Note: Descriptions are shown in the official language in which they were submitted.
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PROCESS FOR REMOVAL OF EXCESS DISPERSE DYE FROM PRINTED OR
DYED TEXTILE MATERIAL
FIELD OF THE INVENTION
The present invention relates to a method for removing excess disperse dye
from dyed or printed textile material.
BACKGROUND OF THE INVENTION
Dyeing of textiles with disperse dyes is carried out by applying the dyes to
the
textile by any appropriate method for binding the dyestuff to the fibres of
the textiles.
Disperse dyes are nonionic and have very limited solubility in water. The need
for a
post-dyeing clearing treatment (removal of excess dye) in disperse dyeing
relates to
the tendency of disperse dyes to aggregate and deposit at the surface of the
fibre. If
not removed, this surface contamination can undermine the brightness of the
shade
~5 as well as the wash, sublimation and crockfastness results. The
conventional treat-
went is a harsh reduction clearing, where the dyed fibre is treated in a
strong alkaline
reducing bath, usually made up of sodium hydrosulfite and caustic soda. An-
thraquinone-based dyes are not fully destroyed by such a treatment, and such
insuf-
ficient clearing often leads to particular poor wash fastness properties.
2o WO 92/18687 discloses a method of bleaching excess dye from fabric by treat-
ing with a liquor containing a peroxidase or oxidase enzyme, an OZ or H202
source,
and optionally an oxidizable substrate.
WO 99/34054 discloses a method of bleaching excess dye from fabric or yarn
by treating with a liquor comprising a peroxidase or oxidase enzyme, an
oxidation
25 agent, and a N-OH mediator.
It is an object of the present invention to provide an efficient method for
post-
dyeing clearing of excess disperse dye from dyed textiles.
SUMMARY OF THE INVENTION
3o The present invention relates to a process for removal of excess disperse
dye
from printed or dyed textile material comprising treatment with a rinse liquor
compris-
ing:
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- at least one enzyme selected from the group consisting of enzymes exhibiting
per-
oxidase activity or laccase activity,
- an oxidation agent, and
- at least one mediator,
wherein the textile material is a fabric, yarn, fiber, garment or film which
comprise at
least 20% of a synthetic material.
Another aspect of the present invention is the use of the components specified
above for the preparation of a multi-component system for removal of excess
dis-
perse dye from dyed or printed textile material.
DETAILED DESCRIPTION OF THE INVENTION
The term "mediator" as used herein is intended to mean an oxidizable sub-
stance improving the enzymatic oxidative or bleaching effect. Mediators are
also re-
ferred to as enhancing agents.
Textile materials
The process of the invention is applicable to all types of textile materials -
such
as a fabric, yarn, fiber, garment or film - made from synthetic materials, and
blends
of natural and synthetic materials. Preferably blends of natural and synthetic
materi-
2o als comprise at least 20%, more preferably at least 40%, even more
preferably at
least 60%, most preferably at least 80%, and in particular at least 95% of a
synthetic
material. Typical examples of synthetic materials are modified cellulose (e.g.
acetate,
diacetate and triacetate), polyamide (e.g. nylon 6 and 6,6), polyester (e.g.
polyethylene terephthalate)), acrylic/polyacrylic, and polyurethane (e.g.
spandex).
Typical examples of natural materials are regenerated cellulosics (e.g.rayon),
solvent
spun cellulosics (e.g. lyocel and tencel), natural cellulosics (e.g. cotton,
flax, linen,
and ramie) and proteins (e.g. wool and silk). The term "synthetic" as used
herein is
intended to mean non-naturally occuring or man-made.
The process of the invention may be applied to dyed yarn, to knitted, woven or
3o non-woven fabric, or to garments made from dyed and/or printed fabric.
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The process of the invention is used for oxidative removal or bleaching of ex-
cess disperse dyes after any kind of disperse dyeing or printing. The process
is also
referred to as a clearing process. Oxidative removal includes modifying or
degrading
the excess disperse dye molecules; or changing the colour of the dye, such as
whit-
ening or fading (bleaching) the color of the dye.
Disperse dyes are characterised by being nonionic and have a very limited
solubility in water. Disperse dyes include azo, nitroarylamine, and
anthraquinone
based dyes. Examples of disperse dyes include Disperse Red 60, Disperse Yellow
3,
Disperse Blue 3, Disperse Blue 27, Disperse Blue 56, and Disperse Violet 1.
Enzyme
Enzymes exhibiting peroxidase activity or laccase activity are those, which by
using hydrogen peroxide or molecular oxygen respectively are capable of
oxidising a
variety of compounds, such as phenols and aromatic amines.
According to the invention the concentration of enzyme is 0.005 to 10 mg en
zyme protein per liter of rinse liquor, preferably, 0.02 to 5 mg enzyme
protein per liter
of rinse liquor, more preferably 0.05 to 2 mg enzyme protein per liter of
rinse liquor.
According to the liquor ratio, this may be translated to dosages of enzyme per
kg of
textile material, e.g. at a liquor ratio of 10:1, the most preferred enzyme
dosage is
2o from 0.5 to 20 mg enzyme per kg of textile material.
Peroxidase activity exhibiting enzymes
An enzyme exhibiting peroxidase activity may be any peroxidase comprised by
the enzyme classification (EC 1.11.1.7), or a haloperoxidase, such as a
chloride per-
oxidase (EC 1.11.1.10) or any fragment or synthetic or semisynthetic
derivatives
thereof exhibiting enzymatic activity (e.g. porphyrin ring systems or micro-
peroxidases, cf. e.g. US 4,077,768, EP 537 381, WO 91/05858 and WO 92/16634).
Such enzymes are known from microbial, plant and animal origins.
Preferably, the peroxidase employed in the method of the invention is produc-
3o ible by plants (e.g. horseradish or soybean peroxidase), in particular
soybean peroxi-
dase, or by microorganisms, such as fungi (including filamentous fungi and
yeasts)
or bacteria.
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Some preferred fungi include strains belonging to the subdivision Deuteromy-
cotina, class Hyphomycetes, e.g., Fusarium, Humicola, Tricoderma, Myrothecium,
Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia, Cladosporium
or
Dreschlera, in particular Fusarium oxysporum (DSM 2672), Humicola insolens,
Trichoderma resii, Myrothecium verrucana (1F0 6113), Verticillum alboatrum,
Verticil-
lum dahlie, Arthromyces ramosus (FERM P-7754), Caldariomyces fumago, Ulo-
cladium chartarum, Embellisia alli or Dreschlera halodes.
Other preferred fungi include strains belonging to the subdivision Basidiomy-
cotina, class Basidiomycetes, e.g. Coprinus, Phanerochaete, Coriolus or
Trametes,
~o in particular Coprinus cinereus f. microsporus (1F0 8371), Coprinus
macrorhizus,
Phanerochaete chrysosporium (e.g. NA-12) or Trametes (some classes previously
called Polyporus have been renamed to Tramefes), e.g., T. versicolor (e.g. PR4
28-A).
Further preferred fungi include strains belonging to the subdivision Zygomy-
~5 cotina, class Mycoraceae, e.g. Rhizopus or Mucor, in particular
Mucorhiemalis.
Some preferred bacteria include strains of the order Actinomycetales, e.g.,
Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus (1F0
12382) or Streptoverticillum verticillium ssp. verticillium.
Other preferred bacteria include Bacillus pumilus (ATCC 12905), Bacillus
2o stearothermophilus, Rhodobacter sphaeroides, Rhodomonas palustri,
Streptococcus
lactis, Pseudomonas purrocinia (ATCC 15958) or Pseudomonas fluorescens (NRRL
B-11 ).
Further preferred bacteria include strains belonging to Myxococcus, e.g., M.
virescens.
25 The peroxidase may furthermore be one which is producible by a method com-
prising cultivating a host cell transformed with a recombinant DNA vector
which car-
ries a DNA sequence encoding said peroxidase as well as DNA sequences encoding
functions permitting the expression of the DNA sequence encoding the
peroxidase,
in a culture medium under conditions permitting the expression of the
peroxidase,
3o and recovering the peroxidase from the culture.
Particularly, a recombinantly produced peroxida.se is a peroxidase derived
from
a Coprinus sp., in particular C. macrorhizus or C. cinereus according to WO
92/16634, or a variant thereof.
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In the context of this invention, peroxidase acting compounds comprise peroxi-
dase active fragments derived from cytochromes, hemoglobin or peroxidase en-
zymes, and synthetic or semisynthetic derivatives thereof, e.g. iron complexes
of por-
phyrin or phthalocyanine and derivatives thereof.
Laccase and laccase related enzymes
In the context of this invention, the term "enzymes exhibiting laccase
activity"
means laccases and laccase related enzymes, such as any laccase comprised by
the enzyme classification (EC 1.10.3.2), any catechol oxidase comprised by the
en-
~o zyme classification (EC 1.10.3.1), any bilirubin oxidase comprised by the
enzyme
classification (EC 1.3.3.5) or any monophenol monooxygenase comprised by the
en-
zyme classification (EC 1.14.18.1 ).
The laccases are known from microbial and plant origin. The microbial laccases
may be derived from bacteria or fungi (including filamentous fungi and yeasts)
and
~5 suitable examples include a laccase derivable from a strain of Aspergillus,
Neuro-
spora, e.g., N. crassa, Podospora, Botrytis, Collybia, Fomes, Lenfinus,
Pleurotus,
Trametes (Polyporus), e.g., T. villosa, T. versicolor and T. pinsitus,
Rhizoctonia, e.g.,
R. solani, Coprinus, e.g. C. plicatilis and C. cinereus, Psatyrella,
Myceliophthora, e.g.
M. thermophila, Schytalidium, Phlebia, e.g., P. radiata (WO 92/01046), or
Coriolus,
2o e.g., C. hirsulus (JP 2-238885), in particular a laccase derivable from a
strain of Fo-
mes, Trametes (Polyporus), Rhizoctonia, Coprinus, Myceliophthora, or
Schytalidium.
The laccase or the laccase related enzyme may furthermore be one which is
producible by a method comprising cultivating a host cell transformed with a
recom
binant DNA vector which carries a DNA sequence encoding said laccase as well
as
25 DNA sequences encoding functions permitting the expression of the DNA
sequence
encoding the laccase, in a culture medium under conditions permitting the
expres-
sion of the laccase, and recovering the laccase from the culture.
Oxidation aaent
3o If the oxidizing enzyme requires a source of hydrogen peroxide, the source
may
be hydrogen peroxide or a hydrogen peroxide precursor for in situ production
of hy-
drogen peroxide, e.g., a percarbonate or a perborate, a persulfate, such as a
tri-
oxo(peroxo)sulfate or a ~-peroxo-bis(trioxosulfate), a hydrogen peroxide-urea
addi-
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tion compound, a peroxycarboxylic acid or a salt thereof or a hydrogen
peroxide
generating enzyme system, e.g., an oxidase and a substrate for the oxidase,
e.g. an
amino acid oxidase and a suitable amino acid.
Hydrogen peroxide may be added at the beginning of or during the process,
e.g., in a concentration corresponding to 0.01-50 mM H202, preferably 0.1 to 5
mM.
If the oxidizing enzyme requires molecular oxygen, molecular oxygen from the
atmosphere will usually be present in sufficient quantity. Otherwise pure OZ
may be
led to the rinse liquor, or an OZ generating enzymatic system, e.g. a system
based on
hydrogen peroxide and a catalase, may be added.
Mediator
According to the invention the textile material is treated with a solution or
rinse
liquor comprising at least one mediator.
The mediators may be selected from the group consisting of aliphatic, cyclo-
aliphatic, heterocyclic or aromatic compounds containing the moiety >N-OH. In
a pre-
ferred embodiment of the invention the mediator is a compound of the general
for-
mula I:
R1
R2
X]
\ I NI
R3
H
R4
wherein R', R2, R3, R4 are individually selected from the group consisting of
hydro-
gen, halogen, hydroxy, formyl, carboxy and salts and esters thereof, amino,
vitro, C~_
~2-alkyl, C~_s-alkoxy, acyl, aryl, in particular phenyl, sulfo, aminosulfonyl,
carbamoyl,
phosphono, phosphonooxy, and salts and esters thereof, wherein the R', R2, R3,
R4
may be substituted with R5, wherein R5 represents hydrogen, halogen, hydroxy,
for
myl, carboxy and salts and esters thereof, amino, vitro, C~_~2-alkyl, C,_6-
alkoxy, acyl,
aryl, in particular phenyl, sulfo, aminosulfonyl, carbamoyl, phosphono, phos
phonooxy, and salts and esters thereof;
[X] represents a group selected from (-N=N-), (-N=CR6-)m, (-CR6=N-)m, (-
CR'=CR8-
)~,.,, (-CR6=N-NR7-), (-N=N-CHR6-), (-N=CR6-NR'-), (-N=CR6-CHR'-), (-CR6=N-
CHR'-
), (-CRs=CR'-NR8-), and (-CR6=CR'-CHRB-), wherein R6, R', and R8 independently
of
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each other are selected from H, OH, NH2, COOH, S03H, C~_6-alkyl, NOZ, CN, CI,
Br,
F, CHZOCH3, OCH3, and COOCH3; and m is 1 or 2.
In a more preferred embodiment of the invention the mediator is a compound of
the general formula II:
R1
R2 N
\\
N
\ /
R3 N
R4 ~H
wherein R', Rz, R3, R4 are individually selected from the group consisting of
hydro-
gen, halogen, hydroxy, formyl, carboxy and salts and esters thereof, amino,
vitro, C~_
~z-alkyl, C,_6-alkoxy, acyl, aryl, in particular phenyl, sulfo, aminosulfonyl,
carbamoyl,
phosphono, phosphonooxy, and salts and esters thereof, wherein the R', R2, R3,
R4
may be substituted with R5, wherein R5 represents hydrogen, halogen, hydroxy,
for-
myl, carboxy and salts and esters thereof, amino, vitro, C~_~2-alkyl, C~_6-
alkoxy, acyl,
aryl, in particular phenyl, sulfo, aminosulfonyl, carbamoyl, phosphono, phos-
phonooxy, and salts and esters thereof.
The mediator may also be a salt or an ester of formula I or II.
Further preferred mediators are oxoderivatives and N-hydroxy derivatives of
~5 heterocyclic compounds and oximes of oxo- and formyl-derivatives of
heterocyclic
compounds, said heterocyclic compounds including five-membered nitrogen
containing heterocycles, in particular pyrrol, pyrazole and imidazole and
their hydro
genated counterparts (e.g. pyrrolidine) as well as triazoles, such as 1,2,4-
triazole;
six-membered nitrogen-containing heterocycles, in particular mono-, di- and
triaz
2o inanes (such as piperidine and piperazine), morpholine and their
unsaturated coun-
terparts (e.g. pyridine and pyrimidine); and condensed heterocycles containing
the
above heterocycles as substructures, e.g. indole, benzothiazole, quinoline and
ben-
zoazepine.
Examples of preferred mediators from these classes of compounds are pyridine
25 aldoximes; N-hydroxypyrrolidinediones such as N-hydroxysuccinimide and N
hydroxyphthalimide; 3,4-dihydro-3-hydroxybenzo[1,2,3]triazine-4-one;
formaldoxime
trimer (N,N',N"-trihydroxy-1,3,5-triazinane); and violuric acid (1,3-diazinane-
2,4,5,6
tetrone-5-oxime).
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Still further mediators which may be applied in the invention include oximes
of
oxo- and formyl-derivatives of aromatic compounds, such as benzoquinone
dioxime
and salicylaldoxime (2-hydroxybenzaldehyde oxime), and N-hydroxyamides and N-
hydroxyanilides, such as N-hydroxyacetanilide.
Preferred mediators are selected from the group consisting of 1-
hydroxybenzotriazole; 1-hydroxybenzotriazole hydrate; 1-hydroxybenzotriazole
so-
dium salt; 1-hydroxybenzotriazole potassium salt; 1-hydroxybenzotriazole
lithium salt;
1-hydroxybenzotriazole ammonium salt; 1-hydroxybenzotriazole calcium salt; 1-
hydroxybenzotriazole magnesium salt; and 1-hydroxybenzotriazole-6-sulphonic
acid.
A particularly preferred mediator is 1-hydroxybenzotriazole.
All the specifications of N-hydroxy compounds above are understood to include
tautomeric forms such as N-oxides whenever relevant.
Another preferred group of mediators comprises a -CO-NOH- group and has
~5 the general formula III:
O
A-N
OH
in which A and B independently of each other are:
R3 R2
R4
R5 R6
or B is H or Ci_~2-alkyl, said alkyl may contain hydroxy, ester or ether
groups (e.g.
2o wherein the ether oxygen is directly attached to A-N(OH)C=O-, thus
including N-
hydroxy carbamic acid ester derivatives), and R2, R3, R4, R5 and R6
independently
of each other are H, OH, NH2, COOH, S03H, C~_8-alkyl, acyl, N02, CN, CI, Br,
F, CF3,
NOH-CO-phenyl, CO-NOH-phenyl, C~_6-CO-NOf-;-A, CO-NOH-A, COR12, phenyl
CO-NOH-A, OR7, NR8R9, COOR10, or NOH-CO-1211, wherein R7, R8, R9, R10,
25 R11 and R12 are C~_~z-alkyl or acyl.
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R2, R3, R4, R5 and RED of A are preferably H, OH, NHz, COOH, S03H, C~_3-
alkyl, acyl, NO2, CN, CI, Br, F, CF3, NOH-CO-phenyl, CO-NOH-phenyl, COR12,
OR7, NRBRg, COOR10, or NOH-CO-R11, wherein R7, R8 and R9 are C,_3-alkyl or
acyl, and R10, R11 and R12 are C~_3-alkyl; more preferably R2, R3, R4, R5 and
R6
of A are H, OH, NH2, COOH, S03H, CH3, acyl, NOZ, CN, CI, Br, F, CF3, CO-NOH-
phenyl, COCH3, OR7, NRBRg, or COOCH3, wherein R7, R8 and R9 are CH3 or
COCH3; even more preferably R2, R3, R4, R5 and R6 of A are H, OH, COOH, S03H,
CH3, acyl, NO2, CN, CI, Br, F, CO-NOH-phenyl, OCH3, COCH3, or COOCH3; and in
particular R2, R3, R4, R5 and R6 of A are H, OH, COOH, S03H, CH3, NOZ, CN, CI,
Br, CO-NOH-phenyl, or OCH3.
R2, R3, R4, R5 and R6 of B are preferably H, OH, NH2, COOH, S03H, C~_3-
alkyl, acyl, NO2, CN, CI, Br, F, CF3, NOH-CO-phenyl, CO-NOH-phenyl, COR12,
OR7, NRBRg, COOR10, or NOH-CO-R11, wherein R7, R8 and R9 are C~_3-alkyl or
acyl, and R10, R11 and R12 are C~_3-alkyl; more preferably R2, R3, R4, R5 and
R6
~5 of B are H, OH, NH2, COOH, S03H, CH3, acyl, N02, CN, CI, Br, F, CF3, CO-NOH
phenyl, COCH3, OR7, NRBRg, or COOCH3, wherein R7, R8 and R9 are CH3 or
COCH3; even more preferably R2, R3, R4, R5 and R6 of B are H, OH, COOH, S03H,
CH3, acyl, NOZ, CN, CI, Br, F, CO-NOH-phenyl, OCH3, COCH3, or COOCH3; and in
particular R2, R3, R4, R5 and R6 of B are H, OH, COOH, S03H, CH3, N02, CN, CI,
2o Br, CO-NOH-phenyl, or OCH3.
B is preferably H or C~_3-alkyl, said alkyl may contain hydroxy, ester or
ether
groups; preferably said alkyl may contain ester or ether groups; more
preferably said
alkyl may contain ether groups.
In an embodiment, A and B independently of each other are:
R3 R2
R4
25 R5 ~R6
or B is H or C~_3-alkyl, said alkyl may contain hydroxy, ester or ether groups
(e.g.
wherein the ether oxygen is directly attached to A-N(OH)C=O-, thus including N-
hydroxy carbamic acid ester derivatives), and R2, R3, R4, R5 and R6
independently
of each other are H, OH, NH2, COOH, S03H, C,_3-alkyl, acyl, N02, CN, CI, Br,
F, CF3,
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NOH-CO-phenyl, CO-NOH-phenyl, COR12, OR7, NR8R9, COOR10, or NOH-CO-
R11, wherein R7, R8 and R9 are C~_3-alkyl or acyl, and R10, R11 and R12 are
C~_3-
alkyl.
In another embodiment, A and B independently of each other are:
R3 R2
R4
R5 ~R6
or B is H or C,_3-alkyl, said alkyl may contain hydroxy or ether groups (e.g.
wherein
the ether oxygen is directly attached to A-N(OH)C=O-, thus including N-hydroxy
car-
bamic acid ester derivatives), and R2, R3, R4, R5 and R6 independently of each
other are H, OH, NHZ, COOH, S03H, CH3, acyl, NOZ, CN, CI, Br, F, CF3, CO-NOH-
~o phenyl, COCH3, OR7, NR8R9, or COOCH3, wherein R7, R8 and R9 are CH3 or
COCH3.
In another embodiment, A and B independently of each other are:
R3 R2
R4
R5 ~R6
or B is H or C~_3-alkyl, said alkyl may contain hydroxy or ether groups (e.g.
wherein
~5 the ether oxygen is directly attached to A-N(OH)C=O-, thus including N-
hydroxy car-
bamic acid ester derivatives), and R2, R3, R4, R5 and R6 independently of each
other are H, OH, COOH, S03H, CH3, acyl, NO2, CN, CI, Br, F, CO-NOH-phenyl,
OCH3, COCH3, or COOCH3.
In another embodiment, A and B independently of each other are:
R3 R2
R4
2o R5 ~R6
or B is C~_3-alkyl, said alkyl may contain ether groups (e.g. wherein the
ether oxygen
is directly attached to A-N(OH)C=O-, thus including N-hydroxy carbamic acid
ester
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derivatives), and R2, R3, R4, R5 and R6 independently of each other are H, OH,
COOH, S03H, CH3, NOZ, CN, CI, Br, CO-NOH-phenyl, or OCH3.
In an embodiment at least one of the substituents R2, R3, R4, R5 and R6 of A
are H, preferably at least two of the substituents R2, R3, R4, R5 and R6 of A
are H,
more preferably at least three of the substituents R2, R3, R4, R5 and R6 of A
are H,
most preferably at least four of the substituents R2, R3, R4, R5 and R6 of A
are H, in
particular all of R2, R3, R4, R5 and R6 of A are H.
In another embodiment at least one of the substituents R2, R3, R4, R5 and R6
of B are H, preferably at least two of the substituents R2, R3, R4, R5 and R6
of B are
~o H, more preferably at least three of the substituents R2, R3, R4, R5 and R6
of B are
H, most preferably at least four of the substituents R2, R3, R4, R5 and R6 of
B are
H, in particular all of R2, R3, R4, R5 and R6 of B are H.
In particular embodiments according to the invention the enhancing agent is
selected from the group consisting of
~5 4-nitrobenzoic acid-N-hydroxyanilide;
4-methoxybenzoic acid-N-hydroxyanilide;
N,N'-dihydroxy-N,N'-diphenylterephthalamide;
decanoic acid-N-hydroxyanilide;
N-hydroxy-4-cyanoacetanilide;
2o N-hydroxy-4-acetylacetanilide;
N-hydroxy-4-hydroxyacetanilide;
N-hydroxy-3-(N'-hydroxyacetamide)acetanilide;
4-cyanobenzoic acid-N-hydroxyanilide;
N-hydroxy-4-nitroacetanilide;
25 N-hydroxyacetanilide;
N-hydroxy-N-phenyl-carbamic acid isopropyl ester;
N-hydroxy-N-phenyl-carbamic acid methyl ester;
N-hydroxy-N-phenyl-carbamic acid phenyl ester;
N-hydroxy-N-phenyl-carbamic acid ethyl ester; and
3o N-hydroxy-N-(4-cyanophenyl)-carbamic acid methyl ester.
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Another group of preferred mediators is phenolic compounds (alkylsyringates)
of the general formula IV:
OB
A ~ ~ OH
OC
wherein A represents any of the following groups: (-D), (-CH=CH-D), (-CH=CH-
CH=CH-D), (-CH=N-D), (-N=N-D), or (-N=CH-D); in which D is selected from the
group consisting of -CO-E, -S02-E, -N-XY, and -N+-XYZ; in which E may be -H, -
OH,
-R, or -OR; and X and Y and Z may be identical or different and selected from -
H and
-R; wherein R is a C~_~z-alkyl, preferably a C~_8-alkyl, which alkyl may be
substituted
with a carboxy, sulpho or amino group; and B and C may be the same or
different
~o and selected from C~_5-alkyl.
In general formula IV, A may be placed meta to the hydroxy group instead of
being placed in the para-position as shown.
In particular embodiments of the invention the mediator is selected from the
group having the general formula V:
OMe
A
OH
O
~ 5 OMe
in which A represents any of the following radicals: H, OH, CH3, OCH3, C~_~z-
alkoxy.
Yet another group of preferred mediators are the compounds as described by
general formula VI:
R2 R1 R10 R9
R3 ~ ~ A ~ ~ R8
2o R4 R5 R6 R7
in which general formula A represents a singly bond, or one of the following
groups: (-CH2-), (-CH=CH-), (-NR11-), (-CH=N-), (-N=IJ-), (-CH=N-N=CH-), or
(>C=O);
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and in which general forrnuia the substituent groups R1-R11, which may be iden-
tical or different, independently represents any of the following radicals:
hydrogen,
halogen, hydroxy, formyl, acetyl, carboxy and esters and salts hereof,
carbamoyl, sulfo
and esters and salts hereof, sulfamoyl, methoxy, vitro, amino, phenyl, C,_8-
alkyl;
which carbamoyl, sulfamoyl, phenyl, and amino groups may furthermore be un-
substituted or substituted once or twice with a substituent group R12; and
which C~_8-
alkyl group may be unsubstituted or substituted with one or more substituent
groups
R12;
which substituent group R12 represents any of the following radicals:
hydrogen,
~o halogen, hydroxy, formyl, acetyl, carboxy and esters and salts hereof,
carbamoyl, sulfo
and esters and salts hereof, sulfamoyl, methoxy, vitro, amino, phenyl, or C~_$-
alkyl;
which carbamoyl, sulfamoyl, and amino groups may furthermore be unsubstituted
or
substituted once or twice with hydroxy or methyl.
and in which general formula R5 and R6 may together form a group -B-, in which
B represents a single bond, one of the following groups (-CH2-), (-CH=CH-), (-
CH=N-);
or B represents sulfur, or oxygen.
In particular embodiments of the invention the mediator is selected from the
group having the general formula VII:
R1 R9
R2 ~ ~ X ~ ~ R8
R3 ~ N ~ R7
R4 R5 R6
2o in which general formula X represents a single bond, oxygen, or sulphur;
and in which general formula the substituent groups R1-R9, which may be identi-
cal or different, independently represents any of the following radicals:
hydrogen, halo-
gen, hydroxy, formyl, acetyl, carboxy and esters and salts hereof, carbamoyl,
sulfo and
esters and salts hereof, sulfamoyl, methoxy, vitro, amino, phenyl, C~_8-alkyl;
which carbamoyl, sulfamoyl, phenyl, and amino groups may furthermore be
unsubstituted or substituted once or twice with a substituent group R10; and
which C~_
8-alkyl group may be unsubstituted or substituted with one or more substituent
groups
R10;
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which substituent group R10 represents any of the following radicals:
hydrogen,
halogen, hydroxy, formyl, acetyl, carboxy and esters and salts hereof,
carbamoyl, sulfo
and esters and salts hereof, sulfamoyl, methoxy, nitro, amino, phenyl, or C,_8-
alkyl;
which carbamoyl, sulfamoyl, and amino groups may furthermore be unsubstituted
or
substituted once or twice with hydroxy or methyl.
The term "C~_~-alkyl" wherein n can be from 2 through 12, as used herein,
represents a saturated or unsaturated, and branched or straight alkyl group
having
from one to the specified number of carbon atoms (n); preferably the alkyl
group is a
~o saturated alkyl group. Typical C,_6-alkyl groups include, but are not
limited to, methyl,
ethyl, ethenyl (vinyl), n-propyl, isopropyl, propenyl, isopropenyl, butyl,
isobutyl, sec-
butyl, tert-butyl, crotyl, methallyl, pentyl, isopentyl, propenyl, prenyl,
hexyl, isohexyl,
and the like.
The term "C~_~-alkoxy" wherein n can be from 2 through 8, as used herein,
~5 represents a C,_~-alkyl group linked through an ether group; such as
methoxy, eth-
oxy, propoxy, isopropoxy, butoxy, isobutoxy, sec-butoxy, tert-butoxy, pentoxy,
and
the like.
The term "acyl" as used herein refers to a monovalent substituent comprising a
C~_$-alkyl group linked through a carbonyl group; such as acetyl, propionyl,
butyryl,
2o isobutyryl, pivaloyl, valeryl, and the like.
The term "halogen" as used herein represents a halogen substituent, such as
flouride (F), chloride (CI), bromide (Br), and iodide (I).
Usually, the concentration of the mediator in the rinse liquor is from 0.1 ~M
to
25 50 mM, preferably 0.5 ~M to 10 mM, more preferably 1 ~M to 1 mM, and most
pref-
erably 10 ~.M to 0.5 mM.
Additives
The rinse liquor may comprise further additives, such as wetting agents,
surfac-
3o tants and/or water conditioning agents.
Multi-component system
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In order to carry out the process described above a multi-component system is
added to the solution (rinse liquor) used in at least one of the rinsing
steps.
The components of the multi-component system may individually be in one of
several product forms, such as a slurry, a solution or a granulate.
In one embodiment of the invention two components are mixed in the repre-
sented form, such as a co-granulate, a solution or a slurry comprising enzyme
and
mediator.
In cases of co-granulates, the co-granulate may comprise at least one enzyme
and at least one mediator. Another example of a co-granulate is a granulate
compris
~o ing at least two different enzymes and optionally at least one mediator.
In a further embodiment the system is a mixture of granulates wherein the com-
ponents) in one granulate is(are) enzymes) and the components) in another
granulate is(are) mediator(s).
According to the present invention a preferred multi-component system com
prises at least one enzyme selected from the group consisting of enzymes
exhibiting
peroxidase activity or laccase activity, optionally an oxidation agent, and at
least one
mediator.
The enzymes exhibiting peroxidase activity or laccase activity are preferably
as
described above.
2o The system may comprise an oxidation agent, but in cases where the enzyme
is an enzyme exhibiting laccase activity, molecular oxygen from the atmosphere
is
normally sufficient, and the system used will not comprise an oxidation agent.
How
ever, when the enzymes used require addition of an oxidation agent those are
as
described above. In all cases wherein a H202 source is the oxidation agent the
en
zyme and oxidation agent may not be mixed before use.
The system comprises at least one mediator. In a preferred embodiment, the
mediator is described by general formulas I, II, III, IV, V, VI, and/or VII as
shown
above.
A further aspect of the present invention is the use of components comprising:
3o - at least one enzyme selected from the group consisting of enzymes
exhibiting per-
oxidase activity or laccase activity, and
- optionally an oxidation agent, and
- at least one mediator,
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for the preparation of a multi-component system for removal of excess disperse
dye
or print from a dyed or printed textile material, wherein the textile material
is a fabric,
yarn, fiber, garment or film which comprise at least 20% of a synthetic
material.
Process conditions
The removal of excess disperse dye, according to the invention, may comprise
rinsing with rinse liquor in one or more rinse steps. In an embodiment 1 to 6
rinse
steps, more preferred in 1 to 4 rinse steps, even more preferred in 1 to 2
rinse steps,
in particular in one rinse step is used. The number of rinse steps used
depends on
~o how the invention is practiced in an industrial process.
The multi-component system as defined according to this invention may be
used in any of the rinse steps performed, however it is preferably added in
the early
rinse steps, in particular in the first, second and/or third rinse step.
The process of the invention may be carried out any time after the dye-
~5 ing/rinsing process.
The process may be run in batch mode or continuous mode. The process may
be applied on a winch, a beck, a jet dyer, an open-width washing machine, a J
or U
box, a steamer, or any other equipment available suitable for a rinsing
process.
The process conditions must be chosen according to the characteristics of the
2o enzyme in question. The temperature employed in the rinsing steps)
comprising a
multi-component system as defined above is preferably ranging from 20°C
to 120°C,
more preferably ranging from 30°C to 80°C, most preferably
ranging from 40°C to
80°C, and in particular ranging from 50°C to 70°C. The pH
employed is typically in
the range of pH 4-9.5, preferably in the range of pH 4-9, more preferably in
the range
25 of pH 4-8, most preferably in the range of pH 4.5-7, and in particular in
the range of
pH 5-6.5.
Fastness
Fastness (wash, crock, light, etc.) may be measured by various methods. Wash
3o fastness may be measured as described below Colour fastness to crocking,
which is
designed to determine the amount of colour transferred from the surface of
coloured
materials to other surfaces by rubbing, may be measured according to AATCC
Test
Method 8-1996. Colour fastness to light, in which samples of the material to
be
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tested and the agreed upon comparison standard (s) are exposed simultaneously
to a
light source under specified conditions, may be measured according to AATCC
Test
Method 16-1993.
Removal of excess disperse dye
The multi-component system as defined above is added to the rinsing liquor to
remove excess disperse dye from the fabric surface.
The "Wash fastness" reflects the degree to which this has successfully been
achieved.
In the present invention the wash fastness is measured by AATCC TM 61-2A,
1994. Briefly, in this method a dyed fabric is subjected to appropriate
conditions of
temperature, detergent solution, and abrasive action such that color change is
similar
to that occurring in five hand, home or commercial launderings. The swatches
are
evaluated for color change of the sample and staining on multi-fiber adjacent
fabrics.
~5 The degree of wash fastness is gauged with a scale; the higher number the
bet-
ter wash fastness. 1 means very low wash fastness, whereas 5 means very high
wash fastness. The wash fastness obtained with the method of the invention is
pref-
erably at least 1.5, more preferably at least 2, and most preferably at least
2.5.
2o Colour Measurement
A HunterLab Labscan XE Spectrophotometer was used according to the
manufacturer's instructions to evaluate the chromaticity using the change in
the
colour space coordinates L*a*b* (CIELAB-system), where as usual:
L* gives the change in white/black on a scale from 0 to 100, and a decrease in
2s L* means an increase in black colour (decrease in white colour) and an
increase in
L* means an increase in white colour (decrease in black colour).
a* gives the change in red/green, and a decrease in a* means an increase in
green colour (decrease in red colour), and an increase in a* means an increase
in
red colour (decrease in green colour).
so b* gives the change in blue/yellow, and a decrease in b* means an increase
in
blue colour (decrease in yellow colour), and an increase in b* means an
increase in
yellow colour (decrease in blue colour) (Vide WO 96/12846 NOVO).
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The HunterLab Labscan XE Spectrophotometer was operated in the L*a*b*
colour space. The light source was D65 standard light. The software used for
evalua-
tion was Universal Software Version 3.5. This instrument has a 0°
illumination/45 °
circumferential viewing optical geometry and was calibrated using the white
and
black tiles. Each result was an average of 8 measurements. Fabric rinsed
without
enzyme and mediator was measured and the coordinates L*a*b* were calculated
and entered as a reference. The coordinates of the samples were then for each
of
L*, a*, b* calculated as the difference of the average of the measurements on
each
swatch from the reference value.
Another color parameter, K/S, can also be obtained from the HunterLab Lab-
scan. K/S is calculated from the Kubelka-Munk equation as follows:
KIS=( 1-R)212R
where:
K = absorption coefficient, depending on the concentration of the colorant;
~5 S = scattering coefficient, often caused only by the substrate being dyed;
and
R = reflectance factor (from 0 to 1 ).
This equation describes the relationship between reflection and the concentra-
tion of the colorants of the opaque reflecting samples. K/S values can be used
to
2o monitor the change in color strength of the dyed swatches treated with en-
zyme/mediator system versus that of the reference.
The present invention is further illustrated in the following examples, which
are
not in any way intended to limit the scope of the invention as claimed.
EXAMPLES
The chemicals used in the following examples were commercial products of at
least reagent grade.
3o EXAMPLE 1
Disperse dyeing of polyester fabric followed by an enzymatic clearing process
(POD/HOBT system)
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Knitted, bleached 100% polyester was dyed in a Mathis Labomat machine
(Werner Mathis U.S.A. Inc.) under the following conditions:
Water: softened water
Polyester fabric: 20 g (100% Texturized Dacron 56 Double Knit - no heat set,
supplied by Textile Innovators Corporation)
Liquor : fabric ratio: 15 : 1
Dyestuff: 4% Disperse Violet 1 (Akasperse Violet 3R from Aakash
Chemicals & Dyestuffs, Inc.)
EDTA: 0.5 g/L (chelating agent)
Sodium acetate: 2 g/L (dyebath pH control at 4-5)
The dyeing process started by cold addition of EDTA, sodium acetate, dyestuff
and fabric. The dyebath was pre-heated to 60°C at 3.5°C/min and
circulating for 10
minutes. Thereafter, the temperature was raised at 1.5°C/min to
130°C, where the
~5 dyeing process lasted 60 min.
Upon the completion of the dyeing process, the dyebath was rapidly cooled
down to 70°C followed by draining off the dyeing liquor, whereafter the
afterclearing
process was started.
The afterclearing process was conducted as follows:
20 ~ Filling with 5 mM phosphate buffer (pH 7); 20 mL/g fabric.
~ Raising rinse bath temperature to 60°C.
~ Addition of 2 mL SP502 peroxidase stock (240 POXU/mL), 4 mL HOBT stock (10
mM) and 2 mL H202 stock (20 mM).
~ Rinsing 20 minutes at 60°C.
25 ~ Draining the rinse liquor.
SP502 was a liquid preparation of recombinant Coprinus cinereous peroxidase
supplied by Novozymes A/S (produced as described in WO 92/16634). HOBT was 1-
hydroxybenzotriazole distributed by Sigma.
3o The fabric was squeezed and dried. The wash fastness was determined ac-
cording to AATCC TM 61-2A, 1994. The staining evaluation scores were found to
be
3.5 (silk), 2.5 (Nylon) and 2.0 (Acetate).
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EXAMPLE 2
Disperse dyeing of polyester fabric followed by conventional chemical
reduction
clearing
The dyeing process was carried out as described in Example 1. The afterclear-
ing process was conducted as follows:
~ Addition of 2 g/L sodium hydroxide (or soda ash) and 2 g/L sodium
hydrosulfite in
fresh softened water; 20 mUg fabric.
~ Raising rinse bath temperature to 70°C.
~ Rinsing 20 minutes at 70°C.
Draining the rinse liquor.
~ Refilling and neutralizing with 0.5-1 g/L acetic acid.
The fabric was squeezed and dried. The wash fastness was determined ac-
cording to AATCC TM 61-2A, 1994. The staining evaluation scores were found to
be
~ 5 3.5 (silk), 2.0 (Nylon) and 2.5 (Acetate).
EXAMPLE 3
Disperse dyeina of polyester fabric followed by an enzymatic clearin4 process
(MtL/MeS system)
2o The dyeing process was carried out as described in Example 1. The
afterclear-
ing process was conducted as follows:
~ Filling with 5 mM phosphate buffer (pH 7); 20 mUg fabric.
~ Raising rinse bath temperature to 60°C.
~ Addition of 2 mL Novozyme 809 stock (8 LAMU/mL) and 4 mL MeS stock (10 mM
25 - dissolved in methanol).
~ Rinsing 20 minutes at 60°C.
~ Draining the rinse liquor.
Novozyme 809 was a liquid preparation of recombinant Myceliophthora ther-
3o mophila laccase (MtL) supplied by Novozymes A/S (~~roduced as described in
WO
92/16634). MeS was Methyl Syringate supplied by Lancaster.
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The fabric was squeezed and dried. The wash fastness was determined ac-
cording to AATCC TM 61-2A, 1994. The staining evaluation scores from wash fast-
ness test were found to be 4.5 (silk), 4.0 (Nylon) and 4.0 (Acetate).
Calculated IVS
values were:
K/S value before treatment: 27.273
IUS value after treatment: 27.659
CONCLUSION TO EXAMPLES 1-3
Both the peroxidase/HOBT system (Example 1 ) and the laccase/MeS system
~o (Example 3) are excellent alternatives to the conventional chemical
reduction clear-
ing (Example 2). Both enzymatic systems showed excellent wash fastness
properties
without causing undesirable color fading/shade shifting to the dyed fabric.
EXAMPLE 4
~5 Removal of water insoluble disperse dues with two enzyme/mediator systems
The dyes tested were:
Disperse Blue 27 (Dorospers Blue GLF from D&G Dyes),
Disperse Red 60 (Dianix Red E-Fb from Dystar L.P.),
Disperse Violet 1 (Akasperse Violet 3R from Aakash Chemicals & Dyestuffs,
Inc.),
2o Disperse Blue 56, (Dianix Blue E-R from Dystar L.P.),
Disperse Blue 3 (Akasperse Blue GLF from Aakash Chemicals & Dyestuffs, Inc.),
Disperse Yellow 3 (Akasperse Yellow G from Aakash Chemicals & Dyestuffs,
Inc.).
All dyes were evenly dispersed in 20 mM phosphate buffer (pH 7.0) with the ini-
tial absorbance of approximately 0.8 (measured in 1-Butanol) at the wavelength
25 ~.max of the maximum absorbance within the visible range. The solution was
initially
placed in a glass tube in water bath set at 60°C. The components of two
en-
zyme/mediator systems were dosed as follows:
CiP/HOBT/H~OZ system
30 2.4 POXU/mL Coprinus cinereous peroxidase (CiP)
0.4 mM HOBT
0.4 mM Hz02
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MtL/MeS system
160 LAMU/L Myceliophthora thermophila laccase (MtL)
0.4 mM Methyl Syringate (MeS)
After 10 min, 5 mL 1-butanol were added to the test tube to stop the reaction.
The mixture was centrifuged and the dye degradation products were extracted
into 1-
butanol phase, which was transferred into a thermo-stated quartz curette in a
HP
845x UV-vis spectrophotometer for final absorbance measurement. The degree of
oxidative removal, i.e. the decrease in ABS (~.max) over 10 min divided by the
initial
ABS (~,max), is summarized in table 1.
Table 1. Oxidative removal of disperse dyes treated with enzyme/mediator
systems
~,max Structural CiPlHOBT MtUMeS
C.I. Name (nm) Class (/ removal
) (% removal)
Disperse Blue 610 Anthraquinone 88 89
27
Disperse Red 518 Anthraquinone 26 36
60
Disperse Violet594 Anthraquinone 77 82
1
Disperse Blue 628 Anthraquinone 80 89
56
Disperse Blue 644 Anthraquinone 87 72
3
Disperse Yellow 3 I 357 Monoazo 58 75
This example demonstrates that two of the preferred mediators according to
~5 this invention, HOBT (1-hydroxybenzotriazole, a derivative of N-hydroxy
heterocyclic
compounds) combined with Coprinus cinereous peroxidase (CiP) and hydrogen per-
oxide; and MeS (Methyl Syringate, a derivative of substituted phenol
compounds)
combined with Myceliophthora thermophila laccase (MtL), provide a high degree
of
removal of a range of water insoluble disperse dyes.
