CN1522323A - Single-bath preparation of cellulosic materials - Google Patents
Single-bath preparation of cellulosic materials Download PDFInfo
- Publication number
- CN1522323A CN1522323A CNA02813091XA CN02813091A CN1522323A CN 1522323 A CN1522323 A CN 1522323A CN A02813091X A CNA02813091X A CN A02813091XA CN 02813091 A CN02813091 A CN 02813091A CN 1522323 A CN1522323 A CN 1522323A
- Authority
- CN
- China
- Prior art keywords
- enzyme
- cellulose material
- biological degumming
- destarch
- bleaching
- 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.)
- Granted
Links
- 239000000463 material Substances 0.000 title claims abstract description 74
- 239000003788 bath preparation Substances 0.000 title description 2
- 102000004190 Enzymes Human genes 0.000 claims abstract description 155
- 108090000790 Enzymes Proteins 0.000 claims abstract description 155
- 238000004061 bleaching Methods 0.000 claims abstract description 120
- 238000000034 method Methods 0.000 claims abstract description 89
- 150000004965 peroxy acids Chemical class 0.000 claims abstract description 40
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical group [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 claims description 81
- KFSLWBXXFJQRDL-UHFFFAOYSA-N Peracetic acid Chemical compound CC(=O)OO KFSLWBXXFJQRDL-UHFFFAOYSA-N 0.000 claims description 79
- 229920002678 cellulose Polymers 0.000 claims description 66
- 239000001913 cellulose Substances 0.000 claims description 66
- 239000004744 fabric Substances 0.000 claims description 56
- 230000008569 process Effects 0.000 claims description 47
- 108010087558 pectate lyase Proteins 0.000 claims description 37
- 150000001875 compounds Chemical class 0.000 claims description 31
- 239000002253 acid Substances 0.000 claims description 19
- 102000004882 Lipase Human genes 0.000 claims description 18
- 108090001060 Lipase Proteins 0.000 claims description 18
- -1 organic peroxy acid compound Chemical class 0.000 claims description 17
- 238000011534 incubation Methods 0.000 claims description 16
- 239000004753 textile Substances 0.000 claims description 16
- 239000004367 Lipase Substances 0.000 claims description 15
- 235000019421 lipase Nutrition 0.000 claims description 15
- 239000004365 Protease Substances 0.000 claims description 14
- 108091005804 Peptidases Proteins 0.000 claims description 13
- 238000012545 processing Methods 0.000 claims description 12
- 229920000742 Cotton Polymers 0.000 claims description 7
- 239000004094 surface-active agent Substances 0.000 claims description 7
- 239000003153 chemical reaction reagent Substances 0.000 claims description 6
- 150000003839 salts Chemical class 0.000 claims description 6
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical group OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 5
- 150000001768 cations Chemical class 0.000 claims description 5
- 239000002738 chelating agent Substances 0.000 claims description 5
- 230000002255 enzymatic effect Effects 0.000 claims description 5
- 150000001451 organic peroxides Chemical class 0.000 claims description 5
- QPCDCPDFJACHGM-UHFFFAOYSA-N N,N-bis{2-[bis(carboxymethyl)amino]ethyl}glycine Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(=O)O)CCN(CC(O)=O)CC(O)=O QPCDCPDFJACHGM-UHFFFAOYSA-N 0.000 claims description 4
- 229940009662 edetate Drugs 0.000 claims description 4
- 229910052757 nitrogen Inorganic materials 0.000 claims description 4
- 229960003330 pentetic acid Drugs 0.000 claims description 4
- 108090000915 Aminopeptidases Proteins 0.000 claims description 3
- 102000004400 Aminopeptidases Human genes 0.000 claims description 3
- RPNUMPOLZDHAAY-UHFFFAOYSA-N Diethylenetriamine Chemical compound NCCNCCN RPNUMPOLZDHAAY-UHFFFAOYSA-N 0.000 claims description 3
- 102000005593 Endopeptidases Human genes 0.000 claims description 3
- 108010059378 Endopeptidases Proteins 0.000 claims description 3
- 108090000856 Lyases Proteins 0.000 claims description 3
- 102000004317 Lyases Human genes 0.000 claims description 3
- 108010029182 Pectin lyase Proteins 0.000 claims description 3
- 108010059820 Polygalacturonase Proteins 0.000 claims description 3
- 108010019077 beta-Amylase Proteins 0.000 claims description 3
- NFDRPXJGHKJRLJ-UHFFFAOYSA-N edtmp Chemical class OP(O)(=O)CN(CP(O)(O)=O)CCN(CP(O)(O)=O)CP(O)(O)=O NFDRPXJGHKJRLJ-UHFFFAOYSA-N 0.000 claims description 3
- 239000000314 lubricant Substances 0.000 claims description 3
- JJJOZVFVARQUJV-UHFFFAOYSA-N 2-ethylhexylphosphonic acid Chemical compound CCCCC(CC)CP(O)(O)=O JJJOZVFVARQUJV-UHFFFAOYSA-N 0.000 claims description 2
- LJGHYPLBDBRCRZ-UHFFFAOYSA-N 3-(3-aminophenyl)sulfonylaniline Chemical compound NC1=CC=CC(S(=O)(=O)C=2C=C(N)C=CC=2)=C1 LJGHYPLBDBRCRZ-UHFFFAOYSA-N 0.000 claims description 2
- 101100345345 Arabidopsis thaliana MGD1 gene Proteins 0.000 claims description 2
- KVPMCFRZLDLEJW-UHFFFAOYSA-N C(C(=O)O)(=O)O.NCCC(=O)O Chemical compound C(C(=O)O)(=O)O.NCCC(=O)O KVPMCFRZLDLEJW-UHFFFAOYSA-N 0.000 claims description 2
- QDWXBVYRECADHW-UHFFFAOYSA-N CNCC(=O)O.C(C(=O)O)(=O)O Chemical compound CNCC(=O)O.C(C(=O)O)(=O)O QDWXBVYRECADHW-UHFFFAOYSA-N 0.000 claims description 2
- 108010006232 Neuraminidase Proteins 0.000 claims description 2
- 102000005348 Neuraminidase Human genes 0.000 claims description 2
- 108090000083 Serine Endopeptidases Proteins 0.000 claims description 2
- 102000003667 Serine Endopeptidases Human genes 0.000 claims description 2
- 101710151579 Zinc metalloproteinase Proteins 0.000 claims description 2
- 150000001732 carboxylic acid derivatives Chemical class 0.000 claims description 2
- 125000005843 halogen group Chemical group 0.000 claims description 2
- 125000004356 hydroxy functional group Chemical group O* 0.000 claims description 2
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 claims description 2
- OHOTVSOGTVKXEL-UHFFFAOYSA-K trisodium;2-[bis(carboxylatomethyl)amino]propanoate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)C(C)N(CC([O-])=O)CC([O-])=O OHOTVSOGTVKXEL-UHFFFAOYSA-K 0.000 claims description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 2
- 102000003950 Cysteine Endopeptidases Human genes 0.000 claims 1
- 108090000395 Cysteine Endopeptidases Proteins 0.000 claims 1
- 125000000254 aspartoyl group Chemical group 0.000 claims 1
- 239000000872 buffer Substances 0.000 claims 1
- 238000009990 desizing Methods 0.000 abstract description 6
- 238000009991 scouring Methods 0.000 abstract description 3
- 229940088598 enzyme Drugs 0.000 description 99
- 239000000203 mixture Substances 0.000 description 44
- 239000007864 aqueous solution Substances 0.000 description 17
- 239000000835 fiber Substances 0.000 description 16
- 239000000243 solution Substances 0.000 description 16
- 230000000694 effects Effects 0.000 description 15
- 150000002978 peroxides Chemical class 0.000 description 15
- 102000035195 Peptidases Human genes 0.000 description 11
- 235000019419 proteases Nutrition 0.000 description 11
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 11
- 239000007788 liquid Substances 0.000 description 10
- 238000005406 washing Methods 0.000 description 10
- 239000003795 chemical substances by application Substances 0.000 description 9
- 239000000428 dust Substances 0.000 description 9
- 239000006210 lotion Substances 0.000 description 9
- 241000193830 Bacillus <bacterium> Species 0.000 description 8
- 239000007844 bleaching agent Substances 0.000 description 8
- 229920002230 Pectic acid Polymers 0.000 description 7
- 238000005516 engineering process Methods 0.000 description 7
- 238000002360 preparation method Methods 0.000 description 7
- 239000000126 substance Substances 0.000 description 7
- 238000012360 testing method Methods 0.000 description 7
- 239000000080 wetting agent Substances 0.000 description 7
- 239000003513 alkali Substances 0.000 description 6
- 239000007853 buffer solution Substances 0.000 description 6
- 239000001814 pectin Substances 0.000 description 6
- 229920001277 pectin Polymers 0.000 description 6
- 235000010987 pectin Nutrition 0.000 description 6
- GCLGEJMYGQKIIW-UHFFFAOYSA-H sodium hexametaphosphate Chemical compound [Na]OP1(=O)OP(=O)(O[Na])OP(=O)(O[Na])OP(=O)(O[Na])OP(=O)(O[Na])OP(=O)(O[Na])O1 GCLGEJMYGQKIIW-UHFFFAOYSA-H 0.000 description 6
- 241000894006 Bacteria Species 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 5
- 238000002156 mixing Methods 0.000 description 5
- 239000010318 polygalacturonic acid Substances 0.000 description 5
- 229920001817 Agar Polymers 0.000 description 4
- 108010059892 Cellulase Proteins 0.000 description 4
- 241000233866 Fungi Species 0.000 description 4
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
- 239000008272 agar Substances 0.000 description 4
- 125000000217 alkyl group Chemical group 0.000 description 4
- 150000001413 amino acids Chemical class 0.000 description 4
- 239000002585 base Substances 0.000 description 4
- 238000009954 braiding Methods 0.000 description 4
- 125000004432 carbon atom Chemical group C* 0.000 description 4
- 210000004027 cell Anatomy 0.000 description 4
- 229940106157 cellulase Drugs 0.000 description 4
- 238000011010 flushing procedure Methods 0.000 description 4
- 239000012535 impurity Substances 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 108090000765 processed proteins & peptides Proteins 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 230000008521 reorganization Effects 0.000 description 4
- 241000196324 Embryophyta Species 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 241001480714 Humicola insolens Species 0.000 description 3
- 241000589516 Pseudomonas Species 0.000 description 3
- 229920002472 Starch Polymers 0.000 description 3
- 108010056079 Subtilisins Proteins 0.000 description 3
- 102000005158 Subtilisins Human genes 0.000 description 3
- 150000007513 acids Chemical class 0.000 description 3
- 229910052799 carbon Inorganic materials 0.000 description 3
- 238000004040 coloring Methods 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 239000002002 slurry Substances 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- 229910052708 sodium Inorganic materials 0.000 description 3
- 239000001488 sodium phosphate Substances 0.000 description 3
- 229910000162 sodium phosphate Inorganic materials 0.000 description 3
- 239000003381 stabilizer Substances 0.000 description 3
- 239000008107 starch Substances 0.000 description 3
- 235000019698 starch Nutrition 0.000 description 3
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 3
- 238000009941 weaving Methods 0.000 description 3
- 229920002955 Art silk Polymers 0.000 description 2
- 108090000101 Asclepain Proteins 0.000 description 2
- 241000228212 Aspergillus Species 0.000 description 2
- 241000194103 Bacillus pumilus Species 0.000 description 2
- 240000008564 Boehmeria nivea Species 0.000 description 2
- 244000025254 Cannabis sativa Species 0.000 description 2
- 235000012766 Cannabis sativa ssp. sativa var. sativa Nutrition 0.000 description 2
- 235000012765 Cannabis sativa ssp. sativa var. spontanea Nutrition 0.000 description 2
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 2
- RKWGIWYCVPQPMF-UHFFFAOYSA-N Chloropropamide Chemical compound CCCNC(=O)NS(=O)(=O)C1=CC=C(Cl)C=C1 RKWGIWYCVPQPMF-UHFFFAOYSA-N 0.000 description 2
- 235000008733 Citrus aurantifolia Nutrition 0.000 description 2
- 240000000491 Corchorus aestuans Species 0.000 description 2
- 235000011777 Corchorus aestuans Nutrition 0.000 description 2
- 235000010862 Corchorus capsularis Nutrition 0.000 description 2
- 108700033921 EC 3.4.23.20 Proteins 0.000 description 2
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 2
- 241000223198 Humicola Species 0.000 description 2
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 2
- 240000006240 Linum usitatissimum Species 0.000 description 2
- 235000004431 Linum usitatissimum Nutrition 0.000 description 2
- BPQQTUXANYXVAA-UHFFFAOYSA-N Orthosilicate Chemical compound [O-][Si]([O-])([O-])[O-] BPQQTUXANYXVAA-UHFFFAOYSA-N 0.000 description 2
- 206010033546 Pallor Diseases 0.000 description 2
- 108090000284 Pepsin A Proteins 0.000 description 2
- 102000057297 Pepsin A Human genes 0.000 description 2
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 2
- 239000004115 Sodium Silicate Substances 0.000 description 2
- 241000223257 Thermomyces Species 0.000 description 2
- 241000223258 Thermomyces lanuginosus Species 0.000 description 2
- 235000011941 Tilia x europaea Nutrition 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 230000000996 additive effect Effects 0.000 description 2
- 229910052783 alkali metal Inorganic materials 0.000 description 2
- AEMOLEFTQBMNLQ-BKBMJHBISA-N alpha-D-galacturonic acid Chemical compound O[C@H]1O[C@H](C(O)=O)[C@H](O)[C@H](O)[C@H]1O AEMOLEFTQBMNLQ-BKBMJHBISA-N 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 230000003625 amylolytic effect Effects 0.000 description 2
- 239000002518 antifoaming agent Substances 0.000 description 2
- 238000003287 bathing Methods 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 150000001555 benzenes Chemical class 0.000 description 2
- 235000009120 camo Nutrition 0.000 description 2
- 235000005607 chanvre indien Nutrition 0.000 description 2
- 238000004140 cleaning Methods 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 238000007598 dipping method Methods 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 238000004043 dyeing Methods 0.000 description 2
- 108010093305 exopolygalacturonase Proteins 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 239000011487 hemp Substances 0.000 description 2
- 238000013537 high throughput screening Methods 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 239000004571 lime Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000002703 mutagenesis Methods 0.000 description 2
- 231100000350 mutagenesis Toxicity 0.000 description 2
- 239000000049 pigment Substances 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 230000000630 rising effect Effects 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 238000004513 sizing Methods 0.000 description 2
- 235000019795 sodium metasilicate Nutrition 0.000 description 2
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 2
- 229910052911 sodium silicate Inorganic materials 0.000 description 2
- GEHJYWRUCIMESM-UHFFFAOYSA-L sodium sulfite Chemical compound [Na+].[Na+].[O-]S([O-])=O GEHJYWRUCIMESM-UHFFFAOYSA-L 0.000 description 2
- 239000002689 soil Substances 0.000 description 2
- 238000009955 starching Methods 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- 229920002994 synthetic fiber Polymers 0.000 description 2
- 239000012209 synthetic fiber Substances 0.000 description 2
- 238000010792 warming Methods 0.000 description 2
- 239000002759 woven fabric Substances 0.000 description 2
- JCZPMGDSEAFWDY-SQOUGZDYSA-N (2r,3s,4r,5r)-2,3,4,5,6-pentahydroxyhexanamide Chemical compound NC(=O)[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO JCZPMGDSEAFWDY-SQOUGZDYSA-N 0.000 description 1
- DNIAPMSPPWPWGF-GSVOUGTGSA-N (R)-(-)-Propylene glycol Chemical compound C[C@@H](O)CO DNIAPMSPPWPWGF-GSVOUGTGSA-N 0.000 description 1
- IEORSVTYLWZQJQ-UHFFFAOYSA-N 2-(2-nonylphenoxy)ethanol Chemical compound CCCCCCCCCC1=CC=CC=C1OCCO IEORSVTYLWZQJQ-UHFFFAOYSA-N 0.000 description 1
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108090000886 Ananain Proteins 0.000 description 1
- 108090000145 Bacillolysin Proteins 0.000 description 1
- 241000194108 Bacillus licheniformis Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000589513 Burkholderia cepacia Species 0.000 description 1
- UQTQTIBOAUUMKO-UHFFFAOYSA-N C1=CC=CC=C1C(=O)OO.C(C1=CC=CC=C1)OO Chemical group C1=CC=CC=C1C(=O)OO.C(C1=CC=CC=C1)OO UQTQTIBOAUUMKO-UHFFFAOYSA-N 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- 102000004308 Carboxylic Ester Hydrolases Human genes 0.000 description 1
- 108090000863 Carboxylic Ester Hydrolases Proteins 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 108090000391 Caricain Proteins 0.000 description 1
- CXRFDZFCGOPDTD-UHFFFAOYSA-M Cetrimide Chemical compound [Br-].CCCCCCCCCCCCCC[N+](C)(C)C CXRFDZFCGOPDTD-UHFFFAOYSA-M 0.000 description 1
- 108090001069 Chymopapain Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 229920000858 Cyclodextrin Polymers 0.000 description 1
- 102100034560 Cytosol aminopeptidase Human genes 0.000 description 1
- GUBGYTABKSRVRQ-CUHNMECISA-N D-Cellobiose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-CUHNMECISA-N 0.000 description 1
- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 description 1
- 108010092681 DNA Primase Proteins 0.000 description 1
- 102000016559 DNA Primase Human genes 0.000 description 1
- 108010083608 Durazym Proteins 0.000 description 1
- 229940120146 EDTMP Drugs 0.000 description 1
- 241000588698 Erwinia Species 0.000 description 1
- 108090000270 Ficain Proteins 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 241000223221 Fusarium oxysporum Species 0.000 description 1
- 241000159512 Geotrichum Species 0.000 description 1
- 102100027612 Kallikrein-11 Human genes 0.000 description 1
- 241000588748 Klebsiella Species 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- 108010048733 Lipozyme Proteins 0.000 description 1
- 239000006142 Luria-Bertani Agar Substances 0.000 description 1
- 108010006035 Metalloproteases Proteins 0.000 description 1
- 102000005741 Metalloproteases Human genes 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 108090000192 Methionyl aminopeptidases Proteins 0.000 description 1
- 102000034452 Methionyl aminopeptidases Human genes 0.000 description 1
- 241000226677 Myceliophthora Species 0.000 description 1
- 241000194105 Paenibacillus polymyxa Species 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 108010044725 Pectate disaccharide-lyase Proteins 0.000 description 1
- 241000228143 Penicillium Species 0.000 description 1
- 108010047320 Pepsinogen A Proteins 0.000 description 1
- 241000222385 Phanerochaete Species 0.000 description 1
- 102100037883 Phospholipase B1, membrane-associated Human genes 0.000 description 1
- 108010058864 Phospholipases A2 Proteins 0.000 description 1
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical class OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 1
- 229920000388 Polyphosphate Polymers 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 241000168225 Pseudomonas alcaligenes Species 0.000 description 1
- 241000589540 Pseudomonas fluorescens Species 0.000 description 1
- 241000589630 Pseudomonas pseudoalcaligenes Species 0.000 description 1
- 241000577556 Pseudomonas wisconsinensis Species 0.000 description 1
- 241000222480 Schizophyllum Species 0.000 description 1
- 241000223255 Scytalidium Species 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- UIIMBOGNXHQVGW-DEQYMQKBSA-M Sodium bicarbonate-14C Chemical compound [Na+].O[14C]([O-])=O UIIMBOGNXHQVGW-DEQYMQKBSA-M 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 241001137870 Thermoanaerobacterium Species 0.000 description 1
- ISWQCIVKKSOKNN-UHFFFAOYSA-L Tiron Chemical compound [Na+].[Na+].OC1=CC(S([O-])(=O)=O)=CC(S([O-])(=O)=O)=C1O ISWQCIVKKSOKNN-UHFFFAOYSA-L 0.000 description 1
- 241000223259 Trichoderma Species 0.000 description 1
- 241000499912 Trichoderma reesei Species 0.000 description 1
- 101710152431 Trypsin-like protease Proteins 0.000 description 1
- 108030000963 Tryptophanyl aminopeptidases Proteins 0.000 description 1
- 108010009135 Uca pugilator serine collagenase 1 Proteins 0.000 description 1
- 108010038900 X-Pro aminopeptidase Proteins 0.000 description 1
- 241000589634 Xanthomonas Species 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 108090000350 actinidain Proteins 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 150000001340 alkali metals Chemical class 0.000 description 1
- 150000001447 alkali salts Chemical class 0.000 description 1
- 150000008051 alkyl sulfates Chemical class 0.000 description 1
- 125000005211 alkyl trimethyl ammonium group Chemical group 0.000 description 1
- 108090000637 alpha-Amylases Proteins 0.000 description 1
- 229910000323 aluminium silicate Inorganic materials 0.000 description 1
- 125000003368 amide group Chemical group 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 239000003899 bactericide agent Substances 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 238000005452 bending Methods 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 230000031709 bromination Effects 0.000 description 1
- 238000005893 bromination reaction Methods 0.000 description 1
- 229910001424 calcium ion Inorganic materials 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000004568 cement Substances 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 229960002976 chymopapain Drugs 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 238000013329 compounding Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 238000005336 cracking Methods 0.000 description 1
- 108090000200 cucumisin Proteins 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 229960003067 cystine Drugs 0.000 description 1
- 230000001461 cytolytic effect Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- GSPKZYJPUDYKPI-UHFFFAOYSA-N diethoxy sulfate Chemical compound CCOOS(=O)(=O)OOCC GSPKZYJPUDYKPI-UHFFFAOYSA-N 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- HNPSIPDUKPIQMN-UHFFFAOYSA-N dioxosilane;oxo(oxoalumanyloxy)alumane Chemical compound O=[Si]=O.O=[Al]O[Al]=O HNPSIPDUKPIQMN-UHFFFAOYSA-N 0.000 description 1
- 229940048820 edetates Drugs 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 235000019387 fatty acid methyl ester Nutrition 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 235000019836 ficin Nutrition 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000012239 gene modification Methods 0.000 description 1
- 230000005017 genetic modification Effects 0.000 description 1
- 235000013617 genetically modified food Nutrition 0.000 description 1
- 238000000227 grinding Methods 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000002650 habitual effect Effects 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000009897 hydrogen peroxide bleaching Methods 0.000 description 1
- OUUQCZGPVNCOIJ-UHFFFAOYSA-N hydroperoxyl Chemical compound O[O] OUUQCZGPVNCOIJ-UHFFFAOYSA-N 0.000 description 1
- 238000005213 imbibition Methods 0.000 description 1
- 238000007654 immersion Methods 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 239000002563 ionic surfactant Substances 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 150000002576 ketones Chemical class 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- FCCDDURTIIUXBY-UHFFFAOYSA-N lipoamide Chemical compound NC(=O)CCCCC1CCSS1 FCCDDURTIIUXBY-UHFFFAOYSA-N 0.000 description 1
- 238000007433 macroscopic evaluation Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 108010020132 microbial serine proteinases Proteins 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 238000006386 neutralization reaction Methods 0.000 description 1
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- 229920000847 nonoxynol Polymers 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 150000004967 organic peroxy acids Chemical class 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000012188 paraffin wax Substances 0.000 description 1
- LCLHHZYHLXDRQG-ZNKJPWOQSA-N pectic acid Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)O[C@H](C(O)=O)[C@@H]1OC1[C@H](O)[C@@H](O)[C@@H](OC2[C@@H]([C@@H](O)[C@@H](O)[C@H](O2)C(O)=O)O)[C@@H](C(O)=O)O1 LCLHHZYHLXDRQG-ZNKJPWOQSA-N 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 229940066716 pepsin a Drugs 0.000 description 1
- FHHJDRFHHWUPDG-UHFFFAOYSA-N peroxysulfuric acid Chemical compound OOS(O)(=O)=O FHHJDRFHHWUPDG-UHFFFAOYSA-N 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000447 polyanionic polymer Polymers 0.000 description 1
- 239000001205 polyphosphate Substances 0.000 description 1
- 235000011176 polyphosphates Nutrition 0.000 description 1
- 229920001296 polysiloxane Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 235000019422 polyvinyl alcohol Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 108010017378 prolyl aminopeptidase Proteins 0.000 description 1
- CZPZWMPYEINMCF-UHFFFAOYSA-N propaneperoxoic acid Chemical compound CCC(=O)OO CZPZWMPYEINMCF-UHFFFAOYSA-N 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 235000018102 proteins Nutrition 0.000 description 1
- 102000004169 proteins and genes Human genes 0.000 description 1
- 108090000623 proteins and genes Proteins 0.000 description 1
- 238000004080 punching Methods 0.000 description 1
- 239000002994 raw material Substances 0.000 description 1
- 229920006395 saturated elastomer Polymers 0.000 description 1
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 229960001922 sodium perborate Drugs 0.000 description 1
- 235000010265 sodium sulphite Nutrition 0.000 description 1
- YKLJGMBLPUQQOI-UHFFFAOYSA-M sodium;oxidooxy(oxo)borane Chemical compound [Na+].[O-]OB=O YKLJGMBLPUQQOI-UHFFFAOYSA-M 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 238000009987 spinning Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 229960005137 succinic acid Drugs 0.000 description 1
- 125000000020 sulfo group Chemical group O=S(=O)([*])O[H] 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 108010075550 termamyl Proteins 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 239000012085 test solution Substances 0.000 description 1
- WCTAGTRAWPDFQO-UHFFFAOYSA-K trisodium;hydrogen carbonate;carbonate Chemical compound [Na+].[Na+].[Na+].OC([O-])=O.[O-]C([O-])=O WCTAGTRAWPDFQO-UHFFFAOYSA-K 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 239000001993 wax Substances 0.000 description 1
- 108010078692 yeast proteinase B Proteins 0.000 description 1
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
- 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
- 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
- D06L4/10—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen
- D06L4/15—Bleaching fibres, filaments, threads, yarns, fabrics, feathers or made-up fibrous goods; Bleaching leather or furs using agents which develop oxygen using organic 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
-
- 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
- D06L4/70—Multi-step processes
- D06L4/75—Multi-step processes combined with cleaning or washing
Landscapes
- Engineering & Computer Science (AREA)
- Textile Engineering (AREA)
- Chemical & Material Sciences (AREA)
- Inorganic Chemistry (AREA)
- Detergent Compositions (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
Abstract
The present invention provides methods for single-bath desizing, scouring and bleaching of cellulosic materials, which are carried out by contracting the cellulosic simultaneously or sequentially with an enzyme system and a peracid bleaching system under conditions that do not require emptying the bath or rinsing the cellulosic materials between desizing, scouring and bleaching steps.
Description
Invention field
The present invention relates to handle the method and composition of cellulose material (cellulosic materials), relate more specifically to be used for destarch (desizing), come unstuck (scouring) and bleach the method and composition of (bleaching) cellulose material.
Background of invention
Cellulose material, for example cotton fiber are processed into clothes manufacturing raw material will involve some steps: with the fiber spun yarn; Fabric from weaving of yarn structure or braiding; Be prepared subsequently, dyeing and housekeeping operation.Preparation process may involve destarch (being used for textiles), comes unstuck and bleach, and produces to be suitable for the textiles that dyes or put in order.
A. destarch: textiles is the principal mode of textile fabric structure.Fabrication processes requires the yarn " starching " with bending, avoids wearing and tearing to protect it.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 surfactant 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 residue and impurity, and then it is inhomogeneous to cause dyeing in process subsequently.
In addition, because chemicals that is adopted and the material that extracts from fiber, chemical Degumming can produce environmental problem on effluent is disposed.The someone proposes with the alternative of enzyme degumming quality as the chemical Degumming process, and for example WO 98/24965, and WO 00/71808, and JP 6220772, JP10088472, 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 absorbability 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: NaOH, surfactant, optical brightener, stabilizing agent and bleaching agent.Bleaching can be in batches, carry out in the semicontinuous or continuous or discrete process.When using enzyme in the destarch or the process of coming unstuck, for the high quality results of the unanimity that obtains commercialization quantity textiles, destarch and the step tradition of coming unstuck are separated with blanching step and are carried out, and require high temperature and basicity because alkaline peroxide is bleached.
Summary of the invention
The invention provides cellulose material mono bath (single-bath) destarch, come unstuck and method for bleaching, cellulose material is the textiles of crude fibre, yarn, weaving or braiding for example, by cotton, linen, flax, ramie, artificial silk, hemp, jute or these fibers each other or the admixture of or synthetic fiber natural with other.
The inventive method is performed such, and cellulose material is contacted with (i i) bleaching system with (i) enzyme system; In containing the same solution of cellulose material to be processed to some extent, add enzyme system and bleaching system, not emptying dipping bath liquid (without emptying the bath) or cleaning cellulose material between enzyme processing and blanching step, 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 cellulose material under proper condition with the enzyme system full contact time, so that effectively biological degumming (bioscouring) and/or destarch, (ii) directly add bleaching system then, do not have emptying dipping bath liquid or washing the fibre quality to the solution that contains cellulose material and enzyme system.
In one aspect of the invention, the method of handling cellulose material is disclosed, comprise cellulose material (i) is contacted with enzyme system, be used for destarch and/or come unstuck, (ii) contact with bleaching system, comprise at least a peracid compound, wherein enzyme system and peracid bleaching system while or priority join in the same solution in mono bath is handled.
In one embodiment of the invention, described enzyme system and peracid bleaching system add in the mono bath process successively, by at first (i) solution of fibre-bearing quality is contacted with enzyme system and incubation solution composition time enough, and under the condition that be fit to promote effective biological degumming and/or destarch, then by in the solution that (ii) the peracid bleaching system is joined same fibre-bearing quality and enzyme system and incubation finish processing.
In another embodiment, enzyme system and peracid bleaching system join in the solution of fibre-bearing quality simultaneously, promptly about same time or do not have in the middle of incubation step.
Method and composition of the present invention provides a kind of like this product, it shows as, and wettability (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 time is shorter; (ii) preserved moisture; (iii) reduced the waste liquid outflow.
Detailed Description Of The Invention
In the inventive method, biological degumming and/or destarch are in conjunction with bleaching in mono bath is handled.
In preferred embodiments, in the aqueous solution or flushing liquor (wash liquor), carry out the mono bath processing by adding enzyme system and bleaching system simultaneously, comprise (i) and add enzyme system and bleaching system simultaneously in the aqueous solution or flushing liquor, it comprises or contacts cellulose material, (ii) according to selected enzyme system, effectively come unstuck and/or destarch being fit to reach, effectively incubation time enough under the condition of bleaching.
In another preferred embodiment, successively add enzyme system and bleaching system and in the aqueous solution or flushing liquor (wash liquor), carry out the mono bath processing, comprise (i) and add enzyme system and bleaching system simultaneously in the aqueous solution or flushing liquor, it comprises or contacts cellulose material, (ii) according to selected enzyme system, effectively come unstuck and/or destarch be fit to causing and cause to reach, effectively time enough carries out the incubation first time under the condition of bleaching; (iii) the peracid bleaching system is joined in the same solution that comprises cellulose material and enzyme system, incubation is finished processing.
Cellulose material
" cellulose material " used herein expression cellulosic substrate to be processed comprises cotton, linen, flax, ramie, artificial silk, hemp, jute and they and other admixtures natural or synthetic fiber without limitation.Cellulose material can also comprise textiles or fabric or the clothes or the finished product of crude fibre, yarn, weaving 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.
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, Thermoaraerobactor 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 cellulose material 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 pectase, protease, lipase, at and combination thereof without limitation, and more preferably, the biological degumming enzyme is a pectase, and then more preferably, the biological degumming enzyme is pectate lyase (pectate lyase).
Pectase: any pectin decomposing enzyme composition with ability of degrading plant cell membrane combination of pectins may be used to implement the present invention.The pectase that is fit to comprises those of fungi or bacterial origin without limitation.The pectase of also containing chemistry or genetic modification.Preferably, pectase used in this invention is that reorganization produces, and is the one pack system enzyme.
Pectase 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.Pectase 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 polymer, generates monomer or dimer.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, pectase is the pectate lyase.The enzymatic activity of pectate lyase used herein represents that the 4-glycosidic bond is the catalytic action of cracking at random by shifting the cancellation effect to α-1 in the pectic acid (also claiming polygalacturonic acid).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 bivalent cation in the presence of show enzymatic 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, pseudomonas, klebsiella and xanthomonas, and bacillus subtilis (Nasser et al. (1993) FEBS Letts.335:319-326) and 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), bacillus stearothermophilus (Karbassi and Vaughn (1980) Can.J.Microbiol.26:377-384), bacillus (Hasegawa and Nagel (1966) J.Food Sci.31:838-845) and bacillus RK9 (Kelly and Fogarty (1978) Can.J.Microbiol.24:1164-1172).Arbitrarily above-mentioned and bivalent cation independence and/or heat endurance pectate lyase may be used to implement the present invention.In preferred embodiment, the pectate lyase comprises the al. as Heffron et, (199 5) Mol.PlantMicrobeInteract.8:331-334 and Henrissat et al., the amino acid sequence of the disclosed pectate lyase of (1995) Plant Physiol.107:963-976.
The amount of mixing pectase 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 pectase 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.
Protease: can adopt any protease of the present invention that is applicable to.The protease that is fit to comprises animal, plant or microbe-derived those, the preferred microorganism source.Preferably, protease can be serine protease or metalloproteinases, more preferably alkaline microbial protease or trypsin-like protease.The example of protease 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), tryptophanyl aminopeptidase (3.4.11.17) and methionyl aminopeptidase (3.4.11.18); The serine endopeptidase comprises chymotrypsin (3.4.21.1), trypsase (3.4.21.4), cucumisin (3.4.21.25), brachyurin (3.4.21.32), cerevisin (3.4.21.48) and subtilopeptidase A (3.4.21.62); The cystine endopeptidase, comprise papain (3.4.2 2.2), ficain (3.4.2 2.3), chymopapain (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 pepsin (3.4.23.25); And Zinc metalloproteinase, comprise Bacillolysin (3.4.24.28).
Commercial available protease 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 protease 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 hydrolases) 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.lanuginosus), as EP 258,068 and EP 305,216 is described, perhaps from H.insolens, as described in WO 96/13580; Pseudomonas lipase, for example from Pseudomonas alcaligenes or pseudomonas pseudoalcaligenes (EP218,272), (EP 331 for pseudomonas cepacia, 376), Situ Ci Shi pseudomonad (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 hay bacillus (Dartois et al., Biochem.Biophys.Acta, 1131:253-360,1993), bacillus stearothermophilus (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
TMWith LipolaseUltra
TM, Lipozyme
TM, Palatase
TM, Novozym
TM435 and Lecitase
TM(Novovozymes A/S).The activity of lipase can be as " Methods of EnzymaticAnalysis ", 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 the at of deriving from Humicolainsolens at strain DSM 1800, as U.S. Patent No. 4,810,414 embodiment 2 are described.
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 also comprises the biological degumming enzyme of deriving from above-mentioned enzyme, and wherein one or more amino acid are added into, leave out or replace, and comprise the hybrid polypeptide, 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 descended incubation 6 hours at specified temp (for example 75 ℃).Then with flat board (i) at 1M CaCl
2The middle immersion 0.5 hour perhaps (ii) soaked 1 hour in the 1% bromination alkyltrimethylammonium (MTAB, Sigma M-7635) that mixes.These two kinds of technologies all cause Polygalacturonate to be deposited in the agar.The zone that clarification in the galacturonic hydrochlorate background that is precipitated, occurs, the activity of detection pectate lyase.Sensitivity is measured in the dilution calibration of use standard pectate lyase prepared product.
Utilization is effectively come unstuck and is improved wettability usually according to the dropping liquid experimental measurement of AATCC test method 39-1980.Preferably, the wettability of the fabric after the bleaching be 20 seconds (seconds) or below, most preferably be 10 seconds or below.
Destarch used in this invention and biological degumming enzyme can be to derive from their cell source, perhaps can be that reorganization produces, and can be purifying or separate." purifying " used herein or " separation " 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 synthesizes, can the interferases activity.Usually, destarch separates from bacterium or fungi microbe with the biological degumming enzyme, and wherein it is produced as endogenous component or recombinant products.If enzyme is secreted in the culture medium, so purifying can comprise utilize conventional method by centrifugal, filter or precipitation is come isolation medium and living beings.Select as an alternative, can from host cell, discharge enzyme with separating of living beings 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 isoelectric 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 amino acid 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 chemical modification, to strengthen one or more character, gives they and then more advantage, for example improves solubility, reduces unstability or divalent ion dependence etc.Modification comprises phosphorylation, acetylation, sulphation, acidylate or other protein modification effects well known by persons skilled in the art without limitation.
Bleaching system
" peracid bleaching system " of the present invention comprises one or more peracid bleaching compounds, optional comprising, and base reagent, and optionally comprise at least a bleaching stibilizer.
The peracid bleaching compounds
" peracid bleaching compounds " of the present invention or " peroxy acid bleach compound " are to comprise (acid OOH) of at least one perhydroxyl radical.Preferably, described peracid bleaching compounds is selected from a few class organic peracid materials.Preferred described peracid is a performic acid, or comprises the carboxylic acid aliphatic series peroxy acid (carboxylicaliphatic peroxyacids) of single percarboxylic acids base and the straight or branched saturated alkyl chain that is less than 11 carbon atoms.The aliphatic carboxylic acid peroxy acid that comprises the straight chain saturated alkyl chain that is less than 6 carbon atoms also is preferred.Such peroxy acid example is a peracetic acid, perpropionic acid, mistake-n-butyric acid and mistake-n-valeric acid.Special preferred acetic hydroperoxide is because its validity and relative simple preparation method.
In another specific embodiment of the present invention, organic peroxide acid be selected from contain the straight or branched alkyl chain that is less than 16 carbon atoms and, two percarboxylic acids (diperoxycarboxylic acid) that have two percarboxylic acids groups to replace at the carbon atom that is positioned at relative alpha-omega position.Such peroxy acid for example 1, the own diperoxy diacid of 6-(1,6-hexanediperoxydioic acid), 1, the hot diperoxy diacid of 8-, 1,10-diperoxy in last of the ten Heavenly stems diacid, 1,12-dodecane diperoxy diacid (1,12-dodecanediperoxydioic acid).In another specific embodiment of the present invention, organic peroxide acid is selected from the aromatic series peroxy acid, and its each benzene nucleus contains at least one and crosses carboxylic group.Preferred each benzene nucleus only contains an aromatic series peroxy acid of crossing carboxylic group.Such peroxy acid for example is benzylhydroperoxide (peroxybenzoic acid).In another specific embodiment of the present invention, organic peroxide acid is replaced by one or more halogen atom or any other organic functions substituting group, as carbonyl (ketone, aldehyde or carboxylic acid), alcohol radical, nitrogen-containing group such as itrile group, nitro, amino and amide groups, sulfur-containing group such as sulfo group, sulfydryl.Permonosulphuric acid (peroxymonosulphuric acid) for example.
The peracid bleaching compounds joins in the aqueous solution or the cleaning solution (being treatment compositions) with effective dose, to remove foreign pigment, improves absorbability, reaches suitable whiteness and/or stainability (dyeability).Preferably, the peracid bleaching compounds amount in the treatment compositions that joins is the about 15g/l composition of about 0.01g/l-, the more preferably from about about 10g/l composition of 0.1g/l-, the most preferably from about about 5g/l composition of 0.5g/l-.
Base reagent
Base reagent is well known in the art.Preferred alkaline agent used in this invention comprises NaOH, sodium carbonate, sodium bicarbonate, sodium perborate, vulcanized sodium and sodium sulfite.The preferred amount that adds treatment compositions is the about 10g/l composition of about 0.1g/l-, more preferably from about the about 5g/l composition of 0.5g/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 alkali metal or the alkali salts that neutralize 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 compounding ingredient, for example edetate (EDTA), diethylene-triamine pentaacetic acid (DTPA), complexon I (NTA), methylglycine oxalic acid (MGDA), Beta-alanine oxalic acid (ADA), ethylenediamine-N, N '-disuccinate (EDDS) and phosphonates, for example ethylenediamine tetramethylene phosphonic acid salt, diethylenetriamine pentamethylenophosphonic acid salt (DTMPA) or hydroxy ethylene-1, the sour form of 1-di 2 ethylhexyl phosphonic acid or the alkali metal salt of neutralization 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 mensuration, for example use Macbeth coloreye); (ii) dedusting uniformity satisfactory (by macroscopic evaluation).Preferably, the whiteness of fabric is a 50Ganz unit or higher, most preferably is 60Ganz unit or higher.
Extra component:
In some invention embodiment, the aqueous solution or washing lotion further comprise other components, comprise other enzymes without limitation, and surfactant, antifoaming agent, lubricant, synergistic device (builder system), 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 imbibition is relevant with colouring power.
The enzyme that is suitable for use among the present invention comprises aforesaid pectase, protease 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 derive from microorganism, 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.0495 257, PCT patent application No.WO 91/17244 and the european patent application No.EP-A2-271004.
Enzyme can be to separate 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 determination 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 surfactant of the present invention and comprise nonionic (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.Anionic surfactant comprises linear alkylbenzene sulfonate (LAS), alpha-alkene sulfonate, alkyl sulfate (aliphatic alcohol sulfate), alcohol ethoxy sulfate, secondary paraffin sulfonate, alpha-sulfo fatty acid methyl ester, alkyl-or thiazolinyl-butanedioic 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 aminoglucose without limitation.
Synergistic device comprises alumino-silicate, silicate, multi-carboxylate, aliphatic 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, their concentration is between about 5% to 80%, by weight, preferably between about 5% and about 30%, by weight.
Antifoaming agent 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 suspender, soil releasing agent (soil-releasingagent), brightener, grinding agent and/or bactericide, 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 cellulose material will depend on the processing system is continuous, discontinuous pad-batch or in batches.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 cellulose material passes, and cellulose material absorbs 0.5-1.5 usually doubly to the working fluid of its weight during this process.In batch operation, make cellulose material be exposed to enzyme solutions 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.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 continuous and other (batch) processes in batches, 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 crude 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 continuous, discontinuous pad-batch or in batches.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 time can have nothing in common with each other, and estimate (a) pectin elimination efficiency of gained cellulose material or textiles afterwards; (b) come unstuck character, for example wettability; (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.The first time also can be different at aspects such as temperature, stir speed (S.S.), times with the condition of the incubation second time.
Embodiment
Be to non-limiting illustrating of the present invention below.
Embodiment 1: utilize H
2O
2Mono bath is biological 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 (interlock knit fabric).With fabric Labomat beaker (the Mathis Labomat that packs into, Werner Mathis USA, Inc, NC), pour 250ml 20mM sodium bicarbonate-sodium carbonate cushioning liquid (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 stabilizing agent (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 running water, to remove residual chemicals, 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 wettability, 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 wettability all are low-down.This example shows, do not having alkali to exist to place an order the fabric with the hydrogen peroxide bleaching braiding to improve whiteness, wettability and efficiency of dust collection only limitedly.
Embodiment 2: utilize H
2O
2/ NaOH mono bath is biological degumming and bleaching simultaneously
Use fabric and the equipment identical with last example 1.Experimentize according to identical with example 1 basically mode, except adding 2g/l NaOH to biological degumming/liquid lime chloride.
The result is as shown in table 1.The existence of alkali improves the whiteness of fabric dramatically.But because alkali makes enzyme denaturation, wettability is very poor.
Embodiment 3: utilize H
2O
2/ NaOH mono bath order (sequential) biological degumming and bleaching
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 (pH 9.2) 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, NaOH and sodium metasilicate.H
2O
2, NaOH and sodium metasilicate ultimate density identical with last example 1.℃ reach 1 hour by 5 ℃ of/minute rising Labomat temperature to 70, drain water afterwards.Then fabric is thoroughly washed with running water, to remove residual alkali, at room temperature dry.
The result is as shown in table 1.Wettability is better than pattern simultaneously.
Embodiment 4: use H
2O
2/ NaOH two bath (two-bath) biological degumming and bleaching
Experimentize according to identical with last example 3 basically mode, except draining after the stage at biological degumming come unstuck solution and water replace.
The result is as shown in table 1 below.The peroxide bleaching of two bath tupes (embodiment 4) is better than mono bath pattern (embodiment 3): wettability is better, and whiteness is higher, and dedusting is more effective.
Embodiment 5: use H
2O
2The two baths of/NaOH (two-bath) are come unstuck and are bleached
Experimentize according to identical with last example 4 basically mode, in the solution that comes unstuck, do not contain the pectate lyase.
The result is as shown in table 1 below.Owing to do not contain the pectate lyase, the wettability of fabric is very poor.This embodiment shows that the biological degumming enzyme is very important for the wettability of improving fabric.
The mono bath biological degumming and the bleaching of table 1. knit goods (knitted fabrics)
| Embodiment # | Procedure schema | Come unstuck | Bleaching | Whiteness Ganz 82 | Wettability second | Dust |
| ????1 | Mono bath simultaneously | Enzyme | Peroxide | ??44.3 | ????＞60 | ???5 |
| ????2 | Mono bath simultaneously | Enzyme | Peroxide/NaOH | ??59.2 | ????＞60 | ???1 |
| ????3 | Mono bath successively | Enzyme | Peroxide/NaOH | ??58.5 | ????39 | ???2 |
| ????4 | Two baths | Enzyme | Peroxide/NaOH | ??63.0 | ????10 | ???1 |
| ????5 | Two baths | Buffer solution | Peroxide/NaOH | ??62.7 | ????＞60 | ???1 |
* dust grade: 1 is minimum, and 5 is maximum
Embodiment 6: with peracetic acid (PA) mono bath biological degumming and bleaching simultaneously
(4600 types, Ramseur Co. NC) cut the heavily about 25 45cm * 21.5cm fabrics that restrain from binding type knit goods.With fabric Labomat beaker (the Mathis Labomat that packs into, WernerMathis 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 (KierlonJet B, BASF), 50mM peracetic acid and 0.75g/l stabilizing agent (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 running water, to remove residual chemicals, at room temperature dried overnight.
The result is as shown in table 2 below.Evidence shows that under this experimental condition peracetic acid is than the more efficiently bleaching agent of hydrogen peroxide (peroxide) (embodiment 6 compares embodiment 1).
Embodiment 7: adopt peracetic acid (PA) mono bath order biological degumming and bleaching
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 (pH 9.2) 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 peracetic acid and Calgon to same beaker.The ultimate density of peracetic acid and Calgon is identical with last example 6.℃ reach 1 hour by 5 ℃ of/minute rising Labomat temperature to 70, drain water afterwards.Then fabric is thoroughly washed with running water, to remove residual alkali, at room temperature dry.
The result is as shown in table 2.Test shows that the mono bath ordered mode carries out the fabric moisture degree that biological degumming and peroxyacetic acid bleaching obtain and be better than pattern simultaneously.
Embodiment 8: the mono bath of employing peracetic acid (PA) is come unstuck in proper order and is bleached
Experimentize according to identical with last example 7 basically mode, in the solution that comes unstuck, do not contain the pectate lyase.
The result is as shown in table 2 below.Test has proved that further the pectate lyase can improve the wettability of fabric.
Embodiment 9: adopt peracetic acid (PA) and NaOH mono bath order biological degumming and bleaching
Experimentize according to identical with last example 7 basically mode, in liquid lime chloride, add the 2g/L NaOH.
The result is as shown in table 2 below.Evidence add whiteness and the wettability that alkali can improve fabric in the bleaching bath.
Embodiment 10: adopt two bath biological degummings of peracetic acid (PA) and bleaching
Experimentize according to identical with last example 7 basically mode, except draining degumming baths and water consumption substitution after the biological degumming step.
The result is as shown in table 2 below.Surprisingly, whiteness and dust removal that (embodiment 9) are handled in two baths are good not as mono bath ordered mode (embodiment 7), and this is with observed very different in biological degumming and peroxide bleaching.
Embodiment 11: the two baths of employing peracetic acid (PA) are come unstuck and are bleached
Experimentize according to identical with last example 10 basically mode, in the solution that comes unstuck, do not contain the pectate lyase.
The result is as shown in table 2 below.The wettability of fabric is very poor.Test has proved that further the pectate lyase can improve the wettability of fabric.
The biological degumming and the peroxyacetic acid bleaching of table 2. knit goods (knitted fabrics)
| Embodiment # | Tupe | Come unstuck | Bleaching | Whiteness Ganz 82 | Wettability second | Dust |
| Initial fabric | ????8.5 | ????＞60 | ??5 | |||
| ????6 | Mono bath simultaneously | Enzyme | ????PA | ????62.6 | ????40 | ??1 |
| ????7 | The mono bath order | Enzyme | ????PA | ????62.1 | ????4 | ??1 |
| ????8 | The mono bath order | Buffer solution | ????PA | ????61.8 | ????26 | ??1 |
| ????9 | The mono bath order | Enzyme | ????PA/NaOH | ????64.2 | ????2 | ??1 |
| ????10 | Two baths | Enzyme | ????PA | ????59.3 | ????3 | ??2 |
| ????11 | Two baths | Buffer solution | ????PA | ????59.6 | ????＞60 | ??2 |
* dust grade: 1 is minimum, and 5 is maximum
* PA: peracetic acid
Embodiment 12: utilize H
2O
2/ NaOH mono bath order biological degumming and bleaching
Experimentize according to identical with last example 3 basically mode, except (INC. PA) replaces knit goods (knitted fabric) for 428U, Testfabric with 25 gram destarch braided fabrics (woven fabric).
The result is as shown in table 3.Mono bath order biological degumming and peroxide bleaching.The braided fabric whiteness that obtains is very low.
Embodiment 13: utilize H
2O
2/ NaOH two bath biological degumming and bleaching
Experimentize according to identical with last example 4 basically mode, except (INC. PA) replaces knit goods for 428U, Testfabric with 25 gram destarch braided fabrics (woven fabric).
The result is as shown in table 3.Test shows that further two peroxide (peroxide) bleachings of bathing ordered mode are better than the mono bath pattern.
Embodiment 14: utilize peracetic acid (PA)/NaOH mono bath order biological degumming and bleaching
Experimentize according to identical with last example 12 basically mode, except bleaching liquid comprises 50mM peracetic acid (Aldrich), 2g/L NaOH and 0.75g/L Calgon (BASF).
The result is as shown in table 3.Test shows that peracetic acid (embodiment 14) is than the more effective bleaching agent of peroxide (embodiment 12).
Embodiment 15: utilize peracetic acid (PA)/NaOH mono bath order biological degumming and bleaching
Experimentize according to identical with last example 13 basically mode, except bleaching liquid comprises 50mM peracetic acid (Aldrich), 2g/L NaOH and 0.75g/L Calgon (BASF).
The result is as shown in table 3.With observed similar from knit goods embodiment (6-10), this embodiment shows the mono bath ordered mode aspect improvement whiteness and dust removal, be better than two tupes (embodiment 9) of bathing greatly.
Table 3: the biological degumming of braided fabric and bleaching
| Embodiment # | Tupe | Come unstuck | Bleaching | Whiteness Ganz 82 | Wettability second | Dust |
| ????12 | The mono bath order | Enzyme | Peroxide/NaOH | ????50.3 | ????1 | ????2 |
| ????13 | Two baths | Enzyme | Peroxide/NaOH | ????55.4 | ????1 | ????1 |
| ????14 | The mono bath order | Enzyme | ????PA/NaOH | ????63.3 | ????1 | ????1 |
| ????15 | Two baths | Enzyme | ????PA/NaOH | ????59.5 | ????1 | ????1 |
* dust grade: 1 is minimum, and 5 is maximum
All patents, patent application and the list of references 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 (44)
1. handle the method for cellulose material, comprise cellulose material (i) is contacted with enzyme system, the destarch and/or the biological degumming that are used for cellulose material, (ii) contact, wherein add enzyme system and bleaching system to the single solution while or the priority that contain cellulose material with the bleaching system that comprises at least a peracid bleaching compounds.
2. the process of claim 1 wherein and add enzyme system and bleaching system simultaneously to the solution that contains cellulose material.
3. the process of claim 1 wherein successively to add enzyme system and bleaching system that comprise (i) and add enzyme system, incubation (ii) adds bleaching system, incubation subsequently to the solution that contains cellulose material.
4. the process of claim 1 wherein cellulose material is contacted with bleaching system with enzyme system, form wettability and be 20 seconds or following, whiteness is the fabric of 50Ganz unit at least.
5. the process of claim 1 wherein that (i) makes cellulose material contact with enzyme system, forming wettability is 20 seconds or lower fabric, (ii) adds bleaching system to the solution that contains cellulose material afterwards.
6. the method for claim 3, 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.
7. this enzyme system that the process of claim 1 wherein comprises at least a enzyme and at least a enzyme that is used for the biological degumming cellulose material that makes the cellulose material destarch.
8. the process of claim 1 wherein that this enzyme system is the biological degumming enzyme system.
9. the process of claim 1 wherein that this enzyme system is the destarch enzyme system.
10. the process of claim 1 wherein that this destarch enzyme system comprises at least a destarch enzyme, be selected from the group of forming by α-Dian Fenmei and beta amylase and combination thereof.
11. the process of claim 1 wherein that this biological degumming enzyme system comprises at least a biological degumming enzyme, be selected from the group of forming by pectase, protease, lipase and any above-mentioned combination.
12. the method for claim 1, 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.
13. the process of claim 1 wherein that this biological degumming enzyme system comprises the pectate lyase.
14. the process of claim 1 wherein that this biological degumming enzyme system comprises protease, is selected from the group of being made up of aminopeptidase, serine endopeptidase, cysteine endopeptidase, aspartoyl endopeptidase and Zinc metalloproteinase.
15. the process of claim 1 wherein that this biological degumming enzyme system comprises lipase, is selected from the group of being made up of triacylglycerol lipases and phosphatidase.
16. the process of claim 1 wherein that this biological degumming enzyme system comprises a kind of like this pectate lyase, the enzymatic activity of the pectate lyase of performance maximum under about temperature more than 70 ℃.
17. the process of claim 1 wherein that this biological degumming enzyme system comprises a kind of like this pectate lyase, the enzymatic activity of the pectate lyase of performance maximum under about pH more than 8.
18. the process of claim 1 wherein that this cellulose material comprises textiles.
19. the process of claim 1 wherein that described cellulose material comprises cotton.
20. the process of claim 1 wherein that described single solution further comprises one or more buffers, surfactant, chelating agent and/or lubricant, or any above-mentioned salt.
21. the process of claim 1 wherein that described at least a peracid bleaching compounds is the organic peroxy acid compound.
22. the process of claim 1 wherein that described at least a peracid bleaching compounds is a peracetic acid.
23. the process of claim 1 wherein that described at least a peracid bleaching compounds is selected from the lower class organic peroxide acid: performic acid and carboxylic acid aliphatic series peroxy acid; The diperoxy carboxylic acid; The aromatics peroxy acid; The organic peroxide acid that one or more halogen atom or any other organo-functional group replace.
24. the process of claim 1 wherein that described cellulose material carries out with at least a bleaching stibilizer with the contact of at least a peracid bleaching compounds.
25. the method for claim 23, wherein said bleaching stibilizer is selected from edetate (EDTA), diethylene-triamine pentaacetic acid (DTPA), complexon I (NTA), methylglycine oxalic acid (MGDA), Beta-alanine oxalic acid (ADA), ethylenediamine-N, N '-disuccinate (EDDS), ethylenediamine tetramethylene phosphonic acid salt, diethylenetriamine pentamethylenophosphonic acid salt (DTMPA) or hydroxy ethylene-1, the 1-di 2 ethylhexyl phosphonic acid.
26. the process of claim 1 wherein that described cellulose material carries out with at least a base reagent with the contact of at least a peracid bleaching compounds.
27. the method for claim 26, wherein said base reagent is a NaOH.
28. the process of claim 1 wherein that described cellulose material carries out with at least a bleaching stibilizer and at least a base reagent with the contact of at least a peracid bleaching compounds.
29. handle the method for cellulose material, described method is protected to contain cellulose material is contacted in comprising the single-bath solution of cellulose material with (b) at least a peracid bleaching compounds with (a) at least a biological degumming enzyme.
30. the method for claim 29, wherein at least a biological degumming enzyme and at least a peracid bleaching compounds join in the single-bath solution that comprises cellulose material simultaneously.
31. the method for claim 29, wherein at least a biological degumming enzyme and at least a peracid bleaching compounds join in the single-bath solution that comprises cellulose material in proper order, described sequential process comprises (i) and adds at least a biological degumming enzyme in the solution that comprises cellulose material, and incubation cellulose material and biological degumming enzyme, (ii) add at least a peracid bleaching compounds then in the solution that comprises cellulose material and biological degumming enzyme and incubation.
32. the method for claim 29 also comprises cellulose material is contacted with at least a destarch enzyme.
33. the method for claim 32, wherein said destarch enzyme joins in the single-bath solution.
34. the method for claim 32 wherein before adding described biological degumming enzyme, adds the destarch enzyme to single-bath solution.
35. the method for claim 32, wherein said biological degumming enzyme and destarch enzyme add in the single-bath solution simultaneously.
36. the method for claim 32, wherein said destarch enzyme, biological degumming enzyme and peracid bleaching compounds add in the single-bath solution simultaneously.
37. the method for claim 30 is wherein carried out cellulose material and contacted with described at least a destarch enzyme in independent bath, described then monobath solution is as cellulose material is contacted with at least a peracid bleaching compounds with at least a biological degumming enzyme.
38. handle the method for cellulose material, described method comprises that (b) at least a destarch enzyme contacts in single-bath solution with (c) at least a peracid bleaching compounds with cellulose material and (a) at least a biological degumming enzyme.
39. the method for claim 38, wherein said at least a biological degumming enzyme, at least a destarch enzyme and at least a peracid bleaching compounds join in the monobath solution that comprises cellulose material simultaneously.
40. the method for claim 38, wherein said method comprises at least a biological degumming enzyme and at least a destarch enzyme is joined in the monobath solution that comprises cellulose material, the described at least a biological degumming enzyme of incubation, described at least a destarch enzyme and cellulose material add at least a peracid bleaching compounds and incubation then.
41. the method for processing cellulose material, this method comprise cellulose material is contacted in comprising the monobath solution of cellulose material with (b) at least a peracid bleaching compounds with (a) at least a destarch enzyme.
42. the method for claim 41, wherein said at least a destarch enzyme and at least a peracid bleaching compounds join in the monobath solution that comprises cellulose material simultaneously.
43. the method for claim 41, wherein said at least a destarch enzyme and described at least a peracid bleaching compounds join in the monobath solution that comprises cellulose material successively, described processing successively comprises (i) described at least a destarch enzyme is joined in the solution that comprises cellulose material, incubation cellulose material and destarch enzyme, (ii) add described at least a peracid bleaching compounds then in the solution that comprises cellulose material and destarch enzyme, and incubation.
44. the fabric that each method of claim 1-41 produces.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US30251201P | 2001-06-29 | 2001-06-29 | |
| US60/302,512 | 2001-06-29 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN1522323A true CN1522323A (en) | 2004-08-18 |
| CN1253627C CN1253627C (en) | 2006-04-26 |
Family
ID=23168045
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CNB02813091XA Expired - Fee Related CN1253627C (en) | 2001-06-29 | 2002-07-01 | Single-bath preparation of cellulosic materials |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US20030041387A1 (en) |
| EP (1) | EP1425462A4 (en) |
| CN (1) | CN1253627C (en) |
| BR (1) | BR0210718A (en) |
| CA (1) | CA2450755A1 (en) |
| WO (1) | WO2003002810A1 (en) |
Cited By (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102212975A (en) * | 2011-04-07 | 2011-10-12 | 孝感学院 | Separation method of pteroceltis tatarinowii fiber |
| CN102535177A (en) * | 2011-12-06 | 2012-07-04 | 常熟市凯达印染有限公司 | Bio-enzyme pretreatment technology for pure cotton fabric |
| CN102943391A (en) * | 2007-06-11 | 2013-02-27 | 诺维信公司 | Combining biopolishing and bleach clean-up |
| CN105625021A (en) * | 2016-03-31 | 2016-06-01 | 太仓市锦达印染有限公司 | Continuous production process for blended fabric printing and dyeing pretreatment |
| CN108130708A (en) * | 2018-01-12 | 2018-06-08 | 江门市宝发纺织服饰制造有限公司 | A kind of desizing ferment that single bath process is washed suitable for cowboy's desizing ferment washes auxiliary agent and preparation method thereof |
Families Citing this family (23)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20020086837A (en) * | 2002-09-16 | 2002-11-20 | 한국생산기술연구원 | Simultaneous desizing and bio-scouring method using enzyme in one bath |
| NL1021820C2 (en) * | 2002-11-01 | 2004-05-06 | Tno | Process for treating cellulose-containing raw textile cloth, textile cloth obtained with the method, the use of the treated textile cloth for the manufacture of textile products, and textile products made from the treated textile cloth. |
| US7931700B2 (en) * | 2002-12-27 | 2011-04-26 | Hbi Branded Apparel Enterprises, Llc | Composition for dyeing of cellulosic fabric |
| US7931699B2 (en) * | 2002-12-27 | 2011-04-26 | Hbi Branded Apparel Enterprises, Llc | Compositions for spray dyeing cellulosic fabrics |
| US7931701B2 (en) * | 2002-12-27 | 2011-04-26 | Hbi Branded Apparel Enterprises, Llc | Composition for dyeing of cellulosic fabric |
| US7592434B2 (en) | 2003-04-04 | 2009-09-22 | Verenium Corporation | Pectate lyases, nucleic encoding them and methods for making and using them |
| CN1308538C (en) * | 2003-08-27 | 2007-04-04 | 上海市纺织科学研究院 | One-bath process continuous production process for treating cotton and its blended fabric before dyeing and printing |
| MXPA06005652A (en) | 2003-12-03 | 2006-08-17 | Genencor Int | Perhydrolase. |
| US8476052B2 (en) | 2003-12-03 | 2013-07-02 | Danisco Us Inc. | Enzyme for the production of long chain peracid |
| US7754460B2 (en) | 2003-12-03 | 2010-07-13 | Danisco Us Inc. | Enzyme for the production of long chain peracid |
| WO2006002034A1 (en) * | 2004-06-15 | 2006-01-05 | Novozymes North America, Inc | Simultaneous desizing and scouring process |
| WO2006106097A1 (en) * | 2005-04-04 | 2006-10-12 | Basf Aktiengesellschaft | Process for treating non-dyed textile |
| EP1712673A1 (en) * | 2005-04-04 | 2006-10-18 | Basf Aktiengesellschaft | Process for treating non-dyed textile |
| WO2007067473A2 (en) | 2005-12-06 | 2007-06-14 | Genencor International, Inc. | Perhydrolase epitopes |
| MX2008012999A (en) | 2006-04-14 | 2008-10-17 | Genencor Int | One-step treatment of textiles. |
| EP2495316A3 (en) | 2006-06-21 | 2013-11-20 | Novozymes North America, Inc. | Desizing and scouring process of starch |
| MX2009003070A (en) * | 2006-09-22 | 2009-04-02 | Danisco Us Inc Genencor Div | Novel pectate lyase and method of use for bio-scouring. |
| US8404628B1 (en) | 2008-12-08 | 2013-03-26 | Hbi Branded Apparel Enterprises, Llc | Method for spray bleaching cellulosic fabrics |
| US20100140545A1 (en) * | 2008-12-08 | 2010-06-10 | May Ruth E | Compositions for spray bleaching cellulosic fabrics |
| WO2011045629A1 (en) | 2009-10-15 | 2011-04-21 | Danisco A/S | Lipid acyltransferase proteins and methods of making them |
| CN102817227B (en) * | 2012-08-14 | 2014-07-02 | 安徽舒城县翰文运动用品有限责任公司 | Feather decolorization treatment process |
| WO2014086659A2 (en) * | 2012-12-06 | 2014-06-12 | Ahmedabad Textile Industry's Research Association | Method for enzymatical preparation of textiles |
| EP3748065A1 (en) * | 2019-06-03 | 2020-12-09 | Aquitex Acabamentos Químicos Têxteis, Sa | Process for fabric bleaching, products and uses thereof |
Family Cites Families (15)
| 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 |
| US5234616A (en) * | 1987-10-30 | 1993-08-10 | The Clorox Company | Method of laundering clothes using a delayed onset active oxygen bleach composition |
| 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 |
| DE4407801A1 (en) * | 1993-03-15 | 1994-09-22 | Sandoz Ag | Treatment of textiles |
| 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 |
| DE19634448C2 (en) * | 1996-08-26 | 1999-06-24 | Voith Sulzer Papiermasch Gmbh | Method and device for applying a liquid or pasty medium to a running material web |
| JP2001506708A (en) * | 1996-12-04 | 2001-05-22 | ノボ ノルディスク バイオケム ノース アメリカ，インコーポレイティド | Alkaline enzyme scouring of cotton woven fabric |
| US6124127A (en) * | 1997-11-24 | 2000-09-26 | Novo Nordisk A/S | Pectate lyase |
| US6258590B1 (en) * | 1998-11-02 | 2001-07-10 | Novozymes A/S | Biopreparation of textiles at high temperatures |
| US6146428A (en) * | 1998-04-03 | 2000-11-14 | Novo Nordisk A/S | Enzymatic treatment of denim |
| US6162260A (en) * | 1999-05-24 | 2000-12-19 | Novo Nordisk Biochem North America, Inc. | Single-bath biopreparation and dyeing of textiles |
| AU5403500A (en) * | 1999-06-23 | 2001-01-31 | Breel, Greta J. | Bleaching detergent compositions |
| DE60129670D1 (en) * | 2000-02-15 | 2007-09-13 | Procter & Gamble | One-step process for the production of textiles |
-
2002
- 2002-07-01 EP EP02748030A patent/EP1425462A4/en not_active Withdrawn
- 2002-07-01 US US10/187,518 patent/US20030041387A1/en not_active Abandoned
- 2002-07-01 CN CNB02813091XA patent/CN1253627C/en not_active Expired - Fee Related
- 2002-07-01 WO PCT/US2002/020925 patent/WO2003002810A1/en not_active Application Discontinuation
- 2002-07-01 CA CA002450755A patent/CA2450755A1/en not_active Abandoned
- 2002-07-01 BR BR0210718-0A patent/BR0210718A/en active Pending
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN102943391A (en) * | 2007-06-11 | 2013-02-27 | 诺维信公司 | Combining biopolishing and bleach clean-up |
| CN102212975A (en) * | 2011-04-07 | 2011-10-12 | 孝感学院 | Separation method of pteroceltis tatarinowii fiber |
| CN102212975B (en) * | 2011-04-07 | 2012-10-31 | 孝感学院 | Separation method of pteroceltis tatarinowii fiber |
| CN102535177A (en) * | 2011-12-06 | 2012-07-04 | 常熟市凯达印染有限公司 | Bio-enzyme pretreatment technology for pure cotton fabric |
| CN105625021A (en) * | 2016-03-31 | 2016-06-01 | 太仓市锦达印染有限公司 | Continuous production process for blended fabric printing and dyeing pretreatment |
| CN108130708A (en) * | 2018-01-12 | 2018-06-08 | 江门市宝发纺织服饰制造有限公司 | A kind of desizing ferment that single bath process is washed suitable for cowboy's desizing ferment washes auxiliary agent and preparation method thereof |
Also Published As
| Publication number | Publication date |
|---|---|
| CA2450755A1 (en) | 2003-01-09 |
| WO2003002810A1 (en) | 2003-01-09 |
| US20030041387A1 (en) | 2003-03-06 |
| EP1425462A1 (en) | 2004-06-09 |
| CN1253627C (en) | 2006-04-26 |
| EP1425462A4 (en) | 2008-01-02 |
| BR0210718A (en) | 2004-07-20 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CN1253627C (en) | Single-bath preparation of cellulosic materials | |
| CN1116471C (en) | Alkaline enzyme scouring of cotton textiles | |
| CN1177966C (en) | Single-bath bioscouring and dyeing of textiles | |
| JP5485705B2 (en) | Enzyme foam treatment for laundry | |
| AU2009291795B2 (en) | Enzymatic textile bleaching compositions and methods of use thereof | |
| EP1159479B1 (en) | Enzymatic treatment of textiles at high temperatures | |
| BRPI0718506A2 (en) | LIASE PECTATE AND METHOD OF USE FOR BIOLIMPEZA | |
| MX2008012999A (en) | One-step treatment of textiles. | |
| WO2019057758A1 (en) | Use of enzymes for improving water absorption and/or whiteness | |
| CN1723272A (en) | Preparation of cellulosic materials | |
| JP4954414B2 (en) | Bleaching using natural non-cotton cellulosic fiber enzymes | |
| Nyanhongo et al. | Microbial applications for fabric and textile industries | |
| CA2394964C (en) | Enzymatic bleaching of natural non-cotton cellulosic fibers | |
| WO2004040054A1 (en) | Method for treating cellulosic grey fabric, products obtained by this process and their use | |
| MXPA01004326A (en) | Biopreparation of textiles at high temperatures |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| C06 | Publication | ||
| PB01 | Publication | ||
| C10 | Entry into substantive examination | ||
| SE01 | Entry into force of request for substantive examination | ||
| C14 | Grant of patent or utility model | ||
| GR01 | Patent grant | ||
| C19 | Lapse of patent right due to non-payment of the annual fee | ||
| CF01 | Termination of patent right due to non-payment of annual fee |