JP4410413B2 - 糸状菌での発現クローニング - Google Patents
糸状菌での発現クローニング Download PDFInfo
- Publication number
- JP4410413B2 JP4410413B2 JP2000525536A JP2000525536A JP4410413B2 JP 4410413 B2 JP4410413 B2 JP 4410413B2 JP 2000525536 A JP2000525536 A JP 2000525536A JP 2000525536 A JP2000525536 A JP 2000525536A JP 4410413 B2 JP4410413 B2 JP 4410413B2
- Authority
- JP
- Japan
- Prior art keywords
- expression
- cdna
- vector
- cloning
- interest
- 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.)
- Expired - Fee Related
Links
- 238000001400 expression cloning Methods 0.000 title claims abstract description 29
- 241000233866 Fungi Species 0.000 title claims description 19
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 110
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 58
- 238000000034 method Methods 0.000 claims abstract description 49
- 108091028043 Nucleic acid sequence Proteins 0.000 claims abstract description 33
- 230000002538 fungal effect Effects 0.000 claims abstract description 27
- 239000012634 fragment Substances 0.000 claims description 54
- 210000004027 cell Anatomy 0.000 claims description 41
- 108020004414 DNA Proteins 0.000 claims description 39
- 239000013604 expression vector Substances 0.000 claims description 31
- 238000004458 analytical method Methods 0.000 claims description 27
- 241000228245 Aspergillus niger Species 0.000 claims description 26
- 239000013599 cloning vector Substances 0.000 claims description 26
- 238000012216 screening Methods 0.000 claims description 20
- 241000228212 Aspergillus Species 0.000 claims description 18
- 102000004190 Enzymes Human genes 0.000 claims description 18
- 108090000790 Enzymes Proteins 0.000 claims description 18
- 239000003550 marker Substances 0.000 claims description 14
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 claims description 13
- 102100022624 Glucoamylase Human genes 0.000 claims description 11
- 241000351920 Aspergillus nidulans Species 0.000 claims description 8
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 6
- 241000223259 Trichoderma Species 0.000 claims description 5
- 241000499912 Trichoderma reesei Species 0.000 claims description 3
- 241000894007 species Species 0.000 claims description 3
- 240000006439 Aspergillus oryzae Species 0.000 claims description 2
- 235000002247 Aspergillus oryzae Nutrition 0.000 claims description 2
- 108010048241 acetamidase Proteins 0.000 claims description 2
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims 1
- 238000002955 isolation Methods 0.000 abstract description 7
- 230000008569 process Effects 0.000 abstract description 5
- 239000002299 complementary DNA Substances 0.000 description 102
- 239000013598 vector Substances 0.000 description 77
- 235000018102 proteins Nutrition 0.000 description 47
- 238000010367 cloning Methods 0.000 description 44
- 239000013612 plasmid Substances 0.000 description 43
- 108010011619 6-Phytase Proteins 0.000 description 38
- 229940085127 phytase Drugs 0.000 description 33
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 32
- 230000009466 transformation Effects 0.000 description 30
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 29
- 238000010276 construction Methods 0.000 description 26
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 25
- 108091034117 Oligonucleotide Proteins 0.000 description 25
- 108020004999 messenger RNA Proteins 0.000 description 23
- 230000000694 effects Effects 0.000 description 21
- 239000000243 solution Substances 0.000 description 21
- 101150108358 GLAA gene Proteins 0.000 description 20
- 238000004519 manufacturing process Methods 0.000 description 20
- 241000588724 Escherichia coli Species 0.000 description 19
- 239000002609 medium Substances 0.000 description 19
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 19
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 18
- 239000000872 buffer Substances 0.000 description 17
- 238000006243 chemical reaction Methods 0.000 description 17
- 229940088598 enzyme Drugs 0.000 description 17
- DLFVBJFMPXGRIB-UHFFFAOYSA-N Acetamide Chemical compound CC(N)=O DLFVBJFMPXGRIB-UHFFFAOYSA-N 0.000 description 16
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 16
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 16
- 238000003556 assay Methods 0.000 description 15
- 101150073906 gpdA gene Proteins 0.000 description 15
- 101150052264 xylA gene Proteins 0.000 description 14
- 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 13
- 101150078331 ama-1 gene Proteins 0.000 description 13
- 230000015572 biosynthetic process Effects 0.000 description 13
- 238000003786 synthesis reaction Methods 0.000 description 13
- QRBLKGHRWFGINE-UGWAGOLRSA-N 2-[2-[2-[[2-[[4-[[2-[[6-amino-2-[3-amino-1-[(2,3-diamino-3-oxopropyl)amino]-3-oxopropyl]-5-methylpyrimidine-4-carbonyl]amino]-3-[(2r,3s,4s,5s,6s)-3-[(2s,3r,4r,5s)-4-carbamoyl-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)- Chemical compound N=1C(C=2SC=C(N=2)C(N)=O)CSC=1CCNC(=O)C(C(C)=O)NC(=O)C(C)C(O)C(C)NC(=O)C(C(O[C@H]1[C@@]([C@@H](O)[C@H](O)[C@H](CO)O1)(C)O[C@H]1[C@@H]([C@](O)([C@@H](O)C(CO)O1)C(N)=O)O)C=1NC=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C QRBLKGHRWFGINE-UGWAGOLRSA-N 0.000 description 12
- LTQCLFMNABRKSH-UHFFFAOYSA-N Phleomycin Natural products N=1C(C=2SC=C(N=2)C(N)=O)CSC=1CCNC(=O)C(C(O)C)NC(=O)C(C)C(O)C(C)NC(=O)C(C(OC1C(C(O)C(O)C(CO)O1)OC1C(C(OC(N)=O)C(O)C(CO)O1)O)C=1NC=NC=1)NC(=O)C1=NC(C(CC(N)=O)NCC(N)C(N)=O)=NC(N)=C1C LTQCLFMNABRKSH-UHFFFAOYSA-N 0.000 description 12
- 108010035235 Phleomycins Proteins 0.000 description 12
- 101150095733 gpsA gene Proteins 0.000 description 12
- 230000010354 integration Effects 0.000 description 12
- 239000000047 product Substances 0.000 description 12
- 101150011516 xlnD gene Proteins 0.000 description 12
- 230000029087 digestion Effects 0.000 description 11
- 239000000203 mixture Substances 0.000 description 11
- 230000008685 targeting Effects 0.000 description 11
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 10
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 10
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 10
- 238000000855 fermentation Methods 0.000 description 10
- 230000004151 fermentation Effects 0.000 description 10
- 239000001965 potato dextrose agar Substances 0.000 description 10
- 101100157012 Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485) xynB gene Proteins 0.000 description 9
- 238000010804 cDNA synthesis Methods 0.000 description 9
- 238000005119 centrifugation Methods 0.000 description 9
- 210000001938 protoplast Anatomy 0.000 description 9
- 101150110790 xylB gene Proteins 0.000 description 9
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 8
- 241000894006 Bacteria Species 0.000 description 8
- 101100038180 Caenorhabditis briggsae rpb-1 gene Proteins 0.000 description 8
- 101150048253 PHYA gene Proteins 0.000 description 8
- 238000000746 purification Methods 0.000 description 8
- 101150081158 crtB gene Proteins 0.000 description 7
- 238000001514 detection method Methods 0.000 description 7
- 238000011534 incubation Methods 0.000 description 7
- 230000006698 induction Effects 0.000 description 7
- 230000004048 modification Effects 0.000 description 7
- 238000012986 modification Methods 0.000 description 7
- 239000006228 supernatant Substances 0.000 description 7
- YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical compound OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 7
- 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 6
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- 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 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 6
- 238000001962 electrophoresis Methods 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 239000008103 glucose Substances 0.000 description 6
- 239000008188 pellet Substances 0.000 description 6
- 238000001556 precipitation Methods 0.000 description 6
- 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 6
- 239000000725 suspension Substances 0.000 description 6
- 230000001580 bacterial effect Effects 0.000 description 5
- 239000000499 gel Substances 0.000 description 5
- 239000007788 liquid Substances 0.000 description 5
- 238000002156 mixing Methods 0.000 description 5
- 235000004252 protein component Nutrition 0.000 description 5
- 239000011541 reaction mixture Substances 0.000 description 5
- 108091008146 restriction endonucleases Proteins 0.000 description 5
- 230000028327 secretion Effects 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 229920001221 xylan Polymers 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- 229920001817 Agar Polymers 0.000 description 4
- 108020004635 Complementary DNA Proteins 0.000 description 4
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 4
- AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 4
- 238000012300 Sequence Analysis Methods 0.000 description 4
- 239000008272 agar Substances 0.000 description 4
- 239000011543 agarose gel Substances 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 238000010805 cDNA synthesis kit Methods 0.000 description 4
- 239000001110 calcium chloride Substances 0.000 description 4
- 229910001628 calcium chloride Inorganic materials 0.000 description 4
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 4
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- XLYOFNOQVPJJNP-ZSJDYOACSA-N heavy water Substances [2H]O[2H] XLYOFNOQVPJJNP-ZSJDYOACSA-N 0.000 description 4
- 238000009396 hybridization Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 229910052757 nitrogen Inorganic materials 0.000 description 4
- 239000000523 sample Substances 0.000 description 4
- 239000000600 sorbitol Substances 0.000 description 4
- 150000004823 xylans Chemical class 0.000 description 4
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 3
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- 108700005088 Fungal Genes Proteins 0.000 description 3
- 108091026898 Leader sequence (mRNA) Proteins 0.000 description 3
- 239000007993 MOPS buffer Substances 0.000 description 3
- 229930182555 Penicillin Natural products 0.000 description 3
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- 101100370749 Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) trpC1 gene Proteins 0.000 description 3
- 229930006000 Sucrose Natural products 0.000 description 3
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 3
- 229940041514 candida albicans extract Drugs 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 238000005194 fractionation Methods 0.000 description 3
- 238000002372 labelling Methods 0.000 description 3
- 239000012160 loading buffer Substances 0.000 description 3
- 238000010841 mRNA extraction Methods 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 230000035772 mutation Effects 0.000 description 3
- 108010090409 novozym 234 Proteins 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 150000007523 nucleic acids Chemical class 0.000 description 3
- 229940049954 penicillin Drugs 0.000 description 3
- 230000026731 phosphorylation Effects 0.000 description 3
- 238000006366 phosphorylation reaction Methods 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- LXNHXLLTXMVWPM-UHFFFAOYSA-N pyridoxine Chemical compound CC1=NC=C(CO)C(CO)=C1O LXNHXLLTXMVWPM-UHFFFAOYSA-N 0.000 description 3
- 230000002285 radioactive effect Effects 0.000 description 3
- 239000006152 selective media Substances 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- 239000007974 sodium acetate buffer Substances 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 229960005322 streptomycin Drugs 0.000 description 3
- 239000005720 sucrose Substances 0.000 description 3
- 101150016309 trpC gene Proteins 0.000 description 3
- 239000012138 yeast extract Substances 0.000 description 3
- GHOKWGTUZJEAQD-ZETCQYMHSA-N (D)-(+)-Pantothenic acid Chemical compound OCC(C)(C)[C@@H](O)C(=O)NCCC(O)=O GHOKWGTUZJEAQD-ZETCQYMHSA-N 0.000 description 2
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 239000004382 Amylase Substances 0.000 description 2
- 241000228232 Aspergillus tubingensis Species 0.000 description 2
- 244000075850 Avena orientalis Species 0.000 description 2
- 235000007319 Avena orientalis Nutrition 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- 108010059892 Cellulase Proteins 0.000 description 2
- 229910021580 Cobalt(II) chloride Inorganic materials 0.000 description 2
- AUNGANRZJHBGPY-UHFFFAOYSA-N D-Lyxoflavin Natural products OCC(O)C(O)C(O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-UHFFFAOYSA-N 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 2
- 108090000364 Ligases Proteins 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 108091092724 Noncoding DNA Proteins 0.000 description 2
- 238000000636 Northern blotting Methods 0.000 description 2
- 102000004316 Oxidoreductases Human genes 0.000 description 2
- 108090000854 Oxidoreductases Proteins 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- 241000235648 Pichia Species 0.000 description 2
- 229920001030 Polyethylene Glycol 4000 Polymers 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 108091034057 RNA (poly(A)) Proteins 0.000 description 2
- 238000002123 RNA extraction Methods 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 241000953555 Theama Species 0.000 description 2
- DFPAKSUCGFBDDF-ZQBYOMGUSA-N [14c]-nicotinamide Chemical compound N[14C](=O)C1=CC=CN=C1 DFPAKSUCGFBDDF-ZQBYOMGUSA-N 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 125000003275 alpha amino acid group Chemical group 0.000 description 2
- ROOXNKNUYICQNP-UHFFFAOYSA-N ammonium persulfate Chemical compound [NH4+].[NH4+].[O-]S(=O)(=O)OOS([O-])(=O)=O ROOXNKNUYICQNP-UHFFFAOYSA-N 0.000 description 2
- 238000000137 annealing Methods 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 101150038738 ble gene Proteins 0.000 description 2
- 239000005018 casein Substances 0.000 description 2
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 2
- 235000021240 caseins Nutrition 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 230000000593 degrading effect Effects 0.000 description 2
- 238000003936 denaturing gel electrophoresis Methods 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 239000012149 elution buffer Substances 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 238000011049 filling Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 239000010931 gold Substances 0.000 description 2
- 229910052737 gold Inorganic materials 0.000 description 2
- 230000005484 gravity Effects 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 239000012145 high-salt buffer Substances 0.000 description 2
- 230000001965 increasing effect Effects 0.000 description 2
- 230000001939 inductive effect Effects 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- PHTQWCKDNZKARW-UHFFFAOYSA-N isoamylol Chemical compound CC(C)CCO PHTQWCKDNZKARW-UHFFFAOYSA-N 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 229920001223 polyethylene glycol Polymers 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000000163 radioactive labelling Methods 0.000 description 2
- 230000008929 regeneration Effects 0.000 description 2
- 238000011069 regeneration method Methods 0.000 description 2
- 229960002477 riboflavin Drugs 0.000 description 2
- 235000019192 riboflavin Nutrition 0.000 description 2
- 239000002151 riboflavin Substances 0.000 description 2
- 239000012723 sample buffer Substances 0.000 description 2
- FQENQNTWSFEDLI-UHFFFAOYSA-J sodium diphosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])([O-])=O FQENQNTWSFEDLI-UHFFFAOYSA-J 0.000 description 2
- 229940048086 sodium pyrophosphate Drugs 0.000 description 2
- 239000008223 sterile water Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 235000019818 tetrasodium diphosphate Nutrition 0.000 description 2
- 239000001577 tetrasodium phosphonato phosphate Substances 0.000 description 2
- 229960003495 thiamine Drugs 0.000 description 2
- DPJRMOMPQZCRJU-UHFFFAOYSA-M thiamine hydrochloride Chemical compound Cl.[Cl-].CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N DPJRMOMPQZCRJU-UHFFFAOYSA-M 0.000 description 2
- 235000019190 thiamine hydrochloride Nutrition 0.000 description 2
- 239000011747 thiamine hydrochloride Substances 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000001131 transforming effect Effects 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 229940011671 vitamin b6 Drugs 0.000 description 2
- 239000011592 zinc chloride Substances 0.000 description 2
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-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
- 241001019659 Acremonium <Plectosphaerellaceae> Species 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 101710152845 Arabinogalactan endo-beta-1,4-galactanase Proteins 0.000 description 1
- 101100216041 Aspergillus niger GLAA gene Proteins 0.000 description 1
- 101000757144 Aspergillus niger Glucoamylase Proteins 0.000 description 1
- 241000131386 Aspergillus sojae Species 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 101710130006 Beta-glucanase Proteins 0.000 description 1
- 102100032487 Beta-mannosidase Human genes 0.000 description 1
- 101000583080 Bunodosoma granuliferum Delta-actitoxin-Bgr2a Proteins 0.000 description 1
- 108010084185 Cellulases Proteins 0.000 description 1
- 102000005575 Cellulases Human genes 0.000 description 1
- 241000221955 Chaetomium Species 0.000 description 1
- GHOKWGTUZJEAQD-UHFFFAOYSA-N Chick antidermatitis factor Natural products OCC(C)(C)C(O)C(=O)NCCC(O)=O GHOKWGTUZJEAQD-UHFFFAOYSA-N 0.000 description 1
- 241001535823 Cloeosiphon aspergillus Species 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 241001503016 Ctenomyces Species 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 108010017826 DNA Polymerase I Proteins 0.000 description 1
- 102000004594 DNA Polymerase I Human genes 0.000 description 1
- 238000007399 DNA isolation Methods 0.000 description 1
- 101001096557 Dickeya dadantii (strain 3937) Rhamnogalacturonate lyase Proteins 0.000 description 1
- 101100364969 Dictyostelium discoideum scai gene Proteins 0.000 description 1
- 101710132690 Endo-1,4-beta-xylanase A Proteins 0.000 description 1
- 101710147028 Endo-beta-1,4-galactanase Proteins 0.000 description 1
- 108090000371 Esterases Proteins 0.000 description 1
- 108010058643 Fungal Proteins Proteins 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 101710137787 Glyceraldehyde-3-phosphate dehydrogenase A Proteins 0.000 description 1
- 101100295959 Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) arcB gene Proteins 0.000 description 1
- 108090001042 Hydro-Lyases Proteins 0.000 description 1
- GRRNUXAQVGOGFE-UHFFFAOYSA-N Hygromycin-B Natural products OC1C(NC)CC(N)C(O)C1OC1C2OC3(C(C(O)C(O)C(C(N)CO)O3)O)OC2C(O)C(CO)O1 GRRNUXAQVGOGFE-UHFFFAOYSA-N 0.000 description 1
- IMQLKJBTEOYOSI-GPIVLXJGSA-N Inositol-hexakisphosphate Chemical compound OP(O)(=O)O[C@H]1[C@H](OP(O)(O)=O)[C@@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@@H]1OP(O)(O)=O IMQLKJBTEOYOSI-GPIVLXJGSA-N 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 101710203526 Integrase Proteins 0.000 description 1
- 241000973945 Intrasporangium oryzae Species 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- 239000007836 KH2PO4 Substances 0.000 description 1
- 241000235649 Kluyveromyces Species 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 102000004317 Lyases Human genes 0.000 description 1
- 108090000856 Lyases Proteins 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products 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-PICCSMPSSA-N 0.000 description 1
- 229910021380 Manganese Chloride Inorganic materials 0.000 description 1
- GLFNIEUTAYBVOC-UHFFFAOYSA-L Manganese chloride Chemical compound Cl[Mn]Cl GLFNIEUTAYBVOC-UHFFFAOYSA-L 0.000 description 1
- 108060004795 Methyltransferase Proteins 0.000 description 1
- 101100364971 Mus musculus Scai gene Proteins 0.000 description 1
- KWYHDKDOAIKMQN-UHFFFAOYSA-N N,N,N',N'-tetramethylethylenediamine Chemical compound CN(C)CCN(C)C KWYHDKDOAIKMQN-UHFFFAOYSA-N 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 238000010222 PCR analysis Methods 0.000 description 1
- 241000228143 Penicillium Species 0.000 description 1
- 108010002747 Pfu DNA polymerase Proteins 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- IMQLKJBTEOYOSI-UHFFFAOYSA-N Phytic acid Natural products OP(O)(=O)OC1C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C(OP(O)(O)=O)C1OP(O)(O)=O IMQLKJBTEOYOSI-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 239000013614 RNA sample Substances 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 241000223255 Scytalidium Species 0.000 description 1
- 102000040739 Secretory proteins Human genes 0.000 description 1
- 108091058545 Secretory proteins Proteins 0.000 description 1
- 239000012506 Sephacryl® Substances 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 241000228341 Talaromyces Species 0.000 description 1
- 241000228178 Thermoascus Species 0.000 description 1
- 241001494489 Thielavia Species 0.000 description 1
- 108700009124 Transcription Initiation Site Proteins 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 239000007984 Tris EDTA buffer Substances 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 241001105470 Valenzuela Species 0.000 description 1
- 241000235013 Yarrowia Species 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000011358 absorbing material Substances 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 230000001133 acceleration Effects 0.000 description 1
- 102000004139 alpha-Amylases Human genes 0.000 description 1
- 108090000637 alpha-Amylases Proteins 0.000 description 1
- 229940024171 alpha-amylase Drugs 0.000 description 1
- 229910001870 ammonium persulfate Inorganic materials 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 239000008346 aqueous phase Substances 0.000 description 1
- 101150008194 argB gene Proteins 0.000 description 1
- 108010047754 beta-Glucosidase Proteins 0.000 description 1
- 102000006995 beta-Glucosidase Human genes 0.000 description 1
- 108010055059 beta-Mannosidase Proteins 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 238000007664 blowing Methods 0.000 description 1
- UDSAIICHUKSCKT-UHFFFAOYSA-N bromophenol blue Chemical class C1=C(Br)C(O)=C(Br)C=C1C1(C=2C=C(Br)C(O)=C(Br)C=2)C2=CC=CC=C2S(=O)(=O)O1 UDSAIICHUKSCKT-UHFFFAOYSA-N 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 108010089934 carbohydrase Proteins 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- ZYWFEOZQIUMEGL-UHFFFAOYSA-N chloroform;3-methylbutan-1-ol;phenol Chemical compound ClC(Cl)Cl.CC(C)CCO.OC1=CC=CC=C1 ZYWFEOZQIUMEGL-UHFFFAOYSA-N 0.000 description 1
- 238000007813 chromatographic assay Methods 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical class O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 1
- 235000011180 diphosphates Nutrition 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- ZMMJGEGLRURXTF-UHFFFAOYSA-N ethidium bromide Chemical compound [Br-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 ZMMJGEGLRURXTF-UHFFFAOYSA-N 0.000 description 1
- 229960005542 ethidium bromide Drugs 0.000 description 1
- JCHMFMSWRWHRFI-HMMYKYKNSA-N ethyl (2e)-2-[(2,5-dichlorophenyl)hydrazinylidene]-2-(2,6-dimethylmorpholin-4-yl)acetate Chemical compound C1C(C)OC(C)CN1/C(C(=O)OCC)=N/NC1=CC(Cl)=CC=C1Cl JCHMFMSWRWHRFI-HMMYKYKNSA-N 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000012252 genetic analysis Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Natural products O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 239000003365 glass fiber Substances 0.000 description 1
- 230000036252 glycation Effects 0.000 description 1
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- ZJYYHGLJYGJLLN-UHFFFAOYSA-N guanidinium thiocyanate Chemical compound SC#N.NC(N)=N ZJYYHGLJYGJLLN-UHFFFAOYSA-N 0.000 description 1
- 125000001475 halogen functional group Chemical group 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 229940059442 hemicellulase Drugs 0.000 description 1
- 108010002430 hemicellulase Proteins 0.000 description 1
- 238000000265 homogenisation Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- GRRNUXAQVGOGFE-NZSRVPFOSA-N hygromycin B Chemical compound O[C@@H]1[C@@H](NC)C[C@@H](N)[C@H](O)[C@H]1O[C@H]1[C@H]2O[C@@]3([C@@H]([C@@H](O)[C@@H](O)[C@@H](C(N)CO)O3)O)O[C@H]2[C@@H](O)[C@@H](CO)O1 GRRNUXAQVGOGFE-NZSRVPFOSA-N 0.000 description 1
- 229940097277 hygromycin b Drugs 0.000 description 1
- 230000014726 immortalization of host cell Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 101150039489 lysZ gene Proteins 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 239000011565 manganese chloride Substances 0.000 description 1
- WSFSSNUMVMOOMR-NJFSPNSNSA-N methanone Chemical compound O=[14CH2] WSFSSNUMVMOOMR-NJFSPNSNSA-N 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000006151 minimal media Substances 0.000 description 1
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
- 239000004570 mortar (masonry) Substances 0.000 description 1
- ZIUHHBKFKCYYJD-UHFFFAOYSA-N n,n'-methylenebisacrylamide Chemical compound C=CC(=O)NCNC(=O)C=C ZIUHHBKFKCYYJD-UHFFFAOYSA-N 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 229940055726 pantothenic acid Drugs 0.000 description 1
- 235000019161 pantothenic acid Nutrition 0.000 description 1
- 239000011713 pantothenic acid Substances 0.000 description 1
- 239000001814 pectin Substances 0.000 description 1
- 229920001277 pectin Polymers 0.000 description 1
- 235000010987 pectin Nutrition 0.000 description 1
- 235000002949 phytic acid Nutrition 0.000 description 1
- 239000000467 phytic acid Substances 0.000 description 1
- 229940068041 phytic acid Drugs 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 1
- 230000037452 priming Effects 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 238000002331 protein detection Methods 0.000 description 1
- 101150054232 pyrG gene Proteins 0.000 description 1
- 235000008160 pyridoxine Nutrition 0.000 description 1
- 239000011677 pyridoxine Substances 0.000 description 1
- 235000019171 pyridoxine hydrochloride Nutrition 0.000 description 1
- 239000011764 pyridoxine hydrochloride Substances 0.000 description 1
- 229940048084 pyrophosphate Drugs 0.000 description 1
- 238000003908 quality control method Methods 0.000 description 1
- 239000012857 radioactive material Substances 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- KUIXZSYWBHSYCN-UHFFFAOYSA-L remazol brilliant blue r Chemical compound [Na+].[Na+].C1=C(S([O-])(=O)=O)C(N)=C2C(=O)C3=CC=CC=C3C(=O)C2=C1NC1=CC=CC(S(=O)(=O)CCOS([O-])(=O)=O)=C1 KUIXZSYWBHSYCN-UHFFFAOYSA-L 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000007790 scraping Methods 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 229940079862 sodium lauryl sarcosinate Drugs 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- ADWNFGORSPBALY-UHFFFAOYSA-M sodium;2-[dodecyl(methyl)amino]acetate Chemical compound [Na+].CCCCCCCCCCCCN(C)CC([O-])=O ADWNFGORSPBALY-UHFFFAOYSA-M 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 238000000844 transformation Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- -1 xylosidase Proteins 0.000 description 1
Images
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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1086—Preparation or screening of expression libraries, e.g. reporter assays
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- Organic Chemistry (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Zoology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Physics & Mathematics (AREA)
- General Health & Medical Sciences (AREA)
- Crystallography & Structural Chemistry (AREA)
- Mycology (AREA)
- Bioinformatics & Computational Biology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Agricultural Chemicals And Associated Chemicals (AREA)
- Peptides Or Proteins (AREA)
- Mushroom Cultivation (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP97204079.4 | 1997-12-22 | ||
| EP97204079 | 1997-12-22 | ||
| PCT/EP1998/008577 WO1999032617A2 (en) | 1997-12-22 | 1998-12-22 | Expression cloning in filamentous fungi |
Related Child Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2005152703A Division JP2005261438A (ja) | 1997-12-22 | 2005-05-25 | 糸状菌での発現クローニング |
| JP2009241780A Division JP2010046080A (ja) | 1997-12-22 | 2009-10-20 | 糸状菌での発現クローニング |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2002509698A JP2002509698A (ja) | 2002-04-02 |
| JP4410413B2 true JP4410413B2 (ja) | 2010-02-03 |
Family
ID=8229117
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000525536A Expired - Fee Related JP4410413B2 (ja) | 1997-12-22 | 1998-12-22 | 糸状菌での発現クローニング |
| JP2005152703A Pending JP2005261438A (ja) | 1997-12-22 | 2005-05-25 | 糸状菌での発現クローニング |
| JP2009241780A Pending JP2010046080A (ja) | 1997-12-22 | 2009-10-20 | 糸状菌での発現クローニング |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2005152703A Pending JP2005261438A (ja) | 1997-12-22 | 2005-05-25 | 糸状菌での発現クローニング |
| JP2009241780A Pending JP2010046080A (ja) | 1997-12-22 | 2009-10-20 | 糸状菌での発現クローニング |
Country Status (13)
| Country | Link |
|---|---|
| US (1) | US20020155536A1 (enExample) |
| EP (2) | EP1042461B1 (enExample) |
| JP (3) | JP4410413B2 (enExample) |
| CN (1) | CN1198924C (enExample) |
| AT (1) | ATE367439T1 (enExample) |
| AU (1) | AU736111C (enExample) |
| BR (1) | BR9814404A (enExample) |
| CA (1) | CA2313445C (enExample) |
| DE (1) | DE69838106T2 (enExample) |
| DK (1) | DK1042461T3 (enExample) |
| ES (1) | ES2287989T3 (enExample) |
| PL (1) | PL341760A1 (enExample) |
| WO (1) | WO1999032617A2 (enExample) |
Families Citing this family (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7883872B2 (en) | 1996-10-10 | 2011-02-08 | Dyadic International (Usa), Inc. | Construction of highly efficient cellulase compositions for enzymatic hydrolysis of cellulose |
| EP1224272B1 (en) | 1999-10-01 | 2005-12-07 | Novozymes A/S | Spray dried enzyme product |
| MXPA01012905A (es) * | 2000-04-13 | 2002-11-22 | Mark Aaron Emalfarb | Clasificacion de alto rendimiento de bibliotecas de adn expresado en hongo filamentos. |
| KR20020026456A (ko) | 2000-04-13 | 2002-04-10 | 에말파브 마크 아론 | 사상균에서 발현된 dna 라이브러리의 고산출량 스크리닝 |
| CN100558898C (zh) | 2000-09-21 | 2009-11-11 | 巴斯福股份公司 | 篮霉菌木聚糖酶 |
| KR100867059B1 (ko) | 2000-12-07 | 2008-11-04 | 디에스엠 아이피 어셋츠 비.브이. | 카르복시 말단 프롤린 잔기를 갖는 펩티드가 풍부한단백질 가수분해물 |
| WO2003054186A1 (en) | 2001-12-21 | 2003-07-03 | Dsm Ip Assets B.V. | New rennets |
| TWI328612B (en) | 2002-07-25 | 2010-08-11 | Dsm Ip Assets Bv | Genes and their encoded polypeptides involved in the biosynthetic pathway of vitamin b12, vectors and host cells comprising the genes, and process for producing vitamin b12 |
| AU2003219956A1 (en) * | 2003-02-27 | 2004-09-28 | Midwest Research Institute | Superactive cellulase formulation using cellobiohydrolase-1 from penicillium funiculosum |
| US20050059024A1 (en) | 2003-07-25 | 2005-03-17 | Ambion, Inc. | Methods and compositions for isolating small RNA molecules |
| CN102286483B (zh) * | 2004-04-16 | 2014-06-04 | 中化帝斯曼制药有限公司荷兰公司 | 用于在真菌细胞中表达基因的真菌启动子 |
| US9045748B2 (en) | 2004-05-27 | 2015-06-02 | Novozymes, Inc. | Methods for transforming and expression screening of filamentous fungal cells with a DNA library |
| EP1799822A2 (en) * | 2004-10-15 | 2007-06-27 | DSMIP Assets B.V. | Amidases from aspergillus niger and their use in a food production process |
| EP2410048B1 (en) | 2005-01-24 | 2016-08-10 | DSM IP Assets B.V. | Method for producing a compound of interest in a filamentous fungal cell |
| US20090209007A1 (en) * | 2005-03-18 | 2009-08-20 | Roelf Bernhard Meima | Method of Expression Cloning in a Host Cell |
| WO2007062936A2 (en) | 2005-11-29 | 2007-06-07 | Dsm Ip Assets B.V. | Dna binding site of a transcriptional activator useful in gene expression |
| WO2007063133A2 (en) | 2005-12-01 | 2007-06-07 | Dsm Ip Assets B.V. | Genes useful for the industrial production of citric acid |
| EP2423315B1 (en) | 2006-06-29 | 2015-01-07 | DSM IP Assets B.V. | A method for achieving improved polypeptide expression |
| US8389269B2 (en) | 2006-11-02 | 2013-03-05 | Dsm Ip Assets B.V. | Production of secreted proteins by filamentous fungi |
| US8680252B2 (en) | 2006-12-10 | 2014-03-25 | Dyadic International (Usa), Inc. | Expression and high-throughput screening of complex expressed DNA libraries in filamentous fungi |
| JP2010517587A (ja) | 2007-02-15 | 2010-05-27 | ディーエスエム アイピー アセッツ ビー.ブイ. | 関心のある化合物を生産するための組み換え宿主細胞 |
| EP2113027B1 (en) | 2007-02-20 | 2014-06-18 | DSM IP Assets B.V. | Novel sialidase |
| WO2009033071A2 (en) | 2007-09-07 | 2009-03-12 | Dyadic International, Inc. | Novel fungal enzymes |
| MX346700B (es) | 2009-03-10 | 2017-03-28 | Dsm Ip Assets Bv | Metodo para mejorar el rendimiento de un polipeptido. |
| DK2406372T3 (da) | 2009-03-10 | 2017-11-27 | Dsm Ip Assets Bv | Prægastrisk esterase og derivater deraf |
| CN102414323B (zh) | 2009-04-22 | 2015-07-08 | 帝斯曼知识产权资产管理有限公司 | 用于生产感兴趣的重组多肽的方法 |
| CA2768608A1 (en) | 2009-07-22 | 2011-01-27 | Dsm Ip Assets B.V. | Improved host cell for the production of a compound of interest |
| CA2779796A1 (en) | 2009-11-04 | 2011-05-12 | Dsm Ip Assets B.V. | Talaromyces transformants |
| US20130011876A1 (en) | 2010-02-04 | 2013-01-10 | Dsm Ip Assetts, B.V. | Process for preparing filamentous fungal strains having a sexual cycle and a process for preparing sexually crossed filamentous fungal strains |
| MX2012009274A (es) | 2010-02-11 | 2012-12-05 | Dsm Ip Assets Bv | Celula hospedera capaz de producir enzimas utiles para la degradacion de material lignocelulosico. |
| US8945898B2 (en) | 2010-07-01 | 2015-02-03 | Dsm Ip Assets B.V. | Recombinant host cell with deficiency in non-ribosomal peptide synthase production |
| WO2012007445A1 (en) | 2010-07-13 | 2012-01-19 | Dsm Ip Assets B.V. | Mutarotase in crystallization |
| WO2012007446A1 (en) | 2010-07-13 | 2012-01-19 | Dsm Ip Assets B.V. | Use of a mutarotase in the production of dried powders |
| US20150197760A1 (en) | 2012-06-19 | 2015-07-16 | Dsm Ip Assets B.V. | Promoters for expressing a gene in a cell |
| JP6468561B2 (ja) | 2012-07-19 | 2019-02-13 | ディーエスエム アイピー アセッツ ビー.ブイ.Dsm Ip Assets B.V. | AgsE欠損株 |
| EP3447136B1 (en) | 2013-02-04 | 2020-05-13 | DSM IP Assets B.V. | Carbohydrate degrading polypeptide and uses thereof |
| WO2014142647A1 (en) | 2013-03-14 | 2014-09-18 | Wageningen Universiteit | Fungals strains with improved citric acid and itaconic acid production |
| WO2014202624A2 (en) | 2013-06-19 | 2014-12-24 | Dsm Ip Assets B.V. | Rasamsonia gene and use thereof |
| WO2014202620A2 (en) | 2013-06-19 | 2014-12-24 | Dsm Ip Assets B.V. | Rasamsonia gene and use thereof |
| WO2014202622A2 (en) | 2013-06-19 | 2014-12-24 | Dsm Ip Assets B.V. | Rasamsonia gene and use thereof |
| WO2014202621A1 (en) | 2013-06-20 | 2014-12-24 | Dsm Ip Assets B.V. | Carbohydrate degrading polypeptide and uses thereof |
| ES2706742T3 (es) | 2013-12-02 | 2019-04-01 | Dsm Ip Assets Bv | Proteína estructuradora del hielo |
| US9969988B2 (en) * | 2014-01-31 | 2018-05-15 | Api Corporation | Pipecolinic acid 4-hydroxylase and method for producing 4-hydroxy amino acid using same |
| MX375798B (es) | 2014-05-19 | 2025-03-07 | Dsm Ip Assets Bv | Endoproteasa específica para prolina. |
| WO2015177153A1 (en) | 2014-05-19 | 2015-11-26 | Dsm Ip Assets B.V. | Proline-specific endoprotease |
| WO2015177152A1 (en) | 2014-05-19 | 2015-11-26 | Dsm Ip Assets B.V. | Proline-specific endoprotease |
| US11396665B2 (en) | 2015-01-06 | 2022-07-26 | Dsm Ip Assets B.V. | CRISPR-CAS system for a filamentous fungal host cell |
| AR104205A1 (es) | 2015-04-09 | 2017-07-05 | Dsm Ip Assets Bv | Fosfolipasa c |
| AU2016273208B2 (en) | 2015-06-02 | 2021-01-21 | Dsm Ip Assets B.V. | Use of ice structuring protein AFP19 expressed in filamentous fungal strains for preparing food |
| EP4361240A3 (en) | 2015-11-17 | 2024-07-31 | DSM IP Assets B.V. | Preparation of a stable beer |
| US10913938B2 (en) | 2016-07-29 | 2021-02-09 | Dsm Ip Assets B.V. | Polypeptides having cellulolytic enhancing activity and uses thereof |
| RS60238B1 (sr) * | 2016-09-20 | 2020-06-30 | Clariant Int Ltd | Postupak za selektivnu ekspresiju, nezavisnu od izvora ugljenika, sekvenci koje kodiraju proteine u ćeliji filamentozne gljive |
| EP3516056B1 (en) | 2016-09-23 | 2024-11-27 | DSM IP Assets B.V. | A guide-rna expression system for a host cell |
| EP3559222A1 (en) | 2016-12-21 | 2019-10-30 | DSM IP Assets B.V. | Lipolytic enzyme variants |
| WO2018114938A1 (en) | 2016-12-21 | 2018-06-28 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| WO2018114912A1 (en) | 2016-12-21 | 2018-06-28 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| US10889807B2 (en) | 2016-12-21 | 2021-01-12 | Dsm Ip Assets B.V. | Lipolytic enzyme variants |
| EP3596199A1 (en) | 2017-03-13 | 2020-01-22 | DSM IP Assets B.V. | Zinc binuclear cluster transcriptional regulator-deficient strain |
| EP3607071A1 (en) | 2017-04-06 | 2020-02-12 | DSM IP Assets B.V. | Self-guiding integration construct (sgic) |
| CN112424326A (zh) | 2018-05-07 | 2021-02-26 | 帝斯曼知识产权资产管理有限公司 | 用于酶促油脱胶的方法 |
| MX2020014191A (es) | 2018-06-19 | 2021-03-09 | Dsm Ip Assets Bv | Variantes de enzimas lipoliticas. |
| US20220389458A1 (en) | 2019-11-04 | 2022-12-08 | Dsm Ip Assets B.V. | Low volume transfection |
| JP2021093966A (ja) * | 2019-12-18 | 2021-06-24 | 本田技研工業株式会社 | 糸状菌への遺伝子導入方法及びその利用 |
| WO2022269549A2 (en) | 2021-06-24 | 2022-12-29 | Fonterra Co-Operative Group Limited | Recombinant proteins |
| JP2025520009A (ja) | 2022-05-16 | 2025-07-01 | ディーエスエム アイピー アセッツ ビー.ブイ. | 脂肪分解酵素変異体 |
| WO2025012325A1 (en) | 2023-07-11 | 2025-01-16 | Dsm Ip Assets B.V. | Protein arginine deiminase |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK122686D0 (da) * | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
| JP3153234B2 (ja) * | 1989-06-16 | 2001-04-03 | ジェネンコー インコーポレーテッド | 糸状菌からの目的とするポリペプチドの分泌を増幅するdna配列、ベクター、及び融合ポリペプチド |
| WO1991000920A2 (en) * | 1989-07-07 | 1991-01-24 | Unilever N.V. | Process for preparing a protein by a fungus transformed by multicopy integration of an expression vector |
| JPH0595787A (ja) * | 1991-10-04 | 1993-04-20 | Jozo Shigen Kenkyusho:Kk | ホスホグリセリン酸キナ−ゼ遺伝子プロモ−タ−、 同タ−ミネ−タ−または/及びこれらからなる 遺伝子発現用ユニツト、並びに、ホスホグリセリ ン酸キナ−ゼのゲノム遺伝子及びcDNA遺伝子 |
| MX9206979A (es) * | 1991-12-04 | 1993-07-01 | Novo Nordisk As | Metodo de clonacion de proteinas en levaduras |
| JPH05268964A (ja) * | 1992-03-30 | 1993-10-19 | Meiji Milk Prod Co Ltd | 糸状菌プロモーター |
| EP1321523A3 (en) * | 1993-07-23 | 2004-03-03 | DSM IP Assets B.V. | Selection marker gene free recombinant strains; a method for obtaining them and the use of these strains |
| JP3638657B2 (ja) * | 1995-03-29 | 2005-04-13 | 株式会社資生堂 | Dna修復酵素 |
| JPH11504218A (ja) * | 1995-04-24 | 1999-04-20 | クロマゾーム コーポレーション | 新規代謝経路の生成およびスクリーニングのための方法 |
| JP3343567B2 (ja) * | 1995-06-29 | 2002-11-11 | 大関株式会社 | 糸状菌のエンハンサーdna塩基配列およびその用途 |
| DE69733059T2 (de) * | 1996-01-10 | 2006-03-02 | Novozymes A/S | Methode zur invivo produktion einer mutanten-bibliothek in zellen |
-
1998
- 1998-12-22 AT AT98966868T patent/ATE367439T1/de active
- 1998-12-22 EP EP98966868A patent/EP1042461B1/en not_active Revoked
- 1998-12-22 EP EP07112086A patent/EP1854890A1/en not_active Withdrawn
- 1998-12-22 DE DE69838106T patent/DE69838106T2/de not_active Expired - Lifetime
- 1998-12-22 JP JP2000525536A patent/JP4410413B2/ja not_active Expired - Fee Related
- 1998-12-22 ES ES98966868T patent/ES2287989T3/es not_active Expired - Lifetime
- 1998-12-22 DK DK98966868T patent/DK1042461T3/da active
- 1998-12-22 CA CA2313445A patent/CA2313445C/en not_active Expired - Fee Related
- 1998-12-22 CN CN98812563.3A patent/CN1198924C/zh not_active Expired - Lifetime
- 1998-12-22 PL PL98341760A patent/PL341760A1/xx unknown
- 1998-12-22 BR BR9814404-9A patent/BR9814404A/pt not_active Application Discontinuation
- 1998-12-22 WO PCT/EP1998/008577 patent/WO1999032617A2/en not_active Ceased
- 1998-12-22 AU AU25151/99A patent/AU736111C/en not_active Ceased
-
2001
- 2001-11-05 US US09/993,164 patent/US20020155536A1/en active Pending
-
2005
- 2005-05-25 JP JP2005152703A patent/JP2005261438A/ja active Pending
-
2009
- 2009-10-20 JP JP2009241780A patent/JP2010046080A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| ES2287989T3 (es) | 2007-12-16 |
| DE69838106T2 (de) | 2008-04-03 |
| EP1042461A2 (en) | 2000-10-11 |
| EP1854890A1 (en) | 2007-11-14 |
| JP2002509698A (ja) | 2002-04-02 |
| WO1999032617A2 (en) | 1999-07-01 |
| JP2005261438A (ja) | 2005-09-29 |
| CN1283227A (zh) | 2001-02-07 |
| EP1042461B1 (en) | 2007-07-18 |
| CA2313445C (en) | 2012-03-20 |
| AU2515199A (en) | 1999-07-12 |
| JP2010046080A (ja) | 2010-03-04 |
| WO1999032617A3 (en) | 1999-09-10 |
| US20020155536A1 (en) | 2002-10-24 |
| ATE367439T1 (de) | 2007-08-15 |
| AU736111B2 (en) | 2001-07-26 |
| AU736111C (en) | 2004-02-19 |
| PL341760A1 (en) | 2001-05-07 |
| DK1042461T3 (da) | 2007-09-24 |
| DE69838106D1 (de) | 2007-08-30 |
| BR9814404A (pt) | 2000-10-10 |
| CN1198924C (zh) | 2005-04-27 |
| CA2313445A1 (en) | 1999-07-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4410413B2 (ja) | 糸状菌での発現クローニング | |
| US8067157B2 (en) | Expression cloning in filamentous fungi | |
| EP2278016B1 (en) | Promoter sequences derived from Fusarium Venenatum and uses thereof | |
| CN105586355B (zh) | 在镶片镰孢的酶缺陷突变体中产生多肽的方法 | |
| CN102224245B (zh) | 在丝状真菌细胞中使用阳性和阴性选择性基因的方法 | |
| JP6937740B2 (ja) | ゲノム編集システムおよび使用方法 | |
| US7794974B2 (en) | Fungal transcriptional activators useful in methods for producing a polypeptide | |
| EP2683732B1 (en) | Vector-host system | |
| KR20170087521A (ko) | 진균 게놈 변형 시스템 및 사용 방법 | |
| JP2002528076A (ja) | 糸状面細胞内の問題のdnaライブラリーの作製及びスクリーニング | |
| CN101679993A (zh) | 适于选择产生目标多肽的文库克隆的表达克隆方法 | |
| JP2010075204A (ja) | 工業的組み換え生物を溝築するための手段としての遺伝子変換 | |
| JP7376505B2 (ja) | 粘性が低下した表現型を含む糸状菌株 | |
| CN100480391C (zh) | 用于在真菌细胞中表达基因的启动子变体 | |
| EP1250444A1 (en) | Methods for producing a polypeptide using a consensus translational initiator sequence | |
| JP2002515252A (ja) | 糸状菌変異体細胞においてポリペプチドを生産するための方法 | |
| MXPA00006122A (en) | Expression cloning in filamentous fungi | |
| CN120641568A (zh) | 用于真菌蛋白和精细化学品生产的新型基因组整合位点 | |
| JP4531868B2 (ja) | 1を超える非リボソームrnaをコードしているドメインの染色体ゲノムに組込まれた少なくとも2コピーの所望遺伝子を含む、特にクルイベロミセスによる酵母細胞 | |
| CN121127575A (zh) | 用于真菌蛋白生产的新型纤维素酶启动子 | |
| WO2002036830A2 (en) | Method of determining gene copy number |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20040308 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20040608 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20040615 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20040908 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20050124 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20050427 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20050706 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20050706 |
|
| RD03 | Notification of appointment of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7423 Effective date: 20061006 |
|
| RD04 | Notification of resignation of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7424 Effective date: 20061011 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20090721 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20090730 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20090821 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20090831 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20090924 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20090929 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20091020 |
|
| RD03 | Notification of appointment of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7423 Effective date: 20091020 |
|
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20091113 |
|
| R150 | Certificate of patent or registration of utility model |
Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20121120 Year of fee payment: 3 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20121120 Year of fee payment: 3 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20131120 Year of fee payment: 4 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| LAPS | Cancellation because of no payment of annual fees |