EP1129164B1

EP1129164B1 - Bleach compositions

Info

Publication number: EP1129164B1
Application number: EP99957539A
Authority: EP
Inventors: Michael Eugene Burns; Andrew Russell Graydon; Regine Labeque; Christopher Mark Perkins; Eugene Steven Sadlowski; Barbara Kay Williams
Original assignee: Procter and Gamble Co
Current assignee: Procter and Gamble Co
Priority date: 1998-11-13
Filing date: 1999-11-09
Publication date: 2005-07-27
Anticipated expiration: 2019-11-09
Also published as: EP1129164A1; AR021250A1; JP2002530481A; AU1522300A; CN1333813A; BR9915319A; WO2000029537A1; ATE300601T1; DE69926390D1; CA2349011A1; TR200101330T2; DE69926390T2

Description

FIELD OF THE INVENTION

The present invention relates to bleaching and detergent compositions which comprise a catalytically effective amount of a transition-metal bleach catalyst which is a complex of a transition-metal and a cross-bridged macropolycyclic ligand. The present invention further relates to a method for bleaching/cleaning fabric with a catalytically effective amount of said transition-metal bleach catalyst wherein the method is performed substantially free of any organic or inorganic peroxygen compound or precursors to any organic or inorganic peroxygen compound.

BACKGROUND OF THE INVENTION

Bleaching of fabric is essentially exposing soiled or stained fabric to a chemical reaction the purpose of which is to eliminate the soil or stain. At one point i., time, bleaching involved exposure of fabric to a solution of hypochlorite. Therefore, fabric which was colored or dyed via sensitive pigments were excluded from treatment with bleach. To the benefit of the consumer, formulators developed various forms of bleach inter alia peroxygen bleaching systems which typically comprise a source of hydrogen peroxide and a bleach activator. This combination of source of hydrogen peroxide and activator plays a dominating role in effective, safe bleaching compositions. An effective example of this peroxygen bleaching system employs perborate (peroxygen source) and nonanoyloxybenzene sulfonate (activator).
In order to boost the performance of bleaching agents and to develop bleaching systems which are safe to any type of dyed or colored fabric inter alia silk, polyester blends, cotton, nylon, formulators have continued to develop peroxygen bleaching systems, as well as new methods of forming activated oxygen.
However, there still remains a need in the art for a bleaching system which will effectively bleach fabric without the need for reactive chemicals such as peroxides, sources of peroxide, and/or mixtures thereof.

SUMMARY OF THE INVENTION

The present invention meets the aforementioned needs in that it has been surprisingly discovered that bleaching of soils and stains can be accomplished in the absence of a source of hydrogen peroxide or other peroxygen bleaching agent. In other words, it has been surprisingly discovered that effective bleaching of soils and stains can be accomplished solely with a transition-metal bleach catalyst according to the present invention.
A first aspect of the present invention relates to bleaching compositions comprising:
A) at least 1 ppb of a transition-metal bleach catalyst which is a complex of a transition-metal and a cross-bridged macropolycyclic ligand: and
B) the balance carriers and other adjunct ingredients:
provided said composition is substantially free of any organic or inorganic peroxygen compounds, wherein the composition comprises at least 1 ppb of 5,12-diethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane manganese(II) chloride.
The present invention further relates to a method for cleaning and/or bleaching soils and stains on fabrics, said method comprising the step of contacting the fabric in need of cleaning and/or bleaching with an aqueous solution containing a composition which is substantially free of a peroxygen source and which comprises:
a) at least 1 ppb of a transition-metal bleach catalyst which is a complex of a transition-metal and a cross-bridged macropolycyclic ligand; and
b) the balance carriers, fillers, and other adjunct ingredients; provided the concentration of said transition metal bleach catalyst in the aqueous solution is at least 0.01 ppb and said composition is substantially free of any organic or inorganic peroxygen compounds, wherein the composition comprises at least 1 ppb of 5,12-diethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane manganese(II) chloride.
The compositions and methods of the present invention are suitable for cleaning/bleaching any surface in need of stain removal. For example, hard surface cleaners and automatic dishwashing compositions can employ the bleach catalysts of the present invention in applications which are substantially free of any organic or inorganic peroxygen compounds.
These and other objects, features, and-advantages will become apparent to those 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. All temperatures are in degrees Celsius (° C) unless otherwise specified. EP 549272 relates to bleach catalysts and EP 553607 relates to a dye transfer inhibiting composition comprising a metallo catalyst.

DETAILED DESCRIPTION OF THE INVENTION

The present invention relates to the surprising discovery that bleaching of soils and stains can be accomplished by a transition-metal catalyst in the absence an added peroxygen bleach. Sources of peroxygen bleaches include, but are not limited to, sources of hydrogen peroxide inter alia hydrogen peroxide, percarbonate, perborate. Alkali metal and alkaline earth metal percarbonate and perborate are typically found in laundry bleaching systems. These sources of hydrogen peroxide are typically formulated with one or more bleach activators inter alia nonanoyloxybenzenesulfonate (NOBS), tetraacetylethylenediamine (TAED). Bleach activators are typically viewed as precursors to the less stable but more reactive peroxyacid bleaching agents. Peroxyacids are formed in situ when the bleach activator (peroxyacid precursor) reacts with hydrogen peroxide or hydroperoxide anion via a perhydrolysis reaction.
In addition, peroxyacids can comprise a peroxygen bleaching system. Although these systems do not have the range of formulatability now enjoyed by systems such as NOBS/perborate, nevertheless, suitable methods for formulating peroxyacids inter alia the amido peroxyacid, NAPAA, as described in U.S. 5.536.435 Chapman et al., issued July 16. 1996.

Absence of Peroxygen Sources

The compositions of the present invention, as well as the methods for cleaning and/or bleaching of fabric which utilize the compositions of the present invention are substantially free of any peroxygen source such as hydrogen peroxide, peroxyacid etc. The compositions of the present invention need only have an effective amount of the herein below described catalyst present for effective bleaching. For the purposes of the present invention the term "substantially free" is defined as "the formulator does not include in the composition any peroxygen compound or source of peroxygen at a level required for either effective bleaching without a transition metal catalyst, or which would provide an increase in effectiveness of bleaching in the presence of a transition metal catalyst as defined herein." Therefore, as will be further described herein below, effective bleaching of stains can be accomplished by simply adding an aqueous or non-aqueous solution of a catalyst as described herein to fabric which is stained, preferably the fabric is in an aqueous solution when contacted with the catalyst. However, it is recognized that because of factors outside the control of the formulator inter alia source of product raw materials, unwanted decomposition of one or more ingredients, that a source of peroxygen may be introduced and/or formed unknowingly in the product. The compositions of the present invention do not require any peroxygen source, but the presence of any minor amounts will not effect the performance of the bleaching compositions described herein.
Formulators may typically include a small amount of a source of hydrogen peroxide into compositions for the purposes of stabilizing enzymes, for example, a minor amount of perborate may be added. However, this amount of perborate is typically so minor that it has no effect on the bleaching capacity of the compositions of the present invention. In cases where the formulator has added a minor amount of an oxidant, or other source of peroxide for the purposes of stabilizing an adjunct ingredient, for the purposes of the present invention, those compositions are still defined as "substantially free" of a source of peroxygen as defined herein above if they do not provide additional bleaching activity on stains under typical use conditions. For example, a "substantially free" composition can include an amount of peroxygen source provided the degree to which the catalyst is effective is substantially the same as if the source of peroxygen were absent. For the purposes of the present invention, any composition which comprises less than 0.1%, preferably less than 0.01% of a primary oxidant, such as a pre-formed peracid or a source of hydrogen peroxide is considered "substantially free" as further defined herein above, Additionally, any laundry liquor, laundry wash water, pre-soak bath, or other fabric or surface cleaning solution, wherein the present catalysts are used and which comprises less than 0.001% by weight of a source of peroxygen, pre-formed or otherwise formed in situ, is defined herein as "substantially free" as defined herein above. Stated otherwise, if the catalysts of the present invention are used to bleach stains on fabric, or otherwise clean/bleach a hard surface or dishware, and the solution containing the catalyst has a concentration of a source of peroxygen less than 0.001%, that solution is defined herein as "substantially free" of a source of peroxygen.

Bleach Catalyst

The compositions of the present invention comprise an effective amount of a bleach catalyst. The term "an effective amount" is defined as "an amount of the transition-metal bleach catalyst present in the present invention compositions, or during use according to the present invention methods, that is sufficient, under whatever comparative or use conditions are employed, to result in at least partial oxidation of the material sought to be oxidized by the composition or method." Typically the material to be oxidized is an unwanted substance inter alia food and beverage stains, greasy/oily stains, body soils on fabric, however, this is not the limitation to which the invention is applicable. Oxidation in the absence of a source of peroxygen has wide applicability and the present invention is not limited solely to bleaching and/or cleaning of fabric. For example, automatic dishwashing compositions are an embodiment of the present invention wherein bleaching of a stain with a composition and/or with a solution which is "substantially free" of a source of peroxygen is a part of the present invention. The same is equally true for hard surface cleaning compositions and solutions which comprise hard surface cleaning compositions which are "substantially free" of a source of peroxygen.
The compositions of the present invention comprise from 1 ppb (0.0000001%), more preferably from 100 ppb (0.00001%), yet more preferably from 500 ppb (0.00005%), still more preferably from 1 ppm (0.0001%) to 99.9%, more preferably to 50%, yet more preferably to 5%, still more preferably to 500 ppm (0.05%) by weight of the composition, of a transition-metal bleach catalyst that is 5,12-diethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane manganese (II) chloride.

METHOD OF USE

The present invention further relates to a method for using the catalysts of the present invention to bleach and/or clean fabric without the requirement of a peroxygen source of peroxygen.
The present invention, therefore, relates to a method for bleaching soils and stains on fabric in the absence of a bleaching agent, said method comprising the step of contacting fabric in need of cleaning with an aqueous or non-aqueous solution containing a composition which is substantially free of a peroxygen source, comprising:
a) at least 1 ppb of a transition-metal bleach catalyst which is a complex of a transition-metal and a cross-bridged macropolycyclic ligand: and
b) the balance carriers, fillers, and other adjunct ingredients; provided the concentration of said transition metal bleach catalyst in the solution is at least 0.01 ppb and said composition is substantially free of any organic or inorganic peroxygen compounds. wherein the composition comprises at least 1 ppb of 5,12-diethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane manganese(II) chloride.
Preferably the solution which comprises the transition-metal bleach catalyst has a solution concentration of catalyst of from 1 ppb, more preferably from 10 ppb, yet more preferably from 100 ppb. For example, 100 ppb (parts per billion) is a solution which comprises 0.00001% by weight, of a catalyst. As defined herein above, solutions which comprises less than 0.001% of a source of peroxygen are solutions which are "substantially free" of any organic or inorganic peroxygen compounds.
Methods directed entirely to large scale bleaching per se, for example, an industrial or manufacturing process, may utilized a higher concentration of catalyst, for example, 1 ppm or higher in order to reduce the contact time of the fabric with the catalyst containing solution.

ADJUNCT INGREDIENTS

The bleaching, pre-soak, pre-treatment, laundry or automatic diswashing, or hard surface cleaning compositions of the present invention, whether granular, solid (bar), gel, or liquid may further comprise one or more carriers and adjunct ingredients.
Compositions according to the present invention may comprise:
a) a catalytically effective amount of a transition-metal bleach catalyst which is a complex of a transition-metal and a cross-bridged macropolycyclic ligand; and
b) optionally from 0.001% to 90% by weight, of one or more dye fixing agents;
c) optionally from 0.01% to 50% by weight, of one or more cellulose reactive dye fixing agents;
d) optionally from 0.01% to 15% by weight, of a chlorine scavenger;
e) optionally 0.005% to 1% by weight, of one or more crystal growth inhibitors;
f) optionally from 0.01% to 20% by weight, of a fabric abrasion reducing polymer;
g) optionally from 1% to 12% by weight, of one or more liquid carriers;
h) optionally from 0.001% to 1% by weight, of an enzyme;
i) optionally from 0.01% to 8% by weight, of a polyolefin emulsion or suspension;
j) optionally from 0.01% to 0.2% by weight, of a stabilizer:
k) optionally from 1% to 80% by weight, of a fabric softening active;
l) optionally less than 15% by weight, of a principal solvent; and
m) from 0.01%, preferably from 0.1%, to 60%, preferably to 30% by weight, one or more surfactants, said surfactants selected from the group consisting of anionic, cationic, nonionic, ampholytic, zwitterionic surfactants, and mixtures thereof.

Surfactants

The bleaching, pre-soak, pre-treatment, and laundry detergent compositions of the present invention may comprise at least 0.01% by weight, preferably from 0.1% to 60%, preferably to 30% by weight, of a detersive surfactant system, said system is comprised of one or more category of surfactants depending upon the embodiment, said categories of surfactants are selected from the group consisting of anionic, cationic, nonionic, zwitterionic, ampholytic surfactants, and mixtures thereof. Within each category of surfactant, more than one type of surfactant of surfactant can be selected. For example, preferably the solid (i.e. granular) and viscous semi-solid (i.e. gelatinous, pastes, etc.) systems of the present invention, surfactant is preferably present to the extent of from 0.1% to 60 %, preferably to 30% by weight of the composition.
Nonlimiting examples of surfactants useful herein include:
a) C₁₁-C₁₈ alkyl benzene sulfonates (LAS);
b) C₁₀-C₂₀ primary, branched-chain and random alkyl sulfates (AS);
c) C₁₀-C₁₈ secondary (2,3) alkyl sulfates having the formula:
wherein x and (y + 1) are integers of at least about 7, preferably at least about 9; said surfactants disclosed 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;
d) C₁₀-C₁₈ alkyl alkoxy sulfates (AE_XS) wherein preferably x is from 1-7;
e) C₁₀-C₁₈ alkyl alkoxy carboxylates preferably comprising 1-5 ethoxy units;
f) C₁₂-C₁₈ alkyl ethoxylates, C₆-C₁₂ alkyl phenol alkoxylates wherein the alkoxylate units are a mixture of ethyleneoxy and propyleneoxy units, C₁₂-C₁₈ alcohol and C₆-C₁₂ alkyl phenol condensates with ethylene oxide/propylene oxide block polymers inter alia Pluronic® ex BASF which are disclosed in U.S. 3,929,678 Laughlin et al., issued December 30, 1975;
g) Alkylpolysaccharides as disclosed in U.S. 4,565,647 Llenado, issued January 26, 1986:
h) Polyhydroxy fatty acid amides having the formula:

⁷

₅

₃₁

⁸

₁

₄

₁

₄

₂

_n

₂

_n-1

₂

The bleaching, pre-soak pre-treatment, and laundry detergent compositions of the present invention can also comprise from 0.001% to 100% of one or more (preferably a mixture of two or more) mid-chain branched surfactants, preferably mid-chain branched alkyl alkoxy alcohols having the formula:
mid-chain branched alkyl sulfates having the formula:
and mid-chain branched alkyl alkoxy sulfates having the formula:
wherein the total number of carbon atoms in the branched primary alkyl moiety of these formulae (including the R, R¹, and R² branching, but not including the carbon atoms which comprise any EO/PO alkoxy moiety) is from 14 to 20, and wherein further for this surfactant mixture the average total number of carbon atoms in the branched primary alkyl moieties having the above formula is within the range of greater than 14.5 to 17.5 (preferably from 15 to 17); R. R¹, and R² are each independently selected from hydrogen, C₁-C₃ alkyl, and mixtures thereof, preferably methyl: provided R, R¹, and R² are not all hydrogen and, when z is 1, at least R or R¹ is not hydrogen. M is a water soluble cation and may comprises more than one type of cation, for example, a mixture of sodium and potassium. 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 integer of at least 1: provided w + x + y + z is from 8 to 14. EO and PO represent ethyleneoxy units and propyleneoxy units having the formula:
respectively, however, other alkoxy units inter alia 1,3-propyleneoxy, butoxy, and mixtures thereof are suitable as alkoxy units appended to the mid-chain branched alkyl moieties.
The mid-chain branched surfactants are preferably mixtures which comprise a surfactant system. Therefore, when the surfactant system comprises an alkoxylated surfactant, the index m indicates the average degree of alkoxylation within the mixture of surfactants. As such, the index m is at least 0.01, preferably within the range of from 0.1, more preferably from 0.5, most preferably from 1 to 30, preferably to 10, more preferably to 5. When considering a mid-chain branched surfactant system which comprises only alkoxylated surfactants, the value of the index m represents a distribution of the average degree of alkoxylation corresponding to m, or it may be a single specific chain with alkoxylation (e.g., ethoxylation and/or propoxylation) of exactly the number of units corresponding to m.
The preferred mid-chain branched surfactants of the present invention which are suitable for use in the surfactant systems of the present invention have the formula:
or the formula:
wherein a, b, d, and e are integers such that a + b is from 10 to 16 and d + e is from 8 to 14; M is selected from sodium, potassium, magnesium, ammonium and substituted ammonium, and mixtures thereof.
The surfactant systems of the present invention which comprise mid-chain branched surfactants are preferably formulated in two embodiments. A first preferred embodiment comprises mid-chain branched surfactants which are formed from a feedstock which comprises 25% or less of mid-chain branched alkyl units. Therefore, prior to admixture with any other conventional surfactants, the mid-chain branched surfactant component will comprise 25% or less of surfactant molecules which are non-linear surfactants.
A second preferred embodiment comprises mid-chain branched surfactants which are formed from a feedstock which compnses from 25% to 70% of mid-chain branched alkyl units. Therefore, prior to admixture with any other conventional surfactants, the mid-chain branched surfactant component will comprise from 25% to 70% surfactant molecules which are non-linear surfactants.
The surfactant systems of the laundry detergent compositions of the present invention can also comprise from 0.001%, preferably from 1%, more preferably from 5%, most preferably from 10% to 100%, preferably to 60%, more preferably to 30% by weight, of the surfactant system, of one or more (preferably a mixture of two or more) mid-chain branched alkyl arylsulfonate surfactants, preferably surfactants wherein the aryl unit is a benzene ring having the formula:
wherein L is an acyclic hydrocarbyl moiety comprising from 6 to 18 carbon atoms: R¹, R², and R³ are each independently hydrogen or C₁-C₃ alkyl, provided R¹ and R² are not attached at the terminus of the L unit; M is a water soluble cation having charge q wherein a and b are taken together to satisfy charge neutrality.

Builders

The compositions of the present invention, especially when comprising surfactants, preferably comprise one or more detergent builders or builder systems. When present, the compositions will typically comprise at least about 1% builder, preferably from about 5%, more preferably from 10% to 80%, preferably to 50%, more preferably to 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. When present, the compositions will typically comprise at least 1% builder. Formulations typically comprise from 5% to 50%, more typically 5% to 30%, by weight, of detergent builder. Granular formulations typically comprise from 10% to 80%, more typically from 15% to 50% by weight, of the detergent 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 meta-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 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").
Examples of carbonate builders are the alkaline earth and alkali metal carbonates as disclosed in German Patent Application No. 2,321,001 published on November 15, 1973.
Aluminosilicate builders are useful in the present invention. Examples of suitable aluminosilicate builders are described in U.S. 4,274,975 Corkhill et al. Aluminosilicate builders are of great importance in most currently marketed heavy duty granular detergent compositions, and can also be a significant builder ingredient in liquid detergent formulations. Aluminosilicate builders include those having the empirical formula: [M_z(zAlO₂)_y]·xH₂O wherein z and y are integers of at least 6. the molar ratio of z to y is in the range from 1.0 to 0.5, and x is an integer from 15 to 264. Preferred synthetic crystalline aluminosilicate ion exchange materials useful herein are available under the designations Zeolite A, Zeolite P (B), Zeolite MAP and Zeolite X.
Organic detergent builders suitable for the purposes of the present invention include, but are not restricted to, a wide variety of polycarboxylate compounds. As used herein, "polycarboxylate" refers to compounds having a plurality of carboxylate groups, preferably at least 3 carboxylates. 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 form, alkali metals, such as sodium, potassium, and lithium, or alkanolammonium salts are preferred.
Suitable are disclosed in U.S. 3,128,287 Berg, issued April 7, 1964, U.S. 3,635,830 Lamberti et al., issued January 18, 1972, U.S. 4,663,071 Bush et al., issued May 5, 1987, 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; U.S. 4,566,984, Bush, issued January 28, 1986, U.S. 4,144,226, Crutchfield et al., issued March 13, 1979 and in U.S. 3,308,067, Diehl, issued March 7. 1967. Diehl U.S. Patent 3,723,322, and U.S. 4,102,903 Crutchfield et al., issued July 25, 1978 and further U.S. Patents 3,159,581; 3,213,030; 3,422,021; 3,400,148 and 3.422,137.
Citrate builders. e.g., citric acid and soluble salts thereof (particularly sodium salt), are polycarboxylate builders of particular importance for heavy duty liquid detergent formulations due to their availability from renewable resources and their biodegradability. Citrates can also be used in granular compositions, especially in combination with zeolite and/or layered silicate builders. Oxydisuccinates are also especially useful in such compositions and combinations.

Dispersants

A description of other suitable polyalkyleneimine dispersants which may be optionally combined with the bleach stable dispersants of the present invention can be found in U.S. 4,597,898 Vander Meer, issued July 1, 1986: European Patent Application 111,965 Oh and Gosselink, published June 27, 1984: European Patent Application 111,984 Gosselink, published June 27, 1984; European Patent Application 112.592 Gosselink, 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-redepostion agent can be used in the laundry compositions of the present invention.
In addition, polymeric dispersing agents which include polymeric polycarboxylates and polyethylene glycols, are suitable for use in the present invention. Polymeric polycarboxylate materials can be prepared by polymerizing or copolymerizing suitable unsaturated monomers, preferably in their acid form. Unsaturated monomeric acids that can be polymerized to form suitable polymeric polycarboxylates include acrylic acid, maleic acid (or maleic anhydride), fumaric acid, itaconic acid, aconitic acid, mesaconic acid, citraconic acid and methylenemalonic acid. The presence in the polymeric polycarboxylates herein or monomeric segments, containing no carboxylate radicals such as vinylmethyl ether, styrene, ethylene, etc. is suitable provided that such segments do not constitute more than 40% by weight.
Particularly suitable polymeric polycarboxylates can be derived from acrylic acid. Such acrylic acid-based polymers which are useful herein are the water-soluble salts of polymerized acrylic acid. The average molecular weight of such polymers in the acid form preferably ranges from 2,000 to 10,000. more preferably from 4,000 to 7,000 and most preferably from 4,000 to 5,000. Water-soluble salts of such acrylic acid polymers can include, for example, the alkali metal, ammonium and substituted ammonium salts. Soluble polymers of this type are known materials. Use of polyacrylates of this type in detergent compositions has been disclosed, for example, in Diehl. U.S. Patent 3.308.067. issued march 7, 1967.
Acrylic/maleic-based copolymers may also be used as a preferred component of the dispersing/anti-redeposition agent. Such materials include the water-soluble salts of copolymers of acrylic acid and maleic acid. The average molecular weight of such copolymers in the acid form preferably ranges from 2,000, preferably from 5,000, more preferably from 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 range from 30:1 to 1:1, more preferably from 10:1 to 2:1. Water-soluble salts of such acrylic acid/maleic acid copolymers can include, for example, the alkali metal, ammonium and substituted 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 acrylic/maleic/vinyl alcohol.
Another polymeric material which can be included is polyethylene glycol (PEG). PEG can exhibit dispersing agent performance as well as act as a clay soil removal-antiredeposition agent. Typical molecular weight ranges for these purposes range from 500 to 100,000. preferably from 1.000 to 50,000, more preferably from 1,500 to 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 10,000.

Soil Release Agents

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 0.01%, preferably from 0.1%, more preferably from 0.2% to 10%, preferably to 5%, more preferably to 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 an 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 present 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 Gosselink 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 al., 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 Gosselink et al., issued October 27, 1987; U.S. 711,730 Gosselink et al., 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 Patent Application 0 219 048. published April 22, 1987 by Kud et al.
Further suitable soil release agents are described in U.S. 4,201.824 Voilland et al.; U.S. 4.240,918 Lagasse et al.; U.S. 4.525,524 Tung 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 Rhone-Poulenc Chemie; EP 457.205 A to BASF (1991): and DE 2,335,044 to Unilever N.V., 1974.

Enzymes

The detergent and cleaning compositions herein may also optionally contain one or more types of detergent enzymes. Such enzymes can include other proteases, amylases, cellulases and lipases. Such materials are known in the art and are commercially available under such trademarks as . They may be incorporated into the non-aqueous liquid detergent compositions herein in the form of suspensions, "marumes" or "prills". Another suitable type of enzyme comprises those in the form of slurries of enzymes in nonionic surfactants, e.g., the enzymes marketed by Novo Nordisk under the tradename "SL" or the microencapsulated enzymes marketed by Novo Nordisk under the tradename "LDP." Suitable enzymes and levels of use are described in U.S. Pat. No. 5,576,282, 5,705,464 and 5,710,115.
Enzymes added to the compositions herein in the form of conventional enzyme prills are especially preferred for use herein. Such prills will generally range in size from 100 to 1,000 microns, more preferably from 200 to 800 microns and will be suspended throughout the non-aqueous liquid phase of the composition. Prills in the compositions of the present invention have been found, in comparison with other enzyme forms, to exhibit especially desirable enzyme stability in terms of retention of enzymatic activity over time. Thus, compositions which utilize enzyme prills need not contain conventional enzyme stabilizing such as must frequently be used when enzymes are incorporated into aqueous liquid detergents.
However, enzymes added to the compositions herein may be in the form of granulates, preferably T-granulates.
"Detersive enzyme", as used herein, means any enzyme having a cleaning, stain removing or otherwise beneficial effect in a laundry, hard surface cleaning or personal care detergent composition. Preferred detersive enzymes are hydrolases such as proteases, amylases and lipases. Preferred enzymes for laundry purposes include, but are not limited to, proteases, cellulases, lipases and peroxidases. Highly preferred for automatic dishwashing are amylases and/or proteases, including both current commercially available types and improved types which, though more and more bleach compatible though successive improvements, have a remaining degree of bleach deactivation susceptibility.
Examples of suitable enzymes include, but are not limited to, hemicellulases, peroxidases, proteases, cellulases, xylanases, lipases, phospholipases, esterases, cutinases, pectinases, keratanases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, tannases, pentosanases, malanases, β-glucanases, arabinosidases, hyaluronidase, chondroitinase, laccase, and known amylases, or mixtures thereof.
Examples of such suitable enzymes are disclosed in U.S. Patent Nos. 5,705,464, 5,710,115, 5,576,282, 5,728,671 and 5,707,950
The cellulases useful in the present invention include both bacterial or fungal cellulases. Preferably, they will have a pH optimum of between 5 and 12 and a specific activity above 50 CEVU/mg (Cellulose Viscosity Unit). Suitable cellulases are disclosed in U.S. Patent 4,435,307, J61078384 and WO96/02653 which discloses fungal cellulase produced respectively from Humicola insolens, Trichoderma, Thielavia and Sporotrichum. EP 739 982 describes cellulases isolated from novel Bacillus species. Suitable cellulases are also disclosed in GB-A-2.075.028; GB-A-2.095.275; DE-OS-2.247.832 and WO95/26398.
Examples of such cellulases are cellulases produced by a strain of Humicola insolens (Humicola grisea var, thermoidea), particularly the Humicola strain DSM 1800. Other suitable cellulases are cellulases originated from Humicola insolens having a molecular weight of about 50KDa, an isoelectric point of 5.5 and containing 415 amino acids; and a ^~43kD endoglucanase derived from Humicola insolens, DSM 1800, exhibiting cellulase activity; a preferred endoglucanase component has the amino acid sequence disclosed in WO 91/17243. Also suitable cellulases are the EGIII cellulases from Trichoderma longibrachiatum described in WO94/21801 to Genencor. Especially suitable cellulases are the cellulases having color care benefits. Examples of such cellulases are cellulases described in European patent application No. 91202879.2, tiled November 6. 1991 (Novo). Carezyme and Celluzyme (Novo Nordisk A/S) are especially useful. See also WO91/17244 and WO91/21801. Other suitable cellulases for fabric care and/or cleaning properties are described in WO96/34092, WO96/17994 and WO95/24471.
Cellulases, when present, are normally incorporated in the cleaning composition at levels from 0.0001% to 2% of pure enzyme by weight of the cleaning composition.
Peroxidase enzymes are used in combination with oxygen sources, e.g. percarbonate, perborate, persulfate, hydrogen peroxide, etc and with a phenolic substrate as bleach enhancing molecule. They are used for "solution bleaching", i.e. to prevent transfer of dyes or pigments removed from substrates during wash operations to other substrates in the wash solution. Peroxidase enzymes are known in the art, and include, for example, horseradish peroxidase, ligninase and haloperoxidase such as chloro- and bromo-peroxidase. Suitable peroxidases and peroxidase-containing detergent compositions are disclosed, for example, in U.S. Patent Nos. 5,705,464, 5,710,115, 5,576,282, 5,728,671 and 5,707,950, PCT International Application WO 89/099813, WO89/09813 and in European Patent application EP No. 91202882.6, filed on November 6, 1991 and EP No. 96870013.8, filed February 20, 1996. Also suitable is the laccase enzyme.
Enhancers are generally comprised at a level of from 0.1% to 5% by weight of total composition. Preferred enhancers are substitued phenthiazine and phenoxasine 10-Phenothiazinepropionicacid (PPT), 10-ethylphenothiazine-4-carboxylic acid (EPC), 10-phenoxazinepropionic acid (POP) and 10-methylphenoxazine (described in WO 94/12621) and substitued syringates (C3-C5 substitued alkyl syringates) and phenols. Sodium percarbonate or perborate are preferred sources of hydrogen peroxide. Said peroxidases are normally incorporated in the cleaning composition at levels from 0.0001% to 2% of pure enzyme by weight of the cleaning composition.
Enzymatic systems may be used as bleaching agents. The hydrogen peroxide may also be present by adding an enzymatic system (i.e. an enzyme and a substrate therefore) which is capable of generating hydrogen peroxide at the beginning or during the washing and/or rinsing process. Such enzymatic systems are disclosed in EP Patent Application 91202655.6 filed October 9, 1991.
Other preferred enzymes that can be included in the cleaning compositions of the present invention include lipases. Suitable lipase enzymes for detergent usage include those produced by microorganisms of the Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, as disclosed in British Patent 1,372,034. Suitable lipases include those which show a positive immunological cross-reaction with the antibody of the lipase, produced by the microorganism Pseudomonas fluorescent IAM 1057. This lipase is available from Amano Pharmaceutical Co. Ltd., Nagoya, Japan, under the trade name Lipase P "Amano," hereinafter referred to as "Amano-P". Other suitable commercial lipases include Amano-CES, lipases ex Chromobacter viscosum, e.g. Chromobacter viscosum var, lipolyticum NRRLB 3673 from Toyo Jozo Co., Tagata, Japan; Chromobacter viscosum lipases from U.S. Biochemical Corp., U.S.A. and Disoynth Co., The Netherlands, and lipases ex Pseudomonas gladioli. Especially suitable lipases are lipases such as M1 Lipase^R and Lipomax^R (Gist-Brocades) and Lipolase^R and Lipolase Ultra^R(Novo) which have found to be very effective when used in combination with the compositions of the present invention. Also suitable are the lipolytic enzymes described in EP 258 068, WO 92/05249 and WO 95/22615 by Novo Nordisk and in WO 94/03578, WO 95/35381 and WO 96/00292 by Unilever.
Also suitable are cutinases [EC 3.1.1.50] which can be considered as a special kind of lipase, namely lipases which do not require interfacial activation. Addition of cutinases to cleaning compositions have been described in e.g. WO-A-88/09367 (Genencor); WO 90/09446 (Plant Genetic System) and WO 94/14963 and WO 94/14964 (Unilever).
Lipases and/or cutinases, when present, are normally incorporated in the cleaning composition at levels from 0.0001% to 2% of pure enzyme by weight of the cleaning composition.
In addition to the above referenced lipases, phospholipases may be incorporated into the cleaning compositions of the present invention. Nonlimiting examples of suitable phospholipases included: EC 3.1.1.32 Phospholipase A1; EC 3.1.1.4 Phospholipase A2; EC 3.1.1.5 Lysopholipase; EC 3.1.4.3 Phospholipase C; EC 3.1.4.4. Phospolipase D. Commercially available phospholipases include LECITASE® from Novo Nordisk A/S of Denmark and Phospholipase A2 from Sigma. When phospolipases are included in the compositions of the present invention, it is preferred that amylases are also included. Without desiring to be bound by theory, it is believed that the combined action of the phospholipase and amylase provide substantive stain removal, especially on greasy/oily, starchy and highly colored stains and soils. Preferably, the phospholipase and amylase, when present, are incorporated into the compositions of the present invention at a pure enzyme weight ratio between 4500:1 and 1:5, more preferably between 50:1 and 1:1.
Suitable proteases are the subtilisins which are obtained from particular strains of B. subtilis and B. licheniformis (subtilisin BPN and BPN'). One suitable protease is obtained from a strain of Bacillus, having maximum activity throughout the pH range of 8-12, developed and sold as ESPERASE® by Novo Industries A/S of Denmark, hereinafter "Novo". The preparation of this enzyme and analogous enzymes is described in GB 1,243,784 to Novo. Proteolytic enzymes also encompass modified bacterial serine proteases, such as those described in European Patent Application Serial Number 87 303761.8, filed April 28, 1987 (particularly pages 17, 24 and 98), and which is called herein "Protease B", and in European Patent Application 199,404, Venegas, published October 29, 1986, which refers to a modified bacterial serine protealytic enzyme which is called "Protease A" herein. Suitable is the protease called herein "Protease C". which is a variant of an alkaline serine protease from Bacillus in which 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 EP 90915958:4, corresponding to WO 91/06637, Published May 16, 1991. Genetically modified variants, particularly of Protease C, are also included herein.
A preferred protease referred to as "Protease D" is a carbonyl hydrolase as described in U.S. Patent No. 5,677,272, and WO95/10591. Also suitable is a carbonyl hydrolase variant of the protease described in WO95/10591, having an amino acid sequence derived by replacement of a plurality of amino acid residues replaced in the precursor enzyme corresponding to position +210 in combination with one or more of the following residues : +33, +62, +67, +76, +100, +101, +103, +104, +107, +128, +129, +130, +132, +135, +156, +158, +164, +166, +167, +170, +209, +215, +217, +218, and +222, where the numbered position corresponds to naturally-occurring subtilisin from Bacillus amyloliquefaciens or to equivalent amino acid residues in other carbonyl hydrolases or subtilisins, such as Bacillus lentus subtilisin (co-pending patent application US Serial No. 60/048,550, filed June 04, 1997 and PCT International Application Serial No. PCT/IB98/00853).
Also suitable for the present invention are proteases described in patent applications EP 251 446 and WO 91/06637, protease BLAP® described in WO91/02792 and their variants described in WO 95/23221.
See also a high pH protease from Bacillus sp. NCIMB 40338 described in WO 93/18140 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 detergents suitable herein is described in WO 94/25583 to Novo. Other suitable proteases are described in EP 516 200 by Unilever.
Particularly useful proteases are described in PCT publications: WO 95/30010; WO 95/30011: and WO 95/29979. Suitable proteases are commercially available as ESPERASE®, ALCALASE®, DURAZYM®, SAVINASE®, EVERLASE® and KANNASE® all from Novo Nordisk A/S of Denmark, and as MAXATASE®, MAXACAL®, PROPERASE® and MAXAPEM® all from Genencor International (formerly Gist-Brocades of The Netherlands).
Such proteolytic enzymes, when present, are incorporated in the cleaning compositions of the present invention a level of from 0.0001% to 2%, preferably from 0.001% to 0.2%, more preferably from 0.005% to 0.1% pure enzyme by weight of the composition.
Amylases (α and/or β) can be included for removal of carbohydrate-based stains. WO94/02597 describes cleaning compositions which incorporate mutant amylases. See also WO95/10603. Other amylases known for use in cleaning compositions include both α- and β-amylases. α-Amylases are known in the art and include those disclosed in US Pat. no. 5,003,257; EP 252,666; WO/91/00353; FR 2,676,456; EP 285,123; EP 525,610; EP 368,341; and British Patent specification no. 1,296,839 (Novo). Other suitable amylases are stability-enhanced amylases described in WO94/18314 and WO96/05295, Genencor, and amylase variants having additional modification in the immediate parent available from Novo Nordisk A/S, disclosed in WO 95/10603. Also suitable are amylases described in EP 277 216.
Examples of commercial α-amylases products are Purafect Ox Am® from Genencor and Termamyl®, Ban® ,Fungamyl® and Duramyl®, all available from Novo Nordisk A/S Denmark. WO95/26397 describes other suitable amylases : α-amylases characterised by having a specific activity at least 25% higher than the specific activity of Termamyl® at a temperature range of 25° C to 55°C and at a pH value in the range of 8 to 10, measured by the Phadebas® α-amylase activity assay. Suitable are variants of the above enzymes, described in WO96/23873 (Novo Nordisk). Other amylolytic enzymes with improved properties with respect to the activity level and the combination of thermostability and a higher activity level are described in WO95/35382.
Such amylolytic enzymes, when present, are incorporated in the cleaning compositions of the present invention a level of from 0.0001% to 2%, preferably from 0.00018% to 0,06%, more preferably from 0.00024% to 0.048% pure enzyme by weight of the composition.
The above-mentioned enzymes may be of any suitable origin, such as vegetable, animal, bacterial, fungal and yeast origin. Origin can further be mesophilic or extremophilic (psychrophilic, psychrotrophic, thermophilic, barophilic, alkalophilic, acidophilic, halophilic, etc.). Purified or non-purified forms of these enzymes may be used. Nowadays, it is common practice to modify wild-type enzymes via protein / genetic engineering techniques in order to optimize their performance efficiency in the laundry detergent and/or fabric care compositions of the invention. For example, the variants may be designed such that the compatibility of the enzyme to commonly encountered ingredients of such compositions is increased. Alternatively, the variant may be designed such that the optimal pH, bleach or chelant stability, catalytic activity and the like, of the enzyme variant is tailored to suit the particular cleaning application.
In particular, attention should be focused on amino acids sensitive to oxidation in the case of bleach stability and on surface charges for the surfactant compatibility. The isoelectric point of such enzymes may be modified by the substitution of some charged amino acids, e.g. an increase in isoelectric point may help to improve compatibility with anionic surfactants. The stability of the enzymes may be further enhanced by the creation of e.g. additional salt bridges and enforcing calcium binding sites to increase chelant stability.
These optional detersive enzymes, when present, are normally incorporated in the cleaning composition at levels from 0.0001% to 2% of pure enzyme by weight of the cleaning composition. The enzymes can be added as separate single ingredients (prills, granulates, stabilized liquids, etc... containing one enzyme) or as mixtures of two or more enzymes (e.g. cogranulates).
Other suitable detergent ingredients that can be added are enzyme oxidation scavengers. Examples of such enzyme oxidation scavengers are ethoxylated tetraethylene polyamines.
A range of enzyme materials and means for their incorporation into synthetic detergent compositions is also disclosed in WO 9307263 and WO 9307260 to Genencor International, WO 8908694. and U.S. 3,553,139, January 5, 1971 to McCarty et al. Enzymes are further disclosed in U.S. 4,101,457, and in U.S. 4,507,219. Enzyme materials useful for liquid detergent formulations, and their incorporation into such formulations, are disclosed in U.S. 4,261,868.
Amylase enzymes are suitable for use in the compositions of the present invention. Amylase enzymes and variants used in the present invention include, but are not limited to, the amylase enzymes described in WO 95/26397 and in WO 96/23873 (Novo). These enzymes are incorporated into cleaning compositions at a level of from about 0.0001%, preferably from 0.00018%, more preferably from 0.00024%, most preferably from 0.05% to 0.1%, preferably to 0.060%, more preferably to 0.048% by weight of the cleaning compositions of pure enzyme.
The amylase variants are preferably selected from the group consisting of α-amylase variants.
Suitable α-amylase variants for use in the present invention include, but are not limited to the following α-amylases:
(i) α-amylase characterized by having a specific activity at least 25% higher than the specific activity of Termamyl® at a temperature range of 25°C to 55°C and at a pH value in the range of 8 to 10, measured by Phadebas® α-amylase activity assay and/or;
(ii) α-amylase according to (i) comprising the amino acid sequence shown in SEQ ID No. 1 or an α-amylase being at least 80% homologous with the amino acid sequence shown in SEQ ID No. 1 and/or;
(iii) α-amylase according to (i) comprising the amino acid sequence shown in SEQ ID No. 2 or an α-amylase being at least 80% homologous with the amino acid sequence shown in SEQ ID No. 2 and/or;
(iv) α-amylase according to (i) comprising the following amino acid sequence N-terminal: His-His-Asn-Gly-Thr-Asn-Gly-Thr-Met-Met-Gln-Tyr-Phe-Glu-Trp-Tyr-Leu-Pro-Asn-Asp (SEQ ID No. 3) or an α-amylase being at least 80% homologous with the amino acid sequence shown (SEQ ID No. 3) in the N-terminal and/or;
(v) α-amylase according to (i-iv) wherein the α-amylase is obtainable from an alkalophilic Bacillus species and/or;
(vi) α-amylase according to (v) wherein the amylase is obtainable from any of the strains NCIB 12289, NCIB 12512, NCIB 12513 and DSM 935 and/or;
(vii) α-amylase showing positive immunological cross-reactivity with antibodies raised against an α-amylase having an amino acid sequence corresponding respectively to SEQ ID No. 1, ID No. 2, or ID No. 3 and/or;
(viii) variant of a parent α-amylase, wherein the parent α-amylase (1) has one of the amino acid sequences shown in SEQ ID No. 1, ID No. 2, or ID No. 4, respectively, or (2) displays at least 80% homology with one or more of said amino acid sequences, and/or displays immunological cross-reactivity with an antibody raised against an α-amylase having one of said amino acid sequences, and/or is encoded by a DNA sequence which hybridizes with the same probe as a DNA sequence encoding an α-amylase having one of said amino acid sequences, in which variants: (A) at least one amino acid residue of said parent α-amylase has been deleted; and/or (B) at least one amino acid residue of said parent α-amylase has been replaced by a different amino acid residue; and/or (C) at least one amino acid residue has been inserted relative to said parent α-amylase; said variant having an α-amylase activity and exhibiting at least one of the following properties relative to said parent α-amylase: increased thermostability; increased stability towards oxidation; reduced Ca ion dependency; increased stability and/or α-amylolytic activity at neutral to relatively high pH values; increased α-amylolytic activity at relatively high temperature; and increase or decrease of the isoelectric point (pI) so as to better match the pI value for α-amylase variant to the pH of the medium.
A polypeptide is considered to be X% homologous to the parent amylase if a comparison of the respective amino acid sequences, performed via algorithms, such as the one described by Lipman and Pearson in Science 227. 1985, p. 1435, reveals an identity of X%.
In the context of the present invention, the term "obtainable from" is intended not only to indicate an amylase produced by a Bacillus strain but also an amylase encoded by a DNA sequence isolated from such a Bacillus strain and produced in a host organism transformed with the DNA sequence.

Enzyme Stabilizers

Enzymes for use in detergents can be stabilized by various techniques. Enzyme stabilization techniques are disclosed and exemplified in U.S. 3.600,319, EP 199,405 and EP 200.586. Enzyme stabilization 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. The enzymes employed herein can be stabilized by the presence of water-soluble sources of calcium and/or magnesium ions in the finished compositions which provide such ions to the enzymes. Suitable enzyme stabilizers and levels of use are described in U.S. Pat. Nos. 5.705.464, 5,710,115 and 5,576,282.
The following is a non-limiting example of the preparation of a bleach catalyst which effectively bleaches stains in the absence of a source of peroxygen.

EXAMPLE 1

Synthesis of 5,12-dimethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane manganese (II) chloride, having the formula:

To a 250 mL, 3 necked round bottom flask, equipped with a thermometer, nitrogen inlet, and magnetic stirrer is added N,N'-bis(2-aminoethyl)-1,3-propanediamine (5.00g, 31.3 mmol) and absolute ethanol (100 mL). The solution is stirred under argon and cooled to 15°C using an ice bath. Aqueous glyoxal (4.78 g., 33 mmol, 40% in water) is added dropwise with stirring. Upon completion of the addition, the solution is concentrated under reduced pressure to yield a clear, colorless oil. The isolated oil has the formula 1:
and is obtained in 100% yield (6.0 g).
Cyclic amine 1 (6.0 g) is suspended in acetonitrile (100 mL). Potassium carbonate (25 g) and 1,3-propanediol ditosylate (12.61 g, 32.8 mmol) is added. The solution is stirred vigorously at RT overnight. The reaction is then warmed to 70°C and filtered hot with glass fiber filter paper and vacuum filtration. The resulting solid is washed with acetonitrile (100 mL). The acetonitrile filtrate is concentrated under reduced pressure to yield a light green oil having the formula 2:
and is obtained in 100% yield (7.0 g).
The tetraamine 2, (7.0 g) is dissolved in acetonitrile (150 mL). Methyl sulfate (2.5 equiv.) is added, the reaction warmed to 65°C and stirred for 9 days. The solvent is removed under reduced pressure to yield a brown oil having the formula 3:
and is obtained in approximately 85% yield.
Distilled water (25 mL) and potassium carbonate (13.8 g) are added to a 250 mL round bottomed flask. Absolute ethanol (75 mL) is added and the resulting biphasic solution is stirred and heated to 60°C with an oil bath. Sodium borohydride (1.60 g., 42.3 mmol) and 3 (10.0 g., 21.1 mmol) was added to the solution. The reaction is stirred at 60°C for 75 minutes. The reaction mixture is placed in a separatory funnel and the ethanol layer collected. The solvent is then removed under reduced pressure, the resulting tan solid/oil is dissolved in 5N KOH (5 mL) and extracted with toluene (2 x 50 mL). The toluene is removed under reduced pressure to yield 5,12-dimethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane having the formula:
as an oil, in 95% yield (5.2 g) after distillation.
To a flame dried 12 liter, 3 neck round bottom flask equipped with a heating mantle, stir bar, and oven dried condenser is added anhydrous acetonitrile (5 liters) and yield 5,12-dimethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane (484 gm., 1.9 moles). The milky white suspension is placed under a 10 mm vacuum until the suspension boiled and then the reaction vessel flushed with argon. This degassing is performed 7 times. After degassing is complete manganese (II) chloride (228 gm, 1.81 moles) is added. After refluxing for 4 hours with vigorous stirring, the suspension is immediately filtered through glass filter paper. The solvent is removed from the filtrate under reduced pressure at 45° C to yield a solid. The solid is then suspended in 500 ml. toluene, and the supernatant decanted off. This washing is repeated until the supernatant is free of color (typically 7 times with about 7X500 ml of toluene). The solid which remains I dried in vacuo to yield 575 g (84%) of 5,12-dimethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane magnanese (II) chloride. A second crop of product is obtained by further washing of the solid material and subsequent treatment of the resulting solid in a like manner. Total yield is 636 g (93%).

The following are non-limiting examples of Heavy Duty Granular (HDG) laundry detergent compositions according to the present invention.

(not in accordance with the present invention)
weight %
Ingredients	2	3	4	5	6
Anionic surfactant	22	22	18	18	20
Nonionic surfactant	1.5	1.5	0.5	0.5	1.1
Cationic surfactant	--	--	--	--	0.7
Zeolite	28	28	25	25	--
Phosphate	--	--	--	--	25
Sodium carbonate/bicarbonate	27	27	19	19	14
Sodium sulfate	5.4	5.4	11	11	15
Sodium silicate	0.6	0.6	1.1	1.1	10
Enzymes	0.4	0.4	0.4	0.4	1.6
Polymers	4.3	4.3	6.5	6.5	1.9
Chelants	--	--	0.5	0.5	--
Brighteners	0.2	0.2	0.3	0.3	0.2
Sodium perborate	--	1.0	--	--	--
Sodium percarbonate	--	--	--	0.4	--
Photobleach	--	--	--	--	0.005
Suds suppressors	0.2	0.2	6.4	6.4	--
Bleach catalyst	0.5	1.0	0.5	0.25	0.5
Water and minors	balance	balance	balance	balance	balance

(not in accordance with the present invention)
weight %
Ingredients	7	8	9	10
Anionic surfactant	20	10.6	10.6	28
Nonionic surfactant	1.1	9.4	9.4	3.3
Cationic surfactant	0.7	--	--	0.5
Zeolite	--	24	24	11
Phosphate	25	--	--	--
Silicate	--	8.5	8.5	7.5
Citric acid/citrate	-	7.3	7.3	7.0
Sodium carbonate/bicarbonate	14	8.9	8.9	15
Sodium sulfate	15	11	11	3.5
Sodium silicate	10	--	--	12
Enzymes	1.6	1.5	1.5	0.2
Polymers	1.9	5.0	5.0	0.7
Chelants	1.0	0.5	0.5	--
Brighteners	0.2	--	--	0.3
Photobleach	0.002	--	--	--
Suds suppressors	--	0.4	0.4	0.2
Bleach catalyst	0.5	0.1	0.75	2.0
Water and minors	balance	balance	balance	balance

The following are non-limiting examples of Heavy Duty Liquid (HDL) laundry detergent compositions according to the present invention.

(not in accordance with the present invention)
weight %
Ingredients	11	12	13	14
Anionic surfactant	20	20	27	27
Nonionic surfactant	3.0	3.0	3.0	3.0
Cationic surfactant	--	--	1.0	1.0
Fatty acid	2.0	2.0	8.5	8.5
Citric acid/citrate	3.0	3.0	2.5	2.5
Enzymes	1.1	1.1	1.4	1.4
Polymers	1.9	1.9	2.3	2.3
Chelants	--	--	0.5	0.5
Brighteners	0.1	0.1	0.1	0.1
Photobleach	--	--	--	0.003
Stablizers	19	19	18	18
Suds suppressors	0.1	0.1	0.2	0.2
Bleach catalyst	0.1	1.0	0.25	0.5
Water and minors	balance	balance	balance	balance

(not in accordance with the present invention)
weight %
Ingredients	15	16	17	18
Anionic surfactant	41	41	27	27
Nonionic surfactant	3.0	3.0	3.0	3.0
Cationic surfactant	--	--	1.0	1.0
Fatty acid	3.4	3.4	8.5	8.5
Citric acid/citrate	5.4	5.4	2.5	2.5
Enzymes	1.5	1.5	1.4	1.4
Polymers	1.0	1.0	2.3	2.3
Chelants	--	--	0.5	0.5
Brighteners	0.4	0.4	0.1	0.1
Stablizers	31	31	18	18
Suds suppressors	0.1	0.1	0.2	0.2
Bleach catalyst	0.01	15	5.0	2.5
Water and minors	balance	balance	balance	balance

Claims

A bleaching composition comprising:

A) at least 1 part per billion of a transition-metal bleach catalyst which is a complex of a transition-metal and a cross-bridged macropolycyclic ligand: and

B) the balance carriers and other adjunct ingredients:
provided said composition is substantially free of any organic or inorganic peroxygen compounds, wherein the composition comprises at least 1 ppb of 5,12-diethyl-1,5,8,12-tetraaza-bicyclo[6.6.2]hexadecane manganese(II) chloride.
A composition according to claim 1, wherein the composition is a liquid laundry, laundry pre-soak, or pre-treatment composition.
A method for bleaching soils and stains on fabrics, said method comprising the step of contacting fabric in need of cleaning with an aqueous or non-aqueous solution containing a composition according to claim 1 or 2, provided the concentration of said transition metal bleach catalyst in the solution is at least 0.01 ppb.