ES2593728T3 - Externally structured aqueous liquid detergent - Google Patents

Abstract

A structured aqueous liquid detergent composition comprising: at least 10% by weight of water, at least 0.5% by weight of surfactant, at least 0.0001% by weight of enzyme selected from lipase, cellulase and mixtures thereof, an external structurant, characterized in that the external structurant comprises at least 0.15% by weight, preferably at least 0.2% by weight of the liquid, citric fiber detergent composition that has been mechanically pulped and swollen in water.

Description

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structuring, maximizing breakage and contact with anhydrous structuring material. The premix can be left hydrating further (aging) after mixing with high shear.

The concentration of pulped citrus fiber in the premix depends on the ability of the equipment to handle the highest viscosity due to higher concentrations. Preferably, the minimum will be at least 1% by weight for practical reasons.

The process gives a stable detergent product with sufficient critical stress, 0.3 Pa, to suspend solid material and suspend itself giving a minimal separation of a transparent layer at the top.

Surfactant

In principle, the pulped citrus fiber structuring will structure any type of detergent liquid containing surfactant. However, for cleaning purposes, preferred surfactants assist in removing dirt from textile materials or hard surfaces, and help keep dirt removed in solution or suspension in water. Therefore, anionic and / or non-ionic surfactants are preferred, more preferably provided in a calcium tolerant mixture.

The linear alkylbenzene sulphonate (LAS) used alone is generally calcium intolerant. When required, in order to ensure calcium tolerance, surfactant systems should generally be avoided having LAS levels of approximately 90% by weight. Non-ionic surfactant-free systems with 95% by weight of LAS can be prepared if some zwitterionic surfactant, such as sulfobetaine, is present. Generally, it is preferred to use less than 90% by weight of LAS and at least 10% by weight of non-ionic surfactant. However, an advantage of using citrus fiber pulped above HCO is that it is not necessary to have high levels of non-ionic surfactant in the composition. HCO is frequently added to the mixture from a solution in non-ionic surfactant, and therefore, this is limiting for the composition. It is desirable to include only low levels of non-ionic surfactant, or even remove this component from detergent compositions intended for highly foaming applications. Thus, these compositions structured with pulped citrus fiber advantageously comprise at most 2% by weight, preferably at most 1% by weight, and most preferably zero, non-ionic surfactant.

Preferred alkyl ether sulfates are C8-C15 alkyl and have 1-10 moles of ethoxylation. Preferred alkyl sulfates are alkylbenzene sulfonates, particularly linear alkylbenzene sulphonates having an alkyl chain length of C8-C15. The counterion for anionic surfactants is generally an alkali metal, typically sodium, although other counterions such as MEA, TEA or ammonium can be used. Suitable anionic surfactant materials are available as the "Genapol" ™ range from Clariant.

Nonionic surfactants include ethoxylated primary and secondary alcohols, especially ethoxylated C8-C20 aliphatic alcohols with an average of 1 to 20 moles of ethylene oxide per mole of alcohol, and more especially the primary and secondary aliphatic C10-C15 aliphatic alcohols with a average of 1 to 10 moles of ethylene oxide per mole of alcohol. Non-ethoxylated nonionic surfactants include alkyl polyglycosides, glycerol monoethers and polyhydroxyamides (glucamide). Mixtures of non-ionic surfactants can be used. When included therein, the composition contains from 0.2% by weight to 40% by weight, preferably 1% by weight to 20% by weight, more preferably 5 to 15% by weight of a non-ionic surfactant, such as ethoxylated alcohol, ethoxylated nonylphenol, alkyl polyglycoside, alkyldimethylamine oxide, ethoxylated fatty acid monoethanolamide, fatty acid monoethanolamide, fatty acid polyhydroxyalkylamide, or N-acyl N-alkyl derivatives of glucosamine ("glucamides").

Preferred non-ionic surfactants that can be used include ethoxylated primary and secondary alcohols, especially ethoxylated C8-C20 aliphatic alcohols with an average of 1 to 35 moles of ethylene oxide per mole of alcohol, and more especially, C10- aliphatic alcohols. C15 ethoxylated primary and secondary with an average of 1 to 10 moles of ethylene oxide per mole of alcohol.

The calcium tolerance test used herein is the one defined in EP1771543. A mixture of surfactants is prepared at a concentration of 0.7 g / l in water containing enough calcium ions to give a French hardness of 40 degrees. Other electrolytes such as sodium chloride, sodium sulfate, sodium hydroxide are added as necessary to adjust the ionic strength to 0.5 M and the pH to 10. Light wavelength absorption 540 nm through 4 mm of sample is measured 15 minutes after sample preparation. Ten measurements are made and an average value is calculated. Samples that give an absorption value of less than 0.08 are considered calcium tolerant.

Water

The compositions are aqueous, that is, water forms the bulk of the solvent system. Hydrotropics such as propylene glycol and glycerol / glycerin may be used, but they will be present in an amount less than water. The minimum level of water for an aqueous liquid is 10% by weight. To incorporate 0.15% pulped citrus fiber with a water absorption capacity of 20 times its own weight, it is normal to add a minimum of 3%

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i. it comprises a negatively charged amino acid at position E210 of said wild type lipase;

ii. it comprises a negatively charged amino acid in the region corresponding to positions 90-101 of said wild type lipase; Y

iii. comprises a neutral or negatively charged amino acid at a position corresponding to N94 of said wild type lipase; I

iv. it has a negative charge or neutral charge in the region corresponding to positions 90-101 of said wild type lipase; Y

(IV) mixture thereof.

These are available under the Novozymes Lipex ™ brand. A similar Novozymes enzyme, but believed to fall outside the definition above, is available from Novozymes under the name of Lipoclean ™ and this is also preferred.

Cellulase:

Suitable cellulases include those of bacterial or fungal origin. Mutants modified by genetically engineered or chemically modified proteins are included. Suitable cellulases include cellulases of the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, for example fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila and Fusarium oxysporum, disclosed in US patents 4.4 in US patents .307, US 5,648,263, US 5,691,178 and US

5,776,757 and WO 89/09259, WO 96/029397 and WO 98/012307. Commercially available cellulases include Celluzyme ™, Carezyme ™, Endolase ™, Renozyme ™ (Novozymes A / S), Clazinase ™ and Puradax HA ™ (Genencor International Inc.) and KAC-500 (B) ™ (Kao Corporation).

Phospholipase:

Phospholipase can be classified as EC 3.1.1.4 and / or EC 3.1.1.32. As used herein, the term phospholipase is an enzyme that has activity towards phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an external position (sn-1) and that of the medium (sn-2) and esterified with phosphoric acid in the third position; in turn, phosphoric acid can be esterified to an amino alcohol. Phospholipases are enzymes that participate in the hydrolysis of phospholipids. Various types of phospholipase activity can be distinguished, including phospholipases A1 and A2 that hydrolyse a fatty acyl group (in the sn-1 and sn-2 position, respectively) to form a lysophospholipid; and lysophospholipase (or phospholipase B) that can hydrolyze the remaining fatty acyl group in the lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterase) release diacylglycerol or phosphatidic acid, respectively.

Protease:

Suitable proteases include those of animal, plant or microbial origin. The microbial origin is preferred. Mutants modified by genetically engineered or chemically modified proteins are included. The protease may be a serine protease or a metalloase protease, preferably an alkaline microbial protease or a trypsin-like protease. 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.).

Cutinase:

Cutinase is classified in EC 3.1.1.74. The cutinase can be of any origin. Preferably, the cutinases are of microbial origin, in particular of bacterial, fungal or yeast origin.

Amylase:

Suitable amylases (alpha and / or beta) include those of bacterial or fungal origin. Mutants modified by genetically engineered or chemically modified proteins are included. Amylases include, for example, alpha-amylases obtained from Bacillus, for example a special strain of B. licheniformis described in greater detail in British document GB 1,296,839, or Bacillus sp. disclosed in WO 95/026397 or WO 00/060060. Commercially available amylases are Duramyl ™, Termamyl ™, Termamyl Ultra ™, Natalase ™, Stainzyme ™, Fungamyl ™ and BAN ™ (Novozymes A / S), Rapidase ™ and Purastar ™ (from Genencor International Inc.).

Peroxidases / oxidases:

Suitable peroxidases / oxidases include those of plant, bacterial or fungal origin. Mutants modified by genetically engineered or chemically modified proteins are included. Examples of useful peroxidases include Coprinus peroxidases, for example of C. cinereus, and variants thereof such as those described in WO 93/24618, WO 95/10602 and WO 98/15257. Commercially available peroxidases include

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Guardzyme ™ and Novozym ™ 51004 (Novozymes A / S).

Pectato liasas:

Pectate liases (also called polygalacturonate liases). Examples of pectate liases include pectate liases that have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, and also 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 liases 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) has also been described. (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). Any of the above can be used, as well as pectate liases independent of divalent and / or thermostable cations. The pectate lyase preferably comprises the 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. Pectate lyases specifically contemplated are disclosed in WO 99/27083 and WO 99/27084. Other pectate lyases specifically contemplated (obtained from Bacillus licheniformis) are disclosed in US document no.

6,284,524. Variants of pectate liases disclosed specifically in WO 02/006442 are disclosed, especially the variants disclosed in Examples of WO 02/006442.

Examples of commercially available alkaline pectate liases include BIOPREP ™ and SCOURZYME ™ L from Novozymes A / S, Denmark.

Mananasas:

Examples of mananasas (EC 3.2.1.78) include mananasas of bacterial and fungal origin. Mannanase can be obtained from a strain of filamentous fungi of the genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus (WO 94/25576). WO 93/24622 discloses an isolated mannanase from Trichoderma reseei. Mananases 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 obtained from Bacillus stearothermophilus. Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551555 (1994) describe a beta-mannanase obtained from Bacillus subtilis. JP-A-03047076 discloses a beta-mannanase obtained from Bacillus sp. JP-A-63056289 describes the production of an alkaline thermostable beta-mannanase. JP-A-63036775 refers to the Bacillus FERM P-8856 microorganism that produces beta-mannanase and beta-mannosidase. JP-A-08051975 discloses alkaline betamananases of Bacillus sp. AM-001 alkalophilic. A purified mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/11164. WO 91/18974 describes a hemicellulase such as an active glucanase, xylanase or mannanase. Alkaline mananasas of families 5 and 26 obtained from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp. and Humicola insolens, disclosed in WO 99/64619. Especially contemplated are the mananasas of Bacillus sp. used in Examples of WO 99/64619.

Examples of commercially available mananasas include Mannaway ™ available from Novozymes A / S Denmark.

Any enzyme present in the composition can be stabilized using conventional stabilizing agents, for example a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid or a boric acid derivative, for example an aromatic borate ester, or a derivative of phenyl boronic acid such as 4-formylphenyl boronic acid, and the composition can be formulated as described for example in WO 92/19709 and WO 92/19708.

Polymers

Despite being optional, it is desirable to include soluble polymers in the compositions of the invention. A preferred polymer is modified PEI 600 polyethyleneimine (20EO). Dirt-releasing polymers, especially polyester dirt-releasing polymers, can also be used. The amount of the polymers, when used, is preferably more than 2% by weight, more preferably more than 5% by weight, even more than 10% by weight. Anti-redeposition polymers such as sodium carboxymethyl cellulose can be used additionally.

Kidnappers

Despite being optional, it is desirable to include water soluble sequestrants in the compositions of the invention. Phosphonate sequestrants are preferred. When included, they are advantageously used at levels of 0.3 to 3% by weight.

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Dequest® 2010 is HEDP (1-hydroxyethylidene-1,1-diphosphonic acid). Lipex® is Lipex 100L ex Novozymes. Carezyme® is a former Novozymes cellulase. Endolase® is an endocellulase promoted for its ex-Novozymes bleaching benefits. Stainzyme 12L is an amylase formulated for ex-Novozymes liquids. Mannaway is a mannaasa ex Novozymes. EPEI is PEI 600 20EO ethoxylated polyethyleneimine cleaning polymer ex BASF. SRP is Texcare SRN170 ex Clariant polyester dirt release polymer. Acusol® 190 is polymeric calcium dispersant of water-soluble polycarboxylate ex Dow. Dowanol DPnB is dipropylene glycol n-butyl ether ex Dow.

Comparative Example A

The powdered citrus fiber was added directly to the prepared detergent liquid, and an attempt was made to disperse it using a Silverson high shear mixer. No structure formed. The particles of the added powder material did not swell and simply sank to the bottom of the liquid when the shear was removed.

Example 1

Premixtures of 1 to 2.5% by weight of water-pulped citrus fiber were prepared using high intensity mixing. The researchers used a Silverson mixer located in a recycling circuit around a container for batch production. The premixes formed were all homogeneous.

Example 2

As an alternative to Example 1, the researchers used a high pressure homogenizer to deliver the shear. As in Example 1, a well dispersed and homogeneous structured premix was obtained. The maximum premix concentration is limited by the maximum viscosity that the equipment is capable of handling.

Example 3

The pulped citrus fiber premix prepared in Example 1 or Example 2 (1 or 2% by weight was used) was added to a detergent liquid comprising 40% by weight of active detergent (LAS, SLES, NI 1: 1: 2) and 15% by weight of the propylene glycol hydrotrope, the rest being water. Two addition orders were used successfully:

(3a) Free water, pulped citrus fiber premix and then a premixed surfactant concentrate (~ 60% AD), or (3b) Free water, surfactant concentrate and then pulped citrus fiber premix.

For both procedures, it was necessary to use a high intensity mixing stage (the researchers used a Silverson L4R mixer) for the combination of the three liquids. Successful structuring with as little as 0.15% of citrus fiber pulped in the final liquid detergent has been demonstrated. Researchers have found that avoiding aeration during processing is advantageous. If too much air is incorporated (especially with very low levels of the structurant), it has been shown that the structure is destabilized by small air bubbles that lead to the separation of a transparent layer at the bottom.

Example 4

Part A: Structuring Premix

A structuring premix was prepared using 2% citrus fiber Herbacel Plus AQ powder (type N), 97.9% tap water and 0.1% potassium sorbate preservative. The premix was prepared using a Gaulin high pressure homogenizer at pilot plant scale, operating at 350 bar. The resulting pulped citrus fiber (PCF) premix was easily manageable and pumpable.

Part B: Concentrated base detergent liquid

In a separate container from the structuring premix A, a concentrated base detergent liquid B with the composition shown in Table 1 (except for the 2% by weight PCF premix and perfume), was prepared using a pilot plant container of 50 liters capacity equipped with a mixing element with the geometry of the "Flexible Agitator System (FAS)". 12.5% of the water had been removed from the formulation to allow post-dosing of the 2% PCF premix: Part A. The concentrated mixture was allowed to deaerate for more than 1 hour.

Table 1: Composition of the structured liquid of Example 4 5

Material

Activity % in weigh

Water

100 9.67

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Material

Activity % in weigh

PPG

100 9.21

NaOH

47 5.87

TORCH

100 3.32

NI 7EO

100 20.59

Citric acid

fifty 2.01

LAS acid

97.1 13.71

Prifac 5908

100 4.89

SLES

70 9.79

Dequest 2066

32 1.60

PCF

2 12.80

Fragrance

100 1.42

TOTAL

100.00

Combination of the structuring premix A with the concentrated base detergent liquid B

The concentrated base detergent mixture B was circulated through a Silverson 150/250 high shear mill through a recycling circuit, to ensure that all pipes were fully primed and purged of air. Flow 1450 l / h (residence time of a single pass in the mill 0.1 seconds). The Silverson mill was operated at 6250 rpm (9063 w / kg) to simulate large-scale operating conditions. Next, the structuring premix A was introduced into the main recirculation circuit near the inlet mouth of the high shear mixer, to minimize interaction between currents before intimate dispersion. Then the perfume was added using mixed with low shear.

Then samples of the structured liquid with pulped citrus fiber were taken and its rheology was measured. Again, after 1 week of storage at room temperature, the rheology was measured and the samples were visually evaluated to see if there was separation of an upper transparent layer or separation of a transparent layer at the bottom.

The rheology required for thickening and suspension function was achieved and maintained, and no separation was observed.

Example 5 - Variation in the amount of structuring

Example 4 was repeated but the amount of PCF in premix A was varied, so that when added to the concentrated base detergent mixture B, the final level of PCF in the detergent liquid was only 0.12%. The rheology of this liquid was not enough for the suspension function. See Figure 1, which shows that with 0.12% PCF there was insufficient formulation stability and viscosity accumulation (low yield strength). It is thought that this was due to an insufficient amount of PCF being present to establish a stable network with which to provide the suspension function. Then, the procedure was repeated to form a liquid with 0.16% by weight of the external PCF structurant. After storage for a week, this liquid showed signs of separation from a top transparent layer. This was on the verge of acceptable. It is possible that a different procedure or a different composition for the detergent liquid in Part B could have generated structure even at this low level, but this should be considered as a less preferred level for inclusion of the structurant and indicates a lower end of the range of 0.15%. Finally, the PCF structuring level was increased to 0.32%. Researchers have found that combining the level and obtaining an elastic limit (through the processing conditions and the other ingredients present) is significant for effective structuring.

Lipase could be added to the liquids of Example 4 and Example 5 structured with PCF, without loss of structure.

Example 6 and Comparative Example B-Structuring Lipase Resistance

The base composition of the liquid used for Example 6 and Comparative Example B is given in Table 2.

Table 2 - Liquid composition of Example 6 and Comparative Example B

Material

Activity % in weigh

Glycerin

100 5.00

MPG

100 18.00

NI 7EO

100 12.7

LAS acid

97.1 8.5

Prifac 5908

100 3.0

SLES

70 4.2

Fragrance

100 2.4

PCF *

2 0.25

NaOH

47 Up to pH 7

Water

100 Up to 97%

TOTAL

97.00

* Comparative Example B, which represents the prior art, was structured with 0.25% by weight of HCO, crystallized from a hot melt, instead of the PCF in Table 2.

The 3% "gap" was filled with either Lipex® 100L or 30 parts of sorbitol / 64 parts of demineralized water, that is, the solvent / stabilizer for commercial Lipex samples.

5 The rheology was measured at 25 ° C using an Anton Paar ASC rheometer.

Figure 2 shows the rheology data after 24 hours. Comparative Example B shows that when Lipex is used in a liquid structured with HCO, there is a complete loss of structuring within 24 hours at room temperature. In contrast, Lipex has no effect on the PCF structured liquid, which is otherwise identical, as in Example 6.

10 Example 7 and Comparative Example C-Structuring cellulase resistance

Cellulase was not tested with HCO, since cellulase was not expected to have any effect on such an oily material. For Example 7, two types of cellulase were added to a detergent liquid structured with 0.25% PCF, as described in Example 4.

Figure 3 shows the effect of the addition of each type of 1% cellulase. It can be seen that both for Carezyme

15 As for Endolase, there is no significant effect on the rheology after 2 weeks of storage at 37 ° C. Figure 4 shows the corresponding result for Comparative Example C, which is a structured detergent liquid dispersing a premix of 0.1% by weight of MFC, using a procedure analogous to Example 4 above. It can be seen that for the addition of cellulase (1% Carezyme) at 37 ° C, there is an initial drop in the viscosity of the plateau, which can be caused because the cellulase attacks part of the structurant, but does not

20 fail as catastrophically as the HCO formulated with lipase. It is clear that this causes a reduction in the range between resting viscosity (without shear) and pouring viscosity (high shear); this interval is already lower than that obtained with Example 6 structured with PCF.

Examples 8 to 26 - Other examples of PCF structured detergent liquids

Table 3 shows a range of high-power laundry detergent liquids that can

25 structured with pulped citrus fiber. Examples 8, 9, 10 and 11 are liquids for the laundry of so-called 3-fold concentrates, suitable for use at a dose of approximately 35 ml in a standard European front-loading automatic washing machine. Examples 12, 13 and 14 are compositions suitable for use at a dose of 20 ml in the same type of machine.

Table 3

Formulation

Example 8 Example 9 Example 10 Example 11 Example 12 Example 13 Example 14

Material

% as 100% % as 100% % as 100% % as 100% % as 100% % as 100% % as 100%

LAS acid

16.00 4.85 13.40 8.75 8.49 8.49 8.49

SLES

6.00 2.42 6.70 6.82 4.24 4.24 4.24

NI 7EO

2.00 7.28 20.12 4.58 12.74 12.74 12.74

Prifac 5098

0.85 4.78 3.00 1.50 1.50 3.03

They take BB

0.86 1.50 1.50 1.50

EPEI

3.10 3.00 5.50 5.50 5.50

SRP

2.10 3.75 3.75

NaOH

1.61 0.07 2.70 0.07 0.07

MEA

7.00

TORCH

2.75 2.00 3.23 2.50 3.50 3.50 11.00

Citric acid solution

0.98 3.90 1.71

MPG

15.00 9.00 11.00 20.00 20.00 20.00

Glycerol

5.00 5.00

Heptasodium DTPMP

0.50 0.88

Dequest 2010

1.50 2.62

Opacifying

0.10

Fluorescent agent

0.20 0.10 0.10 0.10 0.10 0.18

Protease

1.00 1.00 1.75 1.75 2.36

Stainzyme 12L

0.40 0.400 0.700 0.700 0.945

Carezyme 1000L

0.95

Lipex or Lipoclean 100L

2.00 2.00 2.00 2.00 3.00 3.00 3.00

Mannaway

0.40 0.40 0.70 0.70 0.35

PCF

0.25 0.25 0.25 0.25 0.25 0.25 0.25

Preservative

0.02 0.16 0.01 0.01 0.01 0.01 0.01

Fragrance

1.39 1.39 1.39 2.43 2.43 2.43

Water and impurities

69.17 57.67 27.94 37.4 29.77 27.15 20,435

TOTAL

100 100 100 100 100 100 100

Table 4 shows the rheology obtained by variants of Examples 12 and 14. Examples of composition 15 to 18 were tested as described above to obtain the rheology profiles shown in Figure 5; without

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have still added the enzyme. Based on the findings for the lack of lipase effect on similar compositions, the addition of lipase would not affect the rheology. Lipase and cellulase can be added without affecting the stability of the rheological profile over time. These examples show that rheology is profitably obtained with the inclusion of various levels of cleaning and dirt-releasing polymers, and also the addition of high levels of polymer and the addition of relatively high levels of sequestrant. All these ingredients could have had a detrimental effect on the rheology.

Table 4

Example 15

Example 16 Example 17 Example 18

Glycerin

4.27 4.27 4.10 4.98

MPG

15.38 15.38 14.76 17.94

NI 7EO

10.85 10.85 10.41 12.66

LAS acid

7.26 7.26 6.97 8.47

Prifac 5908

2.56 2.56 2.46 2.99

SLES

3.59 3.59 3.44 4.19

PCF

0.21 0.21 0.20 0.25

EPEI

0 5.5 5.5 0

They take BB

0 1.5 1.5 0

SRP

0 3.68 3.68 0

Dequest 2010

0 0 2 2

Lipase *

3.00 3.00 3.00 3.00

Water

balance balance balance balance

* A 3% gap was left in the base to make room for the enzyme lipase.

Table 5 - Household cleaners

Ingredients (% by weight)

Example 19 Kitchen cleaner Example 20 Bathroom cleaner

Water

89.86 90.29

91-8

5 3.5

Acusol 190 (24.8% active ag.)

0.5 0.5

Citric acid pH 4

one 4

MEA

one -

Fragrance

0.3 0.29

Dowanol DPnB

one -

Preservative

0.016 0.016

Prifac 7907

0.18

DB310 silicone (36.2% active ag)

0.001 -

Sodium hydroxide

0.893 1,154

PCF

0.25 0.25

Table 6 - Dishwashing liquids

Example (% by weight)

twenty-one 22 2. 3 24 25 26

THE

10.50 11.81 19.65 11.55 0.00 2.54

SLES 1EO

3.06 3.45 0.00 2.19 8.75 0.00

LES Nat

0.00 0.00 3.50 0.00 0.00 3.24

PAS

0.44 0.49 0.00 0.00 0.00 0.00

CAPB

0.00 0.00 0.00 0.70 2.89 0.96

MgSO4 7 H2O

0.61 0.66 0.00 0.00 0.20 0.00

NaCl

0.00 0.00 0.00 0.00 0.00 0.96

Urea

0.00 0.00 4.38 2.63 0.00 0.00

Ethanol

10.50 11.81 19.65 11.55 0.00 2.54

PCF

0.25 0.25 0.25 0.25 0.25 0.25

Preservative

0.015 0.015 0.015 0.015 0.015 0.015

Water

up to 100 up to 100 up to 100 up to 100 up to 100 up to 100

When not yet present, all liquids of Examples 19 to 26 can simply be reformulated to contain Lipase and / or cellulase at levels of 0.0001 to 5% by weight, preferably 0.001 to 0.3% by weight. The structuring rheology is not affected by the inclusion of these enzymes.

Claims (1)

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