ES2602792T3 - Polipéptidos con actividad de xilanasa - Google Patents
Polipéptidos con actividad de xilanasa Download PDFInfo
- Publication number
- ES2602792T3 ES2602792T3 ES09834136.5T ES09834136T ES2602792T3 ES 2602792 T3 ES2602792 T3 ES 2602792T3 ES 09834136 T ES09834136 T ES 09834136T ES 2602792 T3 ES2602792 T3 ES 2602792T3
- Authority
- ES
- Spain
- Prior art keywords
- xylanase
- amino acid
- polypeptide
- seq
- xylanase activity
- 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.)
- Active
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- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 title abstract description 104
- 230000000694 effects Effects 0.000 title abstract description 55
- 229920001184 polypeptide Polymers 0.000 title abstract description 47
- 102000004196 processed proteins & peptides Human genes 0.000 title abstract description 47
- 108090000765 processed proteins & peptides Proteins 0.000 title abstract description 47
- 125000003275 alpha amino acid group Chemical group 0.000 abstract description 47
- 238000012986 modification Methods 0.000 abstract description 26
- 230000004048 modification Effects 0.000 abstract description 26
- 238000006467 substitution reaction Methods 0.000 abstract description 24
- 235000014469 Bacillus subtilis Nutrition 0.000 abstract description 21
- 150000001413 amino acids Chemical class 0.000 abstract description 20
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 abstract description 5
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 abstract description 5
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- 102000004169 proteins and genes Human genes 0.000 description 13
- 108090000623 proteins and genes Proteins 0.000 description 13
- 235000018102 proteins Nutrition 0.000 description 12
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- 241000894006 Bacteria Species 0.000 description 4
- 102220488043 Bone morphogenetic protein receptor type-2_I77L_mutation Human genes 0.000 description 4
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- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 4
- 125000000539 amino acid group Chemical group 0.000 description 4
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- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 4
- 102220228199 rs1064796032 Human genes 0.000 description 4
- 230000035945 sensitivity Effects 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 229920001221 xylan Polymers 0.000 description 4
- 108010001817 Endo-1,4-beta Xylanases Proteins 0.000 description 3
- 241000233866 Fungi Species 0.000 description 3
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- 102220530637 Putative apolipoprotein(a)-like protein 2_G12F_mutation Human genes 0.000 description 3
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- 241000894007 species Species 0.000 description 3
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- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 2
- 241000228212 Aspergillus Species 0.000 description 2
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- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 102220618489 Isocitrate dehydrogenase [NAD] subunit gamma, mitochondrial_N54Q_mutation Human genes 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
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- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 2
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- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 2
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- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241000193397 Paenibacillus pabuli Species 0.000 description 2
- 241000194105 Paenibacillus polymyxa Species 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- 241000187398 Streptomyces lividans Species 0.000 description 2
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- 239000004473 Threonine Substances 0.000 description 2
- 241001136486 Trichocomaceae Species 0.000 description 2
- 241000209140 Triticum Species 0.000 description 2
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- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 101710100170 Unknown protein Proteins 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
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- 235000003704 aspartic acid Nutrition 0.000 description 2
- 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 2
- 235000008429 bread Nutrition 0.000 description 2
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- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- YERABYSOHUZTPQ-UHFFFAOYSA-P endo-1,4-beta-Xylanase Chemical group C=1C=CC=CC=1C[N+](CC)(CC)CCCNC(C(C=1)=O)=CC(=O)C=1NCCC[N+](CC)(CC)CC1=CC=CC=C1 YERABYSOHUZTPQ-UHFFFAOYSA-P 0.000 description 2
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- 235000013922 glutamic acid Nutrition 0.000 description 2
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- 229930182470 glycoside Natural products 0.000 description 2
- 150000002338 glycosides Chemical class 0.000 description 2
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- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
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- 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
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- 101710152845 Arabinogalactan endo-beta-1,4-galactanase Proteins 0.000 description 1
- 241000235349 Ascomycota Species 0.000 description 1
- 241000122821 Aspergillus kawachii Species 0.000 description 1
- 241000228232 Aspergillus tubingensis Species 0.000 description 1
- 241000223651 Aureobasidium Species 0.000 description 1
- 241000193833 Bacillales Species 0.000 description 1
- 241000304886 Bacilli Species 0.000 description 1
- 241000193752 Bacillus circulans Species 0.000 description 1
- 101710104295 Beta-1,4-xylanase Proteins 0.000 description 1
- 102100032487 Beta-mannosidase Human genes 0.000 description 1
- 108010059892 Cellulase Proteins 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 101710089042 Demethyl-4-deoxygadusol synthase Proteins 0.000 description 1
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- 241000223260 Trichoderma harzianum Species 0.000 description 1
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- UGXQOOQUZRUVSS-ZZXKWVIFSA-N [5-[3,5-dihydroxy-2-(1,3,4-trihydroxy-5-oxopentan-2-yl)oxyoxan-4-yl]oxy-3,4-dihydroxyoxolan-2-yl]methyl (e)-3-(4-hydroxyphenyl)prop-2-enoate Chemical compound OC1C(OC(CO)C(O)C(O)C=O)OCC(O)C1OC1C(O)C(O)C(COC(=O)\C=C\C=2C=CC(O)=CC=2)O1 UGXQOOQUZRUVSS-ZZXKWVIFSA-N 0.000 description 1
- 102000005840 alpha-Galactosidase Human genes 0.000 description 1
- 108010030291 alpha-Galactosidase Proteins 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- -1 arabinoxylan Chemical class 0.000 description 1
- 229920000617 arabinoxylan Polymers 0.000 description 1
- SRBFZHDQGSBBOR-KKQCNMDGSA-N beta-D-xylose Chemical group O[C@@H]1CO[C@@H](O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-KKQCNMDGSA-N 0.000 description 1
- 108010055059 beta-Mannosidase Proteins 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000006555 catalytic reaction Methods 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 238000006073 displacement reaction Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000009456 molecular mechanism Effects 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 239000012038 nucleophile Substances 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 102200025388 rs17108378 Human genes 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 235000015099 wheat brans Nutrition 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2477—Hemicellulases not provided in a preceding group
- C12N9/248—Xylanases
- C12N9/2482—Endo-1,4-beta-xylanase (3.2.1.8)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y02—TECHNOLOGIES OR APPLICATIONS FOR MITIGATION OR ADAPTATION AGAINST CLIMATE CHANGE
- Y02E—REDUCTION OF GREENHOUSE GAS [GHG] EMISSIONS, RELATED TO ENERGY GENERATION, TRANSMISSION OR DISTRIBUTION
- Y02E50/00—Technologies for the production of fuel of non-fossil origin
- Y02E50/10—Biofuels, e.g. bio-diesel
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biotechnology (AREA)
- Enzymes And Modification Thereof (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Bakery Products And Manufacturing Methods Therefor (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Fodder In General (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP08172755 | 2008-12-23 | ||
| EP08172755 | 2008-12-23 | ||
| US14617009P | 2009-01-21 | 2009-01-21 | |
| US146170P | 2009-01-21 | ||
| PCT/DK2009/050352 WO2010072225A1 (en) | 2008-12-23 | 2009-12-23 | Polypeptides with xylanase activity |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2602792T3 true ES2602792T3 (es) | 2017-02-22 |
Family
ID=40494933
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES09834136.5T Active ES2602792T3 (es) | 2008-12-23 | 2009-12-23 | Polipéptidos con actividad de xilanasa |
Country Status (13)
| Country | Link |
|---|---|
| US (2) | US8765438B2 (https=) |
| EP (1) | EP2382310B1 (https=) |
| JP (2) | JP2012513207A (https=) |
| KR (1) | KR20110117663A (https=) |
| CN (1) | CN102300985A (https=) |
| AU (1) | AU2009329608B2 (https=) |
| CA (1) | CA2747224C (https=) |
| DK (1) | DK2382310T3 (https=) |
| EA (1) | EA201170879A1 (https=) |
| ES (1) | ES2602792T3 (https=) |
| MX (2) | MX347545B (https=) |
| UA (1) | UA103215C2 (https=) |
| WO (1) | WO2010072225A1 (https=) |
Families Citing this family (21)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20110104539A (ko) | 2008-12-23 | 2011-09-22 | 대니스코 에이/에스 | 자일라나제 활성을 갖는 폴리펩타이드 |
| BR112014005873B1 (pt) | 2011-09-14 | 2021-11-16 | Dupont Nutrition Biosciences Aps | Composição, uso de uma composição, método de alteração da filtrabilidade, método de redução da pressão acumulada, método para a produção de um alimento, método para a produção de uma pasta de brassagem e método para a produção de um biocombustível |
| AU2012387042A1 (en) | 2012-08-03 | 2015-02-19 | Dupont Nutrition Biosciences Aps | Enzymes |
| JP6056870B2 (ja) * | 2012-10-19 | 2017-01-11 | 国立研究開発法人産業技術総合研究所 | 新規キシラナーゼ |
| WO2014140167A1 (en) | 2013-03-14 | 2014-09-18 | Dsm Ip Assets B.V. | Cell wall deconstruction enzymes of malbranchea cinnamomea and uses thereof |
| WO2014140165A1 (en) | 2013-03-14 | 2014-09-18 | Dsm Ip Assets B.V. | Cell wall deconstruction enzymes of paecilomyces byssochlamydoides and uses thereof |
| US9850512B2 (en) | 2013-03-15 | 2017-12-26 | The Research Foundation For The State University Of New York | Hydrolysis of cellulosic fines in primary clarified sludge of paper mills and the addition of a surfactant to increase the yield |
| GB201401699D0 (en) * | 2014-01-31 | 2014-03-19 | Dupont Nutrition Biosci Aps | Protein |
| US9951363B2 (en) | 2014-03-14 | 2018-04-24 | The Research Foundation for the State University of New York College of Environmental Science and Forestry | Enzymatic hydrolysis of old corrugated cardboard (OCC) fines from recycled linerboard mill waste rejects |
| EP3017706A1 (en) | 2014-11-05 | 2016-05-11 | Dupont Nutrition Biosciences ApS | Enzymes for malting |
| WO2016140960A1 (en) | 2015-03-04 | 2016-09-09 | Dupont Nutrition Biosciences Aps | Cereal grain processing |
| WO2017152169A1 (en) | 2016-03-04 | 2017-09-08 | Danisco Us Inc. | Engineered ribosomal promoters for protein production in microorganisms |
| EP3703661A1 (en) | 2017-11-02 | 2020-09-09 | Danisco US Inc. | Freezing point depressed solid matrix compositions for melt granulation of enzymes |
| CN109971737B (zh) * | 2017-12-28 | 2020-11-06 | 中粮集团有限公司 | 木聚糖酶HoXyn11A的突变体及其制备方法和用途 |
| IT201900005588A1 (it) * | 2019-04-11 | 2020-10-11 | Heallo S R L | Idrolizzato di fibra vegetale e suoi usi nell’alimentazione umana ed animale |
| KR102700160B1 (ko) * | 2021-10-29 | 2024-08-28 | 씨제이제일제당 주식회사 | 자일라나제 활성을 갖는 변이형 폴리펩티드 |
| CN118202042A (zh) | 2021-11-09 | 2024-06-14 | Ab酶有限公司 | 改进的木聚糖酶 |
| CN119630280A (zh) | 2022-05-14 | 2025-03-14 | 诺维信公司 | 用于预防、处理、抑制和/或消除植物病原性侵染和感染的组合物和方法 |
| EP4286499A1 (en) * | 2022-06-01 | 2023-12-06 | The Procter & Gamble Company | Dishwashing detergent composition comprising xylanase and sulphonated carboxylate polymer |
| KR20230167903A (ko) * | 2022-06-03 | 2023-12-12 | 씨제이제일제당 (주) | 자일라나제 활성을 갖는 변이형 폴리펩티드 |
| CN120917131A (zh) | 2023-02-01 | 2025-11-07 | 国际营养与健康丹麦有限公司 | 改善的基于黑麦的酒精饮料的生产 |
Family Cites Families (14)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE4226528A1 (de) | 1992-08-11 | 1994-02-17 | Roehm Gmbh | Batterien-Xylanase, Verfahren zu ihrer Herstellung sowie dafür geeigneter Bakterienstamm, Plasmid mit zugehörigem Strukturgen, sowie Backmittel und Backverfahren zur Herstellung von Brot und Backwaren unter Verwendung der Xylanase |
| EP0805856B2 (en) | 1995-01-26 | 2009-04-01 | Novozymes A/S | Animal feed additives comprising xylanase |
| US6682923B1 (en) * | 1999-05-12 | 2004-01-27 | Xencor | Thermostable alkaliphilic xylanase |
| AU785107C (en) * | 2000-03-08 | 2007-05-03 | Dupont Nutrition Biosciences Aps | Xylanase variants having altered sensitivity to xylanase inhibitors |
| EP1184460A1 (en) * | 2000-08-29 | 2002-03-06 | Dsm N.V. | Modified fungal xylanases |
| GB0121387D0 (en) | 2001-09-04 | 2001-10-24 | Danisco | Modified hydrolases |
| US7547534B2 (en) | 2002-06-14 | 2009-06-16 | Verenium Corporation | Methods for making a composition to treat a wood, a pulp or a paper |
| BRPI0414370A (pt) | 2003-09-15 | 2006-11-14 | Genencor Int | enzimas modificadas, processos para produzir enzimas modificadas e usos das mesmas |
| CA2548723A1 (en) * | 2003-12-19 | 2005-06-19 | Syngenta Participations Ag | Microbially expressed xylanases and their use as feed additives and other uses |
| CN1954072A (zh) * | 2004-03-08 | 2007-04-25 | 辛根塔参与股份公司 | 自加工的植物和植物部分 |
| ATE527362T1 (de) * | 2004-03-25 | 2011-10-15 | Iogen Bio Products Corp | Verbesserte expression zeigendemodifizierte xylanasen |
| EP2548955A1 (en) | 2006-02-14 | 2013-01-23 | Verenium Corporation | Xylanases, nucleic acids encoding them and methods for making and using them |
| CN102317451A (zh) | 2008-12-23 | 2012-01-11 | 丹尼斯科公司 | 具有木聚糖酶活性的多肽 |
| KR20110104539A (ko) | 2008-12-23 | 2011-09-22 | 대니스코 에이/에스 | 자일라나제 활성을 갖는 폴리펩타이드 |
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| CA2747224A1 (en) | 2010-07-01 |
| AU2009329608B2 (en) | 2013-12-05 |
| EP2382310A1 (en) | 2011-11-02 |
| WO2010072225A1 (en) | 2010-07-01 |
| EP2382310B1 (en) | 2016-08-24 |
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