[0001] The present invention concerns a viscous laundry product and packaging therefore.
[0002] An objective is to provide an improved pre-treatment device for the precise pre-treatment
of laundry stains.
[0003] Accordingly, in a first aspect, the present invention provides a packaged laundry
product comprising a flowable laundry composition contained in a package, wherein:
- (i) the flowable laundry composition has a viscosity of at least 100 Pa.s. (and preferably
at least 500 Pa.s) when in rest or up to a shear stress of 10 Pa and comprising at
least one surfactant; and
- (ii) the package comprises a squeeze-operated compressible container in which the
flowable laundry composition is stored and a dispensing device and stain treatment
device both located at the base of the compressible container;
- (iii) a reservoir providing a supportive base portion and configured to receive the
dispensed flowable laundry composition from the dispensing device and also receive
at least a portion of the stain treatment device.
[0004] In a second aspect the invention provides a method of treating a stain on a fabric
using the device of the first aspect, the method comprising the steps of:
- (i) squeezing the compressible container to dispense the flowable laundry composition
into the reservoir;
- (ii) inserting the at least a portion of the stain treatment device into the dispensed
flowable laundry composition within the reservoir; and
- (iii) treating the stain by applying the flowable laundry composition on the at least
one portion of the stain treatment device to the stain.
[0005] Steps (ii) and (iii) may be repeated at least once e.g. for larger stains, where
repeated loading of the stain treatment device is needed.
[0006] The advantage of the above arrangement is that it offers great ease in a high viscosity
composition vis-à-vis stained areas. Highly viscous liquids or gels are desirable
for treating as they do not spread out so much after application and so can be restricted
to the stain area. However, stain treating with such high viscosity fluids using squeeze-operated
hand-held products can be difficult ergonomically. One particular problem is how to
dispense a high viscosity composition onto the stain treatment device so it may be
applied to the stain. Various devices are known, such as sponge applicators downstream
of a dispensing orifice, whereby dispensing the fluid forces it through the sponge,
however this is difficult with high viscosity fluids to get large amounts onto the
stain treatment device.
[0007] The arrangement of invention allows the composition to be dispensed in the reservoir,
such that it can be applied to the stain treatment device very easily and repeatedly
for repeated loading with the composition which is useful for larger stains.
[0008] Importantly, as a consequence of the dispensing/stain treatment part being positioned
at the base of the reservoir, means the user does not need to invert the package to
dispense and treat stains as gravity maintains the composition at the bottom of the
container, ready for dispensing. The dispensing device need not involve complicated
and expensive seal/valves as the reservoir encloses the stain treatment device any
drips are collected in the reservoir for later use. This also allows efficient emptying
of the bottle when the composition is nearly all used up.
[0009] The stained area may present in any form such as discolouration, fading, darkening
and may be due to soil or dirt or any other stain-creating substance. Generally stains
affect localised areas (as opposed to the whole garment being affected) but can be
quite large.
[0010] The treatment may precede a further operation such as a main washing operation. However
it may also incorporate a rinsing process whereby the stain is simply treated and
the stained area or whole fabric/article rinsed without a main wash.
[0011] The dispensing device may comprise a channel or duct or valve or aperture or any
combination thereof.
[0012] The reservoir may be part of a closure and may also be used as a dosing device which
can be placed in a washing machine along with the stained fabric (for a main wash
or for a rinse etc) which has been pre-treated using the stain treatment device.
[0013] The reservoir preferably receives the stain treatment device to such a degree that
the stain treatment device projects into the reservoir by more than 50% of the depth
of the reservoir, and more preferably by more than 60%, even more preferably by more
than 75% and most preferably by more than 90%.
[0014] The depth of the reservoir would preferably be the depth measured from the centre
of the reservoir base to the top level of the reservoir sides at its highest point.
For example in the case of a generally hemispherical reservoir the depth would be
measured along the longitudinal axis from the centre of the base which is the deepest
part to the level of the sides - in Fig 1 this is shown from X to Y.
[0015] This feature means that the stain treatment device projects sufficiently deeply into
the reservoir such that the stain treatment device is easily loaded with the composition.
Where the reservoir forms part of a closure device, this is especially advantageous,
since it minimises the risk that inserting the stain treater into the reservoir activates
any closure mechanism (e.g. by snap-fit engagement or screw-on screw-off) as screw-threads
or snap-fit members become engaged by accident.
[0016] The stain treatment device may comprise a device allowing mechanical cleaning, such
as a body with multiple projections. The projections may be flexible so that they
move during cleaning providing a light cleaning action. Alternatively some or all
of the projections may be semi-rigid or rigid so as to provide a harsher mechanical
cleaning action. The projections may be thin e.g. bristles to provide a brush-like
device, or thicker so as to provide finger like projections.
[0017] In one embodiment the stain treatment device comprises a generally hemispherical
body with multiple projections extending radially therefrom.
[0018] The stain treatment device may itself be an extension of the dispensing device. So
it may be continuous with e.g. a dispensing aperture, valve etc. It may comprise a
surface surrounding said aperture or valve etc. so that it can be loaded with, so
as to carry the composition which is then applied to the stained area without any
scrubbing action as might be used with the above described devices containing projections.
The surface may be a ring (full or partial e.g. annular section) around the dispensing
aperture.
[0019] The package may have a convex, preferably a curved e.g. hemispherical top to deter
users from storing the bottle top-down. In this way the package is more likely to
be stored in a stain treatment device - loading position i.e. with the flowable laundry
composition accumulated by gravity in the base of the package.
[0020] The composition is preferably a shear thinning gel-type composition. The viscosity
under shear stress may be less than 300 Pa.s, preferably less than 100 Pa.s and more
preferably less than 5 Pa.s, even more preferably it is at most 1 Pa.s and most preferably
it is at most 0.5 Pa.s.
[0021] Shear thinning compositions may comprise a polymer gum, e.g. Xanthan gum or other
gum capable of forming stable continuous gum networks which can suspend particles.
[0022] Other external structurants e.g. hydrogenated castor oil, micro crystalline cellulose
may be used.
[0023] Another method useful is to change a non-gelled formulation so as to form an internal
structure therein where the structure gives the desired properties to the thus-formed
gel-type detergent. The composition may comprise a soap or fatty acid in combination
with sodium sulphate and one or more surfactants may be used to form a gelled structure
by the formation of lamellar phases.
[0024] The composition may comprise a lamellar phase dispersions from a micellar surfactant
systems, and additionally a structurant for establishing the lamellar phase, whereby
said structurant may be a fatty alcohol.
[0025] The composition of invention contains one or more surfactants and/or optionally other
ingredients such that the composition is fully functional as a laundry cleaning and/or
care composition. A composition of the invention may be provided in solid or liquid
form. If in a solid form, the composition may be rehydrated and/or dissolved in a
solvent, including water, before use. The composition may be provided in a concentrated
form to be diluted or may be a ready-to-use (in-use) composition.
[0026] The present invention is suitable for use in industrial or domestic fabric wash compositions.
The present invention can also be applied to industrial or domestic non-detergent
based fabric care compositions.
[0027] Other contemplated ingredients including hydrotropes, preservatives, fillers, builders,
complexing agents, polymers, stabilizers, perfumes per se, other conventional detergent
ingredients, or combinations of one or more thereof are discussed below.
Surfactants:
[0028] Fabric wash compositions according to the present invention comprise a fabric wash
detergent material selected from non-soap anionic surfactant, nonionic surfactants,
soap, amphoteric surfactants, zwitterionic surfactants and mixtures thereof.
[0029] 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.
[0030] The surfactants may be present in the composition at a level of from 0.1% to 60%
by weight.
[0031] Suitable anionic surfactants 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.
[0032] 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.
[0033] Nonionic surfactants include primary and secondary alcohol ethoxylates, especially
C
8-C
7 aliphatic alcohol ethoxylated with an average of from 1 to 7 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 7 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").
[0034] Nonionic surfactants that may be used include the primary and secondary alcohol ethoxylates,
especially the C
8-C
7 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.
Enzymes:
[0035] The composition may comprise one or more enzymes may be in any suitable. 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).
[0036] The types of enzymes which may appropriately be incorporated in granules of the invention
include oxidoreductases, transferases hydrolases, lyases. isomerases and ligases,
that is, respectively (EC 1.-.-.-), (EC 2.-.-.-),
(EC 3.-.-.-), (EC 4.-.-.-), (EC 5.-.-.-), (EC 6.-.-.-), wherein such enzyme classification
is in accordance with Recommendations (1992) of the
Nomenclature Committee of the International Union of Biochemistry and Molecular Biology,
Academic Press, Inc., 1992.
[0037] Especially contemplated enzymes include proteases, alpha-amylases, cellulases, lipases,
peroxidases/oxidases, pectate lyases, and mannanases, or mixtures thereof. Most preferred
enzymes are proteases.
[0038] 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.
[0039] 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.).
[0040] 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).
[0041] 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.
[0042] Preferred commercially available lipase enzymes include Lipolase™ and Lipolase Ultra™,
Lipex™ (Novozymes A/S).
[0043] The method of the invention may be carried out in the presence of 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.
[0044] 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 which is herby incorporated by reference. The cutinase may be a variant, such as
one of the variants disclosed in
WO 00/34450 and
WO 01/92502, which are hereby incorporated by reference. Preferred cutinase variants include
variants listed in Example 2 of
WO 01/92502, which is hereby specifically incorporated by reference.
[0045] Preferred commercial cutinases include NOVOZYM™ 51032 (available from Novozymes A/S,
Denmark).
[0046] The method of the invention may be carried out in the presence of 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.
[0047] 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.
[0048] 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.
[0049] 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.
[0050] In another preferred embodiment 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.
[0051] In a preferred embodiment of the invention the phospholipase is a phospholipase A
1 (EC. 3.1.1.32). In another preferred embodiment of the invention the phospholipase
is a phospholipase A
2 (EC.3.1.1.4.).
[0052] Examples of commercial phospholipases include LECITASE™ and LECITASE™ ULTRA, YIELSMAX,
or LIPOPAN F (available from Novozymes A/S, Denmark).
[0053] 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.
[0055] Commercially available amylases are Duramyl™, Termamyl™, Termamyl Ultra™, Natalase™,
Stainzyme™, Fungamyl™ and BAN™ (Novozymes A/S), Rapidase™ and Purastar™ (from Genencor
International Inc.).
[0056] 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, Thielavia 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.
[0057] 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.
[0058] Commercially available cellulases include Celluzyme™, Carezyme™, Endolase™, Renozyme™
(Novozymes A/S), Clazinase™ and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™
(Kao Corporation).
[0059] 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).
[0060] 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 (which document is hereby incorporated by reference). Specifically contemplated pectate
lyase variants are disclosed in
WO 02/006442, especially the variants disclosed in the Examples in
WO 02/006442 (which document is hereby incorporated by reference).
[0061] Examples of commercially available alkaline pectate lyases include BIOPREP™ and SCOURZYME™
L from Novozymes A/S, Denmark.
[0062] 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.
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 which document is hereby incorporated by reference.
[0063] Examples of commercially available mannanases include Mannaway™ available from Novozymes
A/S Denmark.
[0064] Any enzyme present in the 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.
Hydrotropes:
[0065] The term "hydrotrope" generally means a compound with the ability to increase the
solubilities, preferably aqueous solubilities, of certain slightly soluble organic
compounds.
[0066] Examples of hydrotropes include sodium xylene sulfonate, SCM.
Solvents:
[0067] The composition may comprise a solvent such as water or an organic solvent such as
isopropyl alcohol or glycol ethers. Solvents may be present in liquid or gel compositions.
Metal Chelation Agents:
[0068] The composition 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.
Builders or Complexing Agents:
[0069] Builder materials may be selected from 1) calcium sequestrant materials, 2) precipitating
materials, 3) calcium ion-exchange materials and 4) mixtures thereof.
[0070] Examples of calcium sequestrant builder materials include alkali metal polyphosphates,
such as sodium tripolyphosphate and organic sequestrants, such as ethylene diamine
tetra-acetic acid.
[0071] Examples of precipitating builder materials include sodium orthophosphate and sodium
carbonate.
[0072] 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.
[0073] The composition 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.
[0074] Where builder is present, the compositions may suitably contain less than 7%wt, preferably
less than 10% by weight, and most preferably less than 10%wt of detergency builder.
[0075] The composition 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.
[0076] 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).
[0077] For low cost formulations carbonate (including bicarbonate and sesquicarbonate) and/or
citrate may be employed as builders.
Polymers:
[0078] 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.
[0079] 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.
[0080] 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.
[0081] 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.
[0082] 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.
[0083] 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.
[0084] 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 70,000, and most preferably
from 10,000 to 7,000, 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.
[0085] 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 700,000, 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.
[0086] 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-1,498,57;
DE-A-28 29022; and
JP-A-06313271.
[0087] Preferably the composition according to 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.
[0088] The amount of dye transfer inhibition agent in the composition 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.
Other Detergent Ingredients:
[0089] The composition may also contain other conventional detergent ingredients such as
e.g. fabric conditioners including clays, foam boosters, suds suppressors (antifoams),
anti-corrosion agents, soil-suspending agents, anti-soil redeposition agents, further
dyes, anti-microbials, optical brighteners, tarnish inhibitors, or perfumes.
[0090] Various non-limiting embodiments of the invention will now be more particularly described
with reference to the following figure in which:
Figure 1 shows a packaged laundry product according to one embodiment of the invention.
[0091] Referring to the drawing, a packaged laundry product 1 is shown. The product 1 comprises
a flowable laundry composition 3 contained in a package 5, the high viscosity laundry
composition 3 according to Example A or B detailed below.
[0092] The package comprises a squeeze-operated compressible container, in this example
a plastic bottle 7 storing the flowable, high viscosity laundry composition 3 and
a dispensing device 9 and a fabric stain treatment device 11. The dispensing device
9 is located at the base 13 of the container 7 and is enclosed by a dosing closure
device 14. The closure 14 comprises the supportive base 13 of the package 5.
[0093] The bottle 7 and a stain treatment device 11 are attached to each other by threaded
connection. The stain treatment device comprises projections (not shown). In an alternative
embodiment it is a sponge, and in a further embodiment it is thin annular section
around the orifice 25 (described below).
[0094] The closure 14 is attached to the bottle also by a threaded connection. (Threaded
connections not shown). In a separate embodiment the closure 14 is connected to the
bottle 7 using a snap-on connection, which negates the requirement to rotate the bottle/closure
to open shut.
[0095] The bottle 7 is fabricated from a flexible plastic material comprising polyethylene
terephthalate.
[0096] The top 21 of the bottle is curved to discourage storage top-down.
[0097] The closure 14 includes an enlarged (with respect to at least the neck region of
the bottle) flat, generally planar bottom surface 15. By providing an enlarged flat
top surface 15, the surface allows the closure 14 to function as a supportive base
with the bottle 7 in an
inverted position thereby allowing the high viscosity gel 3 to accumulate (under gravity)
during storage at the dispensing device 9.
[0098] The closure 14 incorporates a reservoir portion 17 in which the stain treatment device
11 is shown enclosed. The closure 14 has a tapered outer shape, wherein the tapering
is outward in the direction of the base, to provide a stable base area 15 as described
about.
[0099] The stain treatment device projects into the reservoir by approximately 60% of the
depth of the reservoir (the depth being measured along a longitudinal line X-Y. This
affords the advantage that the stain treatment device can be inserted into the reservoir
and contact the dispensed composition so as to be easily loaded with this, without
the screw threads engaging, even when the reservoir is not filled to the top with
composition.
[0100] The dispensing device 9 comprises an orifice 25 through which dispensing may occur.
The orifice includes a valve 22 in fluid communication with duct 23. The valve 22
comprises a membrane extending across orifice 25.
[0101] In an alternative embodiments the orifice/membrane are located further downstream
in the duct. In the extreme examples, it is an the end, as shown in figure ref. 32
[0102] In one embodiment, the membrane has an arcuate portion (not shown) directed toward
the container 7. The arcuate portion of the membrane is provided with a intersecting
slits to define a plurality of generally triangular leaves. When contents of the
container are pressurized for dispensing, the triangular leaves bend toward the open end of
the orifice 25 allowing product to pass through the orifice 25. When the dispensing
pressure is released, the triangular leaves spring back to their original position
and operate to block passage of product through the orifice 25. The leaves of the
valve are sufficiently resilient that they do not bend open unless the applied pressure
exceeds the hydraulic static head pressure generated by a full of condiment. In use,
the fluid is pressurised to flow past and partially collect at the base of the bottle
7 ready for squeeze-operated dispensing into the reservoir. Any of the fluid which
remains on the stain treatment device 11, drips into the reservoir, for later use.
This reduces waste of product.
Exemplary Laundry Formulation A.
[0103] The following gel laundry detergent compositions were prepared, of which composition
A is according to the invention
Component: |
Wt % |
Propylene glycol |
8.0 |
sodium citrate |
3.9 |
Borax |
3.0 |
NaOH (50%) |
1.1 |
Monoethanolamine |
1.0 |
LAS-acid |
4.4 |
Coconut fatty acid |
1.5 |
Nonionic surfactant |
11.1 |
Oleic acid |
2.3 |
1-Dodecanol |
5.0 |
Protease enzyme |
0.3 |
Lipase enzyme |
0.5 |
Perfume |
0.2 |
Water |
balance to 100 |
wherein:
Borax : Sodium tetraborate (10aq)
nonionic surfactant: ethoxylated alcohol with on average 9 ethylene oxide groups.
[0104] The gel detergent composition exemplified by composition A was found to be shear
thinning and stable. Furthermore, typical detergent particles of density between 0.8
and 0.9 g/cm3 and having a diameter up to 5000 microns could be stable suspended in
this composition for more than 2 weeks without any observable net movement of the
particles.
Sample |
Viscosity / Pa.s |
Eta 0 |
Critical Stress |
Tan Delta |
|
20s-1 100s-1 |
Pa.s |
Pa |
at 1 Hz |
A |
2.11 0.61 |
3.00E+05 |
15 |
0.04 |
For obtaining the values shown in the above table, all rheological measurements were
carried out at 25 °C using a Carrimed CSL100 rheometer with a cone and plate geometry
specially roughed to prevent slip.
[0105] Viscosity was measured at varying shear rates from very low shear up to a shear regime
in excess of 100 s
-1. Two situations are shown: the viscosity measured at relatively low shear (20 s
-1) and that measured at much higher shear (100 s
-1). It can be seen that the viscosity of composition A at high shear is much lower
than that obtained at low shear, whereas composition B shows almost equal viscosity's
for high and low shear. In other words composition A is clearly shear thinning, whereas
composition B is not.
[0106] In addition, the critical stress is shown. This parameter represents the stress at
which the material leaves the upper Newtonian plateau and thins under increasing shear.
Also, "Eta 0"-values are shown, referring to the viscosity calculated for zero shear
from creep flow measurements.
[0107] Finally, "Tan delta" values are shown, referring to the ratio of loss over storage
moduli (G"/G') and reflecting the dominance of viscous over elastic properties such
that materials giving very low "Tan delta"-values (tending to zero, such as composition
A in the above table), will be much more elastic than those giving higher "Tan delta"
values (tending to 90).
Exemplary Laundry Formulation B
[0108] The following gel laundry detergent compositions were prepared of which composition
C is according to the invention and composition D is a comparative composition according
to the prior art:
Component: |
Wt % |
Propylene glycol |
4.75 |
sodium citrate |
2.8 |
Borax |
2.3 |
NaOH (50%) |
0.43 |
Monoethanolamine |
0.23 |
LAS-acid |
6.0 |
Coconut fatty acid |
0.77 |
Sodium alcohol EO sulphate |
10.5 |
Nonionic surfactant |
6.6 |
1-Decanol |
6.0 |
Protease enzyme |
0.45 |
Lipase enzyme |
0.25 |
Perfume |
0.2 |
Water |
balance to 100 |
|
wherein:
Borax : Sodium tetraborate (10aq)
nonionic surfactant: ethoxylated alcohol with on average 9 ethylene oxide groups
[0109] Sodium alcohol EO sulphate: ethoxylated alcohol sulphate with on average 3 ethylene
oxide groups.
[0110] Composition B was is a stable, transparent, pourable shear thinning liquid, capable
of stable suspending typical detergent particles having a density of between 0.8 and
0.9 g/cm3 and a diameter of up to 5000 microns, for more than 2 weeks without any
observable net movement of the particles.
[0111] Critical rheological parameters for the two compositions are shown below.
Sample |
Viscosity / Pa.s |
Eta 0 |
Critical Stress |
Tan Delta |
|
20s-1 100s-1 |
Pa.s |
Pa |
at 1 Hz |
B |
1.33 0.48 |
9.85E+05 |
10 |
0.07 |
[0112] For clarification of the rheological values shown in this table, reference is made
to the description concerning the similar table shown in above example A.
[0113] 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.