PH25983A - DNA fragments containing alkaline cellulase gene recombinant plasmids with said DNA fragments inserted therein and recombinant microorganism - Google Patents

DNA fragments containing alkaline cellulase gene recombinant plasmids with said DNA fragments inserted therein and recombinant microorganism Download PDF

Info

Publication number: PH25983A
Authority: PH; Philippines
Prior art keywords: dna fragment; alkaline; base pairs; cellulase; alkaline cellulase
Prior art date: 1986-10-31

Application number

PH35995A

Other languages

English (en)

Inventor

Katsuya Ozaki

Kazushi Oshino

Kenzo Koike

Susumu Ito

Kikuhiko Oshino

Original Assignee

Kao Corp

Priority date (The priority date 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 date listed.)

1986-10-31

Filing date

1987-10-28

Publication date

1992-01-13

1987-10-28 Application filed by Kao Corp filed Critical Kao Corp

1992-01-13 Publication of PH25983A publication Critical patent/PH25983A/en

Links

239000012634 fragment Substances 0.000 title claims description 84
239000013612 plasmid Substances 0.000 title claims description 52
101710166469 Endoglucanase Proteins 0.000 title claims description 37
244000005700 microbiome Species 0.000 title claims description 12
238000000034 method Methods 0.000 description 38
108090000623 proteins and genes Proteins 0.000 description 30
108010059892 Cellulase Proteins 0.000 description 28
239000013598 vector Substances 0.000 description 25
238000003776 cleavage reaction Methods 0.000 description 23
230000007017 scission Effects 0.000 description 23
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 20
229940106157 cellulase Drugs 0.000 description 17
102000004190 Enzymes Human genes 0.000 description 16
108090000790 Enzymes Proteins 0.000 description 16
229940088598 enzyme Drugs 0.000 description 16
230000000694 effects Effects 0.000 description 14
108010085318 carboxymethylcellulase Proteins 0.000 description 13
229920002134 Carboxymethyl cellulose Polymers 0.000 description 12
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 12
235000010948 carboxy methyl cellulose Nutrition 0.000 description 12
239000002609 medium Substances 0.000 description 11
238000006243 chemical reaction Methods 0.000 description 10
239000013611 chromosomal DNA Substances 0.000 description 10
230000014509 gene expression Effects 0.000 description 10
239000011780 sodium chloride Substances 0.000 description 10
241000193830 Bacillus <bacterium> Species 0.000 description 9
241000194110 Bacillus sp. (in: Bacteria) Species 0.000 description 8
230000001580 bacterial effect Effects 0.000 description 8
239000000243 solution Substances 0.000 description 8
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 7
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 7
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 6
238000000246 agarose gel electrophoresis Methods 0.000 description 6
239000000284 extract Substances 0.000 description 6
108091008146 restriction endonucleases Proteins 0.000 description 6
241000894007 species Species 0.000 description 6
108700039691 Genetic Promoter Regions Proteins 0.000 description 5
239000002253 acid Substances 0.000 description 5
229960000723 ampicillin Drugs 0.000 description 5
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 5
239000000872 buffer Substances 0.000 description 5
IQFVPQOLBLOTPF-HKXUKFGYSA-L congo red Chemical compound [Na+].[Na+].C1=CC=CC2=C(N)C(/N=N/C3=CC=C(C=C3)C3=CC=C(C=C3)/N=N/C3=C(C4=CC=CC=C4C(=C3)S([O-])(=O)=O)N)=CC(S([O-])(=O)=O)=C21 IQFVPQOLBLOTPF-HKXUKFGYSA-L 0.000 description 5
238000005304 joining Methods 0.000 description 5
239000002244 precipitate Substances 0.000 description 5
229920001817 Agar Polymers 0.000 description 4
244000063299 Bacillus subtilis Species 0.000 description 4
235000014469 Bacillus subtilis Nutrition 0.000 description 4
241000588724 Escherichia coli Species 0.000 description 4
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
101150042441 K gene Proteins 0.000 description 4
239000008272 agar Substances 0.000 description 4
239000007853 buffer solution Substances 0.000 description 4
229940041514 candida albicans extract Drugs 0.000 description 4
210000004027 cell Anatomy 0.000 description 4
238000005119 centrifugation Methods 0.000 description 4
238000004587 chromatography analysis Methods 0.000 description 4
239000003599 detergent Substances 0.000 description 4
-1 fatty acid ester sodium salt Chemical class 0.000 description 4
238000003780 insertion Methods 0.000 description 4
230000037431 insertion Effects 0.000 description 4
239000000203 mixture Substances 0.000 description 4
230000007935 neutral effect Effects 0.000 description 4
238000001556 precipitation Methods 0.000 description 4
159000000000 sodium salts Chemical class 0.000 description 4
239000012138 yeast extract Substances 0.000 description 4
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
241000894006 Bacteria Species 0.000 description 3
102000012410 DNA Ligases Human genes 0.000 description 3
108010061982 DNA Ligases Proteins 0.000 description 3
241000233866 Fungi Species 0.000 description 3
239000006142 Luria-Bertani Agar Substances 0.000 description 3
229920002678 cellulose Polymers 0.000 description 3
239000001913 cellulose Substances 0.000 description 3
230000003247 decreasing effect Effects 0.000 description 3
108010091371 endoglucanase 1 Proteins 0.000 description 3
238000004519 manufacturing process Methods 0.000 description 3
235000013372 meat Nutrition 0.000 description 3
238000010369 molecular cloning Methods 0.000 description 3
238000007747 plating Methods 0.000 description 3
239000000047 product Substances 0.000 description 3
239000012429 reaction media Substances 0.000 description 3
239000011734 sodium Substances 0.000 description 3
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
LWFUFLREGJMOIZ-UHFFFAOYSA-N 3,5-dinitrosalicylic acid Chemical compound OC(=O)C1=CC([N+]([O-])=O)=CC([N+]([O-])=O)=C1O LWFUFLREGJMOIZ-UHFFFAOYSA-N 0.000 description 2
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
241000588722 Escherichia Species 0.000 description 2
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
239000004471 Glycine Substances 0.000 description 2
101710163270 Nuclease Proteins 0.000 description 2
108091005804 Peptidases Proteins 0.000 description 2
239000004365 Protease Substances 0.000 description 2
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
239000004098 Tetracycline Substances 0.000 description 2
150000007513 acids Chemical class 0.000 description 2
239000001110 calcium chloride Substances 0.000 description 2
229910001628 calcium chloride Inorganic materials 0.000 description 2
239000001768 carboxy methyl cellulose Substances 0.000 description 2
239000008112 carboxymethyl-cellulose Substances 0.000 description 2
230000000875 corresponding effect Effects 0.000 description 2
238000012217 deletion Methods 0.000 description 2
230000037430 deletion Effects 0.000 description 2
235000014113 dietary fatty acids Nutrition 0.000 description 2
239000000194 fatty acid Substances 0.000 description 2
229930195729 fatty acid Natural products 0.000 description 2
238000000855 fermentation Methods 0.000 description 2
230000004151 fermentation Effects 0.000 description 2
239000000499 gel Substances 0.000 description 2
239000008103 glucose Substances 0.000 description 2
229920001519 homopolymer Polymers 0.000 description 2
230000001900 immune effect Effects 0.000 description 2
239000007788 liquid Substances 0.000 description 2
102000004169 proteins and genes Human genes 0.000 description 2
238000000746 purification Methods 0.000 description 2
239000013049 sediment Substances 0.000 description 2
229910052708 sodium Inorganic materials 0.000 description 2
239000002689 soil Substances 0.000 description 2
UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
239000000758 substrate Substances 0.000 description 2
235000000346 sugar Nutrition 0.000 description 2
150000008163 sugars Chemical class 0.000 description 2
239000006228 supernatant Substances 0.000 description 2
239000004094 surface-active agent Substances 0.000 description 2
229960002180 tetracycline Drugs 0.000 description 2
229930101283 tetracycline Natural products 0.000 description 2
235000019364 tetracycline Nutrition 0.000 description 2
239000012137 tryptone Substances 0.000 description 2
239000002023 wood Substances 0.000 description 2
IAYJZWFYUSNIPN-KFRZSCGFSA-N (2s,3r,4s,5s,6r)-2-[(2r,3s,4r,5r,6s)-4,5-dihydroxy-2-(hydroxymethyl)-6-(4-nitrophenoxy)oxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol 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)O[C@@H](OC=2C=CC(=CC=2)[N+]([O-])=O)[C@H](O)[C@H]1O IAYJZWFYUSNIPN-KFRZSCGFSA-N 0.000 description 1
BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 1
241001019659 Acremonium <Plectosphaerellaceae> Species 0.000 description 1
101100238763 Bacillus subtilis hsdRM gene Proteins 0.000 description 1
101100497221 Bacillus thuringiensis subsp. alesti cry1Ae gene Proteins 0.000 description 1
108010023063 Bacto-peptone Proteins 0.000 description 1
241000186321 Cellulomonas Species 0.000 description 1
VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 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
101150105088 Dele1 gene Proteins 0.000 description 1
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
101710156496 Endoglucanase A Proteins 0.000 description 1
108010056771 Glucosidases Proteins 0.000 description 1
102000004366 Glucosidases Human genes 0.000 description 1
241000223198 Humicola Species 0.000 description 1
241001214257 Mene Species 0.000 description 1
244000202563 Meum athamanticum Species 0.000 description 1
101100114416 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) con-10 gene Proteins 0.000 description 1
101150030170 Paat gene Proteins 0.000 description 1
241000791420 Plica Species 0.000 description 1
229920003171 Poly (ethylene oxide) Polymers 0.000 description 1
101710194948 Protein phosphatase PhpP Proteins 0.000 description 1
101000906479 Saitozyma flava Endoglucanase 1 Proteins 0.000 description 1
241000219289 Silene Species 0.000 description 1
241000223259 Trichoderma Species 0.000 description 1
101100020289 Xenopus laevis koza gene Proteins 0.000 description 1
229910021536 Zeolite Inorganic materials 0.000 description 1
FHKPLLOSJHHKNU-INIZCTEOSA-N [(3S)-3-[8-(1-ethyl-5-methylpyrazol-4-yl)-9-methylpurin-6-yl]oxypyrrolidin-1-yl]-(oxan-4-yl)methanone Chemical compound C(C)N1N=CC(=C1C)C=1N(C2=NC=NC(=C2N=1)O[C@@H]1CN(CC1)C(=O)C1CCOCC1)C FHKPLLOSJHHKNU-INIZCTEOSA-N 0.000 description 1
ZVQOOHYFBIDMTQ-UHFFFAOYSA-N [methyl(oxido){1-[6-(trifluoromethyl)pyridin-3-yl]ethyl}-lambda(6)-sulfanylidene]cyanamide Chemical compound N#CN=S(C)(=O)C(C)C1=CC=C(C(F)(F)F)N=C1 ZVQOOHYFBIDMTQ-UHFFFAOYSA-N 0.000 description 1
230000002378 acidificating effect Effects 0.000 description 1
239000011543 agarose gel Substances 0.000 description 1
150000005215 alkyl ethers Chemical group 0.000 description 1
125000000217 alkyl group Chemical group 0.000 description 1
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
229910052921 ammonium sulfate Inorganic materials 0.000 description 1
235000011130 ammonium sulphate Nutrition 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
229910052586 apatite Inorganic materials 0.000 description 1
238000013459 approach Methods 0.000 description 1
238000003556 assay Methods 0.000 description 1
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
108010047754 beta-Glucosidase Proteins 0.000 description 1
102000006995 beta-Glucosidase Human genes 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
238000009395 breeding Methods 0.000 description 1
230000001488 breeding effect Effects 0.000 description 1
229910052792 caesium Inorganic materials 0.000 description 1
TVFDJXOCXUVLDH-UHFFFAOYSA-N caesium atom Chemical compound [Cs] TVFDJXOCXUVLDH-UHFFFAOYSA-N 0.000 description 1
239000006285 cell suspension Substances 0.000 description 1
FYGDTMLNYKFZSV-ZWSAEMDYSA-N cellotriose 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)O[C@@H](O[C@@H]2[C@H](OC(O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-ZWSAEMDYSA-N 0.000 description 1
239000002738 chelating agent Substances 0.000 description 1
229960005091 chloramphenicol Drugs 0.000 description 1
WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
230000005757 colony formation Effects 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
239000012228 culture supernatant Substances 0.000 description 1
230000009089 cytolysis Effects 0.000 description 1
239000008367 deionised water Substances 0.000 description 1
229910021641 deionized water Inorganic materials 0.000 description 1
238000000432 density-gradient centrifugation Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
238000009792 diffusion process Methods 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution 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
238000001962 electrophoresis Methods 0.000 description 1
238000010828 elution Methods 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
230000002255 enzymatic effect Effects 0.000 description 1
238000006911 enzymatic reaction Methods 0.000 description 1
229960005542 ethidium bromide Drugs 0.000 description 1
DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
238000000605 extraction Methods 0.000 description 1
238000012262 fermentative production Methods 0.000 description 1
238000001914 filtration Methods 0.000 description 1
238000005194 fractionation Methods 0.000 description 1
238000005227 gel permeation chromatography Methods 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
101150102883 hsdM gene Proteins 0.000 description 1
101150085823 hsdR gene Proteins 0.000 description 1
230000000951 immunodiffusion Effects 0.000 description 1
230000002779 inactivation Effects 0.000 description 1
238000002347 injection Methods 0.000 description 1
239000007924 injection Substances 0.000 description 1
230000003834 intracellular effect Effects 0.000 description 1
238000007169 ligase reaction Methods 0.000 description 1
238000004811 liquid chromatography Methods 0.000 description 1
235000015250 liver sausages Nutrition 0.000 description 1
238000005259 measurement Methods 0.000 description 1
230000007246 mechanism Effects 0.000 description 1
239000010445 mica Substances 0.000 description 1
229910052618 mica group Inorganic materials 0.000 description 1
230000000813 microbial effect Effects 0.000 description 1
108020004707 nucleic acids Proteins 0.000 description 1
150000007523 nucleic acids Chemical class 0.000 description 1
102000039446 nucleic acids Human genes 0.000 description 1
HWGNBUXHKFFFIH-UHFFFAOYSA-I pentasodium;[oxido(phosphonatooxy)phosphoryl] phosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O HWGNBUXHKFFFIH-UHFFFAOYSA-I 0.000 description 1
239000008363 phosphate buffer Substances 0.000 description 1
238000013492 plasmid preparation Methods 0.000 description 1
239000013600 plasmid vector Substances 0.000 description 1
239000000843 powder Substances 0.000 description 1
210000001938 protoplast Anatomy 0.000 description 1
230000006798 recombination Effects 0.000 description 1
238000005215 recombination Methods 0.000 description 1
239000001044 red dye Substances 0.000 description 1
238000011160 research Methods 0.000 description 1
235000019832 sodium triphosphate Nutrition 0.000 description 1
238000010186 staining Methods 0.000 description 1
229960005322 streptomycin Drugs 0.000 description 1
239000000126 substance Substances 0.000 description 1
OFVLGDICTFRJMM-WESIUVDSSA-N tetracycline Chemical compound C1=CC=C2[C@](O)(C)[C@H]3C[C@H]4[C@H](N(C)C)C(O)=C(C(N)=O)C(=O)[C@@]4(O)C(O)=C3C(=O)C2=C1O OFVLGDICTFRJMM-WESIUVDSSA-N 0.000 description 1
150000003522 tetracyclines Chemical class 0.000 description 1
230000009466 transformation Effects 0.000 description 1
230000001131 transforming effect Effects 0.000 description 1
239000010457 zeolite Substances 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)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2437—Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01004—Cellulase (3.2.1.4), i.e. endo-1,4-beta-glucanase

Landscapes

Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Health & Medical Sciences (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Genetics & Genomics (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
General Engineering & Computer Science (AREA)
Medicinal Chemistry (AREA)
Molecular Biology (AREA)
Biomedical Technology (AREA)
Biotechnology (AREA)
Microbiology (AREA)
Enzymes And Modification Thereof (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)

PH35995A 1986-10-31 1987-10-28 DNA fragments containing alkaline cellulase gene recombinant plasmids with said DNA fragments inserted therein and recombinant microorganism PH25983A (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP25992386		1986-10-31

Publications (1)

Publication Number	Publication Date
PH25983A true PH25983A (en)	1992-01-13

Family

ID=17340805

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
PH35995A PH25983A (en)	1986-10-31	1987-10-28	DNA fragments containing alkaline cellulase gene recombinant plasmids with said DNA fragments inserted therein and recombinant microorganism

Country Status (9)

Country	Link
US (1)	US4904599A (ja)
EP (1)	EP0273125B1 (ja)
JP (1)	JP2530181B2 (ja)
DE (1)	DE3785164T2 (ja)
DK (1)	DK568587A (ja)
ES (1)	ES2054642T3 (ja)
HK (1)	HK37994A (ja)
MY (1)	MY102992A (ja)
PH (1)	PH25983A (ja)

Families Citing this family (25)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5298405A (en) *	1986-04-30	1994-03-29	Alko Limited	Enzyme preparations with recombinantly-altered cellulose profiles and methods for their production
ES2060590T3 (es) *	1986-10-28	1994-12-01	Kao Corp	Celulasas alcalinas y microorganismos para su produccion.
JP2652871B2 (ja) *	1988-04-25	1997-09-10	花王株式会社	アルカリセルラーゼおよびその製造法
US5169554A (en) *	1989-10-04	1992-12-08	The United States Of America As Represented By The Secretary Of The Army	Enzyme detergent formulation and methods of detoxifying toxic organophosphorous acid compounds
US5120463A (en) *	1989-10-19	1992-06-09	Genencor International, Inc.	Degradation resistant detergent compositions based on cellulase enzymes
US5475101A (en) *	1990-10-05	1995-12-12	Genencor International, Inc.	DNA sequence encoding endoglucanase III cellulase
WO1993022428A1 (en) *	1992-05-01	1993-11-11	Genencor International, Inc.	Methods for treating cotton-containing fabrics with cbh i enriched cellulase
US5945327A (en) *	1992-07-02	1999-08-31	Novo Nordisk A/S	DNA constructs and methods of producing cellulytic enzymes
US5514584A (en) *	1993-06-11	1996-05-07	Midwest Research Institute	Cloning of cellulase genes from acidothermus cellulolyticus
US5691295A (en) *	1995-01-17	1997-11-25	Cognis Gesellschaft Fuer Biotechnologie Mbh	Detergent compositions
DE4422433A1 (de) *	1994-06-28	1996-01-04	Cognis Bio Umwelt	Mehrenzymgranulat
US5646044A (en) *	1995-03-02	1997-07-08	Henkel Kommanditgesellschaft Auf Aktien	Expression systems for the production of target proteins in bacillus
CN1230224A (zh)	1996-09-12	1999-09-29	诺瓦提斯公司	表达纤维素分解酶的转基因植物
DE19725508A1 (de)	1997-06-17	1998-12-24	Clariant Gmbh	Wasch- und Reinigungsmittel
DE19914811A1 (de)	1999-03-31	2000-10-05	Henkel Kgaa	Enzym- und bleichaktivatorhaltige Wasch- und Reinigungsmittel
MXPA04001802A (es)	2001-08-27	2004-07-08	Syngenta Participations Ag	Plantas y partes de plantas autoprocesadoras.
MXPA04003737A (es)	2001-10-22	2004-07-23	Henkel Kgaa	Polimeros a base de uretano de remocion de mugre, activos con algodon.
EP1572851B1 (de)	2002-12-20	2007-03-21	Henkel Kommanditgesellschaft auf Aktien	Bleichmittelhaltige wasch- oder reinigungsmittel
DE10351325A1 (de)	2003-02-10	2004-08-26	Henkel Kgaa	Wasch- oder Reinigungsmittel mit wasserlöslichem Buildersystem und schmutzablösevermögendem Cellulosederivat
JP4519122B2 (ja)	2003-02-10	2010-08-04	ヘンケル・アクチェンゲゼルシャフト・ウント・コムパニー・コマンディットゲゼルシャフト・アウフ・アクチェン	水溶性ビルダー系および汚れ解離性セルロース誘導体を含んでなる漂白剤含有洗濯または洗浄剤
JP4629664B2 (ja)	2003-04-29	2011-02-09	ジェネンコー・インターナショナル・インク	新規なバチルス０２９ｃｅｌセルラーゼ
BRPI0418622B1 (pt) *	2004-03-08	2020-01-28	Syngenta Participations Ag	polinucleotídeo isolado, cassete de expressão e método para preparar açúcar fermentável, monossacarídeo ou oligossacarídeo
DE102005026522B4 (de)	2005-06-08	2007-04-05	Henkel Kgaa	Verstärkung der Reinigungsleistung von Waschmitteln durch Polymer
US8524474B2 (en) *	2008-11-20	2013-09-03	E I Du Pont De Nemours And Company	Process for producing a concentrated sugar solution by enzymatic saccharification of polysaccharide enriched biomass
US8372609B2 (en) *	2008-11-20	2013-02-12	E I Du Pont De Nemours And Company	Process for producing a sugar solution by combined chemical and enzymatic saccharification of polysaccharide enriched biomass

1987
- 1987-10-16 JP JP62261488A patent/JP2530181B2/ja not_active Expired - Fee Related
- 1987-10-19 US US07/109,510 patent/US4904599A/en not_active Expired - Lifetime
- 1987-10-21 EP EP87115431A patent/EP0273125B1/en not_active Expired - Lifetime
- 1987-10-21 ES ES87115431T patent/ES2054642T3/es not_active Expired - Lifetime
- 1987-10-21 DE DE87115431T patent/DE3785164T2/de not_active Expired - Fee Related
- 1987-10-28 PH PH35995A patent/PH25983A/en unknown
- 1987-10-30 DK DK568587A patent/DK568587A/da not_active Application Discontinuation
- 1987-10-31 MY MYPI87003002A patent/MY102992A/en unknown
1994
- 1994-04-21 HK HK37994A patent/HK37994A/en not_active IP Right Cessation

Also Published As

Publication number	Publication date
DK568587A (da)	1988-05-01
DE3785164T2 (de)	1993-11-04
US4904599A (en)	1990-02-27
ES2054642T3 (es)	1994-08-16
DE3785164D1 (de)	1993-05-06
EP0273125A3 (en)	1988-11-17
JPS63233792A (ja)	1988-09-29
JP2530181B2 (ja)	1996-09-04
HK37994A (en)	1994-04-29
EP0273125A2 (en)	1988-07-06
DK568587D0 (da)	1987-10-30
EP0273125B1 (en)	1993-03-31
MY102992A (en)	1993-03-31

Publication	Publication Date	Title
PH25983A (en)	1992-01-13	DNA fragments containing alkaline cellulase gene recombinant plasmids with said DNA fragments inserted therein and recombinant microorganism
Reinhold-Hurek et al.	1993	Cloning, expression in Escherichia coli, and characterization of cellulolytic enzymes of Azoarcus sp., a root-invading diazotroph
JP2652871B2 (ja)	1997-09-10	アルカリセルラーゼおよびその製造法
Saul et al.	1990	celB, a gene coding for a bifunctional cellulase from the extreme thermophile" Caldocellum saccharolyticum"
Cornet et al.	1983	Characterization of two cel (cellulose degradation) genes of Clostridium thermocellum coding for endoglucanases
Tsujibo et al.	1992	Purification, properties, and partial amino acid sequences of thermostable xylanases from Streptomyces thermoviolaceus OPC-520
Hakamada et al.	1997	Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237
Barros et al.	1987	Cloning and expression in Escherichia coli of a cellulase gene from Ruminococcus flavefaciens
GB2133408A (en)	1984-07-25	Method for improving the production of proteins in bacillus
US4861718A (en)	1989-08-29	Gene coding for thermostable beta-galactosidase, bacillus subtilis having the gene, enzyme coded by the gene and a process for the production thereof
Hansen et al.	1992	celA from Bacillus lautus PL236 encodes a novel cellulose-binding endo-beta-1, 4-glucanase
Sami et al.	1988	Production of free and substrate-bound cellulases of Cellulomonas flavigena
FI95481C (fi)	1996-02-12	Alkalinen pullulanaasi, sitä tuottava mikro-organismi ja menetelmä sen tuottamiseksi
Rao et al.	1988	Induction and catabolite repression of cellulase in Penicillium funiculosum
Dijkerman et al.	1997	The role of the cellulolytic high molecular mass (HMM) complex of the anaerobic fungus Piromyces sp. strain E2 in the hydrolysis of microcrystalline cellulose
Huang et al.	1989	Molecular cloning and expression of multiple cellulase genes of Ruminococcus flavefaciens strain 186 in Escherichia coli
Gokhale et al.	1989	Differential expression of xylanases and endoglucanases in the hybrid derived from intergeneric protoplast fusion between a Cellulomonas sp. and Bacillus subtilis
EP0626009B1 (en)	1998-11-04	Carboxymethylcellulases and bacillus strains producing same
Kim et al.	1987	Molecular cloning of an endoglucanase gene from an alkalophilic Bacillus sp. and its expression in Escherichia coli
Ganju et al.	1989	Purification and characterization of two cellobiohydrolases from Chaetomium thermophile var. coprophile
KR100341451B1 (ko)	2002-10-30	루미노코쿠스알부스유래의베타-글루코시다제유전자
Imam et al.	1993	Zymographic analyses of carboxymethylcellulases secreted by the bacterium from wood-boring marine shipworms
Honda et al.	1986	Production of extracellular alkaline xylanase of alkalophilic Bacillus sp. C-125 by Escherichia coli carrying pCX 311
JP2879682B2 (ja)	1999-04-05	バンコマイシンまたはリストセチン耐性変異株及びその製法
JP2592289B2 (ja)	1997-03-19	アルカリセルラーゼ遺伝子を含有するｄｎａ断片並びに該ｄｎａ断片を組み込んだベクター及びその含有微生物