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Sommaire du brevet 2293600 

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L'apparition de différences dans le texte et l'image des Revendications et de l'Abrégé dépend du moment auquel le document est publié. Les textes des Revendications et de l'Abrégé sont affichés :

  • lorsque la demande peut être examinée par le public;
  • lorsque le brevet est émis (délivrance).
(12) Demande de brevet: (11) CA 2293600
(54) Titre français: TRAITEMENT DE TISSUS, VETEMENTS OU FILS AU MOYEN D'UNE HALOPEROXYDASE
(54) Titre anglais: TREATMENT OF FABRICS, GARMENTS, OR YARNS WITH HALOPEROXIDASE
Statut: Réputée abandonnée et au-delà du délai pour le rétablissement - en attente de la réponse à l’avis de communication rejetée
Données bibliographiques
(51) Classification internationale des brevets (CIB):
  • D06L 04/12 (2017.01)
  • D06M 16/00 (2006.01)
(72) Inventeurs :
  • WINKLER, JACOB (Danemark)
  • CONRAD, LARS SPARRE (Danemark)
(73) Titulaires :
  • NOVOZYMES A/S
(71) Demandeurs :
  • NOVOZYMES A/S (Danemark)
(74) Agent: NORTON ROSE FULBRIGHT CANADA LLP/S.E.N.C.R.L., S.R.L.
(74) Co-agent:
(45) Délivré:
(86) Date de dépôt PCT: 1998-06-09
(87) Mise à la disponibilité du public: 1998-12-17
Requête d'examen: 2003-05-27
Licence disponible: S.O.
Cédé au domaine public: S.O.
(25) Langue des documents déposés: Anglais

Traité de coopération en matière de brevets (PCT): Oui
(86) Numéro de la demande PCT: PCT/DK1998/000242
(87) Numéro de publication internationale PCT: DK1998000242
(85) Entrée nationale: 1999-12-06

(30) Données de priorité de la demande:
Numéro de la demande Pays / territoire Date
0673/97 (Danemark) 1997-06-09

Abrégés

Abrégé français

L'invention concerne un nouveau procédé de traitement de tissus, de vêtements ou de fils non teintés, consistant à traiter le tissu, le vêtement ou le fil non teinté dans un milieu aqueux au moyen d'une haloperoxydase, d'une source d'halogénure et d'une source de peroxyde d'hydrogène.


Abrégé anglais


A new method of treating undyed fabrics, garments, or yarn comprising treating
the undyed fabric, garment, or yarn in an aqueous medium with a
haloperoxidase, a halide source and a hydrogen peroxide source.

Revendications

Note : Les revendications sont présentées dans la langue officielle dans laquelle elles ont été soumises.


15
CLAIMS
1. A method of treating fabrics, garments, or yarns
comprising treating undyed fabric, garment, or yarn in an
aqueous medium with an effective amount of a haloperoxidase, a
halide source, and a hydrogen peroxide source.
2. A method according to claim 1, wherein the fabric,
garment, or yarn is a cellulosic fabric.
3. A method according to claim 1, wherein the fabric,
garment, or yarn is a silk fabric or a wool fabric.
4. A method according to claim 2, wherein the cellulosic
fabric is denim.
5. A method according to claim 1, wherein the haloperoxidase is
obtainable from fungi, from bacteria, or from algae.
6. A method according to claim 5, wherein the haloperoxidase is
obtainable from a fungus selected from the group consisting of
Caldariomyces, Alternaria, Curvularia, Drechslera, Ulocladium
and Botrytis.
7. A method according to claim 6, wherein the haloperoxidase is
obtainable from Curvularia.
8. A method according to claim 7, wherein the haloperoxidase
is obtainable from Curvularia verruculosa.
9. A method according to claim 5, wherein the haloperoxidase
is obtainable from a bacterium selected from the group
consisting of Pseudomonas and Streptomyces.
10. A method according to claim 1, wherein the concentration
of the haloperoxidase is in the range of from 0.01-100 mg
enzyme protein per liter.

16
11. A method according to claim 1, wherein the halide source
is sodium chloride, potassium chloride, sodium bromide,
potassium bromide, sodium iodide, or potassium iodide.
12. A method according to claim 1, wherein the source of
hydrogen peroxide is hydrogen peroxide, or a hydrogen peroxide
precursor, e.g., percarbonate or perborate, or a hydrogen
peroxide generating enzyme system, e.g., an oxidase and its
substrate, or a peroxycarboxylic acid or a salt thereof.
13. A method according to claim 11, wherein the concentration
of the halide source corresponds to 0.01-1000 mM.
14. A method according to claim 12, wherein the concentration
of the hydrogen peroxide source corresponds to a hydrogen
peroxide concentration in the range of from 0.01-1000 mM.
15. A method according to claim 1, wherein the haloperoxidase
is applied at a temperature below 70°C.
16. A method according to claim 1, wherein the aqueous medium
contains a surfactant.
17. A method of manufacturing a bleached fabric comprising
treating undyed fabric by the method of any of claims 1-16.
18. A method of manufacturing a bleached yarn comprising
treating undyed yarn by the method of any of claims 1-16.
19. A method of bleaching motes in a fabric comprising
treating undyed fabric by the method of any of claims 1-16.
20. A method of any of claims 17-19 wherein the fabric or yarn
is of cellulosic material.
21. A method of manufacturing fabrics, garments, or yarns
with improved shrink-resistance by the method of any of claims
1-16.

17
22. A method of manufacturing fabrics, garments, or yarns
with improved dye-uptake by the method of any of claims 1-16.
23. A method of any of claims 21-22 wherein the fabric,
garment, or yarn is of wool.

Description

Note : Les descriptions sont présentées dans la langue officielle dans laquelle elles ont été soumises.


CA 02293600 1999-12-06
WO 98/56976 PCT/DK98/00242
1
TREATMENT OF FABRICS, GARMENTS, OR YARNS WITH SALOPEROXIDASE
FIELD OF THE INVENTION
The present invention relates to a new method of treating
undyed fabrics, garments, or yarn comprising treating the
undyed fabric, garment, or yarn in an aqueous medium with a
haloperoxidase, a halide source and a hydrogen peroxide
source.
BACKGROUND OF THE INVENTION
Textiles composed of materials such as wool and, in
particular, cellulosics such as cotton, are frequently
bleached during manufacturing. Hydrogen peroxide is often used
as a bleaching agent. In addition to hydrogen peroxide, the
bleaching solutions will normally contain silicates, caustic
agents, chelators, organic stabilizers, magnesium salts, and
wetting agents. The bleaching treatment has two primary
functions; the first is to obtain a high level of whiteness,
and the second (when the textile is a cellulosic material) is
to break down and solubilize mote materials. Typical bleaching
conditions are 0.5-1.5% hydrogen peroxide, 0.5-2o sodium
silicate, 0.1-0.4o caustic, and 0.2o chelators at a
temperature of 100°C. WO 92/18683 describes a process for
bleaching dyed textiles with peroxidases and oxidases.
Furthermore, fabrics, garments, or yarns are sometimes
treated in order to improve dyeing characteristics such as dye
uptake.
Furthermore, fabrics, garments, or yarns of wool or other
animal hair fibers are sometimes treated in order to protect
3o against the tendency to shrink. Methods to generate shrink-
resistant fabrics, garments, or yarns are known. The most
commonly used method for wool is the IWS/CSIRO Chlorine
Hercosett process, which comprises an acid chlorination of
wool, followed by a polymer application. This process imparts
a high degree of shrink-resistance to wool, but adversely
affects the handle of wool, and generates environmentally
damaging waste. Other methods to reduce shrinkage of fabrics,
garments, or yarns which do not result in release of damaging
_.......__._._ __ . _..._. _ ___~ ____._ _~_4_.__

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2
substances to the environment have been described, including
processes such as low-temperature plasma treatments.
gU~ARY OF THE INVENTION
The object of the present invention is to provide an
enzyme-based method for treating fabrics, garments, or yarn,
in order to provide advantages with regard to improved
bleaching effect, dye uptake, and/or shrink-resistance, and by
which methods, it is possible to reduce fiber damage and limit
1o the use of environmentally damaging chemicals.
It has now been found that certain properties of fabrics,
garments, or yarn may be improved by subjecting the undyed
fabric, garment, or yarn to a treatment with a haloperoxidase
together with a hydrogen peroxide source and a halide source
15 in an amount effective for providing the desired effect.
One embodiment of the invention provides a method of
manufacturing a bleached fabric, garment or yarn comprising
treating undyed fabric, garment or yarn in an aqueous medium
with an effective amount of a haloperoxidase, a halide source
2o and a hydrogen peroxide source at a lower temperature
typically at 30-70°C than what is used in a traditional
hydrogen peroxide bleaching. This embodiment provides a
process for bleaching undyed fabric, garment or yarn at a
lower temperature than 100°C, and a bleaching process which
25 requires less chemicals than what is needed today. Another
embodiment provides a method of bleaching motes in a
cellulosic fabric, garment or yarn comprising treating undyed
fabric, garment or yarn in an aqueous medium with an effective
amount of a haloperoxidase, a halide source and a hydrogen
30 peroxide source.
Another embodiment of the invention provides a method of
manufacturing fabrics, garme..ts, or yarns with improved
shrink-resistance or dye uptake. The fabric, garment, or yarn
is preferably of wool.
35 Other aspects of the invention will become apparent from
the following detailed description and the claims.

CA 02293600 1999-12-06
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3
DETAILED DESCRIPTION OF THE INVENTION
Before the methods of the invention are described, it is
to be understood that this invention is not limited to the
particular methods described. The terminology used herein is
for the purpose of describing particular embodiments only, and
is not intended to be limiting since the scope of the present
invention will be limited only by the appended claims.
As used in this specification and the appended claims,
to the singular forms "a", "an", and "the" include plural
references unless the context clearly dictates otherwise.
Thus, for example, references to "haloperoxidase" or
"haloperoxidase preparation" include mixtures of such
haloperoxidase, reference to "the method" includes one or more
methods, and/or steps of the type described herein and/or
which will become apparent to those persons skilled in the art
upon reading this disclosure and so forth.
Unless defined otherwise, all technical and scientific
terms used herein have the same meaning as commonly understood
2o by one of ordinary skill in the art to which the invention
belongs. Although any methods and materials similar or
equivalent to those described herein can be used in the
practice or testing of the present invention, the preferred
methods and materials are now described. All publications
mentioned herein are incorporated herein by reference for the
purpose of disclosing and describing the material for which
the reference was cited in connection with.
The term "undyed" refers to fabric, garment, or yarn that
has not fully completed a dyeing process. Dyeing may
optionally be carried out during or after the method according
to the invention. Preferably the enzyme treatment is carried
out before the dyeing step.
The term "bleaching" is here defined as a whitening of
the fabric, garment, or yarn, and can be measured by using the
change in the color space coordinates L*a*b* (CIELAB-system): L*
gives the change in white/black at a scale of from 0 to 100. A
decrease in L* means an increase in black colour (decrease of
white colour), an increase in L* means an increase in white
_...... ..._........_.w.w v~._...__....._ -,.,-, .._.. _._._ _...... ..._
....~._.~,_..~...r._...,... .

CA 02293600 1999-12-06
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4
colour (a decrease in black colour). Bleaching may also be
measured using Stensby units (W = L + 3a - 3b).
Fabric can be constructed from fibres by weaving,
knitting or non-woven operations. Weaving and knitting require
yarn as the input whereas a non-woven fabric is the result of
random bonding of fibres (paper can be thought of as non-
woven).
Woven fabric is constructed by weaving "filling" or weft
yarns between wrap yarns stretched in the longitudinal
direction on the loom. The wrap yarns must be sized before
weaving in order to lubricate and protect them from abrasion
at the high speed insertion of the filling yarns during
weaving. The filling yarn can be woven through the warp yarns
in a "over one - under the next" fashion (plain weave) or by
"over one - under two" (twill) or any other myriad of
permutations. Strength, texture and pattern are related not
only to the type/quality of the yarn but also the type of
weave. Generally, dresses, shirts, pants, sheeting's, towels,
draperies, etc. are produced from woven fabric.
2o Knitting is forming a fabric by joining together
interlocking loops of yarn. As opposed to weaving which is
constructed from two types of yarn and has many "ends",
knitted fabric is produced from a single continuous strand of
yarn. As with weaving, there are many different ways to loop
yarn together and the final fabric properties are dependent
both upon the yarn and the type of knit. Underwear, sweaters,
socks, sport shirts, sweat shirts, etc. are derived from knit
fabrics.
Non-woven fabrics are sheets of fabric made by bonding
3o and/or interlocking fibres and filaments by mechanical,
thermal, chemical or solvent-mediated processes. The resultant
fabric can be in the form of web-like structures, laminates or
films. Typical examples are disposable baby diapers, towels,
wipes, surgical gowns, garments for the "environmental
friendly" fashion, filter media, bedding, roofing materials,
backing for two-dimensional fabrics and many others.
According to the invention, the process may be applied to
any fabric known in the art (woven, knitted, or non-woven). In
t ___._. __.____.~._______ ________..._.~..~_w____... _..._..._-~._~._.._

CA 02293600 1999-12-06
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particular the bleaching process may be applied to cellulose-
containing or cellulosic fabrics, such as cotton, viscose,
rayon, ramie, linen, lyocell (e.g., Tencel, produced by
Courtaulds Fibers), or mixtures thereof, or mixtures of any of
5 these fibres, or mixtures of any of these fibres together with
synthetic fibres (e. g., polyester, polyamide, nylon) or other
natural fibers such as wool and silk. The term "wool" includes
any commercially useful animal hair product, for example, wool
from sheep, camel, rabbit, goat, or llamas, and includes wool
1o fiber and animal hair. The method of the invention can be used
with wool or animal hair material in the form of top, fiber,
yarn, or woven or knitted fabric. The enzymatic treatment can
also be carried out on loose flock or on garments made from
wool or animal hair material.
The treatment can be performed at many different stages
of processing.
~he term "shrinkage" refers to the felting shrinkage of
fibers as defined in IWS TM 31, i.e., felting shrinkage is the
irreversible shrinkage caused by progressive entanglement of
2o the wool fibers induced by washing in an aqueous solution, and
is defined as the reduction in length and/or width induced by
washing. Shrinkage can be measured in accordance with IWS TM
31, or it can be measured using the following modification.
Wool samples (24 cm x 24 cm) are sewed around the edges and
inscribed with a rectangle (18 cm x 18 cm). Samples are
treated, air-dried, then subjected to five cycles of machine
washing and drying (warm wash, high heat of drying) in
combination with external ballast such as towels and articles
of clothing. The dimensions of the rectangle are measured
after five cycles, and the shrinkage is defined as the change
in dimensions of the rectangle, after accounting for initial
relax<~tion shrinkage.
The term "shrink-resistance" is a measure of the
reduction in shrinkage (as defined above, after wash/dry
cycles) for material that has been treated relative to
material that has not been treated, i.e.,
................_ _.....~____~-_~__ __..._..__..._ _ .___.~ ...

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6
Shrink-resistance= ( Shrinkage"ntrearea -
Shrlrikagetreated) /Shririkagetreated
The value is multiplied by 100 in order to be expressed as a
percentage.
The term "dye uptake" refers to properties associated
with dyeing of fabrics, garments or yarn such as of wool or
animal hair material. Dye uptake is a measure of the capacity
of wool or animal hair material immersed in a dye solution to
to absorb available dyestuff. This property can be measured by
the following test. In a suitable reaction vessel, wool or
animal hair material is added to a buffered solution of acid
black 172 (300 ml of 0.05 M NaOAc buffer, pH 4.5, plus 7.5 mL
of a 1.0% w/w solution of acid black 172 in water). The
vessel is incubated in a shaking water bath at 50°C for 15
minutes with mild agitation. After removal of the material
from solution, it is allowed to air-dry, then measured in a
suitable spectrophotometer to determine CIELAB values. Dye
uptake is determined by the L* reading, and changes in dye
uptake are found by determining dL* relative to untreated
material.
"Mote" particles are dark brown particles found on
unbleached cotton fabric, also called "dark spots". They are
cotton pod and stem residues originating from the mechanical
picking of cotton. The brown colour is due to the high lignin
content of the mote particles.
Haloperoxidases
In the context of the present invention, the term "haloper-
oxidase" is intended to mean an enzyme selected from the group
consisting of chloride peroxidase (EC 1.11.1.10), bromide
peroxidas=, and iodide peroxidase (EC 1.11.1.8).
A chloride peroxidase is an enzyme capable of oxidizing
chloride, bromide and iodide ions with the consumption of H202 .
A bromide peroxidase is an enzyme capable of oxidizing
bromide and iodide ions with the consumption of H202.
A iodide peroxidase is an enzyme capable of oxidizing iodide
ions with the consumption of H20~.
_... _~.__._._____~._~.._.-._....-.d _..~_._.. _ _......_ .~

CA 02293600 1999-12-06
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7
Haloperoxidases form a class of enzymes capable of oxidizing
halides (X = C1-, Br-, or I-) in the presence of hydrogen
peroxide to the corresponding hypohalous acid (HOX) according
to the equation:
H20z + X- + H+ -> H20 + HOX
If an appropriate nucleophile is present, a reaction will
occur with HOX, whereby bleaching may take place.
to Haloperoxidases have been isolated from various organisms:
mammals, marine animals, plants, algae, a lichen, fungi and
bacteria (for reference see Biochimica et Biophysica Acta 1161,
1993, pp. 249-256). It is generally accepted that
haloperoxidases are the enzymes responsible for the formation
of halogenated compounds in nature, although other enzymes may
be involved.
Haloperoxidases have been isolated from many different
fungi, in particular from the fungus group dematiaceous hypho-
mycetes, such as Caldariomyces, e.g., C. fumago, Alternaria,
Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera,
Ulocladium and Botrytis (see US Patent No. 4,937,192).
According to the present invention, a haloperoxidase
obtainable from Curvularia, in particular C. verruculosa, is
preferred. Curvularia haloperoxidase and recombinant production
thereof is described in WO 97/04102.
Haloperoxidase has also been isolated from bacteria such as
Pseudomonas, e.g., P. pyrrocinia (for reference see The Journal
of Biological Chemistry 263, 1988, pp. 13725-13732) and
Streptomyces, e.g., S. aureofaciens (for reference see Struc-
3o tural Biology 1, 1994, pp. 532-537).
Bromide peroxidase has been isolated from algae (see US
Patent No. 4,937,192).
In use, the concentration of the haloperoxidase may be
varied in order to achieve the desired bleaching effect in the
desired time frame. However, according to the invention, the
haloperoxidase will normally be added in a concentration of
0.01-100 mg enzyme protein per liter, preferably in a concen-
tration of 0.1-50 mg enzyme protein per liter, more preferably

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8
in a concentration of 1-10 mg enzyme protein per liter.
Halide Sources
According to the invention, the halide source for the
reaction with haloperoxidase may be achieved in many different
ways: The halide source may be sodium chloride, potassium
chloride, sodium bromide, potassium bromide, sodium iodide, or
potassium iodide. The concentration of the halide source will
typically correspond to 0.01-1000 mM, preferably in the range
of from 0.1-500 mM.
Hydrogen Peroxide Sources
According to the invention, the hydrogen peroxide needed for
the reaction with the haloperoxidase may be achieved in many
different ways: It may be hydrogen peroxide or a hydrogen
peroxide precursor, such as percarbonate or perborate, or a
peroxycarboxylic acid or a salt thereof, or it may be a
hydrogen peroxide generating enzyme system, such as an oxidase
and its substrate. Useful oxidases include glucose oxidase, a
glycerol oxidase or an amino acid oxidase. An example of an
amino acid oxidase is given in WO 99/25574.
2o According to the invention, the hydrogen peroxide source
needed for the reaction with the haloperoxidase may be added in
a concentration corresponding to a hydrogen peroxide
concentration in the range of from 0.01-1000 mM, preferably in
the range of from 0.1-500 mM.
Process
The chosen procedure will depend on the haloperoxidase in
question, regarding pH optimum, temperature optimum, etc.
If a haloperoxidase from Curvularia verruculosa is used,
the processing conditions could be:
30-70°C, pH 5, using 1-5 mg enzyme/liter, 50-500 mM halide
(e.g. sodium chloride), 20 mM hydrogen peroxide, at a
liquor/fabric ratio of from 4:1-30:1, for a reac'W_on time of
30-120 min. (as illustrated in Example 1).
A buffer may be added to the reaction medium to maintain a
suitable pH for the haloperoxidase used. The buffer may
suitably be a phosphate, borate, citrate, acetate, adipate,
triethanolamine, monoethanolamine, diethanolamine, carbonate
(especially alkali metal or alkaline earth metal, in par-
..~....__ ~.. . _ ___.

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9
ticular sodium or potassium carbonate, or ammonium and HC1
salts), diamine, especially diaminoethane, imidazole, or amino
acid buffer.
The process of the invention may be carried out in the
presence of conventional fabric, garment, or yarn finishing
agents, including wetting agents, polymeric agents, dispersing
agents, etc.
A conventional wetting agent may be used to improve the
contact between the substrate and the enzyme used in the
l0 process. The wetting agent may be a nonionic surfactant, e.g.,
an ethoxylated fatty alcohol. A very useful wetting agent is
an ethoxylated and propoxylated fatty acid ester such as Berol
087 (product of Akzo Nobel, Sweden).
Bx<smples of suitable polymers include proteins (e. g.,
bovine serum albumin, whey, casein or legume proteins),
protein hydrolysates (e. g., whey, casein or soy protein
hydrolysate), polypeptides, lignosulfonates, polysaccharides
and derivatives thereof, polyethylene glycol, polypropylene
glycol, polyvinyl pyrrolidone, ethylene diamine condensed with
ethylene or propylene oxide, ethoxylated polyamines, or
ethoxylated amine polymers.
The dispersing agent may suitably be selected from
nonionic, anionic, cationic, ampholytic or zwitterionic
surfactants. More specifically, the dispersing agent may be
selected from carboxymethylcellulose, hydroxypropylcellulose,
alkyl aryl sulphonates, long-chain alcohol sulphates (primary
and secondary alkyl sulphates), sulphonated olefins, sulphated
monoglycerides, sulphated ethers, sulphosuccinates,
sulphonated methyl ethers, alkane sulphonates, phosphate
esters, alkyl isothionates, acylsarcosides, alkyltaurides,
fluorosurfactants, fatty alcohol and alkylphenol condensates,
fatty acid condensates, condensates of ethylene oxide with an
amine, condensates of ethylene oxide with an amide, sucrose
esters, sorbitan esters, alkyloamides, fatty amine oxides,
ethoxylated monoamines, ethoxylated diamines, alcohol
ethoxylate and mixtures thereof. A very useful dispersing
agent is an alcohol ethoxylate such as Berol 08 (product of
Akzo Nobel, Sweden).

CA 02293600 1999-12-06
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The bleaching processing may be performed in any machinery
known in the art.
Inactivation of the haloperoxidase in question will
normally not be necessary; however if an inactivation of the
5 enzyme is wanted it may be performed as known in the art,
e.g., high temperature and/or high pH, but the specific
inactivation conditions will of course depend on the enzyme in
use.
The fabric may be further finished by one or more of the
10 following treatments as known in the art: dyeing,
biopolishing, brightening, softening, and/or anti-wrinkling
treatment(s).
Test Procedure
The test procedure for fabric bleaching may be performed
visually and by using a Minolta Chroma Meter CR200, a Minolta
Chroma Meter CR300 or a Minolta Chroma Meter 5081.
Evaluation: A Minolta Chroma Meter (available from Minolta
Corp.) is used according to Manufacturer's instructions to
evaluate the degree of bleaching as well as to estimate any
2o discoloration using the change in the colour space coordinates
L*a*b* (CIELAB-system) : L* gives the change in white/black at a
scale of from 0 to 100, a* gives the change in green (-a*)/red
(+a*) , and b* gives the change in blue (-b*) /yellow (+b*) . A
decrease in L* means an increase in black colour (decrease of
white colour), an increase in L* means an increase in white
colour (a decrease in black colour), a decrease in a means an
increase in green colour (decrease in red colour), an increase
in a* means an increase in red colour (a decrease in green
colour), a decrease in b* means an increase in blue colour (a
3o decrease in yellow colour), and an increase in b* means an
increase in yellow col~ ~Y (a decrease in blue colour).
The instrument is c .~.brated using a standard calibration
plate (white).
The invention is further illustrated in the following
examples, which are not intended to be in any way limiting to
the scope of the invention as claimed.
_r ........ _.~~.___.__.... _.__-__.._..T.

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EXAMPLE 1
Bleaching of raw cotton swatches with Curvularia verruculosa
haloperoxidase
Experimental conditions:
The bleaching system contained 3 mg/1 recombinant
Curvularia verruculosa haloperoxidase with [NaCl]=100 mM as
substrate and [H202]=20 mM as donor. pH was adjusted to pH=5.
The swatches were bleached for 60 minutes at 40°C. (The
enzyme was produced as described in WO 97/04102).
The bleaching system was tested on twill cotton swatches and
woven cotton swatches.
For twill fabric the fabric/liquor ratio was: 1 g of fabric
in 15 ml of aqueous medium.
For woven fabric the fabric/liquor ratio was: 1 g of fabric
in 20 ml of aqueous medium.
Results:
2o Significant visual bleaching was obtained with the
experimental conditions described above.
Note that the blind test assures that the observed
bleaching effect is enzymatic in nature.
The bleaching results are presented in the Table 1 below:
__._
~..__~.~_~______.~.-~__._.

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12
~L*/Da*/Ob* on raw cotton swatchesa.
Bleaching Twillb Wovenb
system
Blind (-)0.2 / 0.1 / 0.0 (-)0.2 / 0.0 / (-)0.1
Enzymes 2.5 / (-)0.9 / (-)1.5 1.6 / (-)0.6 / (-)1.3
a: Measurements were all done on a Minolta 5081.
Lamp was set to D65 and 2°.
b: Desized swatches obtained from Test Fabrics.
~: System consists of NaCl, hydrogen peroxide and acetate
buffer.
s: System consists of haloperoxidase, NaCl, hydrogen peroxide
and acetate buffer.
to
EXAMPhE 2
Bleaching of motes with Curvularia verruculosa haloperoxidase
Experimental conditions:
The bleaching system was the same as described in Example
1: 3 mg/1 recombinant Curvularia verruculosa haloperoxidase
with [NaCl]=100 mM as substrate and [Hz02]=20 mM as donor. pH
was adjusted to pH=5.
2o The swatches were bleached for 60 minutes at 90°C in an
Atlas LP2 Lauder-o-meter. Linen woven 1000 cotton was supplied
by Nordisk Textil V~veri & Trykkeri A/S. The fabric/liquor
ratio was 1 g of fabric in 20 ml of aqueous medium.
Results
Motes were counted on a fabric area of 10 cm x 15 cm (on
both sides).
A mote was defined as a "dark spot" on the cotton surface
irrespective of size.
3o Double determination of the mote bleaching effect was
carried out.
The numbers 1 and 2 in Table 2 refer to the separate
fabric cloths used.
?. __.__..~..___..T ______... .L

CA 02293600 1999-12-06
WO 98/56976 PCT/DK98/00242
13
Note that a positive difference in mote count can be due
to the motes splitting up due to the mechanical handling of
the fabric cloth.
Table 2:
Mote Mote count Difference
count
before after in
mote
bleaching bleac hing count
Side of Side Side Side Side Side Side2
fabric cloth 1 2 1 2 1
Reference 1 85 74 91 71 - +6 -3
Reference 2a 78 68 69 70 -9 +2
Blind 1~' 60 50 62 52 +2 +2
Blind 2b 72 74 77 75 +5 +1
Enzymatic l~ 53 62 49 42 -4 -20
Enzymatic 2~ 68 62 41 56 -27 -6
a: Fabric washed in buffer only.
b: Conditions as described above in the experimental section
1o but without added enzyme.
~: Conditions as described above in the experimental section.
The reference tests illustrate the effects of the
mechanical washing procedure and as can be seen from Table 2,
the loss of motes is ambiguous. (The mechanical washing
procedure has no significant effect on the number of motes
left on the cloth after the bleaching.)
Table 2 shows that there is a significant loss of motes
when submitting the fabric cloth to the enzymatic bleaching
2o conditions. The blind test assures that the observed effect is
enzymatic in nature.

CA 02293600 1999-12-06
WO 98/56976 PCT/DK98/00242
14
EXAMPLE 3
Treatment of wool with Curvularia verruculosa haloperoxidase
_Experimental conditions:
The enzyme system was the same as described in Example 1:
3 mg/1 recombinant Curvularia verruculosa haloperoxidase with
[NaCl]=100 mM as substrate and [Hz02]=20 mM as donor. pH was
adjusted to pH=5.
Swatches (24 cm x 24 cm, approx. 10 g each) of TF532
Jersey Knit Wool were cut and sewn around the edge with a
Burger. A permanent marker was used to draw an 18 x 18
rectangle on each swatch.
Results:
Treatment Shrinkage
( o)
Blind 29
Enzymatic 23
__._.

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États administratifs

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Historique d'événement

Description Date
Inactive : CIB désactivée 2021-11-13
Inactive : CIB désactivée 2021-11-13
Inactive : CIB désactivée 2021-11-13
Inactive : CIB désactivée 2021-11-13
Inactive : CIB enlevée 2021-01-20
Inactive : CIB enlevée 2021-01-20
Inactive : CIB en 1re position 2021-01-20
Inactive : CIB attribuée 2021-01-20
Inactive : CIB enlevée 2021-01-20
Inactive : CIB expirée 2017-01-01
Inactive : CIB expirée 2017-01-01
Inactive : CIB expirée 2017-01-01
Inactive : CIB expirée 2013-01-01
Inactive : CIB de MCD 2006-03-12
Inactive : CIB de MCD 2006-03-12
Inactive : CIB de MCD 2006-03-12
Inactive : CIB de MCD 2006-03-12
Inactive : CIB de MCD 2006-03-12
Demande non rétablie avant l'échéance 2005-06-09
Le délai pour l'annulation est expiré 2005-06-09
Réputée abandonnée - omission de répondre à un avis sur les taxes pour le maintien en état 2004-06-09
Lettre envoyée 2003-07-03
Requête d'examen reçue 2003-05-27
Exigences pour une requête d'examen - jugée conforme 2003-05-27
Toutes les exigences pour l'examen - jugée conforme 2003-05-27
Modification reçue - modification volontaire 2003-05-27
Lettre envoyée 2001-05-11
Inactive : Page couverture publiée 2000-02-16
Inactive : CIB en 1re position 2000-02-15
Inactive : CIB attribuée 2000-02-15
Inactive : CIB attribuée 2000-02-15
Inactive : Notice - Entrée phase nat. - Pas de RE 2000-01-27
Lettre envoyée 2000-01-27
Demande reçue - PCT 2000-01-24
Demande publiée (accessible au public) 1998-12-17

Historique d'abandonnement

Date d'abandonnement Raison Date de rétablissement
2004-06-09

Taxes périodiques

Le dernier paiement a été reçu le 2003-06-02

Avis : Si le paiement en totalité n'a pas été reçu au plus tard à la date indiquée, une taxe supplémentaire peut être imposée, soit une des taxes suivantes :

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Historique des taxes

Type de taxes Anniversaire Échéance Date payée
TM (demande, 2e anniv.) - générale 02 2000-06-09 1999-12-02
Taxe nationale de base - générale 1999-12-02
Enregistrement d'un document 1999-12-02
Enregistrement d'un document 2001-01-12
TM (demande, 3e anniv.) - générale 03 2001-06-11 2001-04-20
TM (demande, 4e anniv.) - générale 04 2002-06-10 2002-06-10
Requête d'examen - générale 2003-05-27
TM (demande, 5e anniv.) - générale 05 2003-06-09 2003-06-02
Titulaires au dossier

Les titulaires actuels et antérieures au dossier sont affichés en ordre alphabétique.

Titulaires actuels au dossier
NOVOZYMES A/S
Titulaires antérieures au dossier
JACOB WINKLER
LARS SPARRE CONRAD
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Description du
Document 
Date
(aaaa-mm-jj) 
Nombre de pages   Taille de l'image (Ko) 
Description 1999-12-05 14 634
Abrégé 1999-12-05 1 42
Revendications 1999-12-05 3 84
Avis d'entree dans la phase nationale 2000-01-26 1 195
Courtoisie - Certificat d'enregistrement (document(s) connexe(s)) 2000-01-26 1 115
Rappel - requête d'examen 2003-02-10 1 112
Accusé de réception de la requête d'examen 2003-07-02 1 173
Courtoisie - Lettre d'abandon (taxe de maintien en état) 2004-08-03 1 175
PCT 1999-12-05 10 306
Correspondance 2001-02-14 1 23
Correspondance 2001-05-10 3 109