Note: Descriptions are shown in the official language in which they were submitted.
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2005022
Enzyme-Containing DeleL~ t Compositions and their Use
This invention relates to delel~ent compositions, and to their use,
and in particular to compositions containing lipase and to their use.
Prior Art:
DeleLgent compositions comprising lipase are known. For example
GB 1372 034 (Unilever) discloses lipase from Pseudomonas in specific
nonionic-containing deler~,ent compositions for soaking fabrics.
USP 3 950 277 (Procter & Gamble) also describes fabric-soaking
compositions: the described compositions comprise lipase and lipase
activators and a number of lipases from microorganism and other sources
are mentioned: those particularly mentioned as prere,led are ~Amano CE,
~Arnano M-AP, ~Takeda 1969-4-9, and *Meito MY-30 lipases, but no
indications are given of the form in which the lipase is to be prepared or
used.
~ denotes trade mark T
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USP 4 011 169/NL 74 08763 (Procter & Gamble)
describes the use of a similar range of enzymes in the
preparation of additives for washing agents (detergent
compositions).
s
Examples of known lipase-containing detergent
compositions are provided by EP 0 20S 208 and 0 206 390
(Unilever), which relate to lipases related to those from
Ps. fluorescens, P gladioli and Chromobacter in detergent
compositions.
EP 0 214 761 (Novo) and EP 0 258 068 (Novo), each
give detailed description of lipases from certain
microorganisms, and also give certain uses in detergent
additives and detergent compositions for the enzymes
described. EP 0 214 761 gives detailed description of
lipases derived from organisms of the species Pseudomonas
cepacia, and certain uses therefor. EP 0 258 068 gives
detailed description of lipases derived from organisms of
the genus Thermomyces/Humicola, and certain uses
therefor.
Also believed to be in use in certain areas is a
lipase-containing granular detergent composition
containing about 37% detergent actives including 5%
nonionic detergent and the remainder substantially
anionic detergent, about 16% zeolite, about 60 LU/g
lipase, plus protease and other normal detergent
additives.
Further examples of known lipase-containing
detergent compositions are provided by JA 63-078000
(1988) (Lion Corp/K Mukoyama et al) which discloses
properties and uses of a Pseudomonas lipase, including
use in a lipase-containing system based on 10-40 %
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surfactant (e.g. sodium C12-Cl8, e.g. C14 to C18 alpha-
olefin sulphonate), as well as other conventional detergent
ingredients.
The prior art also includes EP 0 268 456 *(Clorox),
which shows in connection with Table 10(b) an experimental
washing solution cont~ining lipase and about 1 micrgram/ml
sodium dodecyl sulphate.
Also in the prior art is Research Disclosure 29056 of
June 1988 which discloses lipase in connection with the
detergents of EP 0 179 533 (Procter & Gamble).
The Present Invention:
One difficulty with prior detergent-formulations
containing lipase is that there is a strong tendency for
many detergent-active materials to inhibit the action of
the lipase.
It is an aim of the present invention to provide
detergent formulations in which the activity of added
lipase is relatively less inhibited.
According to the present invention there is provided
an enzyme-cont~ ing detergent composition for washing
fabrics, comprising:
~3~ *denotes tr~de mark
~ 4 ~ 2 005022
1) 1 to 60% by weight of a surfactant system
S consisting of
(a) at least 50% by weight of a primary alcohol
sulphate having a chain length in the range
of C12 to C~8; and
(b) 0 to 50% by weight of a surfactant selected
from the group consisting of anionic
surfactants other than primary alcohol
sulphates, nonionic surfactants, cationic
surfactants and mixtures thereof; and
2) lipase enzyme in an amount in the range 50 to
30,000 (LU) lipase units per gram of the surfactant system
or of the detergent composition, together with conventional
detergent adjuncts.
In this specification lipase units are defined as they
are in EP 0 258 068 (Novo).
In most practical embodiments, the ingredients of the
detergent compositions also include e.g. conventional
detergent ad~uncts such as one or more of those mentioned
below.
It has been found that, in the composition of the
invention, lipase enzyme shows surprisingly little
inhibition. One reason for surprise at good performance of
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lipase in this system is that at least one member of the
cla~s of primary alcohol sulphates, i.e. sodium dodecyl
sulphate, i~ well-known and used in laboratory
investigations as a denaturant for proteins including
enzymes. By comparison with a lipase-cont~i n ing surfactant
based on alpha-olefin sulphonate, the compositions of the
present invention show stronger detergent action combined
with ade~uately low levels of lipase inhibition.
It is also surprising that the (known) building effect
of primary alcohol sulphate and it~ high calcium affinity by
comparison with the highly inhibitory LAS surfactants does
not lead to greater degrees of lipa3e ~ ~, _
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The primary alcohol sulphates used in these
compositions can for example be based on coco-primary
alcohol sulphates or tallow-primary alcohol slllrh~tes or
mixtures of these with each other and/or analogues having
alkyl chAinc derived from other sources.
Also permissible in the compositions are quantities
of other surfactant types, especially anionic, nonionic
or cationic detergents, in small or minor amounts e.g. up
to 10%, possibly up to 20% or up to 35%, sometimes up to
50%, of the surfactant system, e.g. linear alkyl-benzene
sulphonates (LAS) or (branched-chain) alkylbenzene
sulphonates (ABS), which alone have been found to show
unacceptably high degrees of inhibition of lipase.
In certain examples of the compositions of the
invention, especially for example those illustrated in
Example 11-13 below, the alkylbenzene sulphonates (LAS or
ABS) may be present at up to about 66%, or in some cases
up to about 70% or even 75%, of the surfactant system
including the primary alcohol sulphate.
For example, certain of the formulations may
comprise a surfactant system consisting essentially of a
mixture of PAS with ABS and/or LAS. Here the proportion
of ABS or LAS in such mixture may be for example up to
about 75%, e.g. up to about 70%, often somewhat lower as
for example about 66% or 60%, by weight.
A preferred surfactant system for use in this
invention is based on a mixture (e.g. about 1:1 w/w) of
C12-C14 coco-alkyl and C16-C18 tallow-alkyl sulphates.
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The lipolytic enzyme can usefully be added in the
form of a granular composition of lipolytic enzyme with
carrier material.
The added amount of lipolytic enzyme can be chosen
within wide limits, for example 50 to 30,000 LU/g of
granular detergent composition, e.g. often at least 100
LU/g, very usefully at least 500 LU/g, sometimes
preferably above 1000, above 2000 LU/g or above 4000 LU/g
or more, thus very often within the range 50-4000 LU/g
and possibly within the range 200-1000 LU/g.
The lipolytic enzyme can be chosen from among a wide
range of lipases: in particular the lipases described in
for example the following patent specifications, EP O
214 761 (Novo), EP 0 258 068 (Novo) and especially
lipases showing immunological cross-reactivity with
antisera raised against lipase from Thermomyces
lanuginosus ATCC 22070, EP 0 205 208 (Unilever) and EP 0
206 390 (Unilever), and especially lipases showing
immunological cross-reactivity with antisera raised
against lipase from Chromobacter viscosum var lipolyticum
NRRL B-3673, or against lipase from Alcaligenes PL-679,
ATCC 31371 and FERM-P 3783, also the lipases described in
specifications WO 87/00859 (Gist-Brocades) and EP 0 204
284 (Sapporo Breweries). Suitable in particular are for
example the following commercially available lipase
preparations: Novo Lipolase, Amano Iipases CE, P, B, AP,
M-AP, AML, and CES, and Meito lipases MY-30, OF, and PL,
also esterase MM, Lipozym, SP225, SP285, Saiken lipase,
Enzeco lipase, Toyo Jozo lipase and Diosynth lipase
(Trade Marks).
Genetic engineering of the enzymes can be achieved
by extraction of an appropriate lipase gene, e.g. the
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gene for lipase from Thermomyces lanuginosus or from a
mutant thereof, and introduction and expression of the
gene or derivative thereof in a suitable producer
organism such as an Aspergillus. The t~chniques described
in WO 88/02775 (Novo), EP 0 243 338 (Labofina) and EP 0
268 452 (Genencor) may be applied and adapted.
A preferred non-limitative example of a granular or
powder-form detergent composition according to the
present invention comprises:
Primary alkyl sulphate 9
(50:50 coco/tallow alkyl sulphates)
Sodium sulphate 34.4%
Sodium carbonate 6.7%
Sodium chloride 3.4%
Sodium C-Silicate 6.5%
Zeolite A (anhydrous) 30.2%
Sokolan CP5 (TM) 4.5%
Synperonic A4 (TM) 4%
(polyethoxylated alcohol c. C12-E4)
Lipase (Lipolase 30T granulate, Novo) 1
or lipase from Pseudomonas gladioli.
The detergent compositions may furthermore include
the following usual detergent ingredients in the usual
amounts. They may be built or unbuilt, and may be of the
zero-P type (i.e. not contA;n;ng any
phosphorus-containing builders). Thus the composition
may contain from 1-4S%, e.g. 5-30~ by weight of one or
more organic and/or inorganic builders. Typical examples
of such builders include alkali metal ortho, pyro, and
tripolyphosphates, alkali metal carbonates, either alone
2005022
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or in admixture with calcite, alkali metal citrates,
alkali metal nitrilotriacetates,
carboxymethyloxysuccinates, zeolites,
polyacetalcarboxylates and so on. Furthermore, they may
contain from 1-35% of a bleaching agent or a bleach
precursor or a system comprising bleaching agent and/or
precursor with activator therefor. Further optional
ingredients are lather boosters, foam depressors,
anticorrosion agents, soil-suspending agents,
sequestering agents, anti-soil redeposition agents,
perfumes, dyes, stabilising agents for the enzymes and so
on. The enzymes other than lipase that may be present
include protease, amylase, oxidase and cellulase.
The compositions may be formulated in any desired
way, e.g. as powders, bars, pastes, liquids.
The compositions can be used for the washing of
textile materials, especially but without limitation
cotton and polyester-based textiles and mixtures thereof.
Especially suitable are for example washing proc~sses
carried out at temperatures of about 60-65 deg C or
lower, e.g. about 30-35 deg C or lower.
The invention is further illustrated
non-limitatively by the following examples, which also
show the performance estimated in terms of reflectance at
460nm of test cloths soiled with lipid and then washed,
after 5 washes with a number of different
lipase-containing detergent formulations.
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Examples 1-5
In each example, a detergent formulation was used to
wash cotton test cloths soiled with a fatty mix based on
olive oil (up to 10-15% by weight of the test cloths)
after three-times prewashing. The detergent formulations
used corresponded to the one given in detail above,
except for the use of various surfactant systems (each in
10 an amount of 9% by weight) as follows:
Ex 1 Coco-alkyl sulphate (Elfan 280 ex Akzo)
Ex 2 Tallow-alkyl sulphate
(Sulphopon T55 ex Henkel)
Ex 3 50:50 coco-alkyl/tallow-alkyl sulphates
Ex 4 25:25:50 coco-alkyl-tallow alkyl-DOB113
Ex 5 DOB113 (linear alkyl benzene sulphonate
alone for comparison)
In the above formulation, 'DOB113' refers to the
sulphonation product of Shell alkylbenzene DOB113 (TM).
Examples 6-10 correspond to Examples 1-5 except for
wash temperature.
In each example, isothermal washes were performed at
30 deg.C. or 60 deg.C. for 30 minutes with and without
lipase enzyme, with predissolved detergent compositions
used at 4 g/l. Cloth/Liquor ratios were uniformly 10:1
containing 50:50 soiled:unsoiled load.
In each experiment, one of two lipases was used:
Lipolase from Novo as specified above, or lipase from
Pseudomonas gladioli, used in the form of a
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conventionally purified culture preparation (600 LU/mg)
at equivalent lipase activity to that of the Lipolase.
Results are quoted as average reflectances at 460nm
of S test pieces after 5 soil/wash cycles.
Examples 1-5 were carried out at 60 deg C, Examples
6-10 were carried out at 30 deg C.
Reflectances (% at 460nm):
Control (no lipase) Experiments
(Lipolase) ('gladioli')
Ex 1 68 72 73.4
Ex 2 68.3 73.8 73.9
Ex 3 69.6 72.8 73.5
Ex 4 68.7 74.0 74.2
Ex 5 71.8 71.9 72.8
Ex 6 69 72.3 73.7
Ex 7 69.2 72.1 73.6
Ex 8 70.6 70.9 73.3
Ex 9 69.6 71.9 73.4
Ex 10 70.5 71.2 73.2
The results generally show an incremental benefit
due to lipolytic activity. The general trend is to show
that lipase in the presence of LAS-type detergent gives
substantially less benefit (ex 5,10) than on average in
the other examples (primary alcohol sulphates and their
mixtures), which are accordingly preferred for use.
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Examples 11 to 13
The following detergent bar formulations support well the
liplytic action of lipase.
Primary alcohol sulphate (PAS) 28 15.5 12
(e.g. EMAL 10, ex Kao Corp, av. chain length C10)
Alkyl-benzene sulphonate (ABS)
-- 15.5 18
(e.g. from Escane F ex Exxon, av. chain length C11)
Sodium pyrophosphate 16 10 10
Soda ash 10 18 18
Calcite 32 31 31
Aluminosilicate 2 2 2
Lipolase
Minors and Water to 100% in each case.
The formulations are compounded in per-se conventional
manner for detergent bars.
The present invention is susceptible of
modifications and variations, and the present disclosure
extends to the use of all combinations and
subcombinations of the features described herein,
optionally in combination with each of the features of
the above-cited published patent specifications.
Y
