[0001] The present invention concerns the sequential delivery of enzymes in a washing process.
[0003] US 5733763 discloses an enzyme granulate comprising a first enzyme in the core and a second
enzyme in a shell surrounding said core.
US 20050245418 relates to a detergent composition comprising an enzyme partially disposed within
particles in a gel.
[0004] An objective is to provide an improved washing/stain removal process involving enzymes.
It is also very difficult to provide a blend of enzymes whereby protease is one of
those major components due to hydrolysis of the other components.
[0005] Accordingly the invention provides a washing machine incorporating a device for sequentially
treating fabrics with at least first and second enzymes, the device comprising a plurality
of separate chambers containing respectively first and second enzymes, from which
chambers the enzymes are sequentially dispensed, wherein the first enzyme(s) comprise
a protease and the second enzyme(s) comprise one or more enzymes of a different family
to the first enzyme. The device preferably comprises the drawer of a washing machine.
[0006] The first and second enzymes may comprise a single enzyme or a mixture of enzymes.
[0007] Surprisingly, the above arrangement allows the enzymes to work with minimal interference
from other enzymes. The proteases, dosed first, might be expected to attack the other
enzyme(s) on addition to the wash liquor preventing the non proteolytic treatment
of stains. However, the stain removal performance of the enzymes due to sequential
dosing is vastly improved.
[0008] Suitable proteases include those of animal, vegetable or microbial origin. Microbial
origin is preferred. Chemically modified or protein engineered mutants are included.
The protease may be a serine protease or a metallo protease, preferably an alkaline
microbial protease or a trypsin-like protease. Examples of alkaline proteases are
subtilisins, especially those derived from
Bacillus, e.g., subtilisin Novo, subtilisin Carlsberg, subtilisin 309, subtilisin 147 and subtilisin
168 (described in
WO 89/06279). Examples of trypsin-like proteases are trypsin (e.g. of porcine or bovine origin)
and the
Fusarium protease described in
WO 89/06270 and
WO 94/25583.
[0009] Examples of useful proteases are the variants described in
WO 92/19729,
WO 98/20115,
WO 98/20116, and
WO 98/34946, especially the variants with substitutions in one or more of the following positions:
27, 36, 57, 76, 87, 97, 101, 104, 120, 123, 167, 170, 194, 206, 218, 222, 224, 235
and 274. Preferred commercially available protease enzymes include Alcalase
™, Savinase
™, Primase
™, Duralase
™, Dyrazym
™, Esperase
™, Everlase
™, Polarzyme
™, and Kannase
™, (Novozymes A/S), Maxatase
™, Maxacal
™, Maxapem
™, Properase
™, Purafect
™, Purafect OxP™, FN2™, and FN3™ (Genencor International Inc.).
[0010] Suitable lipases include those of bacterial or fungal origin. Chemically modified
or protein engineered mutants are included. Examples of useful lipases include lipases
from
Humicola (synonym
Thermomyces), e.g. from
H. lanuginosa (
T. lanuginosus) as described in
EP 258 068 and
EP 305 216 or from
H. insolens as described in
WO 96/13580, a
Pseudomonas lipase, e.g. from
P. alcaligenes or
P. pseudoalcaligenes (
EP 218 272),
P. cepacia (
EP 331 376),
P. stutzeri (
GB 1,372,034),
P. fluorescens, Pseudomonas sp. strain SD 705 (
WO 95/06720 and
WO 96/27002),
P. wisconsinensis (
WO 96/12012), a
Bacillus lipase, e.g. from
B. subtilis (
Dartois et al. (1993), Biochemica et Biophysica Acta, 1131, 253-360),
B. stearothermophilus (
JP 64/744992) or
B. pumilus (
WO 91/16422).
[0011] Other examples are lipase variants such as those described in
WO 92/05249,
WO 94/01541,
EP 407 225,
EP 260 105,
WO 95/35381,
WO 96/00292,
WO 95/30744,
WO 94/25578,
WO 95/14783,
WO 95/22615,
WO 97/04079 and
WO 97/07202.
[0012] Preferred commercially available lipase enzymes include Lipolase
™ and Lipolase Ultra
™, Lipex
™ (Novozymes A/S).
[0013] It is to be understood that enzyme variants (produced, for example, by recombinant
techniques) are included within the meaning of the term "enzyme". Examples of such
enzyme variants are disclosed, e.g., in
EP 251,446 (Genencor),
WO 91/00345 (Novo Nordisk),
EP 525,610 (Solvay) and
WO 94/02618 (Gist-Brocades NV).
[0014] Accordingly the types of enzymes which may appropriately be incorporated in granules
of the invention include oxidoreductases (EC 1.-.-.-), transferases (EC 2.-.-.-),
hydrolases (EC 3.-.-.-), lyases (EC 4.-.-.-), isomerases (EC 5.-.-.-) and ligases
(EC 6.-.-.-).
[0015] The sequentially delivered proteases and lipolytic enzymes may be dosed in isolation
from other main wash components or they may be dosed with such components, but preferably
not combining the protease with other enzymes.
[0016] The sequentially delivered enzymes used in the invention may be delivered together
with one or more surfactants and/or optionally other ingredients such that at least
one of the sequential doses is a fully functional laundry cleaning and/or care compositions.
Such compositions used in the invention may be in dry solid or liquid form. The composition
may be a concentrate to be diluted, rehydrated and/or dissolved in a solvent, including
water, before use. The composition may also be a ready-to-use (in-use) composition.
[0017] The present invention is suitable for use in industrial or domestic fabric wash applications,
fabric conditioning applications and applications for both washing and conditioning
fabrics (so-called through the wash conditioner compositions). The present invention
can also be applied to industrial or domestic non-detergent based fabric care applications,
for example spray-on applications.
[0018] Fabric wash compositions used in the present invention may be in any suitable form,
for example powdered, tableted powders, liquid or solid detergent bars.
[0019] Other contemplated ingredients including surfactants, hydrotropes, preservatives,
fillers, builders, complexing agents, polymers, stabilizers, perfumes per se, other
detergent ingredients, or combinations of one or more thereof are discussed below.
[0020] The enzymes may be present as the sole reactive stain removal agent, or other stain
removal agents may be incorporated.
[0021] Additional enzymes may be dosed as part of the overall washing process, providing
this follows the initial process according to the invention (i.e. treatment with an
enzyme such as a protease/s and then a second or more enzyme such as lipase/s).
[0022] Such additional (i.e. subsequently dosed) enzymes may include further proteases and
lipases as above, and also alpha-amylases, cellulases, peroxidases/oxidases, pectate
lyases, and mannanases, or mixtures thereof.
[0023] Additional components may also include cutinase classified in EC 3.1.1.74. The cutinase
used according to the invention may be of any origin. Preferably cutinases are of
microbial origin, in particular of bacterial, of fungal or of yeast origin.
[0024] Cutinases are enzymes which are able to degrade cutin. In a preferred embodiment,
the cutinase is derived from a strain of
Aspergillus, in particular
Aspergillus oryzae, a strain of
Alternaria, in particular
Alternaria brassiciola, a strain of
Fusarium, in particular
Fusarium solani, Fusarium solani pisi, Fusarium roseum culmorum, or
Fusarium roseum sambucium, a strain of
Helminthosporum, in particular
Helminthosporum sativum, a strain of
Humicola, in particular
Humicola insolens, a strain of
Pseudomonas, in particular
Pseudomonas mendocina, or
Pseudomonas putida, a strain of
Rhizoctonia, in particular
Rhizoctonia solani, a strain of
Streptomyces, in particular
Streptomyces scabies, or a strain of
Ulocladium, in particular
Ulocladium consortiale. In a most preferred embodiment the cutinase is derived from a strain of
Humicola insolens, in particular the strain
Humicola insolens DSM 1800.
Humicola insolens cutinase is described in
WO 96/13580. The cutinase may be a variant, such as one of the variants disclosed in
WO 00/34450 and
WO 01/92502. Preferred cutinase variants include variants listed in Example 2 of
WO 01/92502.
[0025] Preferred commercial cutinases include NOVOZYM
™ 51032 (available from Novozymes A/S, Denmark).
[0026] Additional components may also include phospholipase classified as EC 3.1.1.4 and/or
EC 3.1.1.32. As used herein, the term phospholipase is an enzyme which has activity
towards phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, consist
of glycerol esterified with two fatty acids in an outer (sn-1) and the middle (sn-2)
positions and esterified with phosphoric acid in the third position; the phosphoric
acid, in turn, may be esterified to an amino-alcohol. Phospholipases are enzymes which
participate in the hydrolysis of phospholipids. Several types of phospholipase activity
can be distinguished, including phospholipases A
1 and A
2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively)
to form lysophospholipid; and lysophospholipase (or phospholipase B) which can hydrolyze
the remaining fatty acyl group in lysophospholipid. Phospholipase C and phospholipase
D (phosphodiesterases) release diacyl glycerol or phosphatidic acid respectively.
[0027] The term phospholipase includes enzymes with phospholipase activity, e.g., phospholipase
A (A
1 or A
2), phospholipase B activity, phospholipase C activity or phospholipase D activity.
The term "phospholipase A" used herein in connection with an enzyme of the invention
is intended to cover an enzyme with Phospholipase A
1 and/or Phospholipase A
2 activity. The phospholipase activity may be provided by enzymes having other activities
as well, such as, e.g., a lipase with phospholipase activity. The phospholipase activity
may, e.g., be from a lipase with phospholipase side activity. In other embodiments
of the invention the phospholipase enzyme activity is provided by an enzyme having
essentially only phospholipase activity and wherein the phospholipase enzyme activity
is not a side activity.
[0028] The phospholipase may be of any origin, e.g., of animal origin (such as, e.g., mammalian),
e.g. from pancreas (e.g., bovine or porcine pancreas), or snake venom or bee venom.
Preferably the phospholipase may be of microbial origin, e.g., from filamentous fungi,
yeast or bacteria, such as the genus or species
Aspergillus, e.g.,
A. niger; Dictyostelium, e.g.,
D. discoideum; Mucor, e.g.
M. javanicus, M. mucedo, M. subtilissimus; Neurospora, e.g.
N. crassa; Rhizomucor, e.g.,
R. pusillus;
Rhizopus, e.g.
R. arrhizus, R. japonicus, R. stolonifer; Sclerotinia, e.g.,
S. libertiana; Trichophyton, e.g.
T. rubrum; Whetzelinia, e.g.,
W. sclerotiorum; Bacillus, e.g.,
B. megaterium, B. subtilis; Citrobacter, e.g.,
C. freundii; Enterobacter, e.g.,
E. aerogenes, E. cloacae Edwardsiella, E. tarda; Erwinia, e.g.,
E. herbicola; Escherichia, e.g.,
E. coli; Klebsiella, e.g.,
K. pneumoniae; Proteus, e.g.,
P. vulgaris; Providencia, e.g.,
P. stuartii; Salmonella, e.g.
S. typhimurium; Serratia, e.g.,
S. liquefasciens, S. marcescens; Shigella, e.g.,
S. flexneri; Streptomyces, e.g.,
S. violeceoruber; Yersinia, e.g.,
Y. enterocolitica. Thus, the phospholipase may be fungal, e.g., from the class
Pyrenomycetes, such as the genus
Fusarium, such as a strain of
F. culmorum, F. heterosporum, F. solani, or a strain of
F. oxysporum. The phospholipase may also be from a filamentous fungus strain within the genus
Aspergillus, such as a strain of
Aspergillus awamori, Aspergillus foetidus, Aspergillus japonicus, Aspergillus niger or
Aspergillus oryzae.
[0029] Preferred phospholipases are derived from a strain of
Humicola, especially
Humicola lanuginosa. The phospholipase may be a variant, such as one of the variants disclosed in
WO 00/32758, which are hereby incorporated by reference. Preferred phospholipase variants include
variants listed in Example 5 of
WO 00/32758, which is hereby specifically incorporated by reference. In another preferred embodiment
the phospholipase is one described in
WO 04/111216, especially the variants listed in the table in Example 1.
[0030] Preferably the phospholipase is derived from a strain of
Fusarium, especially
Fusarium oxysporum. The phospholipase may be the one concerned in
WO 98/026057 derived from Fusarium oxysporum DSM 2672, or variants thereof.
[0031] The phospholipase is preferably a phospholipase A
1 (EC. 3.1.1.32). or a phospholipase A
2 (EC.3.1.1.4.).
[0032] Examples of commercial phospholipases include LECITASE
™ and LECITASE
™ ULTRA, YIELSMAX, or LIPOPAN F (available from Novozymes A/S, Denmark).
[0033] Suitable amylases (alpha and/or beta) include those of bacterial or fungal origin.
Chemically modified or protein engineered mutants are included. Amylases include,
for example, alpha-amylases obtained from
Bacillus, e.g. a special strain of
B. licheniformis, described in more detail in
GB 1,296,839, or the
Bacillus sp. strains disclosed in
WO 95/026397 or
WO 00/060060.
[0035] Commercially available amylases are Duramyl
™, Termamyl
™, Termamyl Ultra
™, Natalase
™, Stainzyme
™, Fungamyl
™ and BAN
™ (Novozymes A/S), Rapidase
™ and Purastar
™ (from Genencor International Inc.).
[0036] Suitable cellulases include those of bacterial or fungal origin. Chemically modified
or protein engineered mutants are included. Suitable cellulases include cellulases
from the genera
Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, e.g. the fungal cellulases produced from
Humicola insolens, Thiela via terrestris, Myceliophthora thermophila, and
Fusarium oxysporum disclosed in
US 4,435,307,
US 5,648,263,
US 5,691,178,
US 5,776,757,
WO 89/09259,
WO 96/029397, and
WO 98/012307.
[0037] Especially suitable cellulases are the alkaline or neutral cellulases having color
care benefits. Examples of such cellulases are cellulases described in
EP 0 495 257,
EP 0 531 372,
WO 96/11262,
WO 96/29397,
WO 98/08940. Other examples are cellulase variants such as those described in
WO 94/07998,
EP 0 531 315,
US 5,457,046,
US 5,686,593,
US 5,763,254,
WO 95/24471,
WO 98/12307 and
PCT/DK98/00299.
[0038] Commercially available cellulases include Celluzyme
™, Carezyme
™, Endolase
™, Renozyme
™ (Novozymes A/S), Clazinase
™ and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™ (Kao Corporation).
[0039] Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin.
Chemically modified or protein engineered mutants are included. Examples of useful
peroxidases include peroxidases from
Coprinus, e.g. from
C. cinereus, and variants thereof as those described in
WO 93/24618,
WO 95/10602, and
WO 98/15257. Commercially available peroxidases include Guardzyme
™ and Novozym
™ 51004 (Novozymes A/S).
[0040] Examples of pectate lyases include pectate lyases that have been cloned from different
bacterial genera such as
Erwinia, Pseudomonas, Klebsiella and
Xanthomonas, as well as from
Bacillus subtilis (
Nasser et al. (1993) FEBS Letts. 335:319-326) and
Bacillus sp. YA-14 (
Kim et al. (1994) Biosci. Biotech. Biochem. 58:947-949). Purification of pectate lyases with maximum activity in the pH range of 8-10 produced
by
Bacillus pumilus (
Dave and Vaughn (1971) J. Bacteriol. 108:166-174),
B. polymyxa (
Nagel and Vaughn (1961) Arch. Biochem. Biophys. 93:344-352),
B. stearothermophilus (
Karbassi and Vaughn (1980) Can. J. Microbiol. 26:377-384),
Bacillus sp. (
Hasegawa and Nagel (1966) J. Food Sci. 31:838-845) and
Bacillus sp. RK9 (
Kelly and Fogarty (1978) Can. J. Microbiol. 24:1164-1172) have also been described. Any of the above, as well as divalent cation-independent
and/or thermostable pectate lyases, may be used in practicing the invention. In preferred
embodiments, the pectate lyase comprises the amino acid sequence of a pectate lyase
disclosed in
Heffron et al., (1995) Mol. Plant-Microbe Interact. 8: 331-334 and
Henrissat et al., (1995) Plant Physiol. 107: 963-976. Specifically contemplated pectatel lyases are disclosed in
WO 99/27083 and
WO 99/27084. Other specifically contemplates pectate lyases derived from
Bacillus licheniformis is disclosed in
US patent no. 6,284,524. Specifically contemplated pectate lyase variants are disclosed in
WO 02/006442, especially the variants disclosed in the Examples in
WO 02/006442.
[0041] Examples of commercially available alkaline pectate lyases include BIOPREP
™ and SCOURZYME
™ L from Novozymes A/S, Denmark.
[0042] Examples of mannanases (EC 3.2.1.78) include mannanases of bacterial and fungal origin.
In a specific embodiment the mannanase is derived from a strain of the filamentous
fungus genus Aspergillus, preferably
Aspergillus niger or
Aspergillus aculeatus (
WO 94/25576).
WO 93/24622 discloses a mannanase isolated from
Trichoderma reseei. Mannanases have also been isolated from several bacteria, including
Bacillus organisms. For example,
Talbot et al., Appl. Environ. Microbiol., Vol.56, No. 11, pp. 3505-3510 (1990) describes a beta-mannanase derived from
Bacillus stearothermophilus. Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551-555 (1994) describes a beta-mannanase derived from
Bacillus subtilis.
[0043] JP-A-03047076 discloses a beta-mannanase derived from
Bacillus sp.
JP-A-63056289 describes the production of an alkaline, thermostable beta-mannanase.
JP-A-63036775 relates to the
Bacillus microorganism FERM P-8856 which produces beta-mannanase and beta-mannosidase.
JP-A-08051975 discloses alkaline beta-mannanases from alkalophilic
Bacillus sp. AM-001. A purified mannanase from
Bacillus amyloliquefaciens is disclosed in
WO 97/11164.
WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active. Contemplated
are the alkaline family 5 and 26 mannanases derived from
Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii,
Bacillus sp., and
Humicola insolens disclosed in
WO 99/64619. Especially contemplated are the
Bacillus sp. mannanases concerned in the Examples in
WO 99/64619.
[0044] Examples of commercially available mannanases include Mannaway
™ available from Novozymes A/S Denmark.
[0045] Any enzyme present in a composition may be stabilized using conventional stabilizing
agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol,
lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester,
or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition
may be formulated as described in e.g.
WO 92/19709 and
WO 92/19708.
[0046] The fabric wash compositions may comprise a fabric wash detergent material selected
from non-soap anionic surfactant, nonionic surfactants, soap, amphoteric surfactants,
zwitterionic surfactants and mixtures thereof.
[0047] Detergent compositions suitable for use in domestic or industrial automatic fabric
washing machines generally contain anionic non-soap surfactant or nonionic surfactant,
or combinations of the two in suitable ratio, as will be known to the person skilled
in the art, optionally together with soap.
[0048] Many suitable detergent-active compounds are available and fully described in the
literature, for example in "Surface-Active Agents and Detergents", Volumes I and II,
by Schwartz, Perry & Berch.
[0049] The surfactants may be present in the composition at a level of from 0.1% to 60%
by weight.
[0050] Suitable anionic surfactants are well known to the person skilled in the art and
include alkyl benzene sulphonate, primary and secondary alkyl sulphates, particularly
C
8-C
15 primary alkyl sulphates; alkyl ether sulphates; olefin sulphonates; alkyl xylene
sulphonates, dialkyl sulphosuccinates; ether carboxylates; isethionates; sarcosinates;
fatty acid ester sulphonates and mixtures thereof. The sodium salts are generally
preferred. When included therein the composition usually contains from about 1% to
about 50%, preferably 10 wt%-40 wt% based on the fabric treatment composition of an
anionic surfactant such as linear alkylbenzenesulfonate, alpha-olefinsulfonate, alkyl
sulfate (fatty alcohol sulfate), alcohol ethoxysulfate, secondary alkanesulfonate,
alpha-sulfo fatty acid methyl ester, alkyl- or alkenylsuccinic acid or soap. Preferred
surfactants are alkyl ether sulphates and blends of alkoxylated alkyl nonionic surfactants
with either alkyl sulphonates or alkyl ether sulphates.
[0051] Preferred alkyl ether sulphates are C8-C15 alkyl and have 2-10 moles of ethoxlation.
Preferred alkyl sulphates are alkylbenzene sulphonates, particularly linear alkylbenzene
sulphonates having an alkyl chain length of C
8-C
15. The counter ion for anionic surfactants is typically sodium, although other counter-ions
such as TEA or ammonium can be used. Suitable anionic surfactant materials are available
in the marketplace as the 'Genapol'
™ range from Clariant.
[0052] Nonionic surfactants are also well known to the person skilled in the art and include
primary and secondary alcohol ethoxylates, especially C
8-C
20 aliphatic alcohol ethoxylated with an average of from 1 to 20 moles of ethylene oxide
per mole of alcohol, and more especially the C
10-C
15 primary and secondary aliphatic alcohols ethoxylated with an average of from 1 to
10 moles of ethylene oxide per mole of alcohol. Non-ethoxylated nonionic surfactants
include alkyl polyglycosides, glycerol monoethers and polyhydroxy amides (glucamide).
Mixtures of nonionic surfactant may be used. When included therein the composition
usually contains from about 0.2% to about 40%, preferably 1 to 20 wt%, more preferably
5 to 15 wt% of a non-ionic surfactant such as alcohol ethoxylate, nonylphenol ethoxylate,
alkylpolyglycoside, alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide,
fatty acid monoethanolamide, polyhydroxy alkyl fatty acid amide, or N-acyl N-alkyl
derivatives of glucosamine ("glucamides").
[0053] Nonionic surfactants that may be used include the primary and secondary alcohol ethoxylates,
especially the C
8-C
20 aliphatic alcohols ethoxylated with an average of from 1 to 35 moles of ethylene
oxide per mole of alcohol, and more especially the C
10-C
15 primary and secondary aliphatic alcohols ethoxylated with an average of from 1 to
10 moles of ethylene oxide per mole of alcohol.
[0054] Higher levels of surfactant may be employed (up to almost 100%) but this can leave
little space in the formulation for builders and other components and may lead to
a sticky product which requires special processing.
[0055] Hydrotropes may be included in the composition/s. The term "hydrotrope" generally
means a compound with the ability to increase the solubilities, preferably aqueous
solubilities, of certain slightly soluble organic compounds. Examples of hydrotropes
include sodium xylene sulfonate, SCM.
[0056] The composition/s may comprise a solvent such as water or an organic solvent such
as isopropyl alcohol or glycol ethers. Solvents are typically present in liquid or
gel compositions.
[0057] The composition/s may contain a metal chelating agent such as carbonates, bicarbonates,
and sesquicarbonates. The metal chelating agent can be a bleach stabiliser (i.e. heavy
metal sequestrant). Suitable bleach stabilisers include ethylenediamine tetraacetate
(EDTA), diethylenetriamine pentaacetate (DTPA), ethylenediamine disuccinate (EDDS),
and the polyphosphonates such as the Dequests (Trade Mark), ethylenediamine tetramethylene
phosphonate (EDTMP) and diethylenetriamine pentamethylene phosphate (DETPMP). In general
metal chelating agents will not be present in the part (a) of the composition as microbial
function may be impaired if metal ions are made unavailable.
[0058] Builder materials may be selected from 1) calcium sequestrant materials, 2) precipitating
materials, 3) calcium ion-exchange materials and 4) mixtures thereof.
[0059] Examples of calcium sequestrant builder materials include alkali metal polyphosphates,
such as sodium tripolyphosphate and organic sequestrants, such as ethylene diamine
tetraacetic acid.
[0060] Examples of precipitating builder materials include sodium orthophosphate and sodium
carbonate.
[0061] Examples of calcium ion-exchange builder materials include the various types of water-insoluble
crystalline or amorphous aluminosilicates, of which zeolites are the best known representatives,
e.g. zeolite A, zeolite B (also known as zeolite P), zeolite C, zeolite X, zeolite
Y and also the zeolite P-type as described in
EP-A-0,384,070.
[0062] The composition/s may also contain 0-65 % of a builder or complexing agent such as
ethylenediaminetetraacetic acid, diethylenetriamine-pentaacetic acid, alkyl- or alkenylsuccinic
acid, nitrilotriacetic acid or the other builders mentioned below. Many builders are
bleach-stabilising agents by virtue of their ability to complex metal ions.
[0063] Where builder is present, the composition/s may suitably contain less than 20%wt,
preferably less than 10% by weight, and most preferably less than 10%wt of detergency
builder.
[0064] The composition/s may contain as builder a crystalline aluminosilicate, preferably
an alkali metal aluminosilicate, more preferably a sodium aluminosilicate. This is
typically present at a level of less than 15%w. Aluminosilicates are materials having
the general formula:
0.8-1.5 M
2O. Al
2O
3. 0.8-6 SiO
2
where M is a monovalent cation, preferably sodium. These materials contain some bound
water and are required to have a calcium ion exchange capacity of at least 50 mg CaO/g.
The preferred sodium aluminosilicates contain 1.5-3.5 SiO
2 units in the formula above. They can be prepared readily by reaction between sodium
silicate and sodium aluminate, as amply described in the literature. The ratio of
surfactants to alumuminosilicate (where present) is preferably greater than 5:2, more
preferably greater than 3:1.
[0065] Alternatively, or additionally to the aluminosilicate builders, phosphate builders
may be used. In this art the term 'phosphate' embraces diphosphate, triphosphate,
and phosphonate species. Other forms of builder include silicates, such as soluble
silicates, metasilicates, layered silicates (e.g. SKS-6 from Hoechst).
[0066] For low cost formulations carbonate (including bicarbonate and sesquicarbonate) and/or
citrate may be employed as builders.
[0067] The composition may comprise one or more polymers. Examples are carboxymethylcellulose,
poly(vinylpyrrolidone), poly (ethylene glycol), poly(vinyl alcohol), poly(vinylpyridine-N-oxide),
poly(vinylimidazole), polycarboxylates such as polyacrylates, maleic/acrylic acid
copolymers and lauryl methacrylate/acrylic acid copolymers.
[0068] Modern detergent compositions typically employ polymers as so-called 'dye-transfer
inhibitors'. These prevent migration of dyes, especially during long soak times. Any
suitable dye-transfer inhibition agents may be used in accordance with the present
invention. Generally, such dye-transfer inhibiting agents include polyvinyl pyrrolidone
polymers, polyamine N-oxide polymers, copolymers of N-vinylpyrrolidone and N-vinylimidazole,
manganese pthalocyanine, peroxidases, and mixtures thereof.
[0069] Nitrogen-containing, dye binding, DTI polymers are preferred. Of these polymers and
co-polymers of cyclic amines such as vinyl pyrrolidone, and/or vinyl imidazole are
preferred.
[0070] Polyamine N-oxide polymers suitable for use herein contain units having the following
structural formula: R-A
x-P; wherein P is a polymerizable unit to which an N-O group can be attached or the
N-O group can form part of the polymerizable unit; A is one of the following structures:
- NC(O)-, -C (O) O-, -S-, -O-, -N=; x is 0 or 1; and R is an aliphatic, ethoxylated
aliphatic, aromatic, heterocyclic or alicyclic group or combination thereof to which
the nitrogen of the N-O group can be attached or the N-O group is part of these groups,
or the N-O group can be attached to both units. Preferred polyamine N-oxides are those
wherein R is a heterocyclic group such as pyridine, pyrrole, imidazole, pyrrolidine,
piperidine and derivatives thereof. The N-O group can be represented by the following
general structures: N(O)(R')
0-3, or =N(O)(R')
0-1, wherein each R' independently represents an aliphatic, aromatic, heterocyclic or
alicylic group or combination thereof; and the nitrogen of the N-O group can be attached
or form part of any of the aforementioned groups. The amine oxide unit of the polyamine
N-oxides has a pKa<10, preferably pKa<7, more preferably pKa<6.
[0071] Any polymer backbone can be used provided the amine oxide polymer formed is water-soluble
and has dye transfer inhibiting properties. Examples of suitable polymeric backbones
are polyvinyls, polyalkylenes, polyesters, polyethers, polyamides, polyimides, polyacrylates
and mixtures thereof. These polymers include random or block copolymers where one
monomer type is an amine N-oxide and the other monomer type is an N-oxide. The amine
N-oxide polymers typically have a ratio of amine to the amine N-oxide of 10:1 to 1:1,000,000.
However, the number of amine oxide groups present in the polyamine oxide polymer can
be varied by appropriate copolymerization or by an appropriate degree of N-oxidation.
The polyamine oxides can be obtained in almost any degree of polymerization. Typically,
the average molecular weight is within the range of 500 to 1,000,000; more preferably
1,000 to 500,000; most preferably 5,000 to 100,000. This preferred class of materials
is referred to herein as "PVNO". A preferred polyamine N-oxide is poly(4-vinylpyridine-N-oxide)
which as an average molecular weight of about 50,000 and an amine to amine N-oxide
ratio of about 1:4.
[0072] Copolymers of N-vinylpyrrolidone and N-vinylimidazole polymers (as a class, referred
to as "PVPVI") are also preferred. Preferably the PVPVI has an average molecular weight
range from 5,000 to 1,000,000, more preferably from 5,000 to 200,000, and most preferably
from 10,000 to 20,000, as determined by light scattering as described in
Barth, et al., Chemical Analysis, Vol. 113. "Modern Methods of Polymer Characterization". The preferred PVPVI copolymers typically have a molar ratio of N-vinylimidazole
to N-vinylpyrrolidone from 1:1 to 0.2:1, more preferably from 0.8:1 to 0.3:1, most
preferably from 0.6:1 to 0.4:1. These copolymers can be either linear or branched.
Suitable PVPVI polymers include Sokalan
(™) HP56, available commercially from BASF, Ludwigshafen, Germany.
[0073] Also preferred as dye transfer inhibition agents are polyvinylpyrrolidone polymers
("PVP") having an average molecular weight of from about 5,000 to about 400,000, preferably
from about 5,000 to about 2000,000, and more preferably from about 5,000 to about
50,000. PVP's are disclosed for example in
EP-A-262,897 and
EP-A-256,696. Suitable PVP polymers include Sokalan
(™) HP50, available commercially from BASF. Compositions containing PVP can also contain
polyethylene glycol ("PEG") having an average molecular weight from about 500 to about
100,000, preferably from about 1,000 to about 10,000. Preferably, the ratio of PEG
to PVP on a ppm basis delivered in wash solutions is from about 2:1 to about 50:1,
and more preferably from about 3:1 to about 10:1.
[0074] Also suitable as dye transfer inhibiting agents are those from the class of modified
polyethyleneimine polymers, as disclosed for example in
WO-A-0005334. These modified polyethyleneimine polymers are water-soluble or dispersible, modified
polyamines. Modified polyamines are further disclosed in
US-A-4,548,744;
US-A-4,597,898;
US-A-4,877,896;
US-A- 4,891,
160;
US-A- 4,976,879;
US-A-5,415,807;
GB-A-1,537,288;
GB-A-1,498,520;
DE-A-28 29022; and
JP-A-06313271.
[0075] Preferably the composition/s used in the present invention comprises a dye transfer
inhibition agent selected from polyvinylpyrridine N-oxide (PVNO), polyvinyl pyrrolidone
(PVP), polyvinyl imidazole, N-vinylpyrrolidone and N-vinylimidazole copolymers (PVPVI),
copolymers thereof, and mixtures thereof.
[0076] The amount of dye transfer inhibition agent in the composition/s according to the
present invention will be from 0.01 to 10 %, preferably from 0.02 to 5 %, more preferably
from 0.03 to 2 %, by weight of the composition.
[0077] The composition/s may also contain other detergent ingredients such as e.g. fabric
conditioners including clays, foam boosters, suds suppressors (anti-foams), anticorrosion
agents, soil-suspending agents, anti-soil redeposition agents, further dyes, anti-microbials,
optical brighteners, tarnish inhibitors, or perfumes.
[0078] The dispensing drawer of the automatic washing machine may be used to sequentially
dose the enzymes, for example by using the pre-wash chamber to dose the protease/s
and the main wash chamber to dose the lipase/s.
EXAMPLES OF NON LIMITING EMBODIMENTS OF THE INVENTION
Example 1
Wash Evaluation of protease and a lipase in grass stain removal (tergotometer)
[0079] Wash performance was evaluated by washing grass stained polyester swatches (wfk30A)
in a detergent solution with a protease (Savinase 12TXT) and a lipase (Lipex 100T
or lipolase 100T) in single enzyme, combination and sequence (2 wash) treatments.
[0080] Preparation of grass stain swatches: Consumer relevant stains were prepared manually
by rigorously rubbing clumps of lawn grass on clean cotton fabric swatches, to create
circular homogeneous dark green stains.
[0081] Wash: Grass stain swatches (7 x 7 cm) were placed in tergotometer tubs with the model
formulation components (table 1) in 11 demin water and incubated for 30 min at 37°C,
with mechanical stirring. At t= 15 minutes, stirring was paused, all stains were rinsed
in 11 demin water, and stains were transferred to second-in-sequence enzyme wash tubs.
Stirring was continued for the further 15 minutes. The swatches were rinsed in tap
water, span and allowed to dry in the dark, at room temperature overnight.
[0082] Evaluation: Colour remission of the swatches was measured at 410 nm using a Hunterlab
UltraScan VIS remission spectrophotometer. The results are expressed as delta remission=
(
Rafter wash-
Rbefore wash)
enzyme- (
Rafter wash -
Rbefore wash)
control, where R is the remission at 410 nm using the CIE L*a*b* (CIELAB) values generated
(figure 1).
Table 1. Formulation components
NaCl |
0.05 M |
Ca2+ |
6 FH |
CAPS buffer, pH 10 |
20 mM |
Surfactant (80:20 LAS:E07, w/w) |
0.5 g/l |
Enzyme (total) |
1 mg/L |
Table 2
Wash performance of savinase, savinase and lipase and savinase followed by lipase
on cotton and at low FH (FH6) in tergotometer. All stains are washed with surfactant.
Total enzyme protein concentration = 1µg/ml. |
Enzyme |
d[DE]minus control |
Savinase |
0.82 |
Savinase + Lipex |
0.68 |
Savinase + Lipolase |
1.61 |
Savinase followed by Lipex |
2.81 |
Savinase followed by Lipolase |
3.46 |
[0083] The table shows how the sequential dosing of a protease followed by a lipase provides
much improved stain removal.
Example 2
Wash Evaluation of protease and a lipase in grass stain removal (microtiter)
[0084] Wash performance was evaluated by washing grass stained cotton testcloth in a detergent
solution with a protease (Savinase 12TXT) and a lipase (Lipex 100T) in single enzyme,
combination and sequence (2 wash) treatments.
[0085] Preparation of grass stain testcloth: Consumer relevant stains were prepared manually
by rigorously rubbing blended grass (3:1 ration in water), prefiltered through a polyester
fabric, on clean cotton fabric using a nailbrush.
[0086] Wash: Grass stain testcloths were placed in microtiter plates with the model formulation
components (table 1) in 200µl demin water and incubated for 30 min at 37°C on an orbital
shaker, with agitation (1150rpm). This time low (FH60) and high (FH40) water hardness
was tested. At t= 15 minutes, agitation was paused, all stains were rinsed in 200µl
demin water, and exposed to second-in-sequence enzyme solution. Agitation was continued
for the further 15 minutes. The swatches were rinsed in tap water twice and allowed
to dry in the dark, at 45°C for at least 3 hours.
[0087] Evaluation: Colour remission of the swatches was measured at 410 nm using a flatbed
remission spectrophotometer. The results are expressed as delta remission = (
Rafter wash-
Rbefore wash)
enzyme- (
Rafter wash-
Rbefore wash)
control, where R is the remission at 410 nm using the CIE L*a*b* (CIELAB) values generated
(tables 3 and 4).
Savinase |
15.39, |
16.12, |
Savinase + Lipase |
14.17 |
17.95, |
Savinase followed by Lipase |
20.40 |
21.10 |
[0088] Table 3 Wash performance of savinase, savinase and lipase and savinase followed by
lipase on cotton and at low FH (FH6) in microtiter plates. All stains are washed with
surfactant. Total enzyme protein concentration = 1 or 40µg/ml. S-L, savinase followed
by lipase.
Savinase |
6.66 |
12.19 |
Savinase + Lipase |
6.52 |
10.72, |
Savinase followed by Lipase |
8.90 |
13.94 |
[0089] Table 4 Wash performance of savinase, savinase and lipase and savinase followed by
lipase on cotton and at high FH (FH40)in microtiter plates. All stains are washed
with surfactant. Total enzyme protein concentration = 1 or 40µg/ml. S-L, savinase
followed by lipase.
[0090] It is of course to be understood that the invention is not intended to be restricted
to the details of the above embodiment which are described by way of example only.