CN1723272A - Preparation of cellulosic materials - Google Patents
Preparation of cellulosic materials Download PDFInfo
- Publication number
- CN1723272A CN1723272A CNA028130634A CN02813063A CN1723272A CN 1723272 A CN1723272 A CN 1723272A CN A028130634 A CNA028130634 A CN A028130634A CN 02813063 A CN02813063 A CN 02813063A CN 1723272 A CN1723272 A CN 1723272A
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- CN
- China
- Prior art keywords
- enzyme
- cellulosic materials
- bleaching
- enzyme system
- biological degumming
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
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Classifications
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L1/00—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L1/00—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods
- D06L1/12—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods using aqueous solvents
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L1/00—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods
- D06L1/12—Dry-cleaning or washing fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods using aqueous solvents
- D06L1/14—De-sizing
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
- D06L4/10—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
- D06L4/10—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen
- D06L4/12—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen combined with specific additives
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
- D06L4/10—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen
- D06L4/13—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen using inorganic agents
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06L—DRY-CLEANING, WASHING OR BLEACHING FIBRES, FILAMENTS, THREADS, YARNS, FABRICS, FEATHERS OR MADE-UP FIBROUS GOODS; BLEACHING LEATHER OR FURS
- D06L4/00—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs
- D06L4/40—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using enzymes
Abstract
The present invention provides methods and compositions for desizing, scouring and bleaching of cellulosic materials, which are carried out by contacting the cellulosic materials simultaneously or sequentially in a single-bath process with an enzyme system and a bleaching system comprising hydrogen peroxide or at least one peroxy compound which generates hydrogen peroxide when dissolved in water, or combinations thereof, and at least one bleach activator.
Description
Invention field
The present invention relates to handle the method and composition of cellulosic materials (cellulosic materials), more properly relate to and be used for destarch (desizing), come unstuck (scouring) and the method and composition of bleached fiber quality.
Background of invention
Cellulosic materials, for example cotton fibre are processed into clothes manufacturing raw material will involve some steps: with the fiber spun yarn; From braiding of yarn structure or knitting fabric; Be prepared subsequently, dyeing and housekeeping operation.Preparation process may involve destarch (being used for yarn fabric), comes unstuck and bleach, and produces to be suitable for the textiles that dyes or put in order.
A. destarch: yarn fabric is the principal mode of textile fabric structure.Fabrication processes requires the yarn " starching " with bending, avoids wearing and tearing to protect it.After fabrication processes, must remove slurry, as the first step of preparation yarn fabric.Starch, polyvinyl alcohol, carboxymethyl cellulose, wax and acryloid cement are the examples of typical sizing agent commonly used in the industry.Good in order to ensure whiteness height and/or colouring power, slurry and other coating must thoroughly be removed.Generally believe, effectively destarch for subsequently preparation process, promptly come unstuck and bleaching process is conclusive.---rope form or open shape---contacts with the process fluid that contains desizing agent to make the fabric after the starching.The desizing agent that is adopted depends on the type of the slurry that will remove.Modal cotton fabric sizing agent is based on starch.Therefore, often be that combination by hot water, α-Dian Fenmei and wetting agent or tensio-active agent makes the spun cotton fabric desizing.
B. come unstuck: the process of coming unstuck is removed most of natural non-cellulose compounds that see in the cotton.Except natural non-cellulosic impurity, come unstuck and to remove the material that residual manufacturing is introduced, for example spinning, coning tower tray or isolate lubricant.The conventional process of coming unstuck is utilized the highly chemical treatment of alkalescence usually, and this has not only removed impurity, has also weakened the cellulosic component of fiber or fabric.After the chemical Degumming is to clean widely, to reduce the danger of redeposited impurity.Clean insufficient meeting and on fabric, form the inhomogeneous removing of alkaline resistates and impurity, and then it is inhomogeneous to cause dyeing in process subsequently.In addition, because chemical that is adopted and the material that extracts from fiber, chemical Degumming can produce environmental problem on effluent is disposed.The someone proposes to come unstuck as the alternative of chemical Degumming process with enzyme, and for example WO 98/24965, and WO 00/71808, and JP 6220772, and JP 10088472, U.S. Patent No. 5,912,407; Hartzell et al., Textile Res.68:233 (1998); Hsieh et al., Textile Res.69:590 (1999); Buchertet al., Text.Chem.Col.﹠amp; Am.Dyestuff Reptr.32:48 (2000); Liet al., Text.Chem.Color.29:71 (1997).
C. bleaching: the bleaching of textiles is the final preparation process during textile fabric and clothes are made.The purpose of bleaching is to remove foreign pigment fully, improves absorptivity and realizes suitable whiteness and colouring power.The most extensive bleaching process that is used in the textile industry is the alkaline hydrogen peroxide method.Conventional textile bleaching is bathed and is contained usually: sodium hydroxide, tensio-active agent, optical brightener, stablizer and SYNTHETIC OPTICAL WHITNER.Bleaching stage can be in batch, carry out in the semicontinuous or successive process.When in the destarch or the process of coming unstuck, using enzyme, high quality results for the unanimity that obtains commercialization quantity textiles, the destarch and the step of coming unstuck are normally separated with blanching step and are carried out, because alkaline peroxide bleaching requires high temperature and basicity, be very difficult so enzyme process and alkaline peroxide bleaching were united in the single stage.
Summary of the invention
The invention provides cellulosic materials mono bath (single-bath) destarch, come unstuck and bleaching method, cellulosic materials is the textiles of robust fibre, yarn, knitting (knit) or braiding (woven) for example, by cotton, linen, flax, ramie, artificial silk, hemp, jute or these fibers each other or the adulterant of or synthon natural with other.
This method is performed such, and cellulosic materials and (i) enzyme system are contacted with (ii) bleaching system; In containing the same solution of cellulosic materials to be processed to some extent, add enzyme system and bleaching system, destarch, come unstuck and blanching step between not emptying bathe (without emptying the bath) or clean cellulosic materials, mono bath process just.Can add enzyme system and bleaching system simultaneously to solution.Select as an alternative, can successively add enzyme system and bleaching system to solution, wherein (i) make cellulosic materials under proper condition with the enzyme system full contact time, so that effectively biological degumming (bioscouring) and/or destarch (ii) directly add bleaching system to the solution that contains cellulosic materials and enzyme system then.
In one embodiment of the invention, the method of handling cellulosic materials is disclosed, comprise cellulosic materials (i) is contacted with enzyme system, the destarch and/or the biological degumming that are used for cellulosic materials, (ii) contact with bleaching system, comprise hydrogen peroxide or at least a compound or its combination and at least a bleach-activating agent (bleach activator) that when water-soluble, generates hydrogen peroxide, wherein add enzyme system and bleaching system to the single solution while or the priority that contain cellulosic materials.
In another embodiment, the method of handling cellulosic materials is disclosed, comprise cellulosic materials (i) is contacted with enzyme system, the destarch and/or the biological degumming that are used for cellulosic materials, (ii) contact with bleaching system, comprise hydrogen peroxide or at least a compound or its combination and at least a bleach-activating agent that when water-soluble, generates hydrogen peroxide, wherein add enzyme system and bleaching system, and under the adding that does not have alkali, contact to the single solution while or the priority that contain cellulosic materials.
In another embodiment, the method of handling cellulosic materials is disclosed, comprise cellulosic materials (i) is contacted with enzyme system, the destarch and/or the biological degumming that are used for cellulosic materials, (ii) contact with bleaching system, comprise hydrogen peroxide or at least a compound or its combination and at least a bleach-activating agent that when water-soluble, generates hydrogen peroxide, wherein add enzyme system and bleaching system to the single solution while or the priority that contain cellulosic materials, and under high pH, contact, preferred more than 9.
Method and composition of the present invention provides a kind of like this product, it shows as, and hydroscopicity (wettability) is high, whiteness (whiteness) is high and dedusting (mote removal) is even, have the advantage that is better than conventional preparation process simultaneously, comprising: (i) process period is shorter; (ii) preserved moisture; (iii) reduced the waste liquid outflow.
Detailed Description Of The Invention
Cellulosic materials
" cellulosic materials " used herein expression cellulosic substrate to be processed comprises cotton, linen, flax, ramie, artificial silk, hemp, jute and they and other adulterants natural or synthon without limitation.Cellulosic materials can also comprise textiles or fabric or the clothes or the finished product of robust fibre, yarn, knitting or braiding without limitation.
Enzyme system
The used enzyme system of the present invention is represented biological degumming enzyme system and/or destarch enzyme system.Therefore, enzyme system can comprise one or more biological degumming enzymes, have or not one or more destarch enzymes all can, perhaps one or more destarch enzymes have or not one or more biological degumming enzymes all can.Preferably, enzyme system and following condition are compatible: (i) bleaching is carried out simultaneously with biological degumming and/or destarch process, and perhaps (ii) bleaching is successively carried out with biological degumming and/or destarch process, and is as described herein.
The destarch enzyme:
Any suitable destarch enzyme can be with in the present invention.Preferably, the destarch enzyme is an amylolytic enzyme.More preferably, the destarch enzyme is α-or beta-amylase and combination thereof.
Be suitable for α of the present invention-and beta-amylase comprise those of bacterium or originated from fungus.Also comprise this kind of starch enzyme mutant through modifying in chemistry or heredity in this.Preferred α-Dian Fenmei for example comprises the α-Dian Fenmei that can obtain from the bacillus bacterial classification, is specially the Bacillus licheniformis bacterial strain, such as GB 1296839 detailed description.Preferred amylase comprises Duramyl
TM, Termamyl
TM, Fungamyl
TMWith BAN
TM(all can be from Novozymes AIS, Bagsvaerd, Denmark obtains) and Rapidase and Maxamyl (can be from Gist-Brocades, Holland obtains).Other preferred amylolytic enzymes have the CGT enzyme (cyclodextrin glucanotrasferase enzyme, EC2.4.1.19), those that obtain from bacillus, Thermoanaerobactor or Thermoanaero-bacterium bacterial classification for example.
The destarch enzyme also can preferably be derived from above-mentioned enzyme, and wherein one or more amino acid are added into, leave out or replace, and comprises the hybrid polypeptide, as long as gained polypeptide performance destarch is active.Can be used for implementing this class variant of the present invention and can utilize conventional mutagenesis technology to produce, for example utilize high throughput screening technology to be differentiated, for example the agar plate screening technology.
Amount to the aqueous solution or washing lotion (being treatment compositions) adding destarch enzyme is enough to make the cellulosic materials destarch.Usually, the amount that adds destarch enzyme, for example α-Dian Fenmei to treatment compositions is 0.00001% to 2% zymoprotein, weight by composition, be preferably 0.0001% to 1% zymoprotein, by the weight of composition, 0.001% to 0.5% zymoprotein more preferably is by the weight of composition, and then 0.01% to 0.2% zymoprotein more preferably, by the weight of composition.The usage level of destarch enzyme is preferably about 2-30,000KNU/I, and 20-30 more preferably, 000KNU/I most preferably is 200-300KNU/I, perhaps about 3-50,000NAU/I is preferably 30-5, and 000NAU/I most preferably is 350-500NAU/I.
The biological degumming enzyme:
Any suitable biological degumming enzyme can be with in the present invention.Preferred biological degumming enzyme comprises polygalacturonase, proteolytic enzyme, lipase, at and combination thereof without limitation, and more preferably, the biological degumming enzyme is a polygalacturonase, and then more preferably, the biological degumming enzyme is pectate lyase (pectate lyase).
Polygalacturonase: any pectin decomposing enzyme composition with ability of degrading plant cell walls combination of pectins may be used to implement the present invention.The polygalacturonase that is fit to comprises those of fungi or bacterial origin without limitation.The polygalacturonase of also containing chemistry or genetic modification.Preferably, polygalacturonase used in this invention is that reorganization produces, and is the single component enzyme.
Polygalacturonase can be according to their preferential substrate---the pectin of high methyl-esterified or the pectin of low methyl-esterified and polygalacturonic acid (polygalacturonic acid) (pectate (pectate)), with their reaction mechanism, β-cancellation or hydrolysis are classified.Polygalacturonase can be based on interior-functionality, and random site cutting polymer in chain obtains the mixture of oligomer, and perhaps they can be outer-functionalities, from the end game of polymkeric substance, generates monomer or dipolymer.Some pectin that act on are smoothly distinguished the pectinase activity of (smooth region) and are included in the enzyme classification that is provided by Enzyme Nomenclature (1992), for example pectate lyase (EC 4.2.2.2), pectin lyase (EC 4.2.2.10), polygalacturonase (EC3.2.1.15), outer-polygalacturonase (exo-polygalacturonase) (EC3.2.1.67), outer-Polygalacturonate lyase (EC 4.2.2.9) and outer-gather-α-galacturonic neuraminidase (EC 3.2.1.82).
In preferred implementation of the present invention, polygalacturonase is the pectate lyase.The enzymic activity of pectate lyase used herein is represented by shifting the cancellation effect to α-1 in the pectic acid (also claiming polygalacturonic acid), the cracked katalysis at random of 4-glycosidic link.The pectate lyase is also referred to as Polygalacturonate lyase and poly-(1,4-α-D-galacturonic acidifying thing) lyase.
Any pectate lyase may be used to implement the present invention.In preferred embodiment, this method is utilized the pectate lyase of performance maximum activity under about temperature more than 70 ℃.The pectate lyase also can preferably show maximum activity under about pH more than 8, and/or do not add divalent cation in the presence of show enzymic activity, calcium ion for example.The limiting examples of pectate lyase used in this invention comprises the pectate lyase that belongs to the clone from different bacteriums, for example erwinia, Rhodopseudomonas, klebsiella and xanthomonas, and subtilis (Nasser et al. (1993) FEBS Letts.335:319-326) and genus bacillus YA-14 (Kim et al. (1994) Biosci.Biotech.Biochem.58:947-949).The purifying that has the pectate lyase of maximum activity in the pH scope of also having described at 8-10, they are by following bacteriogenic: bacillus pumilus (Dave and Vaughn (1971) J.Bacteriol.108:166-174), bacillus polymyxa (Nagel and Vaughn (1961) Arch.Biochem.Biophys.93:344-352), bacstearothermophilus (Karbassi and Vaughn (1980) Can.J.Microbiol.26:377-384), genus bacillus (Hasegawa and Nagel (1966) J.Food Sci.31:838-845) and genus bacillus RK9 (Kelly and Fogarty (1978) Can.J.Microbiol.24:1164-1172).Arbitrarily above-mentioned and divalent cation independence and/or thermostability pectate lyase may be used to implement the present invention.In preferred embodiment, the pectate lyase comprises the al. as Heffron et, (1995) Mol.Plant MicrobeInteract.8:331-334 and Henrissat et al., the aminoacid sequence of the disclosed pectate lyase of (1995) Plant Physiol.107:963-976.
The amount of mixing polygalacturonase in enzyme aqueous solution or washing lotion can be 0.00001% to 2% zymoprotein, weight by composition, be preferably 0.0001% to 1% zymoprotein, weight by composition, 0.001% to 0.5% zymoprotein more preferably, by the weight of composition, and then 0.01% to 0.2% zymoprotein more preferably, by the weight of composition.It is about 2.5 to 500 that the usage level of polygalacturonase is preferably, and the 000APSU/g fabric is more preferably about 25 to 50, the 000APSU/g fabric, most preferably be about 250 to 5, the 000APSU/g fabric.
Proteolytic enzyme: can adopt any proteolytic enzyme of the present invention that is applicable to.The proteolytic enzyme that is fit to comprises animal, plant or microbe-derived those, the preferred microorganism source.Preferably, proteolytic enzyme can be serine protease or metalloprotease, more preferably alkaline microbial protease or trypsin-like proteolytic enzyme.The example of proteolytic enzyme comprises aminopeptidase, comprises prolyl aminopeptidase (3.4.11.5), X-pro aminopeptidase (3.4.11.9), bacterium leucylamino peptase (3.4.11.10), thermophilic aminopeptidase (3.4.11.12), lysylamino peptase (3.4.11.15), tryptophyl aminopeptidase (3.4.11.17) and methionyl aminopeptidase (3.4.11.18); The Serine endopeptidase comprises Quimotrase (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); The Gelucystine endopeptidase, comprise papoid (3.4.22.2), ficain (3.4.22.3), Disken (3.4.22.6), asclepain (asclepain) (3.4.22.7), actinidain (3.4.22.14), caricain (3.4.22.30) and ananain (3.4.22.31); The aspartic acid endopeptidase comprises that pepsin A (3.4.23.1), aspergillus pepsinogen I (3.4.23.18), Penicillopepsin (Penicillopepsin) are (3.4.23.20) and sugared stomach en-(3.4.23.25); And Zinc metalloproteinase, comprise Bacillolysin (3.4.24.28).
Commercial available proteolytic enzyme comprises Alcalase, Savinase, Primase, Duralase, Esperase, Kannase and Durazym (Novozymes A/S), Maxatase, Maxacal, Maxapem, Properase, Purafect, Purafect OxP, FN2, FN3 and FN4 (Genencor International Inc.).
Also can be used for of the present invention is ease variants, for example be 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 etal., (1985), Nature.318, p.375-376, Thomas et al., (1987), J.Mol.Biol., 193, pp.803-813, Russel et al., (1987), Nature, 328, p.496-500, WO 88/08028 (Genex), WO 88/08033 (Amgen), WO 89/06279 (Novozymes A/S), WO 91/00345 (Novozymes A/S), among EP 525,610 (Solvay) and the WO 94/02618 (Gist-Brocades N.V.) those.Protease activities can be as " Methods of Enzymatic Analysis ", and the 3rd edition, 1984, Verlag Chemie, Weinheim, vol.5 is described to be measured.
The amount of mixing proteolytic enzyme to enzyme aqueous solution or washing lotion is preferably 0.00001% to 2% zymoprotein, weight by composition, be preferably 0.0001% to 1% zymoprotein, weight by composition, 0.001% to 0.5% zymoprotein more preferably, by the weight of composition, and then 0.01% to 0.2% zymoprotein more preferably, by the weight of composition.
Lipase: can use any lipase of the present invention that is applicable to.The lipase (also claiming carboxylic ester hydrolase) that is fit to preferably includes those of bacterium or originated from fungus, comprises that triacylglycerol lipases (triacylglycerol lipases) (3.1.1.3) and Phospholipase A2 (3.1.1.4).Lipase used in this invention comprises the lipase from Humicola (synonym is Thermomyces) without limitation, for example from H.lanuginosa (T.lahuginosus), as EP 258,068 and EP 305,216 is described, perhaps from H.insolens, as described in WO 96/13580; Rhodopseudomonas lipase, for example from Pseudomonas alcaligenes or pseudomonas pseudoalcaligenes (EP218,272), (EP 331 for pseudomonas cepacia, 376), Situ Ci Shi pseudomonas (GB1,372,034), Pseudomonas fluorescens, pseudomonad strain SD 705 (WO 95/06720 and WO96/27002), P.wisconsinensis (WO 96/12012); Bacillus lipase is for example from Bacillus subtilus (Dartois et al., Biochem.Biophys.Acta, 1131:253-360,1993), bacstearothermophilus (JP 64/744992) or bacillus pumilus (WO91/16422).Other examples are as WO 92/05249, WO 94/01541, EP 407,225, EP 260,105, WO 95/35381, WO 96/00292, WO 95/30744, WO 94/25578, WO 95/14783, WO 95/22615, WO 97/04079 and WO 97/07202 described lipase Variant.Preferred commercial available lipase comprises Lipolase and LipolaseUltra, Lipozyme, Palatase, Novozym 435 and Lecitase
TM(NovovozymesA/S).The activity of lipase can be as " Methods of Enzymatic Analysis ", and the 3rd edition, 1984, Verlag Chemie, Weinhein, vol.4 is described to be measured.
The amount of mixing lipase to enzyme aqueous solution or washing lotion is preferably 0.00001% to 2% zymoprotein, weight by composition, be preferably 0.0001% to 1% zymoprotein, weight by composition, 0.001% to 0.5% zymoprotein more preferably, by the weight of composition, and then 0.01% to 0.2% zymoprotein more preferably, by the weight of composition.
At: can use any at of the present invention that is applicable to, for example comprise that as U.S. Patent No. 4,810,414 embodiment 2 are described from Humicola insolens at strain DSM 1800 deutero-at.
The amount of mixing to enzyme aqueous solution is preferably 0.00001% to 2% zymoprotein, weight by composition, be preferably 0.0001% to 1% zymoprotein, weight by composition, 0.001% to 0.5% zymoprotein more preferably, by the weight of composition, and then 0.01% to 0.2% zymoprotein more preferably, by the weight of composition.
The biological degumming enzyme that is fit to for example comprises also that wherein one or more amino acid are added into, leave out or replace, and comprise the hybrid polypeptide from above-mentioned enzyme deutero-biological degumming enzyme, as long as gained polypeptide performance biological degumming is active.Can be used for implementing this class variant of the present invention and can utilize conventional mutagenesis technology to produce, for example utilize high throughput screening technology to be differentiated, for example the agar plate screening technology.For example, the pectate lyase can be measured like this, and test solution is coated in punching press 4mm hole in agar plate (for example LB agar), wherein contains 0.7%w/v polygalacturonic acid sodium (SigmaP1879).Then flat board was cultivated 6 hours down at specified temp (for example 75 ℃).Then flat board (i) was soaked 0.5 hour in 1M CaCl2, perhaps (ii) in 1% blended bromination alkyltrimethylammonium (MTAB, Sigma M-7635), soaked 1 hour.These two kinds of technologies all cause Polygalacturonate to be deposited in the agar.In the sedimentary galacturonic hydrochlorate background of institute, clarifying zone occurs, detect the activity of pectate lyase.Sensitivity is measured in the diluent calibration of use standard pectate lyase prepared product.
Utilization is effectively come unstuck and is improved hydroscopicity usually according to the dropping liquid experimental measurement of AATCC test method 39-1980.Preferably, the hydroscopicity of the fabric after the bleaching be 20 seconds or below, most preferably be 10 seconds or below.
Destarch used in this invention and biological degumming enzyme can be the cell source deutero-from them, perhaps can be that reorganization produces, and can be purifying or isolating." purifying " used herein or " isolating " enzyme are a kind of like this enzymes, and it is processed, and to remove non-enzyme material or other from cell-derived enzyme, wherein it is a synthetic, can the interferases activity.Usually, destarch and biological degumming enzyme are isolating from bacterium or fungi microbe, and wherein it is produced as endogenous component or recombinant products.If enzyme is secreted in the substratum, so purifying can comprise utilize ordinary method by centrifugal, filter or precipitation is come isolation medium and biomass.Select as an alternative, can from host cell, discharge enzyme with separating of biomass by cytoclasis.In some cases, can realize further purifying by the method for purifying protein of routine, comprise ammonium sulfate precipitation without limitation; Acid or chaotropic agent extraction; Ion-exchange, molecular sieve and hydrophobicity chromatogram comprise FPLC and HPLC; Preparation type iso-electric point is assembled; With preparation type polyacrylamide gel electrophoresis.Select as an alternative, can utilize affinity chromatography to realize purifying, comprise immunoaffinity chromatography.For example, can use hybrid reorganization pectate lyase, it has extra aminoacid sequence, serves as affinity " mark ", and this helps utilizing suitable solid-phase matrix to carry out purifying.
With in the methods of the invention destarch and biological degumming enzyme can also be through chemically modified, to strengthen one or more character, gives they and then more advantage, for example improves solubleness, reduces unstable or divalent ion dependency etc.Modification comprises phosphorylation, acetylize, sulfation, acidylate or other protein modification effects well known by persons skilled in the art without limitation.
Bleaching system
Any bleaching system can be with in the present invention, and it is compatible with the destarch and/or the used condition of coming unstuck, no matter (i) destarch and/or come unstuck and bleaching process carries out simultaneously, still (ii) destarch and/or come unstuck and bleaching process is that priority is carried out.Preferably, bleaching system comprises at least a bleaching compounds, at least a bleach-activating agent and optional at least a bleaching stibilizer, and is as described below.
Bleaching compounds:
Bleaching compounds is hydrogen peroxide or generate the compound of hydrogen peroxide when water-soluble preferably, for example peralcohol.The examples for compounds that generates hydrogen peroxide when water-soluble that is fit to has alkali metal perborate or alkaline carbonate perhydrate, especially sodium salt.Amount to the aqueous solution or washing lotion adding bleaching compounds hydrogen peroxide is preferably about 0.01 to about 10g/l aqueous solution or washing lotion, and more preferably 0.1 to 5g/l, most preferably is 0.5 to 2.5g/l.Add the compound that generates hydrogen peroxide the amount of---for example alkali metal perborate or alkaline carbonate---is preferably about 0.001 to the 20g/l aqueous solution or washing lotion to the aqueous solution or washing lotion, and more preferably about 0.1 to 10g/l, most preferably is about 0.5 to 5g/l.
Bleach-activating agent:
Any suitable bleach-activating agent can be with in the present invention.The bleach-activating agent that preferably uses according to the present invention for example comprises the compound of following kind: many acidylates sugar or sugar derivatives can be used as bleach-activating agent, and they have C
1-10-acyl group atomic group, preferred ethanoyl, propionyl, capryloyl, nonanoyl or benzoyl atomic group, preferred especially ethanoyl atomic group.Operable sugar or sugar derivatives are monose or disaccharides and their reduction or oxidized derivatives, preferred glucose, seminose, fructose, sucrose, wood sugar or lactose.Particularly suitable bleach-activating agent for example has five acetyl glucose, wood sugar tetraacethyl, 1-benzoyl-2,3,4 in this class material, 6-tetrem acyl glucose and 1-decoyl-2,3,4,6-tetrem acyl glucose.
The another kind of preferred material that is used as bleach-activating agent in the present invention comprises acyloxy Phenylsulfonic acid and their basic metal and alkaline earth salt, for example C
1-14-acyl group atomic group.Ethanoyl, propionyl, capryloyl, nonanoyl and benzoyl atomic group are preferred, especially ethanoyl atomic group and nonanoyl atomic group.Particularly suitable bleach-activating agent is acetoxyl group Phenylsulfonic acid and benzoyloxy Phenylsulfonic acid in this class material.Preferably adopt their sodium-salt form.
Other bleach-activating agents used in this invention comprise MMA and OCL, single with or each other or with the TAED coupling; O-acyl group oxime ester, for example acetone O-acetyl oxime (acetoneO-acetyloxime), acetone O-benzoyl oxime, two (third imino-) carbonic ether, two (hexamethylene imino-) carbonic ether.Can be according to the present invention as the acidylate oxime of bleach-activating agent for example as described in the EP-A-0028432.Can be according to the present invention as the oxime ester (oxime esters) of bleach-activating agent for example as described in the EP-A-0267046.
Preferred in addition bleach-activating agent comprises the N-acyl caprolactam, for example the two hexanolactams of N-acetyl hexanolactam, N-benzoyl caprolactam, N-decoyl hexanolactam and carbonyl; N, N-two acidylates and N, N, N ', N '-four acylated amine, N for example, N, N ', N '-tetra acetyl methylene diamine and-quadrol (TAED), N, diacetanilide N,, N, N-diacetyl-right-Tolylamine or 1,3-two acidylate glycolylurea, for example 1,3-diacetyl-5,5-T10; N-alkyl-N-alkylsulfonyl acid amides, for example N-methyl-N-methylsulfonyl ethanamide or N-methyl-N-methylsulfonyl benzamide; N-acidylate ring-type hydrazides, acidylate triazole or urazole, for example monoacylated Regulox; O, N, the trisubstituted azanol of N-, O-benzoyl-N for example, N-succinyl-azanol, O-acetyl-N, N-succinyl-azanol or O, N, N-triacetyl azanol; N, N '-diacyl sulphonamide (diacylsulfamides), N for example, N '-dimethyl-N, N '-diacetyl sulphonamide or N, N '-diethyl-N, N '-two propionyl sulphonamide; Three acyl group cyanurates, for example triacetyl cyanurate or tri-benzoyl cyanurate; Carboxylic acid anhydride, for example benzoyl oxide, chloro-benzoic acid acid anhydride or Tetra hydro Phthalic anhydride; 1,3-diacyl-4,5-two acyloxy tetrahydroglyoxalines, for example 1,3-diacetyl-4,5-diacetoxy tetrahydroglyoxaline; Tetrem acyl glycoluril and four propionyl glycolurils; Two acidylates 2,5-diketo-piperazine, for example 1,4-diacetyl-2,5-diketo-piperazine; The third two ureas and 2, the acylate of 2-dimethyl propylene two ureas, for example four levulinics, two ureas; Many acyl groups of alpha-acyloxy Malonamide, α-acetoxyl group-N for example, N '-diacetyl Malonamide; Diacyl dioxo six hydrogen-1,3,5-triazines, for example 1,5-diacetyl-2,4-dioxo six hydrogen-1,3,5-triazines; The 2-alkyl-or the 2-aryl-(4H)-3,1-benzoxazine-4-ketone, for example as described in EP-B1-0332294 and the EP-B0502013, with 2-phenyl-(4H)-3,1-benzoxazine-4-ketone and 2-methyl-(4H)-3,1-benzoxazine-4-ketone, the positively charged ion nitrite, for example EP303520 and EP458396A1 are described, and for example TMA (TriMethylAmine) is for acetonitrile, N, and the hot ammonium of N-dimethyl-N-is for the metilsulfate or the tosylate of acetonitrile, 2-(TMA (TriMethylAmine) generation) propionitrile, 2-(TMA (TriMethylAmine) generation)-2-methyl propionitrile.N methyl piperazine generation-N, N '-diacetonitrile and methylmorpholine also are fit to for the metilsulfate of acetonitrile (MMA).
Bleach-activating agent used in this invention in addition comprised that carboxylamine (percarbamicacid) or diacyl crossed carbamate and precursor thereof.
The add-on of bleach-activating agent is generally about 0.1 to 30g/l, and more preferably 0.5 to 10g/l.
Bleaching stibilizer:
In another kind of preferred implementation of the present invention, bleaching system contains one or more bleaching stibilizers in addition.Bleaching stibilizer comprises and can adsorb, the additive of bonding or ligand compound trace heavy metal.The example that can use according to the present invention, have the additive of bleach stable effect has polyanion compound, for example polyphosphate, multi-carboxylate, multi-hydroxy multi-carboxy acid's salt, soluble silicate, they are neutral basic metal or alkaline earth salt wholly or in part, definite is neutral Na or Mg salt, and they are weak relatively bleaching stibilizers.The example of the strong bleaching stibilizer that can use according to the present invention has Synergist S-421 95, for example edetate (EDTA), diethylene triaminepentaacetic acid(DTPA) (DTPA), complexon I (NTA), methylglycine oxalic acid (MGDA), Beta-alanine oxalic acid (ADA), quadrol-N, N '-disuccinate (EDDS) and phosphonates, for example ethylenediamine tetramethylene phosphonic acid salt, diethylenetriamine pentamethylenophosphonic acid(DTPP) salt (DTMPA) or hydroxy ethylene-1, the sour form of 1-di 2 ethylhexyl phosphonic acid or neutral alkali metal salt partially or completely.
The amount that adds bleaching stibilizer to treatment compositions is generally about 0.1 to about 5g/ and rises composition, and more preferably about 0.5 to about 2g/l, most preferably is about 1g/l.
Preferably contain at least a bleaching stibilizer according to bleaching composition of the present invention, more preferably at least a above-mentioned strong bleaching stibilizer.Effectively bleaching brings one or more following character usually: (i) required whiteness (measure by Ganz whiteness method of masurement, for example use Macbethcoloreye); (ii) dedusting homogeneity satisfactory (by macroscopic evaluation).Preferably, the whiteness of fabric is a 50Ganz unit or higher, most preferably is 60Ganz unit or higher.
Therefore, in preferred embodiment, the mono bath process comprises enzyme system (for example pectate lyase), hydrogen peroxide, bleach-activating agent (for example TAED) and bleaching stibilizer.
Alkaline agent:
Alkaline agent is well known in the art.Preferred alkaline agent used in this invention comprises sodium hydroxide, yellow soda ash, sodium bicarbonate, Sodium peroxoborate, sodium sulphite and S-WAT.But, in some embodiment, preferably mono bath process be do not have alkaline agent in the presence of carry out, definitely when the cellulosic materials of handling the alkalescence sensitivity, for example silk and wool.
Extra component:
In some invention embodiment, the aqueous solution or washing lotion further comprise other components, comprise other enzymes without limitation, and tensio-active agent, antifoams, lubricant, synergistic device, they strengthen comes unstuck and/or bleaching process, and/or excellent effect is provided, for example with intensity, resist into ball (resistance to pilling), water-absorbent is relevant with colouring power.
The enzyme that is suitable for use among the present invention comprises aforesaid polygalacturonase, proteolytic enzyme and lipase without limitation; And cellulase.Cellulase is included into a series of enzyme families, in containing-and with outward-activity and cellobiose hydrolysis ability.Being used to implement cellulase of the present invention can be from the microorganism deutero-, known they can produce cellulolytic enzyme, for example the bacterial classification of Humicola, Thermomyces, bacillus, Trichoderma, fusarium, myceliophthora, Phanerochaete, rake Pseudomonas, Scytalidium, Schizophyllum, Penicillium, Aspergillus or Geotrichum definitely is Humicola insolens, fusarium oxysporum or Trichoderma reesei.The limiting examples of the cellulase that is fit to is disclosed in U.S. Patent No. 4,435, and 307, among european patent application No.0495257, PCT patent application No.WO91/17244 and the european patent application No.EP-A2-271004.
Enzyme can be isolating from their cell source, perhaps can be that reorganization produces, and can be through modifying in chemistry or heredity.Usually, the level of mixing enzyme in the aqueous solution is about 0.0001% to about 1% zymoprotein, and by the weight of composition, more preferably about 0.001% to about 0.5%, most preferably is 0.01% to 0.2%.Self-evidently be to utilize conventional assay method to determine easily additionally to unite unit of enzyme activity's number of using enzyme in the methods of the invention with the particular organisms degummase about every kind.
Be suitable for implementing tensio-active agent of the present invention and comprise non-ionic type (U.S. Patent No. 4,565,647) without limitation; Anionic; Cationic; And amphoteric ionic surfactant (U.S. Patent No. 3,929,678); Their concentration usually between about 0.2% to about 15%, by weight, preferably from about 1% to about 10%, by weight.Aniorfic surfactant comprises linear alkylbenzene sulfonate, sulfonated, alkyl-sulphate (aliphatic alcohol sulfate), alcohol ethoxy vitriol, secondary paraffin sulfonate, alpha-sulfo fatty acid methyl ester, alkyl-or thiazolinyl-succsinic acid and soap class without limitation.Nonionic surface active agent comprises the N-acyl group N-alkyl derivative (glucamide (glucamide)) of alcohol ethoxylate, nonyl phenol ethoxylate, alkyl polyglycoside, alkyl dimethyl amine oxide, ethoxylated fatty acid single ethanol amide, fatty monoethanol amide, polyhydroxy alkyl fatty acid amide and glycosamine without limitation.
Synergistic device comprises silico-aluminate, silicate, multi-carboxylate, lipid acid without limitation, such as material and metal ion chelation agents such as edetates, aminopolyphosphonic acid salt for example, definite is ethylenediamine tetramethylene phosphonic acid and diethylenetriamine pentamethylenophosphonic acid(DTPP), their concentration is between about 5% to 80%, by weight, preferably between about 5% and about 30%, by weight.
Antifoams comprises silicone (U.S. Patent No. 3,933,672) without limitation; DC-544 (DowCorning), their concentration is usually between about 0.01% and about 1%, by weight.
Composition can also contain soil-suspending agent, soil releasing agent (soil-releasingagent), optical brightener, abrasive and/or sterilant, and they are well known in the art.
Processing conditions:
Whether the mode that the aqueous solution that contains enzyme and bleaching system is contacted with cellulosic materials will depend on the processing system is successive, discontinuous pad-batch or batch-wise.For example, process about continuous or discontinuous pad-batch, enzyme aqueous solution is preferably included in the saturated bath, bathes and is coated with continuously thereon along with cellulosic materials passes, and cellulosic materials absorbs 0.5-1.5 usually doubly to the working fluid of its weight during this process.In batch operation, make cellulosic materials be exposed to enzyme solution and reach about 5 minutes to 24 hours, working fluid is 5 with the ratio of fabric: 1-50: 1.
The pH of the aqueous solution or washing lotion is usually between about 4 and about 11.Preferably, the pH of treatment compositions preferably between about 7 to about 9, most preferably is about 8 to about 9 between about 5 and about 10.
In one embodiment, the one-bath process that is used to handle cellulosic materials is to carry out under the adding that does not have alkali.Preferably, this facture is used to handle alkali-sensitive cellulosic materials, for example silk and wool.In another embodiment, the one-bath process that is used to handle cellulosic materials is to carry out being lower than under 9 the pH, more preferably less than 8, and then more preferably less than 7.
In another embodiment, the one-bath process that is used to handle cellulosic materials is to carry out under the adding of alkali.Preferably, contact be about 8 or above pH under carry out, more preferably pH9 or more than, for example pH9-11 is preferably 9.5-10.5, more preferably 10-11.Add alkaline agent and can control pH, for example NaOH.The amount that adds alkaline agent can be from about 0.1 to about 10%, by the weight of fabric, to obtain required pH degree of being.But, will figure out as the technician, the amount that adds alkaline agent will depend on the amount of used bleaching compounds.
The temperature slurry that carries out combination degumming and/or destarch and bleaching process depends on used process.Under the situation of cold pad-batch process, come unstuck and/or destarch and bleaching temperature preferably between about 15 ℃ and about 45 ℃, most preferably between about 25 ℃ and about 35 ℃.About successive and other process in batch, come unstuck and/or the destarch temperature preferably between about 35 ℃ and about 75 ℃, most preferably between about 45 ℃ and about 65 ℃; Bleaching temperature can be between about 30 ℃ and about 100 ℃, preferably between about 50 ℃ and about 100 ℃, most preferably between about 60 ℃ and about 90 ℃.
Self-evidently be, the optimal dose of enzyme, bleaching compounds, bleaching stibilizer and alkaline agent (if you are using) and the volume of concentration, the aqueous solution or washing lotion and pH and temperature will be different because of following factors: (i) attribute of fiber, just robust fibre, yarn or textiles; (ii) whether simultaneously or successively to come unstuck and bleach; The (iii) used specific enzyme and the specific activity of enzyme; Conditions such as the temperature of (iv) processing, pH, time; (the v) existence of other components in the washing lotion; (type of vi) used processing system, just successive, discontinuous pad-batch or in batch.The optimization of processing conditions can utilize habitual experimental technique to be determined, for example sets up basic condition, tests the difference in the basis again.For example, enzyme amount, contact temperature and total process period can have nothing in common with each other, and estimate (a) pectin elimination efficiency of gained cellulosic materials or textiles afterwards; (b) come unstuck character, for example hydroscopicity; (c) Piao Bai quality, for example whiteness.
In preferred embodiment, can adjusting condition or treatment compositions, the concentration of---for example edetate---further promotes bleaching process helping destarch, to come unstuck or bleaching process, for example by regulating the concentration or the divalent cation chelators of pH, wetting agent.In preferred embodiment, successively pattern can further be included in one or more character that step is regulated the aqueous solution or washing lotion composition (ii) and (iii).For example, can be (ii) and the concentration or the divalent cation chelators of regulating pH, wetting agent (iii) in step the concentration of---for example edetate---, with further promotion bleaching process.For the first time also can be different at aspects such as temperature, stir speed (S.S.), times with the condition of cultivating for the second time.
Embodiment
Be to non-limiting illustrating of the present invention below.
Embodiment 1: utilize H
2O
2Biological degumming and bleaching simultaneously
A. biological degumming and bleaching: (4600 types, Ramseur Co. NC) cut the heavily about 25 45cm * 21.5cm fabrics that restrain from binding type knit goods.With the fabric Labomat beaker (MathisLabomat that packs into, Werner Mathis USA, Inc, NC), pour 250ml 20mM buffer solution of sodium phosphate (pH9.2) then into, wherein contain the 3000APSU/kg fiber pectate lyase, 0.5g/l wetting agent (Kierlon Jet B, BASF), 1.7g/l H
2O
2With the 0.75g/l stablizer (Calgon, Dexter).Fabric was handled 15 minutes down at 55 ℃, be warming up to 70 ℃ by 5 ℃/minute afterwards and reach 1 hour.Then fabric is thoroughly washed with tap water, to remove residual chemical, at room temperature dried overnight.
B. analyze: by the whiteness of Macbeth color eye measurement fabric, with the Ganz unit representation.By dropping liquid test determination hydroscopicity, measure a water by the time that fabric absorbs, show with stopwatch.
The results are shown in the table 1.The whiteness of fabric and hydroscopicity all are low-down.This example shows, places an order in the existence that does not have alkali or bleach-activating agent and improves whiteness, hydroscopicity and efficiency of dust collection with the knitting fabric of hydrogen peroxide bleaching only limitedly.
Embodiment 2: utilize H
2O
2/ TAED is biological degumming and bleaching simultaneously
Use fabric and the equipment identical with last example 1.Experimentize according to identical with example 1 in essence mode, except adding 20mmol TAED (Aldrich) to biological degumming/liquid lime chloride.
The result is as shown in table 1.The existence of TAED improves the whiteness and the hydroscopicity of fabric dramatically in biological degumming/bleaching bath.This also brings significant efficiency of dust collection.
Embodiment 3: utilize H
2O
2/ TAED/NaOH is biological degumming and bleaching simultaneously
Use fabric and the equipment identical with last example 1.Experimentize according to identical with example 1 in essence mode, except adding 2g/l NaOH to biological degumming/liquid lime chloride.
The result is as shown in table 1.Shockingly, do not resemble conventional peroxide bleaching, in biological degumming/bleaching bath, add whiteness and the hydroscopicity that sodium hydroxide does not have further to improve fabric.In fact, this also has certain negative impact to whiteness and efficiency of dust collection.
Embodiment 4: utilize H
2O
2/ TAED is biological degumming and bleaching successively
A. biological degumming: (4600 types, Ramseur Co. NC) cut the 45cm * 21.5cm fabrics of heavily about 25 grams from binding type knit goods.With the fabric Labomat beaker (MathisLabomat that packs into, Werner Mathis USA, Inc, NC), pour 250ml 20mM buffer solution of sodium phosphate (pH9.2) then into, wherein contain the pectate lyase of 3000APSU/kg fiber and 0.5g/l wetting agent (Kierlon Jet B, BASF).Fabric was handled 15 minutes down at 55 ℃.
B. bleaching: add H to same beaker
2O
2, TAED and Calgon (Sodium hexametaphosphate 99).H
2O
2, TAED and Calgon ultimate density identical with last example 2.℃ reach 1 hour by 5 ℃ of/minute rising Labomat temperature to 70, drain water afterwards.Then fabric is thoroughly washed with tap water, to remove residual alkali, at room temperature dry.
The result is as shown in table 1.Obviously, whiteness and the hydroscopicity from the fabric of priority biological degumming and bleaching process pattern is better than pattern (example 2) simultaneously.The oeverall quality of this fabric is best in the fabric of routine 1-10.
Embodiment 5: utilize H
2O
2/ TAED successively comes unstuck and bleaches
Use and described identical fabric of last routine 1-4 and equipment.Experimentize according to identical with example 4 in essence mode, except in the solution that comes unstuck, not having the pectate lyase.
Whiteness and hydroscopicity the results are shown in the following table 1.The hydroscopicity of fabric is non-constant.This illustration is bright, and the existence of biological degumming enzyme is conclusive for the hydroscopicity of fabric.
Embodiment 6: utilize H
2O
2/ TAED/NaOH is biological degumming and bleaching successively
Use and described identical fabric of last routine 1-4 and equipment.Experimentize according to identical with example 4 in essence mode, except adding 2g/l NaOH to liquid lime chloride.
The result is as shown in table 1 below.The whiteness of fabric is significantly less than embodiment 4.This example shows that further adding sodium hydroxide to bleaching bath will negatively influence the whiteness of fabric.
The mono bath biological degumming and the bleaching of table 1. knit goods (knitted fabrics)
Embodiment # | Process pattern | Come unstuck | Bleaching | Whiteness Ganz 82 | Hydroscopicity second | Dust |
Initial fabric | 8.5 | >60 | 5 | |||
1 | Mono bath simultaneously | Enzyme | Superoxide | 44.6 | 33 | 4 |
2 | Mono bath simultaneously | Enzyme | Superoxide/TAED | 62.3 | 9 | 1 |
3 | Mono bath simultaneously | Enzyme | Superoxide/TAED/NaOH | 59.7 | 10 | 2 |
4 | Mono bath successively | Enzyme | Superoxide/TAED | 63.4 | 2 | 1 |
5 | Mono bath successively | Damping fluid | Superoxide/TAED | 63.0 | 23 | 1 |
6 | Mono bath successively | Enzyme | Superoxide/TAED/NaOH | 59.8 | 2 | 1 |
* dust grade: 1 is minimum, and 5 is maximum
Embodiment 7: two baths are come unstuck (two-bath) and are bleached
Experimentize according to identical with last example 4 in essence mode, except draining after the stage at biological degumming come unstuck solution and water replace.
The result is as shown in table 2 below.The hydroscopicity of fabric is good, but the whiteness of fabric and dedusting mark are significantly less than (embodiment 2) and successively (embodiment 4) process pattern simultaneously.
Embodiment 8: two bath biological degummings and bleaching
Experimentize according to identical with last example 7 in essence mode, except in the solution that comes unstuck, not having the pectate lyase.
The result is as shown in table 2.Owing to there is not the pectate lyase in biological degumming solution, the hydroscopicity of fabric is non-constant.This example is proof further, and the biological degumming enzyme is very important for the hydroscopicity that improves fabric.
Embodiment 9: two baths are come unstuck and are bleached
Experimentize according to identical with last example 7 in essence mode, except adding 2g/lNaOH to sodium hypochlorite solution.
The result is as shown in table 2.Add the whiteness that sodium hydroxide has improved fabric to bleaching bath.This with at the same time with the priority process pattern in viewed result opposite.
Embodiment 10: two bath biological degummings and bleaching
Experimentize according to identical with last example 9 in essence mode, except in the solution that comes unstuck, not having the pectate lyase.
The result is as shown in table 1.This example further shows, it is necessary to add sodium hydroxide and be the whiteness that improves fabric in two phase process patterns.
The two bath biological degummings and the bleaching of table 2. knit goods
Embodiment # | Process pattern | Come unstuck | Bleaching | Whiteness | Hydroscopicity | Dirt |
(Ganz 82) | (second) | Dust | ||||
7 | Two baths | Enzyme | Superoxide/TAED | 57.7 | 4 | 3 |
8 | Two baths | Damping fluid | Superoxide/TAED | 56.9 | >60 | 3 |
9 | Two baths | Enzyme | Superoxide/TAED/NaOH | 59.1 | 5 | 2 |
10 | Two baths | Damping fluid | Superoxide/TAED/NaOH | 59.6 | 10 | 2 |
* dust grade: 1 is minimum, and 5 is maximum
Embodiment 11: utilize H
2O
2/ NaOH/TAED is biological degumming and bleaching successively
A. biological degumming: (4600 types, Ramseur Co. NC) cut fabric sample (swatch) from 100% cotton knitting knot (cotton knit interlock).The size of sample is 19cm * 19.5cm, heavily about 7.5 grams of every duplicate samples.With the two duplicate samples Labomat beaker (MathisLabomat that packs into, Werner Mathis USA, Inc.NC), pour 150ml 5mM sodium bicarbonate buffer liquid (pH 9.0) then into, wherein contain the pectate lyase of 3000APSU/kg fabric and 0.5g/l wetting agent (Kierion Jet B, BASF).Then fabric was handled 15 minutes down at 55 ℃.
B. bleaching: in same beaker, add the 1g/l stablizer (Prostogen N-S, BASF), 2g/l NaOH, 2.5g/l H
2O
2With 1.32g/l TAED.℃ reach 1 hour by 3 ℃ of/minute rising Labomat temperature to 70.Drain water afterwards.Then fabric is thoroughly washed with tap water, to remove residual alkali, at room temperature dry.
The result is as shown in table 3.Because the adding of NaOH, the pH of solution is 10.83 when reaction finishes.By the whiteness of Macbeth color eye measurement fabric, with Ganz 82 unit representations.Utilize superoxide/NaOH/TAED to carry out after enzyme comes unstuck and bleach, whiteness has reached 67.61.In the dropping liquid test according to AATCC test method 79-1995, the hydroscopicity of fabric was less than 1 second.Dust on the fabric almost completely disappears.
Embodiment 12: utilize H
2O
2/ NaOH is biological degumming and bleaching successively
Use and example 11 described identical fabric and equipment.Experimentize according to identical with last example 11 in essence mode, except in liquid lime chloride, not adding TAED.
The result is as shown in table 3.The terminal point pH of reaction soln is 11.06, is higher than embodiment 11.Whiteness is 62.64, is significantly less than the fabric whiteness among the embodiment 11.Handle the back and on fabric, see some dust.Terminal point pH is high more, and dust is many more, and fabric whiteness is low more, and this all is owing to there is not the existence of TAED, thereby does not generate stronger SYNTHETIC OPTICAL WHITNER in embodiment 12.Also observe the excellent hydroscopicity of fabric, the moistening time is 3 seconds, and this has illustrated the validity that enzyme comes unstuck.
Embodiment 13: utilize H
2O
2/ NaOH/TAED successively cushions and comes unstuck and bleach
Use and embodiment 11 described identical fabric and equipment.Experimentize according to identical with last example 11 in essence mode, except in biological degumming solution, not adding the pectate lyase.
The result is as shown in table 3.The terminal point pH of reaction soln is 10.88, and is similar to embodiment 11.Coming unstuck and bleach back observing on fabric does not almost have dust, similar to embodiment 11 yet.The whiteness of fabric is 64.66, and this is lower than the fabric whiteness among the embodiment 11.The hydroscopicity of fabric surpasses 60 seconds, and this is worse than embodiment 11 greatly.Lower hydroscopicity and whiteness are owing to there is not the existence of enzyme in coming unstuck.
Table 3
Embodiment # | Come unstuck | Bleaching | Terminal point pH | Whiteness Ganz 82 | Hydroscopicity second | Dust |
Initial fabric | 8.5 | >60 | 5 | |||
11 | Enzyme | Superoxide/NaOH/TAED | 10.83 | 67.61 | <1 | 1 |
12 | Enzyme | Superoxide/NaOH | 11.06 | 62.64 | 3 | 2 |
13 | Damping fluid | Superoxide/NaOH/TAED | 10.88 | 64.66 | >60 | 1 |
* dust grade: 1 is minimum, and 5 is maximum
Embodiment 14: utilize H
2O
2/ NaOH/TAED is biological degumming and bleaching successively
A. biological degumming: (4600 types, Ramseur Co. NC) cut the 19cm * 19.5cm fabric samples of heavily about 7.5 grams from 100% cotton knitting knot.With two duplicate samples Labomat beaker (the Mathis Labomat that packs into, Werner Mathis USA, Inc.NC), pour 150ml 5mM sodium bicarbonate buffer liquid (pH9.0) then into, wherein contain 0.1g/l pectate lyase (being the 3000APSU/kg fabric) and 0.5g/l wetting agent (Kierion Jet B, BASF).Then fabric was handled 15 minutes down at 55 ℃.
B. bleaching: in same beaker, add the 4g/l stablizer (Prostogen N-S, BASF), 4g/l NaOH, 10g/l H
2O
2With 5.3g/l TAED.℃ reach 1 hour by 3 ℃ of/minute rising Labomat temperature to 70.Drain water afterwards.Then fabric is thoroughly washed with tap water, to remove residual alkali, at room temperature dry.
The result is as shown in table 4.Compare with embodiment 11, carry out identical enzyme in this example and come unstuck.Absorbent time less than 1 second shows, has reached excellent fabric moisture degree.On the other hand, under higher chemical dosage, bleach, comprise NaOH, the H of greater concn
2O
2, stablizer and TAED.As the result of higher chemical concentration, compare with embodiment 11 gained fabric whitenesses 67.61, reached higher fabric whiteness 72.46 (Ganz 82).All dust on the fabric have all been removed fully in this example.
Embodiment 15: utilize NaOH/H
2O
2Biological degumming and bleaching successively
Use and embodiment 14 described identical fabric and equipment.Experimentize according to identical with last example 14 in essence mode, except in liquid lime chloride, using 2g/l stablizer, 5g/l H
2O
2In addition.
As shown in table 4, the whiteness of fabric is 71.56.The whiteness of fabric is lower than embodiment 14, and this has illustrated the validity of TAED.Fabric also has excellent hydroscopicity, and absorbent time was less than 1 second in the dropping liquid test.Dust is removed fully.
Embodiment 16: utilize H
2O
2/ NaOH/TAED successively cushions and comes unstuck and bleach
Use and embodiment 14 described identical fabric and equipment.Experimentize according to identical with last example 14 in essence mode, except in biological degumming solution, not adding the pectate lyase.
The result is as shown in table 4.Compare with embodiment 14 gained results, the fabric in this example does not have industrial acceptable hydroscopicity (for example<5 second).Because lack degumming effect, the whiteness of fabric also is lower than embodiment 14.Dust on the fabric is removed fully.
Embodiment 17: utilize NaOH/H
2O
2Successively buffering is come unstuck and is bleached
Use and embodiment 14 described identical fabric and equipment.Experimentize according to identical with last example 14 in essence mode, except in biological degumming solution, not adding the pectate lyase and in liquid lime chloride, not adding the TAED.
The result is as shown in table 4.The absorbent time of being longer than embodiment 15 has greatly proved the validity of pectate lyase in coming unstuck.But, the absorbent time that is shorter than embodiment 6 shows, the adding of TAED does not influence the fabric moisture degree or has a negative impact.On the other hand, fabric whiteness 71.17 is lower than the fabric whiteness 71.94 among the embodiment 16.This shows that once more the adding of TAED causes the increase of fabric whiteness.
Table 4
Embodiment # | Come unstuck | Bleaching | CIE whiteness (Ganz 82) | Hydroscopicity (second) | Dust |
14 | Enzyme | Superoxide/NaOH/TAED | 72.46 | <1 | Do not have |
15 | Enzyme | Superoxide/NaOH | 71.56 | <1 | Do not have |
16 | Damping fluid | Superoxide/NaOH/TAED | 71.94 | >60 | Do not have |
17 | Damping fluid | Superoxide/NaOH | 71.17 | 46 | Do not have |
Embodiment 18:NaOH formerly artifact come unstuck and bleach in effect
A. biological degumming: (4600 types, Ramseur Co. NC) cut the 19cm * 19.5cm fabric samples of heavily about 7.5 grams from 100% cotton knitting knot.With two duplicate samples Labomat beaker (the Mathis Labomat that packs into, Werner Mathis USA, Inc.NC), pour 150ml 5mM sodium bicarbonate buffer liquid (pH9.0) then into, wherein contain 0.1g/l pectate lyase (being the 3000APSU/kg fabric) and 0.5g/l wetting agent (Kierion Jet B, BASF).Then fabric was handled 15 minutes down at 55 ℃.
B. bleaching: in same beaker, add the 1g/l stablizer (Prostogen N-S, BASF), 2.5g/l H
2O
2(Dexter Chemical) and 1.32g/l TAED (Peractive AN, it has the active TAED content of 84-88%, from Clariant Co.).Therefore, H
2O
2With the mol ratio of TAED be 14.7.NaOH concentration does not wait from 0-4g/l.℃ reach 1 hour by 3 ℃ of/minute rising Labomat temperature to 70.After when finishing, measuring liquid pH, drain water.Then fabric is thoroughly washed with tap water, to remove residual alkali, at room temperature dry.
The result is as shown in table 5.Along with NaOH concentration increases, terminal point pH increases, and hydroscopicity also increases, and is with absorbent time (second) expression, as shown in table 5.Fabric whiteness is with Ganz 82 expressions.When adding small amount of N aOH at first (being equivalent to terminal point pH in the 5-8 scope), the whiteness of fabric does not increase.When bleaching bath adds a large amount of relatively NaOH, the whiteness of fabric just has substantive increasing.
Embodiment 19:NaOH formerly artifact come unstuck and bleach in effect
Use and embodiment 18 described identical fabric and equipment.Experimentize according to the mode identical, replace the 1.32g/l except using 2.65g/l TAED with last example 18.Therefore, H in this example
2O
2With the mol ratio of TAED be 7.35.
The result is as shown in table 5.Obtain closely similar result and conclusion.Along with NaOH concentration increases, terminal point pH increases, and hydroscopicity also increases, and is with absorbent time (second) expression, as shown in table 5.When adding small amount of N aOH at first (being equivalent to terminal point pH in the 5-8 scope), the whiteness of fabric does not increase.When bleaching bath adds a large amount of relatively NaOH, the whiteness of fabric just has substantive increasing.
In addition, contrast the fabric whiteness of this routine sample G and embodiment 18 sample A, obviously fashionable when there not being NaOH to add, TAED dosage higher in fabric G handles produces higher whiteness.This has illustrated the validity of TAED under acidic conditions.But, when adding a large amount of NaOH (for example fabric e is to j),, do not observe the substantial differences of whiteness although TAED increases to 2.65g/l from 1.32g/l yet.
Table 5
Embodiment | Sample | NaOH(g/l) | H 2O 2/ TAED mol ratio | Final pH | The CIE whiteness | Wettability |
18 | 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 | |
F | 4 | 15 | 11.74 | 67.14 | <1 | |
19 | 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 | |
K | 4 | 7 | 11.73 | 66.56 | 2 |
All patents, patent application and the reference that this paper quotes all is incorporated herein by reference in full.Above-mentioned detailed description will inspire a lot of variations of the present invention of those skilled in the art.This class obvious variation all belongs to the scope of claims.
Claims (39)
1. handle the method for cellulosic materials, comprise cellulosic materials (i) is contacted with enzyme system, the destarch and/or the biological degumming that are used for cellulosic materials, (ii) contact with bleaching system, comprise hydrogen peroxide or at least a compound or its combination and at least a bleach-activating agent that when water-soluble, generates hydrogen peroxide, wherein add enzyme system and bleaching system to the single solution while or the priority that contain cellulosic materials.
2. the contact that the process of claim 1 wherein is to carry out under the adding that does not have alkali.
3. claim 1 or 2 method wherein add enzyme system and bleaching system simultaneously to the solution that contains cellulosic materials.
4. claim 1 or 2 method wherein successively add enzyme system and bleaching system to the solution that contains cellulosic materials, comprise (i) and add enzyme system, cultivate, and (ii) add bleaching system subsequently, cultivate.
5. claim 1 or 2 method wherein make cellulosic materials contact with bleaching system with enzyme system, form hydroscopicity and be 20 seconds or following, whiteness is the fabric of 50Ganz unit at least.
6. claim 1 or 2 method, wherein (i) makes cellulosic materials contact with enzyme system, and forming hydroscopicity is 20 seconds or following fabric, (ii) adds bleaching system to the solution that contains cellulosic materials afterwards.
7. the method for claim 4, further be included in described (i) and described (ii) between, the character of regulator solution, described character are selected from the group of being made up of the concentration of pH, ionic strength, temperature, surfactant concentrations, divalent cation chelators and any above-mentioned combination.
8. claim 1 or 2 method, this enzyme system wherein comprises at least a enzyme and at least a enzyme that is used for the biological degumming cellulosic materials that makes the cellulosic materials destarch.
9. claim 1 or 2 method, wherein this enzyme system is the biological degumming enzyme system.
10. claim 1 or 2 method, wherein this enzyme system is the destarch enzyme system.
11. the method for claim 1 or 2, wherein this destarch enzyme system comprises at least a destarch enzyme, is selected from the group of being made up of α-Dian Fenmei and beta-amylase and combination thereof.
12. the method for claim 1 or 2, wherein this biological degumming enzyme system comprises at least a biological degumming enzyme, is selected from the group of being made up of polygalacturonase, proteolytic enzyme, lipase and any above-mentioned combination.
13. the method for claim 1 or 2, wherein this biological degumming enzyme system comprises at least a biological degumming enzyme, is selected from the group by pectate lyase, pectin lyase, polygalacturonase, outer-polygalacturonase, outer-Polygalacturonate lyase and outer-poly--α-the galacturonic neuraminidase is formed.
14. the method for claim 1 or 2, wherein this biological degumming enzyme system comprises the pectate lyase.
15. the method for claim 1 or 2, wherein this biological degumming enzyme system comprises proteolytic enzyme, is selected from the group of being made up of aminopeptidase, Serine endopeptidase, halfcystine endopeptidase, aspartoyl endopeptidase and Zinc metalloproteinase.
16. the method for claim 1 or 2, wherein this biological degumming enzyme system comprises lipase, is selected from the group of being made up of triacylglycerol lipases and Phospholipid hydrolase.
17. the method for claim 1 or 2, wherein this biological degumming enzyme system comprises a kind of like this pectate lyase, the enzymic activity of the pectate lyase of performance maximum under about temperature more than 70 ℃.
18. the method for claim 1 or 2, wherein this biological degumming enzyme system comprises a kind of like this pectate lyase, the enzymic activity of the pectate lyase of performance maximum under about pH more than 8.
19. the method for claim 1 or 2; wherein this bleach-activating agent is selected from the material of following kind: the N-acyl caprolactam; N; N-two acidylates and N; N; N '; N '-four acylated amine; O-acyl group oxime ester; N-alkyl-N-alkylsulfonyl acid amides; N-acidylate ring-type hydrazides; O; N; the trisubstituted azanol of N-; N; N '-diacyl sulphonamide; three acyl group cyanurates; carboxylic acid anhydride; acyloxy Phenylsulfonic acid and their basic metal and alkaline earth salt; 1; 3-diacyl-4,5-two acyloxy tetrahydroglyoxalines; two acidylates 2, the 5-diketo-piperazine; the third two ureas and 2; the acylate of 2-dimethyl propylene two ureas; many acyl groups of alpha-acyloxy Malonamide; diacyl dioxo six hydrogen-1; 3, the 5-triazine; the 2-alkyl-or the 2-aryl-(4H)-3,1-benzoxazine-4-ketone; positively charged ion nitrite and have a C
1-10The many acidylates sugar or the sugar derivatives of-acyl group atomic group.
20. the method for claim 19, wherein this bleaching system comprises bleaching stibilizer, be selected from by edetate (EDTA), diethylene triaminepentaacetic acid(DTPA) (DTPA), complexon I (NTA), methylglycine oxalic acid (MGDA), Beta-alanine oxalic acid (ADA), quadrol-N, N '-disuccinate (EDDS), ethylenediamine tetramethylene phosphonic acid salt, diethylenetriamine pentamethylenophosphonic acid(DTPP) salt (DTMPA) or hydroxy ethylene-1, the group that the 1-di 2 ethylhexyl phosphonic acid is formed.
21. the method for claim 1 or 2, wherein this cellulosic materials comprises textiles.
22. the method for claim 22, wherein said textiles are cotton.
23. the method for claim 1 or 2, wherein said single-bath solution further comprises one or more buffer reagents, tensio-active agent, sequestrant and/or lubricant, or any above-mentioned salt.
24. handle the method for cellulosic materials, comprise cellulosic materials (i) is contacted with enzyme system, the destarch and/or the biological degumming that are used for cellulosic materials, (ii) contact with bleaching system, comprise hydrogen peroxide or at least a compound or its combination and at least a bleach-activating agent that when water-soluble, generates hydrogen peroxide, wherein add enzyme system and bleaching system, and under the pH more than 8, contact to the single solution while or the priority that contain cellulosic materials.
25. the method for claim 24, contact wherein be 9 or above pH under carry out.
26. the method for claim 24, contact wherein are to carry out under 9 to 11 pH.
27. the method for claim 24, contact wherein are to carry out under 10 to 11 pH.
26. the method for claim 24 wherein adds enzyme system and bleaching system simultaneously to the solution that contains cellulosic materials.
27. the method for claim 24 wherein successively adds enzyme system and bleaching system to the solution that contains cellulosic materials, comprises (i) and adds enzyme system, cultivates, and (ii) adds bleaching system subsequently, cultivates.
28. the method for claim 27, further be included in described (i) and described (ii) between, the character of regulator solution is selected from the group of being made up of concentration and any above-mentioned combination of pH, ionic strength, temperature, surfactant concentrations, divalent cation chelators.
29. the method for claim 24, wherein this enzyme system comprises at least a enzyme of cellulosic materials destarch and the enzyme of at least a biological degumming cellulosic materials of making.
30. the method for claim 24, wherein this enzyme system is the biological degumming enzyme system.
31. the method for claim 24, wherein this enzyme system is the destarch enzyme system.
32. the method for claim 30, wherein this biological degumming enzyme system comprises the pectate lyase.
33. the method for claim 30, wherein this biological degumming enzyme system comprises a kind of like this pectate lyase, the enzymic activity of the pectate lyase of performance maximum under about pH more than 8.
34. the method for claim 24; wherein at least a bleach-activating agent is selected from the material of following kind: the N-acyl caprolactam; N; N-two acidylates and N; N; N '; N '-four acylated amine; O-acyl group oxime ester; N-alkyl-N-alkylsulfonyl acid amides; N-acidylate ring-type hydrazides; O; N; the trisubstituted azanol of N-; N; N '-diacyl sulphonamide; three acyl group cyanurates; carboxylic acid anhydride; acyloxy Phenylsulfonic acid and their basic metal and alkaline earth salt; 1; 3-diacyl-4,5-two acyloxy tetrahydroglyoxalines; two acidylates 2, the 5-diketo-piperazine; the third two ureas and 2; the acylate of 2-dimethyl propylene two ureas; many acyl groups of alpha-acyloxy Malonamide; diacyl dioxo six hydrogen-1; 3, the 5-triazine; the 2-alkyl-or the 2-aryl-(4H)-3,1-benzoxazine-4-ketone; positively charged ion nitrite and have a C
1-10The many acidylates sugar or the sugar derivatives of-acyl group atomic group.
35. the method for claim 24, wherein this bleaching system comprises bleaching stibilizer, be selected from by edetate (EDTA), diethylene triaminepentaacetic acid(DTPA) (DTPA), complexon I (NTA), methylglycine oxalic acid (MGDA), Beta-alanine oxalic acid (ADA), quadrol-N, N '-disuccinate (EDDS), ethylenediamine tetramethylene phosphonic acid salt, diethylenetriamine pentamethylenophosphonic acid(DTPP) salt (DTMPA) or hydroxy ethylene-1, the group that the 1-di 2 ethylhexyl phosphonic acid is formed.
36. the method for claim 24, wherein this cellulosic materials comprises textiles.
37. handle the method for cellulosic materials, comprise cellulosic materials (i) is contacted with enzyme system, the destarch and/or the biological degumming that are used for cellulosic materials, (ii) contact with bleaching system, comprise hydrogen peroxide or at least a compound or its combination and at least a bleach-activating agent that when water-soluble, generates hydrogen peroxide, wherein add enzyme system and bleaching system, and under the adding that does not have alkali, contact to the single solution while or the priority that contain cellulosic materials.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US30241801P | 2001-06-29 | 2001-06-29 | |
US60/302,418 | 2001-06-29 |
Publications (1)
Publication Number | Publication Date |
---|---|
CN1723272A true CN1723272A (en) | 2006-01-18 |
Family
ID=23167658
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CNA028130634A Pending CN1723272A (en) | 2001-06-29 | 2002-07-01 | Preparation of cellulosic materials |
Country Status (5)
Country | Link |
---|---|
US (1) | US20030046773A1 (en) |
EP (1) | EP1404798A4 (en) |
CN (1) | CN1723272A (en) |
CA (1) | CA2450709A1 (en) |
WO (1) | WO2003002705A1 (en) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2009135343A1 (en) * | 2008-05-08 | 2009-11-12 | 江南大学 | Method for scouring and bleaching cotton fabric with composite enzyme preparation in one bath |
CN104080732A (en) * | 2012-01-31 | 2014-10-01 | 加尔各答大学 | Thermostable enzymes and methods of making and using the same |
CN108166240A (en) * | 2017-12-15 | 2018-06-15 | 纤化(上海)生物化工股份有限公司 | A kind of concise finishing agent of denim garment desizing and its preparation process |
Families Citing this family (7)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
PL2341136T3 (en) | 2003-04-04 | 2016-12-30 | Pectate lyases, Nucleic Acids encoding them and methods for making and using them | |
MXPA06014636A (en) * | 2004-06-15 | 2007-03-12 | Novozymes North America Inc | Simultaneous desizing and scouring process. |
EP1880053B1 (en) * | 2005-05-04 | 2019-07-31 | Novozymes North America, Inc. | Chlorine dioxide treatment compositions and processes |
BRPI0713389A2 (en) | 2006-06-21 | 2012-04-17 | Novozymes North America, Inc. e Novozymes A/S | process for combined degreasing and washing of a starched fabric, and, composition |
US20080147026A1 (en) * | 2006-12-15 | 2008-06-19 | Jian Qin | Absorbent fiber with a low absorbent capacity and slow absorption rate |
CN102080331B (en) * | 2010-12-01 | 2012-08-22 | 华纺股份有限公司 | Process for pre-treating fabrics by bio-enzymatic method |
CN114438770B (en) * | 2022-01-06 | 2023-12-05 | 广州市创兴服装集团有限公司 | Waterless fermentation grinding washing method for jeans wear |
Family Cites Families (18)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
BE791622A (en) * | 1971-11-22 | 1973-05-21 | Henkel & Cie Gmbh | METHOD AND AGENTS FOR WASHING AND SOFTENING TEXTILES |
US5130045A (en) * | 1987-10-30 | 1992-07-14 | The Clorox Company | Delayed onset active oxygen bleach composition |
US5130044A (en) * | 1987-10-30 | 1992-07-14 | The Clorox Company | Delayed onset active oxygen bleach composition |
US5234616A (en) * | 1987-10-30 | 1993-08-10 | The Clorox Company | Method of laundering clothes using a delayed onset active oxygen bleach composition |
DE4407801A1 (en) * | 1993-03-15 | 1994-09-22 | Sandoz Ag | Treatment of textiles |
WO1995021283A1 (en) * | 1994-02-07 | 1995-08-10 | Warwick International Group Limited | Process for bleaching textiles |
JPH10509203A (en) * | 1994-11-18 | 1998-09-08 | ザ、プロクター、エンド、ギャンブル、カンパニー | Detergent composition containing lipase and protease |
DE19545729A1 (en) * | 1995-12-08 | 1997-06-12 | Henkel Kgaa | Bleach and detergent with an enzymatic bleaching system |
JP3315851B2 (en) * | 1995-12-19 | 2002-08-19 | シャープ株式会社 | High-speed communication device using broadband amplifier circuit |
JP2000507639A (en) * | 1996-08-09 | 2000-06-20 | ザ、プロクター、エンド、ギャンブル、カンパニー | Detergent composition comprising alkaline pectin degrading enzyme |
DE69738047T2 (en) * | 1996-12-04 | 2008-05-15 | Novozymes North America, Inc. | ALKALIC ENZYMATIC COOKING OF COTTON TEXTILES |
US6258590B1 (en) * | 1998-11-02 | 2001-07-10 | Novozymes A/S | Biopreparation of textiles at high temperatures |
US6124127A (en) * | 1997-11-24 | 2000-09-26 | Novo Nordisk A/S | Pectate lyase |
US6146428A (en) * | 1998-04-03 | 2000-11-14 | Novo Nordisk A/S | Enzymatic treatment of denim |
WO2000042149A1 (en) * | 1999-01-14 | 2000-07-20 | The Procter & Gamble Company | Detergent compositions comprising a pectate lyase and a diacyl peroxide |
US6162260A (en) * | 1999-05-24 | 2000-12-19 | Novo Nordisk Biochem North America, Inc. | Single-bath biopreparation and dyeing of textiles |
WO2001000768A1 (en) * | 1999-06-23 | 2001-01-04 | Unilever N.V. | Bleaching detergent compositions |
CN1224751C (en) * | 2000-02-15 | 2005-10-26 | 宝洁公司 | Method for the one step preparation of textiles |
-
2002
- 2002-07-01 CA CA002450709A patent/CA2450709A1/en not_active Abandoned
- 2002-07-01 CN CNA028130634A patent/CN1723272A/en active Pending
- 2002-07-01 US US10/188,245 patent/US20030046773A1/en not_active Abandoned
- 2002-07-01 WO PCT/US2002/020833 patent/WO2003002705A1/en not_active Application Discontinuation
- 2002-07-01 EP EP02746790A patent/EP1404798A4/en not_active Withdrawn
Cited By (4)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2009135343A1 (en) * | 2008-05-08 | 2009-11-12 | 江南大学 | Method for scouring and bleaching cotton fabric with composite enzyme preparation in one bath |
CN104080732A (en) * | 2012-01-31 | 2014-10-01 | 加尔各答大学 | Thermostable enzymes and methods of making and using the same |
CN104080732B (en) * | 2012-01-31 | 2016-12-07 | 加尔各答大学 | Thermophilic enzyme and generation thereof and using method |
CN108166240A (en) * | 2017-12-15 | 2018-06-15 | 纤化(上海)生物化工股份有限公司 | A kind of concise finishing agent of denim garment desizing and its preparation process |
Also Published As
Publication number | Publication date |
---|---|
US20030046773A1 (en) | 2003-03-13 |
EP1404798A1 (en) | 2004-04-07 |
EP1404798A4 (en) | 2004-08-04 |
CA2450709A1 (en) | 2003-01-09 |
WO2003002705A1 (en) | 2003-01-09 |
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