 30, preferably from about 2 to about 20, more preferably from about 8 to about 12 millimoles of calcium ion per liter of finished detergent composition, though variation is possible depending on factors including the multiplicity, type and levels of enzymes incorporated.
Preferably water-soluble calcium or magnesium salts axe employed, including for example calcium chloride, calcium hydroxide, calcium formate, calcium malate, calcium maleate, calcium hydroxide and calcium acetate; more generally, calcium sulfate or magnesium salts corresponding to the exemplified calcium salts may be used. Further increased levels of Calcium and/or Magnesium may of course be useful, for example for promoting the grease-cutting action of certain types of surfactant.
Another stabilizing approach is by use of borate species disclosed in U.S.
4,537,706 Severson, issued August 27, 1985. Borate stabilizers, when used, may be at levels of up to 10%
or more of the composition though more typically, levels of up to about 3 % by weight of boric acid or other borate compounds such as borax or orthoborate are suitable for liquid detergent use.
Substituted boric acids such as phenylboronic acid, butaneboronic acid, p-bromophenylboronic acid or the like can be used in place of boric acid and reduced levels of total boron in detergent compositions may be possible though the use of such substituted boron derivatives.
Stabilizing systems of certain cleaning compositions may further comprise from 0, preferably from about 0.01 % to about 10%, preferably to about 6% by weight, of chlorine bleach scavengers, added to prevent chlorine bleach species present in many water supplies from attacking and inactivating the enzymes, especially under alkaline conditions. While chlorine levels in water may be small, typically in the range from about 0.5 ppm to about 1.75 ppm, the available chlorine in the total volume of water that comes in contact with the enzyme, for example during fabric-washing, can be relatively large; accordingly, enzyme stability to chlorine in-use is sometimes problematic. Since perborate or percarbonate, which have the ability to react with chlorine bleach,' may present in certain of the instant compositions in amounts accounted for separately from the stabilizing system, the use of additional stabilizers against chlorine, may, most generally, not be essential, though improved results may be obtainable from their use. Suitable chlorine scavenger anions are widely known and readily available, and, if used, can be salts contailiing ammonium cations with sulfite, bisulfite, thiosulfite, thiosulfate, iodide, etc.
Antioxidants such as carbamate, ascorbate, etc., organic amines such as ethylenediaminetetraacetic acid (EDTA) or alkali metal salt thereof, monoethanolamine (MEA), and mixtures thereof can likewise be used.
Likewise, special enzyme inhibition systems can be incorporated such that different enzymes have maximum compatibility. Other conventional scavengers such as bisulfate, nitrate, chloride, souxces of hydrogen peroxide such as sodium perborate tetrahydrate, sodium perborate monohydrate and sodium percarbonate, as well as phosphate, condensed phosphate, acetate, benzoate, citrate, formate, lactate, malate, tartrate, salicylate, etc., and mixtures thereof can be used if desired. In general, since the chlorine scavenger function can be performed by ingredients separately listed under better recognized functions, (e.g., hydrogen peroxide sources), there is no absolute requirement to add a separate chlorine scavenger unless a compound performing that function to the desired extent is absent from an enzyme-containing embodiment of the invention; even then, the scavenger is added only for optimum results. Moreover, the formulator will exercise a chemist's normal skill in avoiding the use of any enzyme scavenger or stabilizer which is majorly incompatible, as formulated, with other reactive ingredients, if used. In relation to the use of ammonium salts, such salts can be simply admixed with the detergent composition but are prone to adsorb water and/or liberate ammonia during storage. Accordingly, such materials, if present, are desirably protected in a particle such as that described in US 4,652,392 Baginski et al., issued March 24, 1987.
Builders The laundry detergent compositions of the present invention preferably comprise one or more detergent builders or builder systems. When present, the compositions will typically comprise from about 1% builder, preferably from about 5%, more preferably from about 10% to about 80%, preferably to about 50%, more preferably to about 30% by weight, of detergent builder.
The level of builder can vary widely depending upon the end use of the composition and its desired physical form, for example, preferred compositions will typically comprise from about 1 builder. Lower or higher levels of builder, however, are not meant to be excluded.
Inorganic or P-containing detergent builders include, but are not limited to, the alkali metal, ammonium and alkanolammonium salts of polyphosphates (exemplified by the tripolyphosphates, pyrophosphates, and glassy polymeric mete-phosphates), phosphonates, phytic acid, silicates, carbonates (including bicarbonates and sesquicarbonates), sulphates, and aluminosilicates. However, non-phosphate builders are required in some locales. Importantly, the compositions herein function surprisingly well even in the presence of the so-called "weak" builders (as compared with phosphates) such as citrate, or in the so-called "underbuilt" situation that may occur with zeolite or layered silicate builders.
Examples of silicate builders are the alkali metal silicates, particularly those having a Si02:Na20 ratio in the range 1.6:1 to 3.2: l and layered silicates, such as the layered sodium silicates described in U.S. 4,664,839 Rieck, issued May 12, 1987. NaSKS-6 is the trademark for a crystalline layered silicate marketed by Hoechst (commonly abbreviated herein as "SKS-6").
Unlike zeolite builders, the Na SKS-6 silicate builder does not contain aluminum. NaSKS-6 has the delta Na2SiOg morphology foam of layered silicate. It can be prepared by methods sack as those described in German DE-A-3,417,649 and DE-A-3,742,043. SKS-6 is a highly preferred layered silicate for use herein, but other such layered silica#es, such as those having the general.
formula NaMSix02x+1'YH20 wherein M is sodium or hydrogen, x is a number fraan 1.9 to 4, preferably 2, and y is a mrmber from 0 to 20, prefwably 0 can be used hezein.
Various other TM TM ?M
layered silicates from Hoechst include NaSKS-5, NaSKS-7 and NaSKS-11, as the alpha, beta and gamma fauns. As noted above, the delta Na2Si05 (NaSKS-6 foam) is most prefuned far use herein.
Bxa~les of carbonate builders are the alkaline earth and alkali metal carbonates as disclosed in. German Patent Applicatiaua No. 2,321,001 published oon Noveanber 15, 1973.
Organic de~terge~nt builders suitable for the purposes of the present invention include, but are not restricted to, a wide variety of polycarbaxylate compounds. As used herein, "poly carboxylate" refers to compounds having a plurality of carboxylate groups, preferably at least 3 caxboxylates. Polycarboxylate builder can generally be added to the composition in acid form, but can also be added in the form of a neutralized salt. When utilized in salt farm, alkali metals, such as sodium, potassium, and lithium or allcanolammonium salts are preferred.
Included among the polycarboxyiate builders are a variety of categories of useful mate-rials. One important category of polycarboxylate builders encompasses the ether polycarboxylates, including oxydisuccnnate, as disclosed in U.S. 3,128,287 Berg, issued Aprr'17, 1964, and U.S.
3,635,830 Lamberti et al., issued January 18, 1972. See also "TMS/TDS"
builders of U.S.
4,663,071 Bush et al., issued May 5, 1987. Suitable etl~r polycarboxylates also include cyclic carnpounds, particularly alicyclic compounds, such as those described in U.S.
3,923,679 Rapko, issued December 2, 1975; U.S. 4,158,635 Crutchfield et al., issued June 19, 1979; U.S. 4,120,874 Crutchfield et al., issued October 17, 1978; nail U.S. 4,102,903 Crutchfield et al., issued July 25, 1978.
Other useful detergency builders include the ether hydroxypolycarboxylatas, copolymers of malefic anhydride wish ethylene os vinyl methyl ether, 1, 3, 5 trihydrarry benzene-2, 4, 6-trisulphonic acid, and carboxymethyloxysuccinic acid, the various alkali metal, ammonium and substituted ammonium salts of polyacetic acids such as ethylenediamane tetcaacetic acid and nitrilotriacetic acid, as well as polycarboxylates such as mellitic acid, succinic acid, oxydisuccinic acid, polymaleic acid, ben~e 1,3,5 tricarboxylic acid, carboxymethyloxysuccinic acid, and soluble sans thereof.

Citrate builders, e.g., citric acid and soluble salts thereof (particularly sodium salt), ate polycarboxylate builders of particular importance for heavy duty liquid detergent fornuilaaons due to their availability firorn renewable resources and their biodegradability..
Also suitable in the detergent compositions of the present invention are the 3,3-dicarboxy_ 4-oxa-1,6 hexanedioates and the related compounds disclosed in U.S. 4,566,984, Bush, issued Jamuuy 28, 1986. Useful succinic acid builders include the C5-C20 al~Cyl and aikenyl succinic acids and salts thereof. A particularly preferred compound of this type is dodeceny)sacc~ic acid.
Specific examples of succinate builders include: lautylsuccinate, myastylsucci~e, pa.linitylsuccinate, 2-dodecenylsuccinate (preferred), 2 pentadecenylsuccinate, anti the like.
Laurylsuccinates are the preferred builders of this group, and are described in European Patent Application 0,200,263, published November 5, 1986.
Other suitable polycarboxylates are disclosed in U.S. 4,144,226, Crutchfield et al., issued March 13, 1979 and in U.S. 3,308,067, Diehl, issued Match 7, 1967. See also Diehl U.S. Patecrt 3,723,322.
Faity acids, e.g., C12-C18 ma~nocarboxylic acids, can also be incorporated into the compositions alone, or in cornbinatian with the aforesaid builders, especially citratie and/or the succinate builders, to provide additional builder activity. Such use of fatty a.ads will generally result in a diminution of sudsing, which should be taken into acco~m~t by the formulator.
Phosphonate builders such as ethanerl~ydmxy 1,1-diphosphoa~ate and other lmown phosphonates (see, for example, U.S. Patents 3,159,581; 3,213,030; 3,422,021;
3,400,148 and 3,422,137) can also be used.
Dispersants A description of other suitable polyallcyleneinnine dispersants which may be optimally combined with the bleach stable dispersants of the present inventim can be found in U.S.
4,597,898 Vander Meer, issued July 1, 1986; European Pates Application 111,965 Oh and Gosselnnlc, published June 27, 1984; European Patent Appficatia~n 111,984 Gosselink, published June 27, 1984; Buropean Patent Applicatim 112,592 C~se>mk, published July 4,1984; U.S.
4,548,744 Connor, issued October 22, 1985; and U.S. 5,565,145 Watson et al., issued October 15, 1996. However, any suitable clay/soil dispersant or anti-redeposition agent can be used in the laundry compositions of the present invention.
Acryli~leic-based copolymers may also be used as a preferred c~pa~ of the dispersing/anti-redeposition agent. Such materials include the water-soluble salts of copolymers of acrylic acid and malefic acid. The average molecular weight of such copolymers in the acid form preferably ranges from about 2,000, preferably from about 5,000, more preferably from about 7,000 to 100,000, more preferably to 75,000, most preferably to 65,000. The ratio of acrylate to maleate segments in such copolymers will generally rouge from about 30:1 to about 1:1, more preferably from about 10:1 to 2:1. Water-soluble salts of such acrylic acid/maleic acid copolymers can inchide, for example, the alkali metal, ammonium and substit~xted ammonium salts. Soluble acrylate/maleate copolymers of this type are known materials which are described in European Patent Application No. 66915, published December 15, 1982, as well as in EP
193,360, published September 3, 1986, which also describes such polymers comprising hydroxypropylacrylate. Still other useful dispersing agents include the maleic/acrylic/vinyl alcohol terpolymers. Such materials are also disclosed in EP 193,360, including, for example, the 45/45/10 terpolymer of acrylicJmaleic/vinyl alcohol.
Another polymeric material which can be included is polyethylene glycol (PEG}.
PEG can extu'bit dispersing agent performance as well as act as a clay soil removahantiredeposition agent.
Typical molecular weight ranges for these purposes range from about 500 to about 100,000, preferably from about 1,000 to about 50,000, more preferably fi~can about 1,500 to about 10,000.
Polyaspartate and polyglutamate dispersing agents may also be used, especially in conjunction with zeolite builders. Dispersing agents such as polyaspartate preferably have a molecular weight (avg.) of about 10,000.
Soil Release A
The compositions according to the present invention may optionally comprise one or more soil release agents. If utilized, soil release agents will generally comprise from about 0.01 %, preferably from about 0.1 %, more preferably from about 0.2% to about 10%, pre~exably to about %, more preferably to about 3% by weight, of the composition. Polymeric soil release agents are characterized by having both hydrophilic segments, to hydrophilize the surface of hydrophobic fibers, such as polyester and nylon, and hydrophobic segments, to deposit upon hydrophobic fibers and remain adhered thereto through completion of the laundry cycle and, thus, serve as as anchor for the hydrophilic segments. This can enable stains occuring subsequent to treatment with the soil release agent to be more easily cleaned in later washing procedures.
The following describe soil release polymers suitable for use in the presexrt invention. U.S. 5,728,671 Rohrbaugh et al., issued March 17, 1998; U.S.
5,691,298 Gosselink et al., issued November 25, 1997; U.S. 5,599,782 Pan et al., issued February 4, 1997; U.S. 5,415,807 Goaselink et al., issued May 16, 1995; U.S. 5,182,043 Morrall et al., issued January 26, 1993; U.S. 4,956,447 Gosselink et a~, issued September 11, 1990; U.S.
4,976,879 Maldonado et aL issued December 11, 1990; U.S. 4,968,451 Scheibel et al., issued November 6, 1990; U.S. 4,925,577 Borcher, Sr. et al,, issued May 15, 1990;
U.S. 4,861,512 Gosselink, issued August 29, 1989; U.S. 4,877,896 Maldonado et al., issued October 31, 1989;
U.S. 4,771,730 Gossevnk et al., issued October 27, 1987; U.S. 711,730 Gossclink et a~, issued December 8, 1987; U.S. 4,721,580 Gosselink issued January 26, 1988; U.S.
4,000,093 Nicol et al., issued December 28, 1976; U.S. 3,959,230 Hayes, issued May 25, 1976; U.S.
3,893,929 Basadur, issued July 8, 1975; and European Pa~emt Application 0 219 048, published April 22, 1987 by Kud et al.
Further suitable soil release agarts are died in U.S. 4,201,824 VoaUand et al.; U.S.
4,240,918 Lagasse et al.; U.S. 4,525,524 Tang et al.; U.S. 4,579,681 Ruppert et al.; U.S.
4,220,918; U.S. 4,787,989; EP 279,134 A, 1988 to Rhon~a-Poulenc Chemie; EP
457,205 Ato BASF (1991); and DE 2,335,044 to Unilever N.V., 1974 .
METHOD OF USE
The present invention fiuther relates to a method foe removing hydrophilic soils form fabric, preferably clothing, said method comprising the step of contacrmg fabric in need of cleaning with an aqueous solution of a laundry detergent composition comprising:
a) from about 0.01%, preferably from about 0.05%, more preferably from 0.1% to about 20%, preferably to about 10%, more preferably to about 3 % by weight, of a zwitterionic polyamine according to the present invention;
b) from about 0.1%, preferably finrn about 0.5%, more preferably from about 1%
to about 7%, preferably to about 5%, more preferably to about 3% by weight, of a P
c) from about 0.01 % by weight, preferably from about 0.1 % morn preferably from about 1 % to about 60%, preferably to about 30% by weigh, of said caanpositiaoi, of a surfactant system as descn'bed herein; and d) the balance carriers and other ingds.
Preferably the aqueous solution comprises at least about 0.01%, preferably at least about 1% by weigbd, of said laundry detergerrt composition.
The caanpositions of the present invention can be suitably prepared by any Process choscn by the formulator, non-limiting examples of which are descn'bed in U.S.
5,691,297 Nassano et al., issued November 11, 1997; U.S. 5,574,005 Welsh et al., issued November 12, 1996; U.S.
5,569,645 Dinniwell et al., issued October 29, 1996; U.S. 5,565,422 Del Gi7eco et al., issued October 15, 1996; U.S. 5,516,448 Capeci et al., issued May 14, 1996; U.S.
5,489,392 Capeci et al., issued February 6, 1996; U.S. 5,486,303 Capeci et al., issued January 23, 1996 .
The following describe heavy duty liquid detergent compositions according to the present invention:
TABLEI
weight Ingrediea~,c 2 3 4 Sodium Clz-Cis alcohol ethoxy (1.25) 18 18 18 salfate 1 Linear allcylbenzene sulphonate 5.8 5.8 5.8 Ce-C,o amide nonionic surfactant z 1.17 1.4 1.4 Clz-C14 alkyl ethoxy (7.0) alcohol 4.1 2.8 2.8 Builder 12.6 11 11 Pratease 4 0.74 0.74 0.74 Amylase 5 0.072 0.072 0.072 _ 0.144 - --~ylase' - 0.105 O.I05 Cellulase $ 0.028 0.028 0.028 Cellulase " 0.12 - -Lipolase '" 0.06 - -Mannanase 11 - - 0.28 0.28 Boric acid 1z 2 2 2 Ca formate/CaClz 0.02 0.02 0.02 ~p~~ i3 0.65 0.90 -~~~ i4 _ - 0.68 0.70 0.7 Soil Release Polymer's 0.147 - --Polyamine' 1.5 2.0 1.4 Chelant 1' 0.61 0.30 0.3 Chelant'$ 0.35 0.35 0.35 Optical brig 0.144 0.144 0.144 Minors '" balancebalancebalance 1. Can comprise either linear or mid-chain branched alkyl units 2. 3 N'-(C$-Clo branched allcanoyl)-N,N-dimethyl-1,3-diamrnopropane.
TM
3. NEODOL 24-7 ex Shell Oil Co.
4. Protease enzyme from Bacillus Amylolique, faciens as described in EP 0130 756 Bl published January 9,1985.
. Ternnamyl~ available ex Novo.

6. Duramyl~ available ex Novo.

7. Natalase~ ex Nov~o as described in WO 95!26397 and WO. 96/23873.

8. Carezymem available ex Novo.

9. Endo A~ available exNovo.

10. Lipolase Ultra available ex Novo.

11. Mannanase enzyme origina~ng fro~u Bacillus sp. I633 available ex Novo, 2.5% ale 12. As part of an enzyme stabilizing system.

13. PEI 189 E15-E18 a:ccozding to U.S. 4,59'7,898 Vande~r Meer, issaed July 1, 1986.

14. Ethoxylated Polyalkylene Dispersant: PEI 600 E20.

15. Dimethylterephtbalate, 1,2 propylene glycol, methyl capped PEG copolymer aa~g to U.S.
4,702,857 Gosselink, issued October 27, 1987.

16. Zwittexiamic polymer accasding to sample 1.

17. Diethylene triamine penta(methyl phosphoric) acid (DTPMP).

18. Hydroxyetbanedunethylenephosphanic acid 19. 1?WA-36.

20. Minors include, inter olio, ethanol, l,2propanediol, methyl ethyl amine, sodiimn hydroxide, suds suppressers, dyes, perfumes, pro-perfumes, and opa,cifiers.
TABLE II
Ingredients 5 6 7 Sodium C-Cu alcob~ol ethoxy (1.25) 18 18 18 sulfate 1 Linear alkylbenzene sulpha~nate 5.8 5.8 5.8 C8-Cl amide nononic surfactant 2 I.17 1.4 1.4 Cia-Cia alkyl ethoxy (7.0) alcohol 3 4.1 2.8 2.8 Builder 12.6 11 11 Protease 4 0.74 0.74 0.74 Amylase 5 0.072 0.072 0.072 Amylase 6 0.144 -- --Amylase' -- 0.105 0.105 Cellulase 8 0.028 0.028 0.028 Cellulase 9 0.12 -- --Lipolase 1 0.06 -- --Mannanase 11 -- 0.28 0.28 ~

Boric acid 12 2 2 2 Ca formate/CaCl2 0.02 0.02 0.02 Dispersant 13 0.65 0.90 --Dispersant 14 0.68 0.70 0.7 Soil Release Polymer 15 0.147 -- --Polyamine 16 1.5 2.0 1.4 Chelant 1' 0.61 0.3 0.3 Chelant 18 0.35 0.35 0.35 Optical brightener 19 0.144 0.144 0.144 Minors 2 balancebalancebalance 1. Can comprise either linear or mid-chain branched allcyl units 2. 3-N'-(C8-Cl° branched alkanoyl) N,N-dimethyl-1,3-diaminopropane.
3. NEODOL 24-7 ex Shell Oil Co.
4. Protease enzyme from Bacillus Amyloliquefaciens as described in EP 0 130 756 Bl published January 9, 1985.
. Termamyl~ available ex Novo.
6. Duramyl~ available ex Novo.
7. Natalase ex Novo as described in WO 95/26397 and W0. 96/23873.
8. Carezyme available ex Novo.
9. Endo A~ available ex Novo.

10. Lipolase Ultra available ex Novo.
11. Mannanase enzyme originating from Bacillus sp. I633 available ex Novo, 2.5% active 12. As part of an enzyme stabilizing system.
I3. PEI 189 E15-E18 according to U.S. 4,597,898 Vander Meer, issued July I, 1986.
14. Ethoxylated Polyalkylene Dispersant: PEI 600 E20.
15. Dimethylterephthalate, 1,2-propylene glycol, methyl capped PEG co-polymer according to U.S.
4,702,857 Gosselink, issued October 27, 1987.
16. Zwitterionic polymer according to Example 1.
17. Diethylene triamine penta(methyl phosphoric) acid (DTPMP).
18. Hydroxyethanedimethylenephosphonic acid 19. FWA-36.
20. Minors include, i~tef~ alia, ethanol, 1,2-propanediol, methyl ethyl amine, sodium hydroxide, suds suppressers, dyes, perfumes, pro-perfumes, and opacifiers.
TABLE III
weight Ingredients 8 9 10 Sodium Cl~-C15 alcohol ethoxy (1.25) 18 18 18 sulfate 1 Linear allcylbenzene sulphonate 5.8 5.8 5.8 C$-Cl amide noilionic surfactant 2 1.17 1.4 1.4 Cia-Cia alkyl ethoxy (7.0) alcohol 3 4.1 2.8 2.8 Builder 12.6 11 11 Protease 4 1.2 1.2 0.88 Amylase 5 0.072 0.072 0.072 Amylase 6 O.I44 -- --Amylase' -- 0.105 0.105 Cellulase $ 0.04 0.04 0.053 Cellulase 9 0.12 -- --Lipolase 1 0.06 -- --Mannanase 11 -- 0.18 0.176 Boric acid 12 2 2 2 Ca formate/CaCl2 0.02 0.1 0.05 Dispersant 13 0.65 0.90 --Dispersant 14 0.68 0.70 0.7 Soil Release Polymer 15 0.147 -- --Polyamine 16 1.5 2.0 1.4 Chelant 1' 0.61 0.30 0.3 Chelant 1$ 0.35 0.35 0.35 Optical brightener 19 0.144 0.144 0.144 Minors Z balancebalancebalance 1, Can comprise either linear or mid-chain branched alkyl units 2. 3-N'-(C8-Cl° branched allcanoyl)-N,N-dimethyl-1,3-diaminopropane.
3. NEODOL 24-7 ex Shell Oil Co.
4. Protease enzyme from Bacillus Amyloliquefaciehs as described in EP 0 130 756 B 1 published January 9, 1985.
5. Termamyl~ available ex Novo.
6. Duramyl~ available ex Novo.
7. Natalase ex Novo as described in WO 95/26397 and W0. 96/23873.
8. Carezyme available ex Novo.
9. Endo A~ available ex Novo.
10. Lipolase Ultra available ex Novo.
11. Mannanase enzyme originating from Bacillus sp. I633 available ex Novo, 2.5% active 12. As part of an enzyme stabilizing system.
13. PEI 189 E15-E18 according to U.S. 4,597,898 Vander Meer, issued July l, 1986.
14. Ethoxylated Polyalkylene Dispersant: PEI 600 E20.
15. Dimethylterephthalate, 1,2-propylene glycol, methyl capped PEG co-polymer according to U.S.
4,702,857 Gosselink, issued October 27, 1987.
16. Zwitterionic polymer according to Example 1.
17. Diethylene triamine penta(methyl phosphoric) acid (DTPMP).
18. Hydroxyethanedimethylenephosphonic acid 19. FWA-36.
20. Minors include, inter alia, ethanol, 1,2-propanediol, methyl ethyl amine, sodium hydroxide, suds suppressers, dyes, perfumes, pro perfumes, and opacifiers.

Claims (9)

1. A liquid laundry detergent composition comprising:
a) from about 0.01 to about 20% by weight, of a zwitterionic polymer having the formula:
wherein R units are C3-C6 alkylene units, R1 is hydrogen, Q, -(R2O)t Y, or mixtures thereof, R2 is ethylene, Y is selected from the group consisting of hydrogen, anionic units selected from the group consisting of -(CH2)f CO2M, -C(O)(CH2)f CO2M, -(CH2)f PO3M, -(CH2)f OPO3M, -(CH2)f SO3M, -CH2(CHSO3M)(CH2)f SO3M, -CH2(CHSO2M)(CH2)f SO3M, and mixtures thereof; M
is hydrogen, a water soluble cation, or mixtures thereof; the index f is from 0 to 10; Q is selected from the group consisting of C1-C4 linear alkyl, benzyl, and mixtures thereof; the index m is from 0 to 20; and the index t is from 15 to 25;
wherein at least one Y is an anionic unit;
b) from about 0.1% to about 7% by weight, of an ethoxylated polyalkyleneimine dispersant;
c) from about 0.01% to about 80% by weight, of a surfactant system comprising one or more surfactants selected from the group consisting of nonionic, anionic, cationic, zwitterionic, ampholytic surfactants, and mixtures thereof;
and d) the balance carriers and adjunct ingredients.

2. A composition according to Claim 1 wherein Y is hydrogen, -(CH2)f SO3M, and mixtures thereof.

3. A composition according to either Claim 2 or 3 wherein 40% of Y units are -(CH2)f SO3M units.

4. A composition according to any one of Claims 1 to 3 wherein R is hexamethylene.

5. A composition according to any one of Claims 1 to 4 wherein Q is methyl.

6. A composition according to any one of Claims 1 to 5 wherein m is 1.

7. A composition according to any one of Claims 1 to 6 wherein said zwitterionic polymer has the formula:
wherein M is a water soluble cation.

8. A liquid laundry detergent composition comprising:
a) from about 0.01 to about 20% by weight, of a zwitterionic polymer having the formula:
wherein R units are C3-C6 alkylene units, R1 is hydrogen, Q, -(R2O)t Y, or mixtures thereof, R2 is ethylene, Y is selected from the group consisting of hydrogen, anionic units selected from the group consisting of --(CH2)f CO2M, -C(O)(CH2)f CO2M, -(CH2)f PO3M, -(CH2)f OPO3M, -(CH2)f SO3M, -CH2(CHSO3M)(CH2)f SO3M, -CH2(CHSO2M)(CH2)f SO3M, and mixtures thereof; M is hydrogen, a water soluble cation, or mixtures thereof; the index f is from 0 to 10; Q is selected from the group consisting of C1-C4 linear alkyl, benzyl, and mixtures thereof;
the index m is from 0 to 20; the index t is from 15 to 25; wherein at least one Y
is an anionic unit;
b) from about 0.1% to about 7% by weight, of an ethoxylated polyalkyleneimine dispersant;

c) from about 0.01% to about 80% by weight, of a surfactant system comprising one or more surfactants selected from the group consisting of nonionic, anionic, cationic, zwitterionic, ampholytic surfactants, and mixtures thereof;
d) from about 0.001% to about 5% by weight, of a detersive enzyme, said enzyme selected from the group consisting of protease, amylases, lipases, cellulases, peroxidases, hydrolases, cutinases, mannanases, xyloglucanases, and mixtures thereof; and e) the balance carriers and adjunct ingredients.

9. A method for providing enhanced soil release cleaning of fabric, said method comprising the step of contacting fabric with a solution containing a liquid laundry detergent composition comprising:
a) from about 0.01 to about 20% by weight, of a zwitterionic polymer having the formula:
wherein R units are C3-C6 alkylene units, R1 is hydrogen, Q, -(R2O)t Y, or mixtures thereof, R2 is ethylene, Y is selected from the group consisting of hydrogen, anionic units selected from the group consisting of --(CH2)f CO2M, -C(O)(CH2)f CO2M, -(CH2)f PO3M, -(CH2)f OPO3M, -(CH2)f SO3M, -CH2(CHSO3M(CH2)f SO3M, -CH2(CHSO2M)(CH2)f SO3M, and mixtures thereof; M is hydrogen, a water soluble cation, or mixtures thereof; the index f is from 0 to 10; Q is selected from the group consisting of C1-C4 linear alkyl, benzyl, and mixtures thereof;
the index m is from 0 to 20; the index t is from 15 to 25; wherein at least one Y
is an anionic unit;
b) from about 0.1% to about 7% by weight, of an ethoxylated polyalkyleneimine dispersant;
c) from about 0.01% to about 80% by weight, of a surfactant system comprising one or more surfactants selected from the group consisting of nonionic, anionic, cationic, zwitterionic, ampholytic surfactants, and mixtures thereof;
and d) the balance carriers and adjunct ingredients.