Note: Descriptions are shown in the official language in which they were submitted.
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PREPARATION OF CELLULOSIC MATERIALS
Field of the Invention
The present invention relates to methods and compositions for treating
cellulosic materials, and more particularly, to methods and compositions for
desizing,
scouring and bleaching cellulosic materials.
Background of the Invention
The processing of cellulosic material, such as, cotton fiber, into a material
ready
for garment manufacture involves several steps: spinning of the fiber into a
yarn;
construction of woven or knit fabric from the yarn; and subsequent
preparation, dyeing
and finishing operations. The preparation process, which may involve desizing
(for
woven goods), scouring, and bleaching, produces a textile suitable for dyeing
or
finishing.
A. Desizina: Woven goods are the prevalent form of textile fabric
construction.
The weaving process requires a "sizing" of the warp yarn to protect it from
abrasion.
The size must be removed after the weaving process as the first step in
preparing the
woven goods . Starch, polyvinyl alcohol, carboxymethyl cellulose, waxes and
acrylic
binders are examples of typical sizing agents commonly used in the industry.
In order
to ensure a high whiteness and/or a good dyeability, the size and other
applied must be
thoroughly removed. It is generally believed that an efficient desizing is
crucial to the
subsequent preparation processes, namely, the scouring and bleaching
processes.
The sized fabric, in either rope or open width form, is contacted with the
processing
liquid containing the desizing agent. The desizing agent employed depends upon
the
type of size to be removed. The most common sizing agent for cotton fabric is
based
upon starch. Therefore, most often, woven cotton fabrics are desized by a
combination
of hot water, the enzyme alpha amylase and a wetting agent or surfactant.
B. Scouring: The scouring process removes much of the non-cellulosic
compounds naturally found in cotton. In addition to the natural non-cellulosic
impurities, scouring can remove residual manufacturing introduced materials
such as
spinning, coning or slashing lubricants. Conventional scouring processes
typically
utilize highly alkaline chemical treatment, which results not only in removal
of impurities
but also in weakening of the underlying cellulose component of the fiber or
fabric. The
chemical scouring is followed by extensive rinsing to reduce the risk of re-
depositing
impurities. Insufficient rinsing yields alkaline residue and uneven removal of
impurities
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on the fabric, which in turn results in uneven dyeing in the subsequent
process.
Furthermore, chemical scouring creates environmental problems in effluent
disposal,
due to the chemicals employed.and the materials extracted from the fibers. The
use of
enzymes for scouring has also been proposed as an alternative to chemical
scouring
processes, as described, e.g., in W09824'965, W00071808, JP6220772,
JP10088472,
U.S. Patent No. 5,912,407; Hartzell et al., Textile Res. 68:233 (1998); Hsieh
et al.,
Textile Res. 69:590 (1999); Buchert et al., Text. Chem. Col. &Am.
DyesfuffReptr.
32:48 (2000); and Li et al., Text. Chem. Color. 29:71 (1997).
C. Bleaching: Bleaching of textiles is the final preparation step in the
manufacturing of textile fabrics and garments. The purpose of bleaching is to
completely remove colored impurities, improve absorbency, and achieve adequate
whiteness and dyeability. The most widely used bleaching process in the
textile
industry is the alkaline hydrogen peroxide process. A conventional textile
bleach bath
typically contains: sodium hydroxide, surfactant, optical brightener,
stabilizers, and
bleaching agents. The bleaching stage can be carried out in batch wise, semi-
continuous, or continuous processes. When enzymes are used in either the
desizing or
scouring process, in order to obtain consistent, high quality results with
commercial
quantities of textiles, the desizing and scouring steps are usually performed
separately
from the bleaching step because it is very difficult to combine the enzymatic
processes
with alkaline peroxide bleaching in a single stage due to the high temperature
and
alkalinity requirement of alkaline peroxide bleaching.
Summarv of the Invention
The present invention provides methods for single-bath desizing, scouring and
bleaching of cellulosic materials, such as, crude fibers, yarn, or woven or
knit textiles, made
of cotton, linen, flax, ramie, rayon, hemp, jute, or blends of these fibers
with each other or
with other natural or synthetic fibers.
The methods are carried out by contacting the cellulosic materials with (i) an
enzyme
system, and (ii) a bleaching system; by adding the enzyme system and the
bleaching system
in the same solution containing the cellulosic material to be treated without
emptying the
bath or rinsing the cellulosic materials between desizing, scouring and
bleaching steps, i.e.,
in a single-bath process. The enzyme system and the bleaching system may be
added
simultaneously to the solution. Alternatively, the enzyme system and the
bleaching system
may be added sequentially to the solution, in which the cellulosic materials
are (i) contacted
with the enzyme system for a sufficient time and under appropriate conditions
that result in
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effective bioscouring and/or desizing, after which (ii) the bleaching system
is added directly
to the solution containing cellulosic materials and the enzyme system.
In one embodiment of the present invention, a method for treating ceiiulosic
material is disclosed, comprising contacting the cellulosic material with (i)
an enzyme
system for desizing andlor bioscouring the cellulosic material and (ii) a
bleaching
system comprising hydrogen peroxide or at least one compound which generates
hydrogen peroxide when dissolved in water, or combinations thereof, and at
least one
bleach activator, wherein the enzyme system and the bleaching system are added
simultaneously or sequentially to a single solution containing the cellulosic
material.
In another embodiment, a method for treating cellulosic material is disclosed,
comprising contacting the cellulosic material with (i) an enzyme system for
desizing
and/or bioscouring the cellulosic material and (ii) a bleaching system
comprising
hydrogen peroxide or at least one compound which generates hydrogen peroxide
when
dissolved in water, or combinations thereof, and at least one bleach
activator, wherein
the enzyme system and the bleaching system are added simultaneously or
sequentially
to a single solution containing the cellulosic material, and wherein the
contacting is
performed without the addition of alkali.
In yet another embodiment, a method for treating cellulosic material is
disclosed,
comprising contacting the cellulosic material with (i) an enzyme system for
desizing andlor
bioscouring the cellulosic material and (ii) a bleaching system comprising
hydrogen peroxide
or at least one compound which generates hydrogen peroxide when dissolved in
wafer, or
combinations thereof, and at least one bleach activator, wherein the enzyme
system and the
bleaching system are added simultaneously or sequentially to a single solution
containing
the cellulosic material, and wherein the contacting is performed at a high pH,
preferably
above 9.
The methods and compositions of present invention provide a product exhibiting
a
high wettability, high whiteness, and uniformity of mote removal, while having
advantages
over convenfiional preparation processes, including: (i) shorter processing
times; (ii)
conservation of water; and (iii) reduction in waste stream.
Detailed Description of the Invention
Cellulosic Materials
As used herein, a "cellulosic material" refers to the cellulosic substrate to
be
treated and comprises, without limitation, cotton, linen, flax, ramie, rayon,
hemp, jute,
and their blends with other natural or synthetic fibers. The cellulosic
material may also
comprise, without limitation, crude fiber, yarn, woven or knit textile or
fabric, or a
garment or finished product.
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Enzyme Svstem
As used in the present invention, an enzyme system refers to a bioscouring
enzyme system and/or a desizing enzyme system. Accordingly, an enzyme system
may comprise one or more bioscouring enzymes with or without one or more
desizing
enzymes or one or more desizing enzymes with or without one or more
bioscouring
enzymes. Preferably, the enzyme system is compatible with (i) the conditions
in which
bleaching is performed simultaneously with bioscouring andlor desizing
processes or
(ii) the conditions in which bleaching is perFormed sequentially with
bioscouring and/or
desizing processes, as described herein.
Desizing Enzymes:
Any suitable desizing enzyme may be used in the present invention. Preferably,
the desizing enzyme is an amylolytic enzyme. More preferably, the desizing
enzyme is
an alpha or beta amylase and combinations thereof.
Alpha and beta amylases which are appropriate in the context of the present
invention include those of bacterial or fungal origin. Chemically or
genetically modified
mutants of such amylases are also included in this connection. Preferred alpha-
amylases include, for example, alpha-amylases obtainable from Bacillus
species, in
particular a special strain of B. licheniformis, described in more detail in
GB 1296839.
More preferred amylases include DuramylT"", TermamylT"", FungamylT"" and BANTM
(all
available from Novozymes AIS, Bagsvaerd, Denmarle), and RapidaseT"" and
MaxamylT""
(available from Gist-Brocades] Holland). Other preferred amylolytic enzymes
are
CGTases (cyclodextrin. glucanotransferases, EC 2.4.1.19), e.g., those obtained
from
species of Bacillus, Thermoanaerobactor or Thermoanaero-bacterium.
The desizing enzymes may also preferably be derived from the enzymes listed
above in which one or more amino acids have been added, deleted, or
substituted,
including hybrid polypeptides, so long as the resulting polypeptides exhibit
desizing
activity. Such variants useful in practicing the present invention can be
created using
conventional mutagenesis procedures and identified using, e.g., high-
throughput
screening techniques such as the agar plate screening procedure.
The desizing enzyme is added to the aqueous solution or wash liquor (i.e., the
treating composition) in an amount effective to desize the cellulosic
materials.
Typically, desizing enzymes, such as alpha-amylases, are incorporated into the
treating
composition in amount from 0.00001 % to 2% of enzyme protein by weight of the
composition, preferably in an amount from 0.0001 % to 1 % of enzyme protein by
weight
of the composition, more preferably in an amount from 0.001 % to 0.5% of
enzyme
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protein by weight of the composition, and even more preferably in an amount
from
0.01 % to 0.2% of enzyme protein by weight of the composition. The desizing
enzyme
is preferably used at a level from about 2 to 30,000 KNUII, more preferably 20-
30,000
KNU/1 and most preferably 200-300 KNU/I or from about 3-50,000 NAU/I, more
preferably 30-5,000 NAU/I, most preferably 350-500 NAU/I.
Bioscouring Enzymes:
Any suitable bioscouring enzyme may be used in the present invention.
Preferred bioscouring enzymes include, without limitation, pectinases,
proteases,
lipases, cutinases and combinations thereof, more preferably, the bioscouring
enzyme
is a pectinases, and even more preferably, the bioscouring enzyme is a pectate
lyase.
Pectinases: Any pectinolytic enzyme composition with the ability to degrade
the pectin composition of plant cell walls may be used in practicing the
present
invention. Suitable pectinases include, without limitation, those of fungal or
bacterial
origin. Chemically or genetically modified pectinases are also encompassed.
Preferably, the pectinases used in the invention are recombinantly produced
and are
mono-component enzymes.
Pectinases can be classified according to their preferential substrate, highly
methyl-esterified pectin or low methyl-esterified pectin and polygalacturonic
acid
(pectate), and their reaction mechanism, beta-elimination or hydrolysis.
Pectinases can
be mainly endo-acting, cutting the polymer at random sites within the chain to
give a
mixture of oligomers, or they may be exo-acting, attacking from one end of the
polymer
and producing monomers or dimers. Several pectinase activities acting on the
smooth
regions of pectin are included in the classification of enzymes provided by
Enzyme
Nomenclature (1992), e.g., pectate lyase (EC 4.2.2.2), pectin lyase (EC
4.2.2.10),
polygalacturonase (EC 3.2.1.15), exo-polygalacturonase (EC 3.2.1.67), exo-
polygalacturonate lyase (EC 4.2.2.9) and exo-poly-alpha-galacturonosidase (EC
3.2.1.82).
In preferred embodiments of the present invention, the pectinase is a pectate
lyase. Pectate lyase enzymatic activity as used herein refers to catalysis of
the random
cleavage of a-1,4-glycosidic linkages in pectic acid (also called
polygalcturonic acid) by
transelimination. Pectate lyases are also termed polygalacturonate lyases and
poly(1,4-a-D-galacturonide) lyases.
Any pectate lyase may be used in practicing the present invention. In
preferred
embodiments, the methods utilize a pectate lyase that exhibits maximal
activity at
temperatures above about 70°C. Pectate lyases may also preferably
exhibit maximal
activity at a pH above about 8 andlor exhibit enzymatic activity in the
absence of added
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divalent cations, such as, calcium ions. Non-limiting examples of pectate
lyases for use
in the present invention 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.
The pectinases may be incorporated in the aqueous enzyme solution or wash
liquor in an amount from 0.00001 % to 2% of enzyme protein by weight of the
composition, preferably in an amount from 0.0001 % to 1 % of enzyme protein by
weight
of the composition, more preferably in an amount from 0.001 % to 0.5% of
enzyme
protein be weight to the composition, and even more preferably in an amount
from
0.01 % to 0.2% of enzyme protein by weight of the composition. Pectinases are
preferably used at a level from about 2.5 to 500,000 APSUIg fabric, more
preferably, at
a level from about 25 to 50,000 APSUIg fabric, and most preferably at a level
from
about 250 to 5,000 APSU/g fabric.
Proteases: Any protease suitable for use in the present invention may be
employed. Suitable proteases include those of animal, vegetable or microbial
origin,
preferably of microbial origin. Preferably, the protease may be a serine
protease or a
metalloprotease, more preferably, an alkaline microbial protease or a trypsin-
like
protease. Examples of proteases include aminopeptidases, including prolyl
aminopeptidase (3.4.11.5), X-pro aminopeptidase (3.4.11.9), bacterial leucyl
aminopeptidase (3.4.11.10), thermophilic aminopeptidase (3.4.11.12), lysyl
aminopeptidase (3.4.11.15), tryptophanyl aminopeptidase (3.4.11.17), and
methionyl
aminopeptidase (3.4.11.18); serine endopeptidases, including chymotrypsin
(3.4.21.1),
trypsin (3.4.21.4), cucumisin (3.4.21.25), brachyurin (3.4.21.32), cerevisin
(3.4.21.48)
and subtilisin (3.4.21.62); cysteine endopeptidases, including papain
(3.4.22.2), ficain
(3.4.22.3), chymopapain (3.4.22.6), asclepain (3.4.22.7), actinidain
(3.4.22.14), caricain
(3.4.22.30) and ananain (3.4.22.31); aspartic endopeptidases, including pepsin
A
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(3.4.23.1), Aspergillopepsin I (3.4.23.18), Penicillopepsin (3.4.23.20) and
Saccharopepsin (3.4.23.25); and metalloendopeptidases, including Bacillolysin
(3.4.24.28).
Commercially available proteases include Alcalase, Savinase, Primase,
Duralase, Esperase, Kannase, and Durazym (available from Novozymes A/S),
Maxatase, Maxacal, Maxapem, Properase, Purafect, Purafect OxP, FN2, FN3 and
FN4
(available from Genencor International Inc.).
Also useful in the present invention are protease variants, such as those
disclosed in EP 130,756 (Genentech), EP 214,435 (Henkel), WO 87/04461 (Amgen),
WO 87/05050 (Genex), EP 251.446 (Genencor), EP 260.105 (Genencor), Thomas et
al., (1985), Nature. 318, p. 375-376, Thomas et al., (1987), J. Mot. Biol.,
193, pp. 803-
813, Russet et al., (1987), Nature, 328, p. 496-500, WO 88/08028 (Genex), WO
88/08033 (Amgen), WO 89/06279 (Novozymes A/S), WO 91100345 (Novozymes A/S),
EP 525 610 (Solvay) and WO 94102618 (Gist-Brocades N.V.). The activity of
proteases
can be determined as described in "Methods of Enzymatic Analysis", third
edition,
1984, Verlag Ghemie, Weinheim, vol. 5.
Proteases are preferably incorporated into the aqueous enzyme solution or
wash liquor in an amount from 0.00001% to 2% of enzyme protein by weight of
the
composition, preferably in an amount from 0.0001 % to 1 % of enzyme protein by
weight
of the composition, more preferably in an amount from 0.001 % to 0.5% of
enzyme
protein be weight to the composition, and even more preferably in an amount
from
0.01% to 0.2% of enzyme protein by weight of the composition.
Lipases: Any lipase suitable for use in the present invention may be used.
Suitable lipases (also termed carboxylic ester hydrolases) preferably include
those of
bacterial or fungal origin, including triacylglycerol lipases (3.1.1.3) and
Phospholipase
A2,(3.1.1.4.). Lipases for use in the present invention include, without
limitation, lipases
from Humicola (synonym Thermomyces), such as 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, such as from P. alca/igenes 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, such as from B. subtilis (Dartois et al.,
Biochem.Biophys. Acta, 1131:253-360, 1993); B. stearothermophilus (JP
64/744992) or
8. pumilus (WO 91/16422). Other examples are lipase variants such as those
described in WO 92105249, WO 94/01541, EP 407 225, EP 260 105, WO 95135381,
WO 96/00292, WO 95/30744, WO 94125578, WO 95/14783, WO 95/22615, WO
97/04079 and WO 97/07202. Preferred commercially available lipase enzymes
include
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LipolaseT"" and Lipolase UItraT"", LipozymeTM , PalataseT"", NovozymT""435,
and
LecitaseT"" (all available from Novovozymes A/S). The activity of the lipase
can be
determined as described in "Methods of Enzymatic Analysis", Third Edition,
1984,
Verlag Chemie, Weinhein, vol. 4.
Lipases are preferably incorporated in the aqueous enzyme solution or'wash
liquor in an amount from 0.00001 % to 2% of enzyme protein by weight of the
composition, preferably in an amount from 0.0001% to 1% of enzyme protein by
weight
of the composition, more preferably in an amount from 0.001 % to 0.5% of
enzyme
protein be weight to the composition, and even more preferably in an amount
from
0.01 % to 0.2% of enzyme protein by weight of the composition.
Cutinases: Any cutinase suitable for use in the present invention may be used,
including, for example, the cutinase derived from Humicola insolens cutinase
strain
DSM 1800, as described in Example 2 of U.S. Patent No. 4,810,414.
Cutinases are preferably incorporated in the aqueous enzyme solution in an
amount from 0.00001 % to 2% of enzyme protein by weight of the composition,
preferably in an amount from 0.0001°lo to 1% of enzyme protein by
weight of the
composition, more preferably in an amount from 0.001 % to 0.5% of enzyme
protein be
weight to the composition, and even more preferably in an amount from 0.01 %
to 0.2%
of enzyme protein by weight of the composition.
Suitable bioscouring enzymes also include, for example, bioscouring enzymes
derived from the enzymes listed above in which one or more amino acids have
been
added, deleted, or substituted, including hybrid polypeptides, may be used, so
long as
the resulting polypeptides exhibit bioscouring activity. Such variants useful
in
practicing the present invention can be created using conventional mutagenesis
procedures and identified using, e.g., high-throughput screening techniques
such as
the agar plate screening procedure. For example, pectate lyase activity may be
measured by applying a test solution to 4 mm holes punched out in agar plates
(such
as, for example, LB agar), containing 0.7% w/v sodium polygalacturonate (Sigma
P
1879). The plates are then incubated for 6 h at a particular temperature (such
as, e.g.,
75°C). The plates are then soaked in either (i) 1M CaCl2 for 0.5h or
(ii) 1% mixed alkyl
trimethylammonium Br (MTAB, Sigma M-7635) for 1 h. Both of these procedures
cause
the precipitation of polygalacturonate within the agar. Pectate lyase activity
can be
detected by the appearance of clear zones within a background of precipitated
polygalacturonate. Sensitivity of the assay is calibrated using dilutions of a
standard
preparation of pectate lyase.
Effective scouring typically results in improvement in wettability, when
measured
using the drop test according to AATCC Test Method 39-1980. Preferably, the
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wettability of the bleached fabric is 20 seconds or less, most preferably, 10
seconds or
less.
Desizing and bioscouring enzymes for use in the invention may be derived from
their cell of origin or may be recombinantly produced, and may be purified or
isolated.
As used herein, a "purified" or "isolated" enzyme is one that has been treated
to
remove non-enzyme material or other enzymes derived from the cell in which it
was
synthesized that could interfere with its enzymatic activity. Typically, the
desizing and
bioscouring enzyme is separated from the bacterial or fungal microorganism in
which it
is produced as an endogenous constituent or as a recombinant product. If the
enzyme
is secreted into the culture medium, purification may comprise separating the
culture
medium from the biomass by centrifugation, filtration, or precipitation, using
conventional methods. Alternatively, the enzyme may be released from the host
cell by
cell disruption and separation of the biomass. In some cases, further
purification may
be achieved by conventional protein purification methods, including without
limitation
ammonium sulfate precipitation; acid or chaotrope extraction; ion-exchange,
molecular
sieve, and hydrophobic chromatography, including FPLC and HPLC; preparative
isoelectric focusing; and preparative polyacrylamide gel electrophoresis.
Alternatively,
purification may be achieved using affinity chromatography, including
immunoaffinity
chromatography. For example, hybrid recombinant pectate lyases may be used
having
an additional amino acid sequence that serves as an affinity "tag", which
facilitates
purification using an appropriate solid-phase matrix.
The desizing and bioscouring enzyme used in the methods of the invention may
also be chemically modified to enhance one or more properties that render them
even
more advantageous, such as, e.g., increasing solubility, decreasing lability
or divalent
ion dependence, etc. The modifications include, without limitation,
phosphorylation,
acetylation, sulfation, acylation, or other protein modifications known to
those skilled in
the art.
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Bleachin_a Systems
Any bleaching system may be used in the present invention that is either
compatible with (i) the conditions used for desizing and/or scouring, when
desizing
and/or scouring are performed simultaneously with the bleaching process, or
(ii) the
conditions used for desizing and/or scouring, when desizing and/or scouring
are
performed sequentially with the bleaching process. Preferably, the bleaching
system
comprises at least one bleach compound, at least one bleach activator, and,
optionally,
at least one bleach stabilizer, as described herein below.
Bleach Compound:
The bleach compound is preferably hydrogen peroxide or a compound which
generate hydrogen peroxide when dissolved in water, such as, a peroxy
compound.
Examples of suitable compounds which generate hydrogen peroxide when dissolved
in
water are alkali metal perborates or alkali metal carbonate perhydrates,
especially the
sodium salts. The bleach compound hydrogen peroxide is preferably added to the
aqueous solution or wash liquor in an amount from about .01 to about 10 g// of
the
aqueous solution or wash liquor, more preferably in an amount from .1 to 5
g//, most
preferably, in an amount from .5 to 2.5 g//. A compound which generates
hydrogen
peroxide, such as an alkali metal perborate or an alkali metal carbonate, is
preferably
added to the aqueous solution or wash liquor in an amount from about .001 to
20 g// of
the aqueous solution or wash liquor, more preferably, in an amount from about
.1 to 10
g//, and most preferably in an amount from about .5 to 5 g//.
Bleach Activator:
Any suitable bleach activator may be employed in the present invention. The
bleach activators preferred for use in accordance with the invention, include,
for
example, compounds of the following classes of substances: Polyacylated sugars
or
sugar derivatives with C sub 1-10 -acyl radicals, preferably acetyl,
propionyl, octanoyl,
nonanoyl or benzoyl radicals, particularly preferably acetyl radicals, can be
used as
bleach activators. Sugars or sugar derivatives which can be used are mono- or
disaccharides and their reduced or oxidized derivatives, preferably glucose,
mannose,
fructose, sucrose, xylose or lactose. Particularly suitable bleach activators
of this class
of substances are, for example, pentaacetylglucose, xylose tetraacetate, 1-
benzoyl-
2,3,4,6-tetraacetylglucose and 1-octanoyl-2,3,4,6-tetraacetylglucose.
Another class of substances which are preferred for use as bleach activators
in
the present invention comprises acyloxybenzenesulfonic acids and their alkali
metal
and alkaline earth metal salts, such as C sub 1-14 -acyl radicals. Acetyl,
propionyl,
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octanoyl, nonanoyl and benzoyl radicals are preferred, especially acetyl
radicals and
nonanoyl radicals. Particularly suitable bleach activators in this class of
substances are
acetyloxybenzenesulfonic acid and benzoyloxybenzenesulfonic acid. They are
preferably employed in the form of their sodium salts.
Other bleach activators for use in the present invention include MMA and OCL,
alone or in combination with each other or with TAED; O-acyloxime esters, such
as
acetone O-acetyloxime, acetone O-benzoyloxime, bis(propyiimino) carbonate,
bis(cyclohexylimino) carbonate as a bleach activator. Acylated oximes which
can be
used as a bleach activator according to the invention are described, for
example, in
EP-A-0 028 432. Oxime esters which can be used as a bleach activator according
to
the invention are described, for example in EP-A-0 267 046.
Additional preferred bleach activators include N-acylcaprolactams, such as N-
acetylcaprolactam, N-benzoylcaprolactam, N-octanoylcaprolactam and
carbonylbiscaprolactam; N,N-diacylated and N,N,N',N'-tetraacylated amines,
such as
N,N,N',N'-tetraacetylmethylenediamine and -ethylenediamine (TAED), N,N-
diacetylaniline, N,N-diacetyl-p-toluidine or 1,3-diacylated hydantoins such as
1,3-
diacetyl-5,5-dimethylhydantoin; N-alkyl-N-sulfonylcarboxamides, such as N-
methyl-N-
mesylacetamide or N-methyl-N-mesylbenzamide; N-acylated cyclic hydrazides,
acylated triazoles or urazoles, such as monoacetylated malefic hydrazide;
O,N,N-
trisubstituted hydroxylamines, such as O-benzoyl-N,N-succinyl-hydroxylamine, O-
acetyl-N,N-succinylhydroxylamine or O,N,N-triacetylhydroxylamine; N,N'-
diacylsulfamides, such as N,N'-dimethyl-N,N'-diacetylsulfamide or N,N'-diethyl-
N,N'-
dipropionylsulfamide; triacylcyanurates, such as triacetylcyanurate or
tribenzoylcyanurate; carboxylic anhydrides, such as benzoic anhydride, m-
chlorobenzoic anhydride or phthalic anhydride; 1,3-diacyl-4,5-
diacyloxyimidazolines,
such as 1,3-diacetyl-4,5-diacetoxyimidazoline; tetraacetylglycoluril and
tetrapropionylglycoluril; diacylated 2,5-diketopiperazines, such as 1,4-
diacetyl-2,5-
diketopiperazine; acylation products of propylenediurea and 2,2-
dimethylpropylenediurea, such as tetraacetylpropylenediurea; alpha.-
acyloxypolyacylmalonamides, such as .alpha.-acetoxy-N,N'-diacetylmalonamide;
diacyldioxohexahydro-1,3,5-triazines, such as 1,5-diacetyl-2,4-dioxohexahydro-
1,3,5-
triazine; 2-alkyl- or 2-aryl-(4H)-3,1-benzoxazin-4-ones as described, for
example, in
EP-B1-0 332'294 and EP-B 0 502 013, and 2-phenyl-(4H)-3,1-benzoxazin-4-one and
2-
methyl-(4H)-3,1-benzoxazin-4-one, cationic nitrites, as described, for
example, in EP
303 520 and EP 458 396 A1, such as, methosulfates or tosylates of
trimethylammonioacetonitrile, N,N-dimethyl-N-octylammonioacetonitrile, 2-
(trimethylammonio)propionitrile, 2-(trimethylammonio)-2-methylpropionitrile.
Also
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suitable are the methosulfates of N-methylpiperazinio-N,N'-diacetonitrile and
N-
methylmorpholinioacetonitrile (MMA).
Additional bleach activators for use in the present invention include
percarbamic
acids or diacyl percarbamates and precursors thereof.
Bleach activators are typically added in an amount from about .1 to 30 g/1,
more
preferably 0.5 to 10 g/1.
Bleach Stabilizer:
In another preferred embodiment of the present invention, the bleaching system
additionally contains one or more bleach stabilizers. The bleach stabilizers
comprise
additives able to adsorb, bind or complex traces of heavy metals. Examples of
additives which can be used according to the invention with a bleach-
stabilizing action
are polyanionic compounds, such as polyphosphates, polycarboxylates,
polyhydroxypolycarboxylates, soluble silicates as completely or partially
neutralized
alkali metal or alkaline earth metal salts, in particular as neutral Na or Mg
salts, which
are relatively weak bleach stabilizers. Examples of strong bleach stabilizers
which can
be used according to the invention are complexing agents such as
ethylenediaminetetraacetate (EDTA), ~diethylenetriaminepentaacetic acid
(DTPA),
nitrilotriacetic acid (NTA), methyl-glycinediacetic acid (MGDA), .beta.-
alaninediacetic
acid (ADA), ethylenediamine-N,N'-disuccinate (EDDS) and phosphonates such as
ethylenediaminetetramethylenephosphonate,
diethylenetriaminepentamethylenephosphonate (DTMPA) or hydroxyethylidene-1,1-
diphosphonic acid in the form of the acids or as partially or completely
neutralized
alkali metal salts.
The bleach stabilizer is typically added to the treating composition in an
amount
from about .1 to about 5/g liter of the composition, more preferably from.
about .5 to
about 2g/1, and most preferably about 1 g/1.
The bleach composition according to the invention preferably contains at least
one bleach stabilizer, and more preferably, at least one of the above
mentioned strong
bleach stabilizers. Effective bleaching typically results in one or more of
the following
properties: (i) a desired whiteness (as determined by Ganz whiteness
measurement
using, e.g., a Macbeth color eye); (ii) a satisfactory uniformity of mote
removal
(assessed by visual examination); Preferably, the whiteness of the fabric is
50 Ganz
units or higher, and most preferably, 60 Ganz units or higher.
Accordingly, in a preferred embodiment, the single-bath process comprises an
enzyme system, such as, pectate lyase, hydrogen peroxide, a bleach activator
(such
as, TAED) and a bleach stabilizer.
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Alkali Agents:
Alkali agents are well known in the art. Preferred alkali agents used in the
present invention include, sodium hydroxide, sodium carbonate, sodium
bicarbonate,
sodium perborate, sodium sulfide and sodium sulfite. However, in some
embodiments,
it is preferred that the single-bath process is carried out in the absence of
an alkali
agent, in particular, when treating alkaline-sensitive cellulosic materials,
such as, silk
and wool.
Additional components:
In some embodiments of the invention, the aqueous solution or wash liquor
further comprises other components, including without limitation other
enzymes, as well
as surfactants, antifoaming agents, lubricants, builder systems, and the like,
that
enhance the scouring and/or bleaching processes and/or provide superior
effects
related to, e.g., strength, resistance to pilling, water absorbency, and
dyeability.
Enzymes suitable for use in the present invention include without limitation
pectinases, proteases, and lipases as described above; and cellulases.
Cellulases are
classified in a series of enzyme families encompassing endo- and exo-
activities as
well as cellobiose hydrolyzing capability. The cellulase used in practicing
the present
invention may be derived from microorganisms which are known to be capable of
producing cellulolytic enzymes, such as, e.g., species of Humicola,
Thermomyces,
Bacillus, Trichoderma, Fusarium, Myceliophthora, Phanerochaete, Irpex,
Scytalidium,
Schizophyllum, Penicillium, Aspergillus, or Geotricum, particularly Humicola
insolens,
Fusarium oxysporum, or Trichoderma reesei. Non-limiting examples of suitable
cellulases are disclosed in U.S. Patent No. 4,435,307; European patent
application No.
0 495 257; PCT Patent Application No. W091/17244; and European Patent
Application
No. EP-A2-271 004.
The enzymes may be isolated from their cell of origin or may be recombinantly
produced, and may be chemically or genetically modified. Typically, the
enzymes are
incorporated in the aqueous solution at a level of from about 0.0001 % to
about 1 % of
enzyme protein by weight of the composition, more preferably from about 0.001
% to
about 0.5% and most preferably from 0.09 % to 0.2%. It will be understood that
the
amount of enzymatic activity units for each additional enzyme to be used in
the
methods of the present invention in conjunction with a particular bioscouring
enzyme
can be easily determined using conventional assays.
Surfactants suitable for use in practicing the present invention include,
without
limitation, nonionic (U.S. Patent No. 4,565,647); anionic; cationic; and
zwitterionic
surfactants (U.S. Patent No. 3,929,678); which are typically present at a
concentration
of between about 0.2% to about 15% by weight, preferably from about 1 % to
about
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10% by weight. Anionic surfactants include, without limitation, linear
alkylbenzenesulfonate, a-olefinsulfonate, alkyl sulfate (fatty alcohol
sulfate), alcohol
ethoxysuifate, secondary alkanesulfonate, alpha-sulfo fatty acid methyl ester,
alkyl- or
alkenylsuccinic acid, and soap. Non-ionic surfactants include, without
limitation,
alcohol ethoxylate, nonylphenol ethoxylate, alkylpolyglycoside,
alkyldimethylamineoxide, ethoxylated fatty acid monoethanolamide, fatty acid
monoethanolamide, polyhydroxy alkyl fatty acid amide, and N-acyl N-alkyl
derivatives
of glucosamine ("glucamides").
Builder systems include, without limitation, aluminosilicates, silicates,
polycarboxylates and fatty acids, materials such as ethylenediamine
tetraacetate, and
metal ion sequestrants such as aminopolyphosphonates, particularly
ethylenediamine
tetramethylene phosphonic acid and diethylene triamine
pentamethylenephosphonic
acid, which are included at a concentration of between about 5% to 80% by
weight,
preferably between about 5% and about 30% by weight.
Antifoam agents include without limitation silicones (U.S. Patent No.
3,933,672;
DC-544 (Dow Corning), which are typically included at a concentration of
between
about 0.01% and about 1% by weight.
The compositions may also contain soil-suspending agents, soil-releasing
agents, optical brighteners, abrasives, and/or bactericides, as are
conventionally
known in the art.
Process conditions:
The manner in which the aqueous solution containing the enzyme and bleaching
system is contacted with the cellulosic material will depend upon whether the
processing regime is continuous, discontinuous pad-batch or batch. For
example, for
continuous or discontinuous pad-batch processing, the aqueous enzyme solution
is
preferably contained in a saturator bath and is applied continuously to
the~cellulosic
material as it travels through the bath, during which process the cellulosic
material
typically absorbs the processing liquor at an amount of 0.5-1.5 times its
weight. In
batch operations, the cellulosic material is exposed to the enzyme solution
for a period
ranging from about 5 minutes to 24 hours at a liquor-to-fabric ratio of 5:1-
50:1.
The aqueous solution or wash liquor typically has a pH of between about 4 and
about 11. Preferably, the pH of the treating composition is between about 5
and about
10, preferably between about 7 to about 9, and most preferably about 8 to
about 9.
In one embodiment, the single-bath method for treating cellulosic material is
carried out without the addition of alkali. Preferably, this treatment is used
for treating
alkaline-sensitive cellulosic materials, such as silk and wool. In another
embodiment,
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the single-bath method for treating cellulosic material is carried out at a pH
below 9,
more preferably, below 8, and even more preferably below 7.
In another embodiment, the single-bath method for treating cellulosic material
is
carried out with the addition of alkaline. Preferably, the contacting is
perFormed at a pH
about 8 or above, more preferably at pH 9 or above, such as, at a pH from pH 9-
11,
preferably, 9.5-10.5, more preferably 10-11. The pH may be controlled, e.g.,
with the
addition of an alkali agent, such as NaOH. Alkali agents may be added in
amounts from
about .1 to about 10% by wt. of fabric, as necessary to obtain the desired pH.
However, as
an artisan would appreciated, the amount of alkali agent added with depend on
the amount
of bleaching compound used.
The temperature at which the combined scouring and/or desizing and bleaching
processes are carried out will depend on the process used. In the case of cold
pad
batch process, the scouring and/or desizing and bleaching temperature is
preferably
between about 15°C and about 45°C, and most preferably between
about 25°C and
about 35°C. For continuous and other batch processes, the scouring
andlor desizing
temperature is preferably between about 35°C and about 75°C, and
most preferably
between about 45°C and about 65°C; and the bleaching temperature
may be between
about 30°C and about 100°C, preferably between about 50°C
and about 100°C, and
most preferably between about 60°C and about 90°C.
It will be understood that the optimum dosage and concentration of the
enzymes, bleaching compounds, bleach stabilizers, and alkali agents (if used),
the
volume of the aqueous solution or wash liquor, and the pH and temperature will
vary,
depending on: (i) the nature of the fiber, i.e., crude fiber, yarn, or
textile; (ii) whether
simultaneous or sequential scouring and bleaching are carried out; (iii) the
particular
enzymes) used, and the specific activity of the enzyme; (iv) the conditions of
temperature, pH, time, etc., at which the processing occurs; (v) the presence
of other
components in the wash liquor; and (vi) the type of processing regime used,
i.e.,
continuous, discontinuous pad-batch, or batch. The optimization of the process
conditions can be determined using routine experimentation, such as, by
establishing a
matrix of conditions and testing different points in the matrix. For example,
the amount
of enzyme, the temperature at which the contacting occurs, and the total time
of
processing can be varied, after which the resulting cellulosic materials or
textile is
evaluated for (a) pectin removal; (b) a scoured property such as, e.g.,
wettability; and
(c) quality of bleaching, such as whiteness.
In a preferred embodiment, the conditions or treating composition may be
adjusted to favor the desizing, scouring or bleaching processes, such as, by
adjusting
pH, concentration of wetting agent, or concentration of divalent cationic
chelator such
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as ethylene diamine tetraacetate so as to further promote the bleaching
process. In a
preferred embodiment, the sequential mode may further comprise adjusting one
or
more properties of the composition of the aqueous solution or wash liquor
between
steps (ii) and (iii). For example, pH, concentration of wetting agent, or
concentration of
divalent cationic chelator, such as, ethylene diamine tetraacetate, may be
adjusted
between steps (ii) and (iii) so as to further promote the bleaching process.
The
conditions of the first and second incubations may also differ with respect to
temperature, agitation, time, and the like.
The following are intended as non-limiting illustrations of the present
invention.
Example 1: Simultaneous Bioscouring and Bleaching with HBO
A. Bioscouring and Bleaching: A 45 cm x 21.5 cm fabric weighing about 25
gram was cut from an interlock knit fabric (type 4600, Ramseur Co., NC). The
fabric
was loaded into a Labomat beaker (Mathis Labomat, Werner Mathis USA, Inc, NC),
which was then filled with 250 mL of 20mM sodium phosphate buffer solution
(pH9.2)
containing 3000 APSUIkg fiber of pectate lyase, 0.5g/1 wetting agent (Kierlon
Jet B,
BASF), 1.7g/L H~02, and 0.75g/1 stabilizer (Calgon, Dexter). The fabric was
treated at
55°C for 15 minutes after which temperature was raised at 5°C
/minute to 70°C for 1
hour. The fabric was then washed thoroughly with tap water to remove the
residual
chemicals and dried at room temperature overnight.
B. Analysis: Whiteness of the fabric was measured by a Macbeth color eye in
Ganz units. Wettability was determined by a drop test, measuring the time in
seconds
for a drop of water to be absorbed by the fabric.
The results are presented in Table 1. Both the whiteness and wettability of
the
fabric were very low. This example illustrates that bleaching the knitted
fabric with
hydrogen peroxide alone in the absence of alkali or bleach activators resulted
in limited
improvement in whiteness, wettability and mote removal.
Example 2: Simultaneous Bioscouring and Bleaching with
H20~ITAED
The same fabric and equipment were used as in Example 1 above. The
experiment was conducted in essentially the same manner as example 1, except
that
20mmol TAED (Aldrich) was added to the bioscouring/bleaching solution.
The results are shown in Table 1. The presence of TAED in the
bioscouring/bieaching bath dramatically improved the whiteness and wettability
of the
fabric. It also resulted in significant mote removal.
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Example 3: Simultaneous Bioscouring and Bleaching with
H~O~ITAEDINaOH
The same fabric and equipment were used as in Example 1 above. The
experiment was conducted in essentially the same manner as example 1, except
that
2g/1 NaOH was added to the bioscouring/bleaching solution.
The results are shown in Table 1. Surprisingly, unlike conventional peroxide
bleaching, addition of sodium hydroxide in the bioscouring/bleaching bath did
not
further improve the whiteness and wettability of the fabric. In fact, it had
some negative
impact on the whiteness and mote removal efficiency.
Example 4: Seauential Bioscouring and Bleaching with H~O~ITAED
A. Bloscouring: A 45 cm x 21.5 cm fabric weighing about 25 gram was cut
from an interlock knit fabric (type 4600, Ramseur Co., NC). The fabric was
loaded into
a Labomat beaker (Mathis Labomat, Werner Mathis USA, Inc, NC), which was then
filled with 250 mL of ZOmM sodium phosphate buffer solution (pH9.2) containing
3000
APSU/kg fiber of pectate lyase and 0.5811 wetting agent (Kierlon Jet B, BASF).
The
fabric was treated at 55°C for 15 minutes.
B. Bleaching: To the same beaker, add HZO2, TAED and Calgon. The final
concentrations of H202, TAED, and Calgon were the same as Example 2 above. The
Labomat temperature was raised at 5°C !minute to 70°C for 1
hour, after which the
water was drained. The fabric was then washed thoroughly with tap water to
remove
the residual alkali and dried at room temperature
The results are shown in Table 1. It is evident that the whiteness and
wettability
of the fabric from sequential bioscouring and bleaching process mode is better
than
that of the simultaneous mode (Example 2). The overall quality of the fabric
was the
best among the fabrics of Examples 1-10.
Example 5: Seauential Scouring and Bleaching with HZO~ITAED
The same fabric and equipment were used as described in Examples 1-4 above.
The experiment was conducted in essentially the same manner as example 4
above,
except that pectate lyase was absent from the scouring solution.
The results of whiteness and wettability are presented in Table 1 below. The
wettability of the fabric is very poor. This example demonstrates that the
presence of a
bioscouring enzyme is critical to the wettability of the fabric.
Example 6: Seauential Bioscourina and Bleaching with
HZO~ITAEDINaOH
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The same fabric and equipment were used as described in Examples 1-4 above.
The experiment was conducted in essentially the same manner as example 4
above,
except that 2gll NaOH was added to the bleaching solution.
The results were shown in Table 1 below. The whiteness of the fabric is much
lower than that of Example 4. This example further illustrates that addition
of sodium
hydroxide to the bleach bath will negatively affect the whiteness of the
fabric.
Table1. Single-bath bioscouring and bleaching of knitted fabrics
ExamplProcess ScourinBleachingWhitenesWettability,Motes
a # Mode g s,Ganz Seconds
82
Startin
9
Fabric g,5 >60 5
1 Single-bathEnzymePeroxide
Simultaneo
us 44.6 33 4
2 Single-bathEnzymePeroxide/
Simultaneo TAED
us 62.3 9 1
3 Single-bathEnzymePeroxide/
Simultaneo TAED/Na0
us H 59.7 10 2
4 Single-bathEnzymePeroxide/
Se uential TAED 63.4 2 1
Single-bathBufferPeroxide/
Se uential TAED 63.0 23 1
6 Single-bathEnzymePeroxide/
Sequential TAED/Na0
H 59.8 2 1
FKatlng of motes: ~: the tewest; 5: the most.
Example 7: Two-bath Scouring and Bleaching
The experiment was conducted in essentially the same manner as example 4
above, except that the scouring solution was drained and replaced with water
after the
bioscouring stage.
The results are shown in Table 2 below. The wettability of the fabric is good,
but
the whiteness and number of motes removed from the fabric are much lower than
that
from the simultaneous (Example 2) and sequential (Example 4) process mode.
Example 8: Two-bath Bioscourina and Bleaching
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The experiment was conducted in essentially the same manner as example 7
above, except that pectate lyase was absent from the scouring solution.
The results are shown in Table 2. Because of the absence of pectate lyase from
the bioscouring solution, the wettability of the fabric was very poor. This
example
further demonstrates that bioscouring enzyme is very important for improving
the
wettability of the fabric.
Example 9: Two-bath Scouring and Bleaching
The experiment was conducted in essentially the same manner as example 7
above, except that 2g/1 NaOH was added to the bleaching liquor.
The results are shown in Table 2. Addition of sodium hydroxide to the
bleaching
bath improved the whiteness of the fabric. This is contrary to what has been
observed
in the simultaneous and sequential process mode.
Example 10: Two-bath Bioscourina and Bleaching
The experiment was conducted in essentially the same manner as example 9
above, except that pectate lyase was absent from the scouring solution.
The results are shown in Table 1. This example further illustrates addition of
sodium hydroxide is necessary to improve the whiteness of the fabric in the
two-stage
process mode.
Table2. Two-bath bioscouring and bleaching of knitted fabrics
ExampleProcess ScourinBleaching WhitenesWettability,Motes
# Mode g s,Ganz Seconds
82
7 Two-bathEnzyme Peroxide/TA
ED 57.7 4 3
8 Two-bathBuffer Peroxide/TA
ED 56.9 >60 3
9 Two-bathEnzyme Peroxide/TA
ED/NaOH 59.1 5 2
Two-bathBuffer Peroxide/TA
ED/NaOH 59.6 10 2
'Rating of motes: 1: the fewest; 5: the most.
Example 11: Seauential Bioscourina and Bleaching with H~O~/NaOHITAED
A. Bioscouring: Fabric swatches were cut from 100% cotton knit interlock (type
4600, Ramseur Co, NC). The size of swatch is 19 cm x 19.5 cm and each swatch
is about
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7.5 gram. Two swatches were loaded into a Labomat beaker (Mathis Labomat,
Werner
Mathis USA, Inc. NC), which was then filled with 150m1 of 5mM sodium
bicarbonate buffer
(pH9.0) containing 3000 APSU/kg fabric of pectate lyase and 0.5 g/1 wetting
agent (I<ierlon
Jet B, BASF). The fabric was then treated at 55AC for 15 minutes.
B. Bleaching: To the same beaker, add 1g11 stabilizer (Prostogen N-S, BASF),
2gll NaOH, 2.5g/1 H20~ and 1.32 gll TAED. The Labomat temperature was raised
at
3AC/minute to 70AC for 1 hour. After which the water was drained. The fabric
was then
washed thoroughly with tap water to remove the residual alkali and dried at
room
temperature.
The results are shown in Table 3. Due to the addition of NaOH, the solution pH
was
10.83 at the end of the reaction. The whiteness of the fabric was measured by
a Macbeth
color eye in Ganz 82 unit. After enzymatic scouring and bleaching with
peroxide/NaOH/TAED, the whiteness has reached 67.61. The fabric wettability is
less than
1 second in a drop test according to AATCC Test Method 79-1995. Motes on the
fabric
almost completely disappeared.
Example 12: Seauential Bioscouring.and Bleaching with H~02INaOH
The same fabric and equipment were used as described in Example 11. The
experiment was conducted in essentially the same manner as Example 11 above,
except
that TAED was not added in the bleaching solution.
The results are shown in Table 3. The ending pH of reaction solution is 11.06,
which
is higher than that in Example 11. The whiteness is 62.64, which is much lower
than the
fabric whiteness in Example 11. A few motes are shown on fabric after the
treatment. The
higher ending pH, more motes, and lower fabric whiteness are due to the
absence of TAED,
thus a stronger bleaching agent is not generated in Example 12. Excellent
wettability of
fabric is also observed as indicated by 3 second wetting time, which indicates
the
effectiveness of enzymatic scouring.
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Example 13: Seauential Buffer Scouring and Bleaching with HZOZ/NaOHITAED
The same fabric and equipment were used as described in Example 11. The
experiment was conducted in essentially the same manner as Example 11 above,
except
that pectate lyase was not added in the bioscouring solution.
The results are shown in Table 3. The ending pH of reaction solution is 10.88,
similar to that in Example 11. There are almost no motes observed on fabric
after scouring
and bleaching, also similar to that observed in Example 11. The fabric
whiteness is 64.66,
which is lower than fabric whiteness in Example 11. Fabric wettability is over
60 seconds,
which is much worse than that in Example 11. The lower wettability and
whiteness are due
to the absence of enzyme in scouring.
Table 3
ExampleScouringBleaching EndingWhitenesslNettabilityMotes*
# H Ganz 82 Seconds
Starting
Fabric 8.5 >60 5
11 Enz Peroxide/NaOH/TAED10.83 67.61 <1 1
a
12 Enz Peroxide/NaOH 11.06 62.64 3 2
me
13 Buffer Peroxide/NaOH/TAED10.88 64.66 >60 1
FKatmg of motes: ~: the tewest; 5: the most.
Example 14: Seauential Bioscouring and Bleaching with H20 INaOHITAED
A. Bioscouring: A 19cm x 19.5 cm fabric swatch weighing about 7.5 gram
was cut from 100% cotton knit interlock (type 4600, Ramseur Co, NC). Two
swatches were
loaded into a Labomat beaker (Mathis Labomat, Werner Mathis USA, Inc. NC),
which was
then filled with 150m1 of 5mM sodium bicarbonate buffer (pH9.0) containing 0.1
g/1 of pectate
lyase (i.e. 3000APSU/kg fabric) and 0.5 g/1 wetting agent (Kierlon Jet B,
BASF). The fabric
was then treated at 556C for 15 minutes.
B. Bleaching: To the same beaker, add 4g/1 stabilizer (Prostogen N-S,
BASF), 4g/1 NaOH, 10g/1 HzOZ and 5.3 g/1 TAED. The Labomat temperature was
raised at
3AC/minute to 70AC for 1 hour. After which the water was drained. The fabric
was then
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washed thoroughly with tap water to remove the residual alkali, and it was
dried at room
temperature.
The results are shown in Table 4. Compared to Example 11, the same
enzymatic scouring is performed in this example. Less than 1 second water
absorbency
time indicates that excellent fabric wettability is obtained. On the other
hand, the bleaching
is conducted at higher chemical dose including higher concentrafions of NaOH,
HZOZ,
stabilizer and TAED. As the consequence of higher chemical concentration, a
higher fabric
whiteness 72.46 (Ganz 82) was obtained compared to fabric whiteness 67.61
obtained in
Example 11. All motes on fabric were completely removed in this example.
Example 15: Seauential Bioscourina and Bleaching with NaOH/H~O,
The same fabric and equipment were used as described in Example 14. The
experiment was conducted in essentially the same manner as in Example 14
above, except
that 2g/1 stabilizer, 5g/1 H202 were used in the bleaching solution.
As indicated in Table 4, fabric has whiteness of 71.56. The fabric whiteness
is lower than that in Example 14, which indicates the effectiveness of TAED.
Fabric also has
an excellent wettability as indicated by less than 1 second of water
absorbency in drop test.
Motes were completely removed.
Example 16: Seauential Buffer Scouring and Bleaching with H~O,INaOHITAED
The same fabric and equipment were used as described in Example 14. The
experiment was conducted in essentially the same manner as Example 14 above,
except
that pectate lyase was not added in the bioscouring solution.
The results are shown in Table 4. Compared to the results obtained in
Example 14, fabric in this example does not have industrial acceptable
wettability (e.g. <5
second). Due to lack of scouring effect, fabric whiteness is also lower than
that in Example
14. Motes on fabric were completely removed.
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Example 17: Seguential Buffer Scouring and Bleaching with NaOHIH~O,
The same fabric and equipment were used as described in Example 14. The
experiment was conducted in essentially the same manner as Example 14 above,
except
that pectate lyase was not added in the bioscouring solution and TAED was not
added in the
bleaching solution.
The results are shown in Table 4. Much longer water absorbency time than
that in Example 15 has demonstrated the effectiveness of pectate lyase enzyme
in scouring.
However, shorter water absorbency time than that in example 6 indicates that
addition of
TAED has no or negative impact on fabric wettability. On the other hand,
fabric whiteness
71.17 is lower that fabric whiteness 71.94 in Example 16. This indicates again
that the
addition of TAED results in an increase of fabric whiteness.
Table 4
Example Scouring Bleaching CIE WettabilityMotes
# Whiteness,(Seconds)
Ganz 82
14 Enz me Peroxide/NaOH/TAED72.46 <1 None
15 Enz me Peroxide/NaOH 71.56 <1 None
16 Buffer Peroxide/NaOHITAED71.94 >60 None
17 Buffer PeroxidelNaOH 71.17 46 None
Example 18: Effect of NaOH in Seguential Bioscourina and Bleachinct
A. Bioscouring: A 19cm x 19.5 cm fabric swatch weighing about 7.5 gram
was cut from 100% cotton knit interlock (type 4600, Ramseur Co, NC). Two
swatches were
loaded into a Labomat beaker (Mathis Labomat, Werner Mathis USA, Inc. NC),
which was
then filled with 150m1 of 5mM sodium bicarbonate buffer (pH9.0) containing 0.1
g/1 of pectate
lyase (i.e.3000APSU/kg fabric) and 0.5 g/1 wetting agent (Kierlon Jet B,
BASF). The fabric
was then treated at 55AC for 15 minutes.
B. Bleaching: To the same beaker, add 1g/1 stabilizer (Prostogen N-S,
BASF), 2.5g/1 H~O~ (Dexter Chemical) and 1.32 g/1 TAED (Peractive AN, which
has 84-88%
active TAED content, from Clariant Co.). Therefore, the molar ratio of H202 to
TAED is 14.7.
NaOH concentration varies from 0-4. g/1. The Labomat temperature was raised at
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38C/minute to 706C for 1 hour. After measuring the liquid pH at the end, the
water was
drained. The fabric was then washed thoroughly with tap water to remove the
residual alkali,
and it was dried at room temperature.
The results are shown in Table 5. As NaOH concentration increases, the
ending pH increases, the wettability measured as water absorbency time in
seconds
increases as shown in Table 5 The fabric whiteness in Ganz 82. Fabric
whiteness does not
increase initially with small amount addition of NaOH (corresponding to ending
pH range 5-
8). Fabric whiteness increases substantially when relatively large amount of
NaOH is added
to the bleaching bath.
Example 19: Effect of NaOH in Seduential Bioscouring and Bleaching
The same fabric and equipment were used as described in Example 18. The
experiment was conducted in essentially the same manner as Example 18 above,
except
that 2.65 g/1 TAED was used instead of 1.32 g/1. Therefore, the molar ratio of
Hz02 to TAED
is 7.35 in this example.
The results are shown in Table 5. Very similar results and conclusions are
obtained. As NaOH concentration increases, the ending pH increases, the
wettability
measured as water absorbency time in seconds increases as shown in Table 5.
Fabric
whifieness does not increase initially with small amount addition of NaOH
(corresponding to
ending pH range 5-8). Fabric whiteness increases substantially when relatively
large
amount of NaOH is added to the bleaching bath.
Furthermore, by comparing fabric whiteness of sample G in this example and
sample A in Example 18, it is evident that higher TAED dose in fabric G
treatment gives
higher whiteness when no NaOH is added. This indicates the effectiveness of
TAED at
acidic conditions. However, when large amount of NaOH is added (e.g. fabric a
vs. j), no
substantial whiteness difference is observed by the increase TAED from 1.32g/1
to 2.65g/1.
Table 5:
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kl2CllTAED GIIE
Foam ~anni ~aCtH Molar R_a~io lFir~atllltt~i~ertes~li~i
1e l< -JI H'
A 0 15 5.42 50.21 13
B 0.5 15 7.78 52.08 16
C 1 15 9.88 59.32 2
D 2 15 10.92 64.59 <1
E 3 15 11.41 65.98 <1
18 F 4 15 11.74 67.14 <1
G 0 7 4.85 54.89 2
H 1 7 8.48 55.29 6
I 2 7 10.64 66.02 2
J 3 7 11.18 66.76 <1
19 K 4 7 11.73 66.56 2
All patents, patent applications, and literature references referred to herein
are
hereby incorporated by reference in their entirety. Many variations of the
present
invention will suggest themselves to those skilled in the art in light of the
above
detailed description. Such obvious variations are within the full-intended
scope of the
appended claims.
