JP7364330B2 - パエニバチルス(Paenibacillus)属種及びバチルス(Bacillus)属種のマンナナーゼ - Google Patents
パエニバチルス(Paenibacillus)属種及びバチルス(Bacillus)属種のマンナナーゼ Download PDFInfo
- Publication number
- JP7364330B2 JP7364330B2 JP2018522947A JP2018522947A JP7364330B2 JP 7364330 B2 JP7364330 B2 JP 7364330B2 JP 2018522947 A JP2018522947 A JP 2018522947A JP 2018522947 A JP2018522947 A JP 2018522947A JP 7364330 B2 JP7364330 B2 JP 7364330B2
- Authority
- JP
- Japan
- Prior art keywords
- mannanase
- amino acid
- seq
- acid sequence
- variant
- 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
Links
- 108010055059 beta-Mannosidase Proteins 0.000 title claims description 424
- 102100032487 Beta-mannosidase Human genes 0.000 title claims description 419
- 241000194110 Bacillus sp. (in: Bacteria) Species 0.000 title description 13
- 241000592795 Paenibacillus sp. Species 0.000 title description 4
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 353
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 337
- 229920001184 polypeptide Polymers 0.000 claims description 330
- 239000000203 mixture Substances 0.000 claims description 240
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 224
- 238000004140 cleaning Methods 0.000 claims description 147
- 229940088598 enzyme Drugs 0.000 claims description 112
- 102000004190 Enzymes Human genes 0.000 claims description 111
- 108090000790 Enzymes Proteins 0.000 claims description 110
- 230000000694 effects Effects 0.000 claims description 85
- 238000000034 method Methods 0.000 claims description 69
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 62
- 238000006467 substitution reaction Methods 0.000 claims description 56
- -1 arabinase Proteins 0.000 claims description 55
- 229920000057 Mannan Polymers 0.000 claims description 47
- 239000003599 detergent Substances 0.000 claims description 47
- 102000004882 Lipase Human genes 0.000 claims description 42
- 108090001060 Lipase Proteins 0.000 claims description 42
- 239000004367 Lipase Substances 0.000 claims description 42
- 235000019421 lipase Nutrition 0.000 claims description 42
- 102000040430 polynucleotide Human genes 0.000 claims description 41
- 108091033319 polynucleotide Proteins 0.000 claims description 41
- 239000002157 polynucleotide Substances 0.000 claims description 41
- 102200042488 rs17883862 Human genes 0.000 claims description 34
- 102220516650 Protein phosphatase 1 regulatory subunit 14B_T38E_mutation Human genes 0.000 claims description 33
- 108091005804 Peptidases Proteins 0.000 claims description 32
- 239000004365 Protease Substances 0.000 claims description 32
- 102000035195 Peptidases Human genes 0.000 claims description 31
- 150000007523 nucleic acids Chemical group 0.000 claims description 30
- 239000000758 substrate Substances 0.000 claims description 30
- 239000004744 fabric Substances 0.000 claims description 28
- 235000013305 food Nutrition 0.000 claims description 27
- 102220509369 Myeloid differentiation primary response protein MyD88_N67A_mutation Human genes 0.000 claims description 24
- 238000005406 washing Methods 0.000 claims description 24
- 239000007844 bleaching agent Substances 0.000 claims description 20
- 239000007788 liquid Substances 0.000 claims description 19
- 239000004094 surface-active agent Substances 0.000 claims description 18
- 108010065511 Amylases Proteins 0.000 claims description 15
- 102000013142 Amylases Human genes 0.000 claims description 15
- 235000019418 amylase Nutrition 0.000 claims description 15
- 108010083879 xyloglucan endo(1-4)-beta-D-glucanase Proteins 0.000 claims description 14
- 102000004316 Oxidoreductases Human genes 0.000 claims description 13
- 108090000854 Oxidoreductases Proteins 0.000 claims description 13
- 108010059820 Polygalacturonase Proteins 0.000 claims description 13
- 239000013604 expression vector Substances 0.000 claims description 13
- 239000007787 solid Substances 0.000 claims description 13
- 108010059892 Cellulase Proteins 0.000 claims description 12
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 11
- 239000002671 adjuvant Substances 0.000 claims description 11
- 238000004851 dishwashing Methods 0.000 claims description 11
- 239000011575 calcium Substances 0.000 claims description 10
- 239000002689 soil Substances 0.000 claims description 10
- 229910052717 sulfur Inorganic materials 0.000 claims description 10
- 108090000637 alpha-Amylases Proteins 0.000 claims description 9
- 229940106157 cellulase Drugs 0.000 claims description 9
- 239000000843 powder Substances 0.000 claims description 9
- 102200040232 rs672601337 Human genes 0.000 claims description 9
- 102100026189 Beta-galactosidase Human genes 0.000 claims description 8
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 claims description 8
- 102000003992 Peroxidases Human genes 0.000 claims description 8
- 108010005774 beta-Galactosidase Proteins 0.000 claims description 8
- 108010005400 cutinase Proteins 0.000 claims description 8
- 108010093305 exopolygalacturonase Proteins 0.000 claims description 8
- 108010087558 pectate lyase Proteins 0.000 claims description 8
- 239000004382 Amylase Substances 0.000 claims description 7
- 101710130006 Beta-glucanase Proteins 0.000 claims description 7
- 108010002430 hemicellulase Proteins 0.000 claims description 7
- 230000001976 improved effect Effects 0.000 claims description 7
- 102200062870 rs61735303 Human genes 0.000 claims description 7
- 108010013043 Acetylesterase Proteins 0.000 claims description 6
- 108010008885 Cellulose 1,4-beta-Cellobiosidase Proteins 0.000 claims description 6
- 102100036617 Monoacylglycerol lipase ABHD2 Human genes 0.000 claims description 6
- 102220544048 Myocyte-specific enhancer factor 2D_S59D_mutation Human genes 0.000 claims description 6
- 108010030291 alpha-Galactosidase Proteins 0.000 claims description 6
- 102000005840 alpha-Galactosidase Human genes 0.000 claims description 6
- 108040007629 peroxidase activity proteins Proteins 0.000 claims description 6
- 102220289518 rs775532257 Human genes 0.000 claims description 6
- 239000003381 stabilizer Substances 0.000 claims description 6
- 101710152845 Arabinogalactan endo-beta-1,4-galactanase Proteins 0.000 claims description 5
- 101710147028 Endo-beta-1,4-galactanase Proteins 0.000 claims description 5
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 claims description 5
- 102100022624 Glucoamylase Human genes 0.000 claims description 5
- 102000003820 Lipoxygenases Human genes 0.000 claims description 5
- 108090000128 Lipoxygenases Proteins 0.000 claims description 5
- 108010006035 Metalloproteases Proteins 0.000 claims description 5
- 102000005741 Metalloproteases Human genes 0.000 claims description 5
- 102200081191 rs749722729 Human genes 0.000 claims description 5
- ZIIUUSVHCHPIQD-UHFFFAOYSA-N 2,4,6-trimethyl-N-[3-(trifluoromethyl)phenyl]benzenesulfonamide Chemical compound CC1=CC(C)=CC(C)=C1S(=O)(=O)NC1=CC=CC(C(F)(F)F)=C1 ZIIUUSVHCHPIQD-UHFFFAOYSA-N 0.000 claims description 4
- 108010011619 6-Phytase Proteins 0.000 claims description 4
- 108700016155 Acyl transferases Proteins 0.000 claims description 4
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 claims description 4
- 108010053835 Catalase Proteins 0.000 claims description 4
- 108010023736 Chondroitinases and Chondroitin Lyases Proteins 0.000 claims description 4
- 101001096557 Dickeya dadantii (strain 3937) Rhamnogalacturonate lyase Proteins 0.000 claims description 4
- 101710111935 Endo-beta-1,4-glucanase Proteins 0.000 claims description 4
- 108090000371 Esterases Proteins 0.000 claims description 4
- 108010003272 Hyaluronate lyase Proteins 0.000 claims description 4
- 102000001974 Hyaluronidases Human genes 0.000 claims description 4
- 108010029541 Laccase Proteins 0.000 claims description 4
- 108010059881 Lactase Proteins 0.000 claims description 4
- 102220624190 Minor histocompatibility antigen H13_N10Q_mutation Human genes 0.000 claims description 4
- 102100031688 N-acetylgalactosamine-6-sulfatase Human genes 0.000 claims description 4
- 229910019142 PO4 Inorganic materials 0.000 claims description 4
- 108010064785 Phospholipases Proteins 0.000 claims description 4
- 102000015439 Phospholipases Human genes 0.000 claims description 4
- 108700019535 Phosphoprotein Phosphatases Proteins 0.000 claims description 4
- 102000045595 Phosphoprotein Phosphatases Human genes 0.000 claims description 4
- 108060008539 Transglutaminase Proteins 0.000 claims description 4
- 102000003425 Tyrosinase Human genes 0.000 claims description 4
- 108060008724 Tyrosinase Proteins 0.000 claims description 4
- 102000004139 alpha-Amylases Human genes 0.000 claims description 4
- 108010084650 alpha-N-arabinofuranosidase Proteins 0.000 claims description 4
- 108010009043 arylesterase Proteins 0.000 claims description 4
- 102000028848 arylesterase Human genes 0.000 claims description 4
- 108010019077 beta-Amylase Proteins 0.000 claims description 4
- YERABYSOHUZTPQ-UHFFFAOYSA-P endo-1,4-beta-Xylanase Chemical compound 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 claims description 4
- 239000002979 fabric softener Substances 0.000 claims description 4
- 235000013373 food additive Nutrition 0.000 claims description 4
- 239000002778 food additive Substances 0.000 claims description 4
- 229940059442 hemicellulase Drugs 0.000 claims description 4
- 229960002773 hyaluronidase Drugs 0.000 claims description 4
- 108010059345 keratinase Proteins 0.000 claims description 4
- 229940116108 lactase Drugs 0.000 claims description 4
- 108010062085 ligninase Proteins 0.000 claims description 4
- 230000002366 lipolytic effect Effects 0.000 claims description 4
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 108010072638 pectinacetylesterase Proteins 0.000 claims description 4
- 102000004251 pectinacetylesterase Human genes 0.000 claims description 4
- 229940085127 phytase Drugs 0.000 claims description 4
- 102220222975 rs1060501885 Human genes 0.000 claims description 4
- 102200133420 rs754200057 Human genes 0.000 claims description 4
- 102200069353 rs8103142 Human genes 0.000 claims description 4
- 102200006156 rs876658534 Human genes 0.000 claims description 4
- 108010038851 tannase Proteins 0.000 claims description 4
- 230000001131 transforming effect Effects 0.000 claims description 4
- 102000003601 transglutaminase Human genes 0.000 claims description 4
- 229920001221 xylan Polymers 0.000 claims description 4
- 150000004823 xylans Chemical class 0.000 claims description 4
- 102000057234 Acyl transferases Human genes 0.000 claims description 3
- ZOXJGFHDIHLPTG-UHFFFAOYSA-N Boron Chemical compound [B] ZOXJGFHDIHLPTG-UHFFFAOYSA-N 0.000 claims description 3
- HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 claims description 3
- 229940024171 alpha-amylase Drugs 0.000 claims description 3
- 229910052796 boron Inorganic materials 0.000 claims description 3
- 229910052791 calcium Inorganic materials 0.000 claims description 3
- 229910052727 yttrium Inorganic materials 0.000 claims description 3
- 239000003674 animal food additive Substances 0.000 claims description 2
- 150000002500 ions Chemical class 0.000 claims description 2
- 229910052725 zinc Inorganic materials 0.000 claims description 2
- 239000011701 zinc Substances 0.000 claims description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims 2
- 239000010452 phosphate Substances 0.000 claims 2
- 102100035882 Catalase Human genes 0.000 claims 1
- 102220480248 G-protein coupled receptor family C group 6 member A_Q78A_mutation Human genes 0.000 claims 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 238000002360 preparation method Methods 0.000 claims 1
- 102220031036 rs3740912 Human genes 0.000 claims 1
- 239000012634 fragment Substances 0.000 description 257
- 235000001014 amino acid Nutrition 0.000 description 123
- 108090000623 proteins and genes Proteins 0.000 description 78
- 229940024606 amino acid Drugs 0.000 description 67
- 150000001413 amino acids Chemical class 0.000 description 61
- 230000035772 mutation Effects 0.000 description 51
- 102000004169 proteins and genes Human genes 0.000 description 50
- 235000018102 proteins Nutrition 0.000 description 45
- 238000003556 assay Methods 0.000 description 32
- 210000004027 cell Anatomy 0.000 description 31
- 229920000926 Galactomannan Polymers 0.000 description 28
- 239000000463 material Substances 0.000 description 28
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 28
- OMDQUFIYNPYJFM-XKDAHURESA-N (2r,3r,4s,5r,6s)-2-(hydroxymethyl)-6-[[(2r,3s,4r,5s,6r)-4,5,6-trihydroxy-3-[(2s,3s,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxyoxan-2-yl]methoxy]oxane-3,4,5-triol Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O[C@H]2[C@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)O)[C@H](O)[C@H](O)[C@H](O)O1 OMDQUFIYNPYJFM-XKDAHURESA-N 0.000 description 24
- 229920000161 Locust bean gum Polymers 0.000 description 24
- 230000027455 binding Effects 0.000 description 24
- 235000010420 locust bean gum Nutrition 0.000 description 24
- 239000000711 locust bean gum Substances 0.000 description 24
- 235000014469 Bacillus subtilis Nutrition 0.000 description 22
- 230000008569 process Effects 0.000 description 22
- 239000000243 solution Substances 0.000 description 22
- 108010076504 Protein Sorting Signals Proteins 0.000 description 21
- 102000039446 nucleic acids Human genes 0.000 description 20
- 108020004707 nucleic acids Proteins 0.000 description 20
- 150000003839 salts Chemical class 0.000 description 20
- 241000196324 Embryophyta Species 0.000 description 19
- 229920002581 Glucomannan Polymers 0.000 description 19
- 235000013405 beer Nutrition 0.000 description 19
- 230000037430 deletion Effects 0.000 description 19
- 238000012217 deletion Methods 0.000 description 19
- 229910052698 phosphorus Inorganic materials 0.000 description 18
- 241001465754 Metazoa Species 0.000 description 17
- 235000013339 cereals Nutrition 0.000 description 17
- 239000003795 chemical substances by application Substances 0.000 description 17
- GXCLVBGFBYZDAG-UHFFFAOYSA-N N-[2-(1H-indol-3-yl)ethyl]-N-methylprop-2-en-1-amine Chemical compound CN(CCC1=CNC2=C1C=CC=C2)CC=C GXCLVBGFBYZDAG-UHFFFAOYSA-N 0.000 description 16
- 239000004615 ingredient Substances 0.000 description 16
- 230000037431 insertion Effects 0.000 description 16
- 238000003780 insertion Methods 0.000 description 16
- LUEWUZLMQUOBSB-FSKGGBMCSA-N (2s,3s,4s,5s,6r)-2-[(2r,3s,4r,5r,6s)-6-[(2r,3s,4r,5s,6s)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2r,4r,5s,6r)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-4,5-dihydroxy-2-(hydroxymethyl)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](O[C@@H]2[C@H](O[C@@H](OC3[C@H](O[C@@H](O)[C@@H](O)[C@H]3O)CO)[C@@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O LUEWUZLMQUOBSB-FSKGGBMCSA-N 0.000 description 15
- 150000001875 compounds Chemical class 0.000 description 15
- 229940046240 glucomannan Drugs 0.000 description 15
- 235000019419 proteases Nutrition 0.000 description 15
- 229910052751 metal Inorganic materials 0.000 description 13
- 239000002184 metal Substances 0.000 description 13
- 230000002351 pectolytic effect Effects 0.000 description 13
- 150000004804 polysaccharides Chemical class 0.000 description 13
- 239000000047 product Substances 0.000 description 13
- 102000004157 Hydrolases Human genes 0.000 description 12
- 108090000604 Hydrolases Proteins 0.000 description 12
- 230000003197 catalytic effect Effects 0.000 description 12
- 239000002738 chelating agent Substances 0.000 description 12
- 102220011156 rs142503093 Human genes 0.000 description 12
- 239000002253 acid Substances 0.000 description 11
- 239000000654 additive Substances 0.000 description 11
- 230000001580 bacterial effect Effects 0.000 description 11
- 239000003054 catalyst Substances 0.000 description 11
- 229920001282 polysaccharide Polymers 0.000 description 11
- 239000005017 polysaccharide Substances 0.000 description 11
- 239000000523 sample Substances 0.000 description 11
- 241000193830 Bacillus <bacterium> Species 0.000 description 10
- 238000002835 absorbance Methods 0.000 description 10
- 229920002678 cellulose Polymers 0.000 description 10
- 239000001913 cellulose Substances 0.000 description 10
- 235000010980 cellulose Nutrition 0.000 description 10
- 235000019985 fermented beverage Nutrition 0.000 description 10
- 229920000642 polymer Polymers 0.000 description 10
- 235000000346 sugar Nutrition 0.000 description 10
- 230000009466 transformation Effects 0.000 description 10
- 229910052721 tungsten Inorganic materials 0.000 description 10
- 240000005979 Hordeum vulgare Species 0.000 description 9
- 235000007340 Hordeum vulgare Nutrition 0.000 description 9
- 229940025131 amylases Drugs 0.000 description 9
- 238000004061 bleaching Methods 0.000 description 9
- 238000006243 chemical reaction Methods 0.000 description 9
- 239000000945 filler Substances 0.000 description 9
- 238000009396 hybridization Methods 0.000 description 9
- 238000006460 hydrolysis reaction Methods 0.000 description 9
- 239000003112 inhibitor Substances 0.000 description 9
- 229920000136 polysorbate Polymers 0.000 description 9
- 230000028327 secretion Effects 0.000 description 9
- 239000013598 vector Substances 0.000 description 9
- 241000894006 Bacteria Species 0.000 description 8
- 108020004414 DNA Proteins 0.000 description 8
- 229920002907 Guar gum Polymers 0.000 description 8
- 239000007993 MOPS buffer Substances 0.000 description 8
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 8
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 8
- 241000282887 Suidae Species 0.000 description 8
- 230000000996 additive effect Effects 0.000 description 8
- 230000002255 enzymatic effect Effects 0.000 description 8
- 238000009472 formulation Methods 0.000 description 8
- 230000002538 fungal effect Effects 0.000 description 8
- 239000000499 gel Substances 0.000 description 8
- 125000003147 glycosyl group Chemical group 0.000 description 8
- 239000000665 guar gum Substances 0.000 description 8
- 235000010417 guar gum Nutrition 0.000 description 8
- 239000011777 magnesium Substances 0.000 description 8
- 229910052700 potassium Inorganic materials 0.000 description 8
- ZMZGIVVRBMFZSG-UHFFFAOYSA-N 4-hydroxybenzohydrazide Chemical compound NNC(=O)C1=CC=C(O)C=C1 ZMZGIVVRBMFZSG-UHFFFAOYSA-N 0.000 description 7
- 108010084185 Cellulases Proteins 0.000 description 7
- 102000005575 Cellulases Human genes 0.000 description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 7
- 229920002324 Galactoglucomannan Polymers 0.000 description 7
- 229920002472 Starch Polymers 0.000 description 7
- 239000012190 activator Substances 0.000 description 7
- 101150009206 aprE gene Proteins 0.000 description 7
- 239000003153 chemical reaction reagent Substances 0.000 description 7
- 239000000975 dye Substances 0.000 description 7
- 239000000284 extract Substances 0.000 description 7
- 108020001507 fusion proteins Proteins 0.000 description 7
- 102000037865 fusion proteins Human genes 0.000 description 7
- 229960002154 guar gum Drugs 0.000 description 7
- 230000007062 hydrolysis Effects 0.000 description 7
- 235000021577 malt beverage Nutrition 0.000 description 7
- 239000006072 paste Substances 0.000 description 7
- 238000003752 polymerase chain reaction Methods 0.000 description 7
- 239000002904 solvent Substances 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 150000008163 sugars Chemical class 0.000 description 7
- 108091026890 Coding region Proteins 0.000 description 6
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 6
- 229920001131 Pulp (paper) Polymers 0.000 description 6
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 235000021307 Triticum Nutrition 0.000 description 6
- 241000209140 Triticum Species 0.000 description 6
- 240000008042 Zea mays Species 0.000 description 6
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 6
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 6
- 150000007513 acids Chemical class 0.000 description 6
- 238000007792 addition Methods 0.000 description 6
- 239000000872 buffer Substances 0.000 description 6
- 239000010949 copper Substances 0.000 description 6
- 235000005822 corn Nutrition 0.000 description 6
- 235000010037 flour treatment agent Nutrition 0.000 description 6
- 125000005647 linker group Chemical group 0.000 description 6
- 239000013612 plasmid Substances 0.000 description 6
- 238000007639 printing Methods 0.000 description 6
- 238000012545 processing Methods 0.000 description 6
- 235000019698 starch Nutrition 0.000 description 6
- 239000008107 starch Substances 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- 238000012546 transfer Methods 0.000 description 6
- 240000006439 Aspergillus oryzae Species 0.000 description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 5
- KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 description 5
- 102220643992 Multiple inositol polyphosphate phosphatase 1_Q78A_mutation Human genes 0.000 description 5
- 241001292348 Salipaludibacillus agaradhaerens Species 0.000 description 5
- 108010056079 Subtilisins Proteins 0.000 description 5
- 102000005158 Subtilisins Human genes 0.000 description 5
- 235000008429 bread Nutrition 0.000 description 5
- 125000004432 carbon atom Chemical group C* 0.000 description 5
- 150000001768 cations Chemical class 0.000 description 5
- 235000013365 dairy product Nutrition 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 235000014113 dietary fatty acids Nutrition 0.000 description 5
- 235000021186 dishes Nutrition 0.000 description 5
- 239000000194 fatty acid Substances 0.000 description 5
- 229930195729 fatty acid Natural products 0.000 description 5
- 150000004665 fatty acids Chemical class 0.000 description 5
- 238000000855 fermentation Methods 0.000 description 5
- 230000004151 fermentation Effects 0.000 description 5
- 239000006260 foam Substances 0.000 description 5
- 230000004927 fusion Effects 0.000 description 5
- 239000008187 granular material Substances 0.000 description 5
- 238000011534 incubation Methods 0.000 description 5
- LUEWUZLMQUOBSB-GFVSVBBRSA-N mannan Chemical class 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](O[C@@H](O[C@H]3[C@H](O[C@@H](O)[C@@H](O)[C@H]3O)CO)[C@@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O LUEWUZLMQUOBSB-GFVSVBBRSA-N 0.000 description 5
- 235000012054 meals Nutrition 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 230000000813 microbial effect Effects 0.000 description 5
- 108010020132 microbial serine proteinases Proteins 0.000 description 5
- 239000002736 nonionic surfactant Substances 0.000 description 5
- 229920001542 oligosaccharide Polymers 0.000 description 5
- 150000002482 oligosaccharides Chemical class 0.000 description 5
- 229920001277 pectin Polymers 0.000 description 5
- 239000001814 pectin Substances 0.000 description 5
- 235000010987 pectin Nutrition 0.000 description 5
- 108020004410 pectinesterase Proteins 0.000 description 5
- 210000001938 protoplast Anatomy 0.000 description 5
- 102220262974 rs1554304971 Human genes 0.000 description 5
- 102220192067 rs886057201 Human genes 0.000 description 5
- 108010038196 saccharide-binding proteins Proteins 0.000 description 5
- 229910052708 sodium Inorganic materials 0.000 description 5
- 239000011734 sodium Substances 0.000 description 5
- 235000019832 sodium triphosphate Nutrition 0.000 description 5
- 239000006228 supernatant Substances 0.000 description 5
- 235000020357 syrup Nutrition 0.000 description 5
- 239000006188 syrup Substances 0.000 description 5
- 239000003826 tablet Substances 0.000 description 5
- 238000013518 transcription Methods 0.000 description 5
- 230000035897 transcription Effects 0.000 description 5
- 229910052723 transition metal Inorganic materials 0.000 description 5
- 229910052720 vanadium Inorganic materials 0.000 description 5
- 241000228245 Aspergillus niger Species 0.000 description 4
- 241000193752 Bacillus circulans Species 0.000 description 4
- 102220612220 Brain-specific homeobox protein homolog_K63R_mutation Human genes 0.000 description 4
- 235000013162 Cocos nucifera Nutrition 0.000 description 4
- 244000060011 Cocos nucifera Species 0.000 description 4
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 4
- MHAJPDPJQMAIIY-UHFFFAOYSA-N Hydrogen peroxide Chemical compound OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 4
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 4
- 229920002752 Konjac Polymers 0.000 description 4
- 241000179039 Paenibacillus Species 0.000 description 4
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 4
- 241000282849 Ruminantia Species 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 108090000787 Subtilisin Proteins 0.000 description 4
- 102220503491 Transmembrane protease serine 9_S30T_mutation Human genes 0.000 description 4
- 241000499912 Trichoderma reesei Species 0.000 description 4
- 229910052783 alkali metal Inorganic materials 0.000 description 4
- 235000019730 animal feed additive Nutrition 0.000 description 4
- 239000003945 anionic surfactant Substances 0.000 description 4
- 230000009286 beneficial effect Effects 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 150000001720 carbohydrates Chemical group 0.000 description 4
- 239000003093 cationic surfactant Substances 0.000 description 4
- 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 4
- 229960005091 chloramphenicol Drugs 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 229910052802 copper Inorganic materials 0.000 description 4
- 238000005260 corrosion Methods 0.000 description 4
- 230000007797 corrosion Effects 0.000 description 4
- 239000013078 crystal Substances 0.000 description 4
- 239000002552 dosage form Substances 0.000 description 4
- 238000005538 encapsulation Methods 0.000 description 4
- 238000011156 evaluation Methods 0.000 description 4
- 235000013312 flour Nutrition 0.000 description 4
- 239000003205 fragrance Substances 0.000 description 4
- 230000003301 hydrolyzing effect Effects 0.000 description 4
- 229910052500 inorganic mineral Inorganic materials 0.000 description 4
- 239000000252 konjac Substances 0.000 description 4
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 4
- 125000000311 mannosyl group Chemical group C1([C@@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 4
- 230000001404 mediated effect Effects 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 239000011707 mineral Substances 0.000 description 4
- 235000010755 mineral Nutrition 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 239000002245 particle Substances 0.000 description 4
- 150000004965 peroxy acids Chemical class 0.000 description 4
- 230000001105 regulatory effect Effects 0.000 description 4
- 102220272575 rs767681165 Human genes 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 239000004753 textile Substances 0.000 description 4
- 150000003624 transition metals Chemical class 0.000 description 4
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 3
- 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 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 241000251468 Actinopterygii Species 0.000 description 3
- 241000228212 Aspergillus Species 0.000 description 3
- 235000007319 Avena orientalis Nutrition 0.000 description 3
- 244000075850 Avena orientalis Species 0.000 description 3
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 3
- 241000149420 Bothrometopus brevis Species 0.000 description 3
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 3
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 3
- 102220499774 Carbonic anhydrase 2_N67Q_mutation Human genes 0.000 description 3
- 102000016938 Catalase Human genes 0.000 description 3
- 102220474812 Chemerin-like receptor 2_H67A_mutation Human genes 0.000 description 3
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- IAYPIBMASNFSPL-UHFFFAOYSA-N Ethylene oxide Chemical compound C1CO1 IAYPIBMASNFSPL-UHFFFAOYSA-N 0.000 description 3
- 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 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 102220469871 Protein argonaute-3_T38L_mutation Human genes 0.000 description 3
- 241000589540 Pseudomonas fluorescens Species 0.000 description 3
- 239000013543 active substance Substances 0.000 description 3
- 238000013019 agitation Methods 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 150000001340 alkali metals Chemical group 0.000 description 3
- 229910052784 alkaline earth metal Inorganic materials 0.000 description 3
- LHAOFBCHXGZGOR-NAVBLJQLSA-N alpha-D-Manp-(1->3)-alpha-D-Manp-(1->2)-alpha-D-Manp Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[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](CO)O2)O)[C@H](O)[C@@H](CO)O1 LHAOFBCHXGZGOR-NAVBLJQLSA-N 0.000 description 3
- 239000003963 antioxidant agent Substances 0.000 description 3
- 235000006708 antioxidants Nutrition 0.000 description 3
- 125000004429 atom Chemical group 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 235000012970 cakes Nutrition 0.000 description 3
- 239000001110 calcium chloride Substances 0.000 description 3
- 229910001628 calcium chloride Inorganic materials 0.000 description 3
- 235000011148 calcium chloride Nutrition 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 239000012876 carrier material Substances 0.000 description 3
- 210000002421 cell wall Anatomy 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 229910017052 cobalt Inorganic materials 0.000 description 3
- 239000010941 cobalt Substances 0.000 description 3
- GUTLYIVDDKVIGB-UHFFFAOYSA-N cobalt atom Chemical compound [Co] GUTLYIVDDKVIGB-UHFFFAOYSA-N 0.000 description 3
- 210000001072 colon Anatomy 0.000 description 3
- 239000003086 colorant Substances 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 229920001577 copolymer Polymers 0.000 description 3
- 239000012228 culture supernatant Substances 0.000 description 3
- 230000000593 degrading effect Effects 0.000 description 3
- 239000013024 dilution buffer Substances 0.000 description 3
- 239000002270 dispersing agent Substances 0.000 description 3
- 239000000835 fiber Substances 0.000 description 3
- 235000019688 fish Nutrition 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 235000015243 ice cream Nutrition 0.000 description 3
- 239000011256 inorganic filler Substances 0.000 description 3
- 229910003475 inorganic filler Inorganic materials 0.000 description 3
- 229910052742 iron Inorganic materials 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 238000005621 mannosylation reaction Methods 0.000 description 3
- FYGDTMLNYKFZSV-UHFFFAOYSA-N mannotriose Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(O)C(O)C2O)CO)C(O)C1O FYGDTMLNYKFZSV-UHFFFAOYSA-N 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 239000004005 microsphere Substances 0.000 description 3
- 235000013336 milk Nutrition 0.000 description 3
- 239000008267 milk Substances 0.000 description 3
- 210000004080 milk Anatomy 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 235000016709 nutrition Nutrition 0.000 description 3
- 239000000049 pigment Substances 0.000 description 3
- 229920005646 polycarboxylate Polymers 0.000 description 3
- 229920001223 polyethylene glycol Polymers 0.000 description 3
- 235000013406 prebiotics Nutrition 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 102200034153 rs201151358 Human genes 0.000 description 3
- 102220135902 rs61731470 Human genes 0.000 description 3
- 102220053377 rs727504500 Human genes 0.000 description 3
- 102220076789 rs747976292 Human genes 0.000 description 3
- 238000012289 standard assay Methods 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- UNXRWKVEANCORM-UHFFFAOYSA-I triphosphate(5-) Chemical compound [O-]P([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O UNXRWKVEANCORM-UHFFFAOYSA-I 0.000 description 3
- 239000011782 vitamin Substances 0.000 description 3
- 235000013343 vitamin Nutrition 0.000 description 3
- 229940088594 vitamin Drugs 0.000 description 3
- 229930003231 vitamin Natural products 0.000 description 3
- CIOXZGOUEYHNBF-UHFFFAOYSA-N (carboxymethoxy)succinic acid Chemical compound OC(=O)COC(C(O)=O)CC(O)=O CIOXZGOUEYHNBF-UHFFFAOYSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 229920001817 Agar Polymers 0.000 description 2
- 241000589155 Agrobacterium tumefaciens Species 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 2
- 244000247812 Amorphophallus rivieri Species 0.000 description 2
- 235000001206 Amorphophallus rivieri Nutrition 0.000 description 2
- 244000105624 Arachis hypogaea Species 0.000 description 2
- 241001513093 Aspergillus awamori Species 0.000 description 2
- 241000351920 Aspergillus nidulans Species 0.000 description 2
- 241001530056 Athelia rolfsii Species 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241001328122 Bacillus clausii Species 0.000 description 2
- 241000193747 Bacillus firmus Species 0.000 description 2
- 241000006382 Bacillus halodurans Species 0.000 description 2
- 241000194108 Bacillus licheniformis Species 0.000 description 2
- 241000194107 Bacillus megaterium Species 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 101000740449 Bacillus subtilis (strain 168) Biotin/lipoyl attachment protein Proteins 0.000 description 2
- 241000186000 Bifidobacterium Species 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 235000004977 Brassica sinapistrum Nutrition 0.000 description 2
- 241000589513 Burkholderia cepacia Species 0.000 description 2
- 241000178335 Caldicellulosiruptor saccharolyticus Species 0.000 description 2
- 241000282994 Cervidae Species 0.000 description 2
- 241000242346 Constrictibacter antarcticus Species 0.000 description 2
- 229920000742 Cotton Polymers 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- 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 2
- 241000588694 Erwinia amylovora Species 0.000 description 2
- 241000233866 Fungi Species 0.000 description 2
- 241000223218 Fusarium Species 0.000 description 2
- 241000287828 Gallus gallus Species 0.000 description 2
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 2
- GLZPCOQZEFWAFX-UHFFFAOYSA-N Geraniol Chemical compound CC(C)=CCCC(C)=CCO GLZPCOQZEFWAFX-UHFFFAOYSA-N 0.000 description 2
- 102000005720 Glutathione transferase Human genes 0.000 description 2
- 108010070675 Glutathione transferase Proteins 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 235000010469 Glycine max Nutrition 0.000 description 2
- 244000068988 Glycine max Species 0.000 description 2
- 244000299507 Gossypium hirsutum Species 0.000 description 2
- 239000007995 HEPES buffer Substances 0.000 description 2
- 241000125500 Hedypnois rhagadioloides Species 0.000 description 2
- 241000208818 Helianthus Species 0.000 description 2
- 235000003222 Helianthus annuus Nutrition 0.000 description 2
- 102220628249 Hemoglobin subunit alpha_N10T_mutation Human genes 0.000 description 2
- 241001138401 Kluyveromyces lactis Species 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- 241000186660 Lactobacillus Species 0.000 description 2
- 241000270322 Lepidosauria Species 0.000 description 2
- 235000004431 Linum usitatissimum Nutrition 0.000 description 2
- 240000006240 Linum usitatissimum Species 0.000 description 2
- 241000219745 Lupinus Species 0.000 description 2
- 241001625930 Luria Species 0.000 description 2
- 102000004317 Lyases Human genes 0.000 description 2
- 108090000856 Lyases Proteins 0.000 description 2
- 239000007987 MES buffer Substances 0.000 description 2
- WAEMQWOKJMHJLA-UHFFFAOYSA-N Manganese(2+) Chemical compound [Mn+2] WAEMQWOKJMHJLA-UHFFFAOYSA-N 0.000 description 2
- 240000003183 Manihot esculenta Species 0.000 description 2
- 235000016735 Manihot esculenta subsp esculenta Nutrition 0.000 description 2
- BPQQTUXANYXVAA-UHFFFAOYSA-N Orthosilicate Chemical compound [O-][Si]([O-])([O-])[O-] BPQQTUXANYXVAA-UHFFFAOYSA-N 0.000 description 2
- 240000007594 Oryza sativa Species 0.000 description 2
- 235000007164 Oryza sativa Nutrition 0.000 description 2
- 241000194105 Paenibacillus polymyxa Species 0.000 description 2
- 241000588912 Pantoea agglomerans Species 0.000 description 2
- 108700020962 Peroxidase Proteins 0.000 description 2
- 241000286209 Phasianidae Species 0.000 description 2
- 235000010582 Pisum sativum Nutrition 0.000 description 2
- 240000004713 Pisum sativum Species 0.000 description 2
- 229920000388 Polyphosphate Polymers 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 2
- 102220607950 Protein inturned_S74E_mutation Human genes 0.000 description 2
- 241000589516 Pseudomonas Species 0.000 description 2
- 241000168225 Pseudomonas alcaligenes Species 0.000 description 2
- 241000589630 Pseudomonas pseudoalcaligenes Species 0.000 description 2
- 241000589614 Pseudomonas stutzeri Species 0.000 description 2
- 102220573044 RNA polymerase II subunit A C-terminal domain phosphatase_T10Q_mutation Human genes 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 241000303962 Rhizopus delemar Species 0.000 description 2
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 2
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 2
- 239000004115 Sodium Silicate Substances 0.000 description 2
- 240000003768 Solanum lycopersicum Species 0.000 description 2
- 235000002595 Solanum tuberosum Nutrition 0.000 description 2
- 244000061456 Solanum tuberosum Species 0.000 description 2
- 244000062793 Sorghum vulgare Species 0.000 description 2
- 241001467541 Streptomyces galbus Species 0.000 description 2
- 241000187398 Streptomyces lividans Species 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 2
- 241000223258 Thermomyces lanuginosus Species 0.000 description 2
- 241000204666 Thermotoga maritima Species 0.000 description 2
- 241000223260 Trichoderma harzianum Species 0.000 description 2
- 244000042182 Trichotosia fusca Species 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 239000008272 agar Substances 0.000 description 2
- 230000001476 alcoholic effect Effects 0.000 description 2
- IAJILQKETJEXLJ-RSJOWCBRSA-N aldehydo-D-galacturonic acid Chemical compound O=C[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)C(O)=O IAJILQKETJEXLJ-RSJOWCBRSA-N 0.000 description 2
- 239000003513 alkali Substances 0.000 description 2
- 125000000217 alkyl group Chemical group 0.000 description 2
- 229910052782 aluminium Inorganic materials 0.000 description 2
- 125000000539 amino acid group Chemical group 0.000 description 2
- 150000003863 ammonium salts Chemical class 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 239000002585 base Substances 0.000 description 2
- QMKYBPDZANOJGF-UHFFFAOYSA-N benzene-1,3,5-tricarboxylic acid Chemical compound OC(=O)C1=CC(C(O)=O)=CC(C(O)=O)=C1 QMKYBPDZANOJGF-UHFFFAOYSA-N 0.000 description 2
- 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 2
- 235000013361 beverage Nutrition 0.000 description 2
- 150000001642 boronic acid derivatives Chemical class 0.000 description 2
- 239000006227 byproduct Substances 0.000 description 2
- 102220351010 c.211A>C Human genes 0.000 description 2
- 229910001424 calcium ion Inorganic materials 0.000 description 2
- 239000002775 capsule Substances 0.000 description 2
- 229910052799 carbon Inorganic materials 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 101150052795 cbh-1 gene Proteins 0.000 description 2
- 210000004671 cell-free system Anatomy 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 238000007385 chemical modification Methods 0.000 description 2
- QMVPMAAFGQKVCJ-UHFFFAOYSA-N citronellol Chemical compound OCCC(C)CCC=C(C)C QMVPMAAFGQKVCJ-UHFFFAOYSA-N 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 238000013270 controlled release Methods 0.000 description 2
- 230000001276 controlling effect Effects 0.000 description 2
- 238000001816 cooling Methods 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 239000008367 deionised water Substances 0.000 description 2
- 229910021641 deionized water Inorganic materials 0.000 description 2
- 230000008021 deposition Effects 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 239000012153 distilled water Substances 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000003623 enhancer Substances 0.000 description 2
- 150000002148 esters Chemical class 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 239000003925 fat Substances 0.000 description 2
- 235000019197 fats Nutrition 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 239000007850 fluorescent dye Substances 0.000 description 2
- 235000012041 food component Nutrition 0.000 description 2
- 239000005417 food ingredient Substances 0.000 description 2
- 229930182830 galactose Natural products 0.000 description 2
- 239000007897 gelcap Substances 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 230000009477 glass transition Effects 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 150000004676 glycans Polymers 0.000 description 2
- 230000036449 good health Effects 0.000 description 2
- 238000012835 hanging drop method Methods 0.000 description 2
- DCAYPVUWAIABOU-UHFFFAOYSA-N hexadecane Chemical compound CCCCCCCCCCCCCCCC DCAYPVUWAIABOU-UHFFFAOYSA-N 0.000 description 2
- 229920001519 homopolymer Polymers 0.000 description 2
- 239000003752 hydrotrope Substances 0.000 description 2
- 230000014726 immortalization of host cell Effects 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- 235000010485 konjac Nutrition 0.000 description 2
- 235000019823 konjac gum Nutrition 0.000 description 2
- 239000004310 lactic acid Substances 0.000 description 2
- 235000014655 lactic acid Nutrition 0.000 description 2
- 229940039696 lactobacillus Drugs 0.000 description 2
- 238000010412 laundry washing Methods 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- XMGQYMWWDOXHJM-UHFFFAOYSA-N limonene Chemical compound CC(=C)C1CCC(C)=CC1 XMGQYMWWDOXHJM-UHFFFAOYSA-N 0.000 description 2
- WPBNNNQJVZRUHP-UHFFFAOYSA-L manganese(2+);methyl n-[[2-(methoxycarbonylcarbamothioylamino)phenyl]carbamothioyl]carbamate;n-[2-(sulfidocarbothioylamino)ethyl]carbamodithioate Chemical compound [Mn+2].[S-]C(=S)NCCNC([S-])=S.COC(=O)NC(=S)NC1=CC=CC=C1NC(=S)NC(=O)OC WPBNNNQJVZRUHP-UHFFFAOYSA-L 0.000 description 2
- YDSWCNNOKPMOTP-UHFFFAOYSA-N mellitic acid Chemical compound OC(=O)C1=C(C(O)=O)C(C(O)=O)=C(C(O)=O)C(C(O)=O)=C1C(O)=O YDSWCNNOKPMOTP-UHFFFAOYSA-N 0.000 description 2
- 150000002739 metals Chemical class 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 238000001823 molecular biology technique Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 150000002772 monosaccharides Chemical class 0.000 description 2
- 238000002887 multiple sequence alignment Methods 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 239000002777 nucleoside Substances 0.000 description 2
- 125000003835 nucleoside group Chemical group 0.000 description 2
- 239000003921 oil Substances 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 239000003002 pH adjusting agent Substances 0.000 description 2
- 238000001139 pH measurement Methods 0.000 description 2
- 239000003346 palm kernel oil Substances 0.000 description 2
- 235000019865 palm kernel oil Nutrition 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 235000020232 peanut Nutrition 0.000 description 2
- 210000001322 periplasm Anatomy 0.000 description 2
- JRKICGRDRMAZLK-UHFFFAOYSA-L peroxydisulfate Chemical compound [O-]S(=O)(=O)OOS([O-])(=O)=O JRKICGRDRMAZLK-UHFFFAOYSA-L 0.000 description 2
- 235000021317 phosphate Nutrition 0.000 description 2
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 2
- 239000001205 polyphosphate Substances 0.000 description 2
- 235000011176 polyphosphates Nutrition 0.000 description 2
- 229920002223 polystyrene Polymers 0.000 description 2
- 239000011591 potassium Substances 0.000 description 2
- 244000144977 poultry Species 0.000 description 2
- 235000013594 poultry meat Nutrition 0.000 description 2
- 239000002243 precursor Substances 0.000 description 2
- 230000001902 propagating effect Effects 0.000 description 2
- 239000012460 protein solution Substances 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 235000009566 rice Nutrition 0.000 description 2
- 102200094890 rs121913565 Human genes 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 239000003352 sequestering agent Substances 0.000 description 2
- 150000004760 silicates Chemical class 0.000 description 2
- 229910052709 silver Inorganic materials 0.000 description 2
- 239000004332 silver Substances 0.000 description 2
- 239000000344 soap Substances 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000001509 sodium citrate Substances 0.000 description 2
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 2
- 239000008247 solid mixture Substances 0.000 description 2
- 239000007921 spray Substances 0.000 description 2
- 238000004659 sterilization and disinfection Methods 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 2
- 108010075550 termamyl Proteins 0.000 description 2
- 238000010361 transduction Methods 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- 239000002888 zwitterionic surfactant Substances 0.000 description 2
- VXWBQOJISHAKKM-UHFFFAOYSA-N (4-formylphenyl)boronic acid Chemical compound OB(O)C1=CC=C(C=O)C=C1 VXWBQOJISHAKKM-UHFFFAOYSA-N 0.000 description 1
- QMVPMAAFGQKVCJ-SNVBAGLBSA-N (R)-(+)-citronellol Natural products OCC[C@H](C)CCC=C(C)C QMVPMAAFGQKVCJ-SNVBAGLBSA-N 0.000 description 1
- RJQKKZNUWRIHCS-YDPWGIMBSA-N 1,4-b-d-mannan Chemical compound O[C@H]1[C@@H](O)[C@H](O)[C@@H](CO)OC1O[C@@H]1[C@@H](CO)OC(O[C@@H]2[C@H](OC(O[C@@H]3[C@H](OC(O[C@@H]4[C@H](OC(O[C@@H]5[C@H](OC(O[C@@H]6[C@H](OC(O[C@@H]7[C@H](OC(O[C@@H]8[C@H](OC(O[C@@H]9[C@H](OC(O)[C@@H](O)[C@H]9O)CO)[C@@H](O)[C@H]8O)CO)[C@@H](O)[C@H]7O)CO)[C@@H](O)[C@H]6O)CO)[C@@H](O)[C@H]5O)CO)[C@@H](O)[C@H]4O)CO)[C@@H](O)[C@H]3O)CO)[C@@H](O)[C@H]2O)CO)[C@@H](O)[C@H]1O RJQKKZNUWRIHCS-YDPWGIMBSA-N 0.000 description 1
- OSSNTDFYBPYIEC-UHFFFAOYSA-N 1-ethenylimidazole Chemical compound C=CN1C=CN=C1 OSSNTDFYBPYIEC-UHFFFAOYSA-N 0.000 description 1
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 1
- 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
- VJSWLXWONORKLD-UHFFFAOYSA-N 2,4,6-trihydroxybenzene-1,3,5-trisulfonic acid Chemical compound OC1=C(S(O)(=O)=O)C(O)=C(S(O)(=O)=O)C(O)=C1S(O)(=O)=O VJSWLXWONORKLD-UHFFFAOYSA-N 0.000 description 1
- CFPOJWPDQWJEMO-UHFFFAOYSA-N 2-(1,2-dicarboxyethoxy)butanedioic acid Chemical compound OC(=O)CC(C(O)=O)OC(C(O)=O)CC(O)=O CFPOJWPDQWJEMO-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-PZPXDAEZSA-N 4β-mannobiose 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](O)[C@H]1O GUBGYTABKSRVRQ-PZPXDAEZSA-N 0.000 description 1
- 108010051457 Acid Phosphatase Proteins 0.000 description 1
- 102000013563 Acid Phosphatase Human genes 0.000 description 1
- NLHHRLWOUZZQLW-UHFFFAOYSA-N Acrylonitrile Chemical compound C=CC#N NLHHRLWOUZZQLW-UHFFFAOYSA-N 0.000 description 1
- 244000251953 Agaricus brunnescens Species 0.000 description 1
- 235000001674 Agaricus brunnescens Nutrition 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- BLIMFWGRQKRCGT-YUMQZZPRSA-N Ala-Gly-Lys Chemical compound C[C@H](N)C(=O)NCC(=O)N[C@H](C(O)=O)CCCCN BLIMFWGRQKRCGT-YUMQZZPRSA-N 0.000 description 1
- 241000282979 Alces alces Species 0.000 description 1
- 101710199313 Alpha-L-arabinofuranosidase Proteins 0.000 description 1
- 244000303258 Annona diversifolia Species 0.000 description 1
- 235000002198 Annona diversifolia Nutrition 0.000 description 1
- 241000272517 Anseriformes Species 0.000 description 1
- 241000282815 Antilocapra americana Species 0.000 description 1
- 241000269350 Anura Species 0.000 description 1
- 241000726096 Aratinga Species 0.000 description 1
- 108010024957 Ascorbate Oxidase Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 241000228215 Aspergillus aculeatus Species 0.000 description 1
- 241001225321 Aspergillus fumigatus Species 0.000 description 1
- 235000002247 Aspergillus oryzae Nutrition 0.000 description 1
- 241000981365 Aspergillus sulphureus Species 0.000 description 1
- 241000134719 Aspergillus tamarii Species 0.000 description 1
- 241000972773 Aulopiformes Species 0.000 description 1
- 235000007558 Avena sp Nutrition 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 101150071434 BAR1 gene Proteins 0.000 description 1
- 241000193749 Bacillus coagulans Species 0.000 description 1
- 241000193422 Bacillus lentus Species 0.000 description 1
- 241000194103 Bacillus pumilus Species 0.000 description 1
- 101100162670 Bacillus subtilis (strain 168) amyE gene Proteins 0.000 description 1
- 241000276408 Bacillus subtilis subsp. subtilis str. 168 Species 0.000 description 1
- 241000193388 Bacillus thuringiensis Species 0.000 description 1
- 241001135228 Bacteroides ovatus Species 0.000 description 1
- 108091005658 Basic proteases Proteins 0.000 description 1
- 101710204694 Beta-xylosidase Proteins 0.000 description 1
- 241000283726 Bison Species 0.000 description 1
- 241001474374 Blennius Species 0.000 description 1
- 108010006654 Bleomycin Proteins 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 241001416153 Bos grunniens Species 0.000 description 1
- 241000283700 Boselaphus Species 0.000 description 1
- 241000282817 Bovidae Species 0.000 description 1
- 235000014698 Brassica juncea var multisecta Nutrition 0.000 description 1
- 240000002791 Brassica napus Species 0.000 description 1
- 235000006008 Brassica napus var napus Nutrition 0.000 description 1
- 235000006618 Brassica rapa subsp oleifera Nutrition 0.000 description 1
- 244000188595 Brassica sinapistrum Species 0.000 description 1
- 102220619184 Calcipressin-2_L66T_mutation Human genes 0.000 description 1
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 1
- 241000178957 Caldanaerobius polysaccharolyticus Species 0.000 description 1
- 241000282836 Camelus dromedarius Species 0.000 description 1
- 102220622512 Cancer-related nucleoside-triphosphatase_T62V_mutation Human genes 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 101710095524 Cellodextrinase Proteins 0.000 description 1
- 241000186320 Cellulomonas fimi Species 0.000 description 1
- 241001370641 Cellulosilyticum ruminicola Species 0.000 description 1
- 241000010977 Cellvibrio japonicus Species 0.000 description 1
- 235000013912 Ceratonia siliqua Nutrition 0.000 description 1
- 240000008886 Ceratonia siliqua Species 0.000 description 1
- 241000700114 Chinchillidae Species 0.000 description 1
- 229920002101 Chitin Polymers 0.000 description 1
- 229920001661 Chitosan Polymers 0.000 description 1
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
- 241001674013 Chrysosporium lucknowense Species 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 241000207199 Citrus Species 0.000 description 1
- 235000008733 Citrus aurantifolia Nutrition 0.000 description 1
- 235000005979 Citrus limon Nutrition 0.000 description 1
- 244000131522 Citrus pyriformis Species 0.000 description 1
- 241000193171 Clostridium butyricum Species 0.000 description 1
- 241000193169 Clostridium cellulovorans Species 0.000 description 1
- 241000186528 Clostridium tertium Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 229920002261 Corn starch Polymers 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 241000238424 Crustacea Species 0.000 description 1
- JPVYNHNXODAKFH-UHFFFAOYSA-N Cu2+ Chemical compound [Cu+2] JPVYNHNXODAKFH-UHFFFAOYSA-N 0.000 description 1
- 241000252867 Cupriavidus metallidurans Species 0.000 description 1
- 244000007835 Cyamopsis tetragonoloba Species 0.000 description 1
- 241000252233 Cyprinus carpio Species 0.000 description 1
- 102100025698 Cytosolic carboxypeptidase 4 Human genes 0.000 description 1
- 102000016559 DNA Primase Human genes 0.000 description 1
- 108010092681 DNA Primase Proteins 0.000 description 1
- 230000004568 DNA-binding Effects 0.000 description 1
- 241000238557 Decapoda Species 0.000 description 1
- 101710089042 Demethyl-4-deoxygadusol synthase Proteins 0.000 description 1
- 241000468577 Desulfomicrobium thermophilum Species 0.000 description 1
- 239000004375 Dextrin Substances 0.000 description 1
- 229920001353 Dextrin Polymers 0.000 description 1
- 241000588700 Dickeya chrysanthemi Species 0.000 description 1
- 101100434864 Drosophila melanogaster Amy-p gene Proteins 0.000 description 1
- 108010083608 Durazym Proteins 0.000 description 1
- 101100223032 Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) dapB gene Proteins 0.000 description 1
- 241000982936 Enterobacter cloacae subsp. dissolvens Species 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000588699 Erwinia sp. Species 0.000 description 1
- 241000588722 Escherichia Species 0.000 description 1
- 241001524679 Escherichia virus M13 Species 0.000 description 1
- VGGSQFUCUMXWEO-UHFFFAOYSA-N Ethene Chemical compound C=C VGGSQFUCUMXWEO-UHFFFAOYSA-N 0.000 description 1
- 239000005977 Ethylene Substances 0.000 description 1
- 108050001049 Extracellular proteins Proteins 0.000 description 1
- CWYNVVGOOAEACU-UHFFFAOYSA-N Fe2+ Chemical compound [Fe+2] CWYNVVGOOAEACU-UHFFFAOYSA-N 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 235000019733 Fish meal Nutrition 0.000 description 1
- 241000589564 Flavobacterium sp. Species 0.000 description 1
- 101150108358 GLAA gene Proteins 0.000 description 1
- 102000002464 Galactosidases Human genes 0.000 description 1
- 108010093031 Galactosidases Proteins 0.000 description 1
- IAJILQKETJEXLJ-UHFFFAOYSA-N Galacturonsaeure Natural products O=CC(O)C(O)C(O)C(O)C(O)=O IAJILQKETJEXLJ-UHFFFAOYSA-N 0.000 description 1
- 102100039556 Galectin-4 Human genes 0.000 description 1
- 241000626621 Geobacillus Species 0.000 description 1
- 239000005792 Geraniol Substances 0.000 description 1
- GLZPCOQZEFWAFX-YFHOEESVSA-N Geraniol Natural products CC(C)=CCC\C(C)=C/CO GLZPCOQZEFWAFX-YFHOEESVSA-N 0.000 description 1
- 241000699694 Gerbillinae Species 0.000 description 1
- 241000282816 Giraffa camelopardalis Species 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 108010068370 Glutens Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 1
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 1
- 235000017367 Guainella Nutrition 0.000 description 1
- 101150026303 HEX1 gene Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000608765 Homo sapiens Galectin-4 Proteins 0.000 description 1
- 241000223198 Humicola Species 0.000 description 1
- 241001480714 Humicola insolens Species 0.000 description 1
- 101001067705 Hypocrea jecorina (strain QM6a) Endoglucanase-7 Proteins 0.000 description 1
- 101100398376 Hypocrea jecorina pki1 gene Proteins 0.000 description 1
- 208000000785 Invasive Pulmonary Aspergillosis Diseases 0.000 description 1
- 108010044467 Isoenzymes Proteins 0.000 description 1
- 102100027612 Kallikrein-11 Human genes 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- 241000194036 Lactococcus Species 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 101710098556 Lipase A Proteins 0.000 description 1
- 101710098554 Lipase B Proteins 0.000 description 1
- 241000192502 Littorina brevicula Species 0.000 description 1
- 241000023320 Luma <angiosperm> Species 0.000 description 1
- 239000006137 Luria-Bertani broth Substances 0.000 description 1
- 235000007688 Lycopersicon esculentum Nutrition 0.000 description 1
- 101710099648 Lysosomal acid lipase/cholesteryl ester hydrolase Proteins 0.000 description 1
- 102100026001 Lysosomal acid lipase/cholesteryl ester hydrolase Human genes 0.000 description 1
- 102100033468 Lysozyme C Human genes 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- JLVVSXFLKOJNIY-UHFFFAOYSA-N Magnesium ion Chemical compound [Mg+2] JLVVSXFLKOJNIY-UHFFFAOYSA-N 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
- PWHULOQIROXLJO-UHFFFAOYSA-N Manganese Chemical compound [Mn] PWHULOQIROXLJO-UHFFFAOYSA-N 0.000 description 1
- 101710136501 Mannan endo-1,4-beta-mannosidase Proteins 0.000 description 1
- 101710089743 Mating factor alpha Proteins 0.000 description 1
- 235000019735 Meat-and-bone meal Nutrition 0.000 description 1
- GYCMBHHDWRMZGG-UHFFFAOYSA-N Methylacrylonitrile Chemical compound CC(=C)C#N GYCMBHHDWRMZGG-UHFFFAOYSA-N 0.000 description 1
- ZOKXTWBITQBERF-UHFFFAOYSA-N Molybdenum Chemical compound [Mo] ZOKXTWBITQBERF-UHFFFAOYSA-N 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- WHNWPMSKXPGLAX-UHFFFAOYSA-N N-Vinyl-2-pyrrolidone Chemical compound C=CN1CCCC1=O WHNWPMSKXPGLAX-UHFFFAOYSA-N 0.000 description 1
- 150000001204 N-oxides Chemical class 0.000 description 1
- 108091061960 Naked DNA Proteins 0.000 description 1
- 235000006508 Nelumbo nucifera Nutrition 0.000 description 1
- 240000002853 Nelumbo nucifera Species 0.000 description 1
- 235000006510 Nelumbo pentapetala Nutrition 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 244000038458 Nepenthes mirabilis Species 0.000 description 1
- VEQPNABPJHWNSG-UHFFFAOYSA-N Nickel(2+) Chemical compound [Ni+2] VEQPNABPJHWNSG-UHFFFAOYSA-N 0.000 description 1
- 239000006057 Non-nutritive feed additive Substances 0.000 description 1
- 108091005461 Nucleic proteins Proteins 0.000 description 1
- DKXNBNKWCZZMJT-UHFFFAOYSA-N O4-alpha-D-Mannopyranosyl-D-mannose Natural products O=CC(O)C(O)C(C(O)CO)OC1OC(CO)C(O)C(O)C1O DKXNBNKWCZZMJT-UHFFFAOYSA-N 0.000 description 1
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 1
- 102220558400 Olfactory receptor 9G1_T62I_mutation Human genes 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- CBENFWSGALASAD-UHFFFAOYSA-N Ozone Chemical compound [O-][O+]=O CBENFWSGALASAD-UHFFFAOYSA-N 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 241000611789 Paenibacillus curdlanolyticus Species 0.000 description 1
- 241000331098 Paenibacillus lactis Species 0.000 description 1
- 241000194109 Paenibacillus lautus Species 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108010044725 Pectate disaccharide-lyase Proteins 0.000 description 1
- 229920002230 Pectic acid Polymers 0.000 description 1
- 108010029182 Pectin lyase Proteins 0.000 description 1
- 241000588701 Pectobacterium carotovorum Species 0.000 description 1
- 244000271379 Penicillium camembertii Species 0.000 description 1
- 235000002245 Penicillium camembertii Nutrition 0.000 description 1
- 102000010292 Peptide Elongation Factor 1 Human genes 0.000 description 1
- 108010077524 Peptide Elongation Factor 1 Proteins 0.000 description 1
- 241000222393 Phanerochaete chrysosporium Species 0.000 description 1
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical class OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 1
- 235000012541 Phytelephas macrocarpa Nutrition 0.000 description 1
- 244000208789 Phytelephas macrocarpa Species 0.000 description 1
- 101000957795 Piromyces sp Mannan endo-1,4-beta-mannosidase B Proteins 0.000 description 1
- 241000193632 Piromyces sp. Species 0.000 description 1
- 108010064851 Plant Proteins Proteins 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 241000605860 Prevotella ruminicola Species 0.000 description 1
- 241000588769 Proteus <enterobacteria> Species 0.000 description 1
- 241000826415 Psammobates geometricus Species 0.000 description 1
- 241000589755 Pseudomonas mendocina Species 0.000 description 1
- 241000287530 Psittaciformes Species 0.000 description 1
- 101710148480 Putative beta-xylosidase Proteins 0.000 description 1
- 241000232299 Ralstonia Species 0.000 description 1
- 102220636493 Ras-related protein Rab-27B_Q78L_mutation Human genes 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- 241000393560 Rhizobium marinum Species 0.000 description 1
- 101000968489 Rhizomucor miehei Lipase Proteins 0.000 description 1
- 241000235527 Rhizopus Species 0.000 description 1
- 244000016016 Rubus hypargyrus var. niveus Species 0.000 description 1
- 241000193448 Ruminiclostridium thermocellum Species 0.000 description 1
- KJTLSVCANCCWHF-UHFFFAOYSA-N Ruthenium Chemical compound [Ru] KJTLSVCANCCWHF-UHFFFAOYSA-N 0.000 description 1
- 101150028158 STE13 gene Proteins 0.000 description 1
- 101100010928 Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) tuf gene Proteins 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 240000000111 Saccharum officinarum Species 0.000 description 1
- 235000007201 Saccharum officinarum Nutrition 0.000 description 1
- 241000277331 Salmonidae Species 0.000 description 1
- 241000235346 Schizosaccharomyces Species 0.000 description 1
- 241000209056 Secale Species 0.000 description 1
- 235000007238 Secale cereale Nutrition 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 241000287231 Serinus Species 0.000 description 1
- 235000003434 Sesamum indicum Nutrition 0.000 description 1
- 244000040738 Sesamum orientale Species 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical group [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 235000011684 Sorghum saccharatum Nutrition 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 241000191965 Staphylococcus carnosus Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 244000057717 Streptococcus lactis Species 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 241001468239 Streptomyces murinus Species 0.000 description 1
- KDYFGRWQOYBRFD-UHFFFAOYSA-N Succinic acid Natural products OC(=O)CCC(O)=O KDYFGRWQOYBRFD-UHFFFAOYSA-N 0.000 description 1
- 102000017952 Sugar transport proteins Human genes 0.000 description 1
- 108050007025 Sugar transport proteins Proteins 0.000 description 1
- 241000216203 Sulfolobus thuringiensis Species 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-N Sulfurous acid Chemical compound OS(O)=O LSNNMFCWUKXFEE-UHFFFAOYSA-N 0.000 description 1
- 101150074253 TEF1 gene Proteins 0.000 description 1
- WPMWEFXCIYCJSA-UHFFFAOYSA-N Tetraethylene glycol monododecyl ether Chemical compound CCCCCCCCCCCCOCCOCCOCCOCCO WPMWEFXCIYCJSA-UHFFFAOYSA-N 0.000 description 1
- 241000204664 Thermotoga neapolitana Species 0.000 description 1
- 102100036407 Thioredoxin Human genes 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 241000276707 Tilapia Species 0.000 description 1
- 235000011941 Tilia x europaea Nutrition 0.000 description 1
- RTAQQCXQSZGOHL-UHFFFAOYSA-N Titanium Chemical compound [Ti] RTAQQCXQSZGOHL-UHFFFAOYSA-N 0.000 description 1
- 102000003929 Transaminases Human genes 0.000 description 1
- 108090000340 Transaminases Proteins 0.000 description 1
- 241000223261 Trichoderma viride Species 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 101710152431 Trypsin-like protease Proteins 0.000 description 1
- LUEWUZLMQUOBSB-UHFFFAOYSA-N UNPD55895 Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(OC3C(OC(O)C(O)C3O)CO)C(O)C2O)CO)C(O)C1O LUEWUZLMQUOBSB-UHFFFAOYSA-N 0.000 description 1
- 101150013568 US16 gene Proteins 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 241000607598 Vibrio Species 0.000 description 1
- 235000010749 Vicia faba Nutrition 0.000 description 1
- 240000006677 Vicia faba Species 0.000 description 1
- 235000002098 Vicia faba var. major Nutrition 0.000 description 1
- 241001416177 Vicugna pacos Species 0.000 description 1
- 235000009754 Vitis X bourquina Nutrition 0.000 description 1
- 235000012333 Vitis X labruscana Nutrition 0.000 description 1
- 235000014787 Vitis vinifera Nutrition 0.000 description 1
- 240000006365 Vitis vinifera Species 0.000 description 1
- 102000007544 Whey Proteins Human genes 0.000 description 1
- 108010046377 Whey Proteins Proteins 0.000 description 1
- 101710158370 Xylan 1,4-beta-xylosidase Proteins 0.000 description 1
- 229920002000 Xyloglucan Polymers 0.000 description 1
- 241000235015 Yarrowia lipolytica Species 0.000 description 1
- 241000193453 [Clostridium] cellulolyticum Species 0.000 description 1
- KRPJTBJJOWPSSN-UHFFFAOYSA-N [Sc+2] Chemical compound [Sc+2] KRPJTBJJOWPSSN-UHFFFAOYSA-N 0.000 description 1
- 125000002777 acetyl group Chemical group [H]C([H])([H])C(*)=O 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 102000045404 acyltransferase activity proteins Human genes 0.000 description 1
- 108700014220 acyltransferase activity proteins Proteins 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 238000005054 agglomeration Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 235000015107 ale Nutrition 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- 229910000288 alkali metal carbonate Inorganic materials 0.000 description 1
- 150000008041 alkali metal carbonates Chemical class 0.000 description 1
- 229910052910 alkali metal silicate Inorganic materials 0.000 description 1
- 239000012670 alkaline solution Substances 0.000 description 1
- 150000008051 alkyl sulfates Chemical class 0.000 description 1
- GUUHFMWKWLOQMM-NTCAYCPXSA-N alpha-hexylcinnamaldehyde Chemical class CCCCCC\C(C=O)=C/C1=CC=CC=C1 GUUHFMWKWLOQMM-NTCAYCPXSA-N 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
- 229910000323 aluminium silicate Inorganic materials 0.000 description 1
- REDXJYDRNCIFBQ-UHFFFAOYSA-N aluminium(3+) Chemical compound [Al+3] REDXJYDRNCIFBQ-UHFFFAOYSA-N 0.000 description 1
- HPTYUNKZVDYXLP-UHFFFAOYSA-N aluminum;trihydroxy(trihydroxysilyloxy)silane;hydrate Chemical compound O.[Al].[Al].O[Si](O)(O)O[Si](O)(O)O HPTYUNKZVDYXLP-UHFFFAOYSA-N 0.000 description 1
- 239000002280 amphoteric surfactant Substances 0.000 description 1
- 101150069712 amyA gene Proteins 0.000 description 1
- 230000003625 amylolytic effect Effects 0.000 description 1
- 150000001449 anionic compounds Chemical class 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000003466 anti-cipated effect Effects 0.000 description 1
- 230000003373 anti-fouling effect Effects 0.000 description 1
- 230000001153 anti-wrinkle effect Effects 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 239000012131 assay buffer Substances 0.000 description 1
- 229960000892 attapulgite Drugs 0.000 description 1
- 239000003899 bactericide agent Substances 0.000 description 1
- 235000015173 baked goods and baking mixes Nutrition 0.000 description 1
- XDFCIPNJCBUZJN-UHFFFAOYSA-N barium(2+) Chemical compound [Ba+2] XDFCIPNJCBUZJN-UHFFFAOYSA-N 0.000 description 1
- 239000000440 bentonite Substances 0.000 description 1
- 229910000278 bentonite Inorganic materials 0.000 description 1
- SVPXDRXYRYOSEX-UHFFFAOYSA-N bentoquatam Chemical compound O.O=[Si]=O.O=[Al]O[Al]=O SVPXDRXYRYOSEX-UHFFFAOYSA-N 0.000 description 1
- DMSMPAJRVJJAGA-UHFFFAOYSA-N benzo[d]isothiazol-3-one Chemical compound C1=CC=C2C(=O)NSC2=C1 DMSMPAJRVJJAGA-UHFFFAOYSA-N 0.000 description 1
- LUEWUZLMQUOBSB-MHJOMNRISA-N beta-D-Manp-(1->4)-beta-D-Manp-(1->4)-beta-D-Manp-(1->4)-D-Manp 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](O[C@@H](O[C@@H]3[C@H](OC(O)[C@@H](O)[C@H]3O)CO)[C@@H](O)[C@H]2O)CO)[C@@H](O)[C@H]1O LUEWUZLMQUOBSB-MHJOMNRISA-N 0.000 description 1
- WQZGKKKJIJFFOK-RWOPYEJCSA-N beta-D-mannose Chemical compound OC[C@H]1O[C@@H](O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-RWOPYEJCSA-N 0.000 description 1
- 108010047754 beta-Glucosidase Proteins 0.000 description 1
- 102000006995 beta-Glucosidase Human genes 0.000 description 1
- JGQFVRIQXUFPAH-UHFFFAOYSA-N beta-citronellol Natural products OCCC(C)CCCC(C)=C JGQFVRIQXUFPAH-UHFFFAOYSA-N 0.000 description 1
- AFYNADDZULBEJA-UHFFFAOYSA-N bicinchoninic acid Chemical compound C1=CC=CC2=NC(C=3C=C(C4=CC=CC=C4N=3)C(=O)O)=CC(C(O)=O)=C21 AFYNADDZULBEJA-UHFFFAOYSA-N 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 235000015895 biscuits Nutrition 0.000 description 1
- 229960001561 bleomycin Drugs 0.000 description 1
- OYVAGSVQBOHSSS-UAPAGMARSA-O bleomycin A2 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC=C(N=1)C=1SC=C(N=1)C(=O)NCCC[S+](C)C)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C OYVAGSVQBOHSSS-UAPAGMARSA-O 0.000 description 1
- 235000020008 bock Nutrition 0.000 description 1
- 235000015496 breakfast cereal Nutrition 0.000 description 1
- 238000005282 brightening Methods 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- KDYFGRWQOYBRFD-NUQCWPJISA-N butanedioic acid Chemical compound O[14C](=O)CC[14C](O)=O KDYFGRWQOYBRFD-NUQCWPJISA-N 0.000 description 1
- 102220417887 c.178T>G Human genes 0.000 description 1
- 229940104939 c12-15 pareth-7 Drugs 0.000 description 1
- 159000000007 calcium salts Chemical class 0.000 description 1
- 238000004422 calculation algorithm Methods 0.000 description 1
- 238000004364 calculation method Methods 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 102000023852 carbohydrate binding proteins Human genes 0.000 description 1
- 108091008400 carbohydrate binding proteins Proteins 0.000 description 1
- 150000004649 carbonic acid derivatives Chemical class 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 108020001778 catalytic domains Proteins 0.000 description 1
- 241001233037 catfish Species 0.000 description 1
- 150000001767 cationic compounds Chemical class 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 229940106135 cellulose Drugs 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 102000021178 chitin binding proteins Human genes 0.000 description 1
- 108091011157 chitin binding proteins Proteins 0.000 description 1
- 150000003841 chloride salts Chemical class 0.000 description 1
- 150000001805 chlorine compounds Chemical class 0.000 description 1
- 235000020140 chocolate milk drink Nutrition 0.000 description 1
- 235000011967 chocolate pudding Nutrition 0.000 description 1
- 229910052804 chromium Inorganic materials 0.000 description 1
- 239000011651 chromium Substances 0.000 description 1
- 235000000484 citronellol Nutrition 0.000 description 1
- 235000020971 citrus fruits Nutrition 0.000 description 1
- 239000004927 clay Chemical class 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- XLJKHNWPARRRJB-UHFFFAOYSA-N cobalt(2+) Chemical compound [Co+2] XLJKHNWPARRRJB-UHFFFAOYSA-N 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000008139 complexing agent Substances 0.000 description 1
- 235000009508 confectionery Nutrition 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 235000014510 cooky Nutrition 0.000 description 1
- 239000008120 corn starch Substances 0.000 description 1
- 239000002537 cosmetic Substances 0.000 description 1
- 235000012343 cottonseed oil Nutrition 0.000 description 1
- 235000012495 crackers Nutrition 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 238000013480 data collection Methods 0.000 description 1
- 230000006196 deacetylation Effects 0.000 description 1
- 238000003381 deacetylation reaction Methods 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000000432 density-gradient centrifugation Methods 0.000 description 1
- 239000000645 desinfectant Substances 0.000 description 1
- 235000011850 desserts Nutrition 0.000 description 1
- 235000019425 dextrin Nutrition 0.000 description 1
- GUJOJGAPFQRJSV-UHFFFAOYSA-N dialuminum;dioxosilane;oxygen(2-);hydrate Chemical compound O.[O-2].[O-2].[O-2].[Al+3].[Al+3].O=[Si]=O.O=[Si]=O.O=[Si]=O.O=[Si]=O GUJOJGAPFQRJSV-UHFFFAOYSA-N 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 150000002009 diols Chemical class 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- GVGUFUZHNYFZLC-UHFFFAOYSA-N dodecyl benzenesulfonate;sodium Chemical compound [Na].CCCCCCCCCCCCOS(=O)(=O)C1=CC=CC=C1 GVGUFUZHNYFZLC-UHFFFAOYSA-N 0.000 description 1
- 238000005553 drilling Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- NFDRPXJGHKJRLJ-UHFFFAOYSA-N edtmp Chemical compound OP(O)(=O)CN(CP(O)(O)=O)CCN(CP(O)(O)=O)CP(O)(O)=O NFDRPXJGHKJRLJ-UHFFFAOYSA-N 0.000 description 1
- 229920001971 elastomer Polymers 0.000 description 1
- 239000000806 elastomer Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 239000008393 encapsulating agent Substances 0.000 description 1
- 238000005265 energy consumption Methods 0.000 description 1
- 230000007515 enzymatic degradation Effects 0.000 description 1
- 239000003248 enzyme activator Substances 0.000 description 1
- RTZKZFJDLAIYFH-UHFFFAOYSA-N ether Substances CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 1
- SFNALCNOMXIBKG-UHFFFAOYSA-N ethylene glycol monododecyl ether Chemical compound CCCCCCCCCCCCOCCO SFNALCNOMXIBKG-UHFFFAOYSA-N 0.000 description 1
- 108010092086 exo-poly-alpha-galacturonosidase Proteins 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 235000012438 extruded product Nutrition 0.000 description 1
- 230000006126 farnesylation Effects 0.000 description 1
- 235000019387 fatty acid methyl ester Nutrition 0.000 description 1
- 239000006052 feed supplement Substances 0.000 description 1
- 239000012065 filter cake Substances 0.000 description 1
- 239000004467 fishmeal Substances 0.000 description 1
- 235000004426 flaxseed Nutrition 0.000 description 1
- 238000005187 foaming Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 239000000417 fungicide Substances 0.000 description 1
- 108010066429 galactomannanase Proteins 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 229940113087 geraniol Drugs 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 235000021312 gluten Nutrition 0.000 description 1
- 230000002414 glycolytic effect Effects 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 244000005709 gut microbiome Species 0.000 description 1
- 229910052621 halloysite Inorganic materials 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 150000004687 hexahydrates Chemical class 0.000 description 1
- PMYUVOOOQDGQNW-UHFFFAOYSA-N hexasodium;trioxido(trioxidosilyloxy)silane Chemical compound [Na+].[Na+].[Na+].[Na+].[Na+].[Na+].[O-][Si]([O-])([O-])O[Si]([O-])([O-])[O-] PMYUVOOOQDGQNW-UHFFFAOYSA-N 0.000 description 1
- 238000012203 high throughput assay Methods 0.000 description 1
- 238000012615 high-resolution technique Methods 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 125000004435 hydrogen atom Chemical class [H]* 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 229910052900 illite Inorganic materials 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 239000003262 industrial enzyme Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 229960004903 invert sugar Drugs 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 239000000797 iron chelating agent Substances 0.000 description 1
- 229940075525 iron chelating agent Drugs 0.000 description 1
- 125000000959 isobutyl group Chemical group [H]C([H])([H])C([H])(C([H])([H])[H])C([H])([H])* 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 229910052622 kaolinite Inorganic materials 0.000 description 1
- CYPPCCJJKNISFK-UHFFFAOYSA-J kaolinite Chemical compound [OH-].[OH-].[OH-].[OH-].[Al+3].[Al+3].[O-][Si](=O)O[Si]([O-])=O CYPPCCJJKNISFK-UHFFFAOYSA-J 0.000 description 1
- 235000008960 ketchup Nutrition 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 239000002655 kraft paper Substances 0.000 description 1
- 235000015095 lager Nutrition 0.000 description 1
- 210000002429 large intestine Anatomy 0.000 description 1
- 238000004900 laundering Methods 0.000 description 1
- LFEUVBZXUFMACD-UHFFFAOYSA-H lead(2+);trioxido(oxo)-$l^{5}-arsane Chemical compound [Pb+2].[Pb+2].[Pb+2].[O-][As]([O-])([O-])=O.[O-][As]([O-])([O-])=O LFEUVBZXUFMACD-UHFFFAOYSA-H 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 235000021440 light beer Nutrition 0.000 description 1
- 229920005610 lignin Polymers 0.000 description 1
- 239000004571 lime Substances 0.000 description 1
- 235000001510 limonene Nutrition 0.000 description 1
- 229940087305 limonene Drugs 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 238000001638 lipofection Methods 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000012263 liquid product Substances 0.000 description 1
- XIXADJRWDQXREU-UHFFFAOYSA-M lithium acetate Chemical compound [Li+].CC([O-])=O XIXADJRWDQXREU-UHFFFAOYSA-M 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 239000006210 lotion Substances 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 229910001425 magnesium ion Inorganic materials 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- FPYJFEHAWHCUMM-UHFFFAOYSA-N maleic anhydride Chemical compound O=C1OC(=O)C=C1 FPYJFEHAWHCUMM-UHFFFAOYSA-N 0.000 description 1
- 229910052748 manganese Inorganic materials 0.000 description 1
- 239000011572 manganese Substances 0.000 description 1
- 150000002697 manganese compounds Chemical class 0.000 description 1
- BQKYBHBRPYDELH-UHFFFAOYSA-N manganese;triazonane Chemical compound [Mn].C1CCCNNNCC1 BQKYBHBRPYDELH-UHFFFAOYSA-N 0.000 description 1
- 150000008146 mannosides Chemical class 0.000 description 1
- 238000005360 mashing Methods 0.000 description 1
- 230000000873 masking effect Effects 0.000 description 1
- 239000008268 mayonnaise Substances 0.000 description 1
- 235000010746 mayonnaise Nutrition 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000002844 melting Methods 0.000 description 1
- 230000008018 melting Effects 0.000 description 1
- 230000008384 membrane barrier Effects 0.000 description 1
- 108010003855 mesentericopeptidase Proteins 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- HNYWOTATUXXCHR-UHFFFAOYSA-N methyl 2-methyl-2-phenylhexanoate Chemical compound CCCCC(C)(C(=O)OC)C1=CC=CC=C1 HNYWOTATUXXCHR-UHFFFAOYSA-N 0.000 description 1
- OSWPMRLSEDHDFF-UHFFFAOYSA-N methyl salicylate Chemical compound COC(=O)C1=CC=CC=C1O OSWPMRLSEDHDFF-UHFFFAOYSA-N 0.000 description 1
- XJRBAMWJDBPFIM-UHFFFAOYSA-N methyl vinyl ether Chemical compound COC=C XJRBAMWJDBPFIM-UHFFFAOYSA-N 0.000 description 1
- 108010009355 microbial metalloproteinases Proteins 0.000 description 1
- 235000020124 milk-based beverage Nutrition 0.000 description 1
- 235000019713 millet Nutrition 0.000 description 1
- 229910052750 molybdenum Inorganic materials 0.000 description 1
- 239000011733 molybdenum Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229910052901 montmorillonite Inorganic materials 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 150000002825 nitriles Chemical class 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- VGIBGUSAECPPNB-UHFFFAOYSA-L nonaaluminum;magnesium;tripotassium;1,3-dioxido-2,4,5-trioxa-1,3-disilabicyclo[1.1.1]pentane;iron(2+);oxygen(2-);fluoride;hydroxide Chemical compound [OH-].[O-2].[O-2].[O-2].[O-2].[O-2].[F-].[Mg+2].[Al+3].[Al+3].[Al+3].[Al+3].[Al+3].[Al+3].[Al+3].[Al+3].[Al+3].[K+].[K+].[K+].[Fe+2].O1[Si]2([O-])O[Si]1([O-])O2.O1[Si]2([O-])O[Si]1([O-])O2.O1[Si]2([O-])O[Si]1([O-])O2.O1[Si]2([O-])O[Si]1([O-])O2.O1[Si]2([O-])O[Si]1([O-])O2.O1[Si]2([O-])O[Si]1([O-])O2.O1[Si]2([O-])O[Si]1([O-])O2 VGIBGUSAECPPNB-UHFFFAOYSA-L 0.000 description 1
- 229920000847 nonoxynol Polymers 0.000 description 1
- 239000004745 nonwoven fabric Substances 0.000 description 1
- 235000003170 nutritional factors Nutrition 0.000 description 1
- 235000014571 nuts Nutrition 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 235000014593 oils and fats Nutrition 0.000 description 1
- 239000011368 organic material Substances 0.000 description 1
- 150000004967 organic peroxy acids Chemical class 0.000 description 1
- 235000016046 other dairy product Nutrition 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 235000020007 pale lager Nutrition 0.000 description 1
- 229910052625 palygorskite Inorganic materials 0.000 description 1
- 239000012188 paraffin wax Substances 0.000 description 1
- 235000019809 paraffin wax Nutrition 0.000 description 1
- 235000014594 pastries Nutrition 0.000 description 1
- LCLHHZYHLXDRQG-ZNKJPWOQSA-N pectic acid Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)O[C@H](C(O)=O)[C@@H]1OC1[C@H](O)[C@@H](O)[C@@H](OC2[C@@H]([C@@H](O)[C@@H](O)[C@H](O2)C(O)=O)O)[C@@H](C(O)=O)O1 LCLHHZYHLXDRQG-ZNKJPWOQSA-N 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 239000004466 pelleted feed Substances 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 230000008823 permeabilization Effects 0.000 description 1
- 238000005502 peroxidation Methods 0.000 description 1
- 150000002978 peroxides Chemical class 0.000 description 1
- XCRBXWCUXJNEFX-UHFFFAOYSA-N peroxybenzoic acid Chemical class OOC(=O)C1=CC=CC=C1 XCRBXWCUXJNEFX-UHFFFAOYSA-N 0.000 description 1
- 125000005342 perphosphate group Chemical group 0.000 description 1
- 235000019271 petrolatum Nutrition 0.000 description 1
- 101150079312 pgk1 gene Proteins 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 229910052615 phyllosilicate Inorganic materials 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 235000021118 plant-derived protein Nutrition 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920002006 poly(N-vinylimidazole) polymer Polymers 0.000 description 1
- 229920003214 poly(methacrylonitrile) Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920002239 polyacrylonitrile Polymers 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920001515 polyalkylene glycol Polymers 0.000 description 1
- 229920000768 polyamine Polymers 0.000 description 1
- 239000010318 polygalacturonic acid Substances 0.000 description 1
- 229920001444 polymaleic acid Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 229920000056 polyoxyethylene ether Polymers 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920001451 polypropylene glycol Polymers 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 235000019422 polyvinyl alcohol Nutrition 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 235000020004 porter Nutrition 0.000 description 1
- 230000029279 positive regulation of transcription, DNA-dependent Effects 0.000 description 1
- 238000012805 post-processing Methods 0.000 description 1
- 229910000160 potassium phosphate Inorganic materials 0.000 description 1
- 235000011009 potassium phosphates Nutrition 0.000 description 1
- 235000012015 potatoes Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000013823 prenylation Effects 0.000 description 1
- 150000003138 primary alcohols Chemical class 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 239000006041 probiotic Substances 0.000 description 1
- 230000000529 probiotic effect Effects 0.000 description 1
- 235000018291 probiotics Nutrition 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- BDERNNFJNOPAEC-UHFFFAOYSA-N propan-1-ol Chemical compound CCCO BDERNNFJNOPAEC-UHFFFAOYSA-N 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- ROSDSFDQCJNGOL-UHFFFAOYSA-N protonated dimethyl amine Natural products CNC ROSDSFDQCJNGOL-UHFFFAOYSA-N 0.000 description 1
- 238000004537 pulping Methods 0.000 description 1
- 235000021251 pulses Nutrition 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 235000021067 refined food Nutrition 0.000 description 1
- 230000003362 replicative effect Effects 0.000 description 1
- 239000013557 residual solvent Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000000979 retarding effect Effects 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 239000011435 rock Substances 0.000 description 1
- 102200134872 rs119489103 Human genes 0.000 description 1
- 102220249201 rs1553260740 Human genes 0.000 description 1
- 102220267610 rs1555198862 Human genes 0.000 description 1
- 102220011217 rs281865122 Human genes 0.000 description 1
- 102220001969 rs696217 Human genes 0.000 description 1
- 102220081134 rs767317022 Human genes 0.000 description 1
- 102220092092 rs876657864 Human genes 0.000 description 1
- 229910052707 ruthenium Inorganic materials 0.000 description 1
- 235000019515 salmon Nutrition 0.000 description 1
- 235000015067 sauces Nutrition 0.000 description 1
- 238000005201 scrubbing Methods 0.000 description 1
- 150000003333 secondary alcohols Chemical class 0.000 description 1
- 239000002453 shampoo Substances 0.000 description 1
- 235000020374 simple syrup Nutrition 0.000 description 1
- RYMZZMVNJRMUDD-HGQWONQESA-N simvastatin Chemical compound C([C@H]1[C@@H](C)C=CC2=C[C@H](C)C[C@@H]([C@H]12)OC(=O)C(C)(C)CC)C[C@@H]1C[C@@H](O)CC(=O)O1 RYMZZMVNJRMUDD-HGQWONQESA-N 0.000 description 1
- 238000004513 sizing Methods 0.000 description 1
- 239000002002 slurry Substances 0.000 description 1
- 150000003385 sodium Chemical class 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 229940080264 sodium dodecylbenzenesulfonate Drugs 0.000 description 1
- 235000019795 sodium metasilicate Nutrition 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 1
- 229910052911 sodium silicate Inorganic materials 0.000 description 1
- 235000019351 sodium silicates Nutrition 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- MWNQXXOSWHCCOZ-UHFFFAOYSA-L sodium;oxido carbonate Chemical compound [Na+].[O-]OC([O-])=O MWNQXXOSWHCCOZ-UHFFFAOYSA-L 0.000 description 1
- 235000014347 soups Nutrition 0.000 description 1
- 239000004458 spent grain Substances 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 235000011044 succinic acid Nutrition 0.000 description 1
- 150000003871 sulfonates Chemical class 0.000 description 1
- 238000006277 sulfonation reaction Methods 0.000 description 1
- 230000037072 sun protection Effects 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 239000000454 talc Chemical class 0.000 description 1
- 229910052623 talc Chemical class 0.000 description 1
- 238000005494 tarnishing Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229920001169 thermoplastic Polymers 0.000 description 1
- 239000004416 thermosoftening plastic Substances 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 108060008226 thioredoxin Proteins 0.000 description 1
- 229940094937 thioredoxin Drugs 0.000 description 1
- IUTCEZPPWBHGIX-UHFFFAOYSA-N tin(2+) Chemical compound [Sn+2] IUTCEZPPWBHGIX-UHFFFAOYSA-N 0.000 description 1
- 229910052719 titanium Inorganic materials 0.000 description 1
- 239000010936 titanium Substances 0.000 description 1
- 239000000606 toothpaste Substances 0.000 description 1
- 229940034610 toothpaste Drugs 0.000 description 1
- 235000012184 tortilla Nutrition 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- ILJSQTXMGCGYMG-UHFFFAOYSA-N triacetic acid Chemical compound CC(=O)CC(=O)CC(O)=O ILJSQTXMGCGYMG-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- WFKWXMTUELFFGS-UHFFFAOYSA-N tungsten Chemical compound [W] WFKWXMTUELFFGS-UHFFFAOYSA-N 0.000 description 1
- 239000010937 tungsten Substances 0.000 description 1
- 108010087967 type I signal peptidase Proteins 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- LEONUFNNVUYDNQ-UHFFFAOYSA-N vanadium atom Chemical compound [V] LEONUFNNVUYDNQ-UHFFFAOYSA-N 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000012800 visualization Methods 0.000 description 1
- 235000013522 vodka Nutrition 0.000 description 1
- 235000012431 wafers Nutrition 0.000 description 1
- 235000012773 waffles Nutrition 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 229940100445 wheat starch Drugs 0.000 description 1
- 235000011845 white flour Nutrition 0.000 description 1
- 230000002087 whitening effect Effects 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
- 239000002676 xenobiotic agent Substances 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- 235000013618 yogurt Nutrition 0.000 description 1
- 239000010457 zeolite Substances 0.000 description 1
- 239000004711 α-olefin Substances 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
- 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
- C12N9/2488—Mannanases
- C12N9/2494—Mannan endo-1,4-beta-mannosidase (3.2.1.78), i.e. endo-beta-mannanase
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K20/00—Accessory food factors for animal feeding-stuffs
- A23K20/10—Organic substances
- A23K20/189—Enzymes
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23K—FODDER
- A23K50/00—Feeding-stuffs specially adapted for particular animals
- A23K50/40—Feeding-stuffs specially adapted for particular animals for carnivorous animals, e.g. cats or dogs
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23L—FOODS, FOODSTUFFS, OR NON-ALCOHOLIC BEVERAGES, NOT COVERED BY SUBCLASSES A21D OR A23B-A23J; THEIR PREPARATION OR TREATMENT, e.g. COOKING, MODIFICATION OF NUTRITIVE QUALITIES, PHYSICAL TREATMENT; PRESERVATION OF FOODS OR FOODSTUFFS, IN GENERAL
- A23L33/00—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof
- A23L33/10—Modifying nutritive qualities of foods; Dietetic products; Preparation or treatment thereof using additives
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38636—Preparations containing enzymes, e.g. protease or amylase containing enzymes other than protease, amylase, lipase, cellulase, oxidase or reductase
-
- 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
- C12N9/2488—Mannanases
-
- 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)
- C12Y302/01078—Mannan endo-1,4-beta-mannosidase (3.2.1.78), i.e. endo-beta-mannanase
-
- A—HUMAN NECESSITIES
- A23—FOODS OR FOODSTUFFS; TREATMENT THEREOF, NOT COVERED BY OTHER CLASSES
- A23V—INDEXING SCHEME RELATING TO FOODS, FOODSTUFFS OR NON-ALCOHOLIC BEVERAGES AND LACTIC OR PROPIONIC ACID BACTERIA USED IN FOODSTUFFS OR FOOD PREPARATION
- A23V2002/00—Food compositions, function of food ingredients or processes for food or foodstuffs
Description
本出願は、2015年11月5日出願の米国仮特許出願第62/251516号明細書、及び2016年1月13日出願の米国仮特許出願第62/278383号明細書の優先権の利益に関し、且つこれを主張する。これらの出願は双方とも、それらの全体が参照によって本明細書に組み込まれる。
ASCIIテキストファイル(名前:NB40831WOPCT_ST25;サイズ:59.3KB;作成日:2016年11月2日)として本出願と共に電子的に提出された配列表の内容は、本出願の一部を形成し、そしてその全体が参照によって本明細書に組み込まれる。
アッセイ
以下に記載する実施例に用いる以下のアッセイは、標準的なアッセイである。時折、特定のプロトコルが、これらの標準的なアッセイからの逸脱を必要とする。そのような場合、以下の標準的なアッセイプロトコルからの逸脱を、実施例において同定する。
酵素の性能指数(PI)は、変異体の性能(測定値)を親酵素(理論値又は測定値)と、同じタンパク質濃度にて比較している。親酵素の洗浄性能についての理論値を、親酵素の標準曲線のLangmuirフィットから抽出したパラメータを用いて算出することができる。1を超えるPI(PI>1)は、特定の親、例えばPspMan4(配列番号2)又はBspMan5(配列番号16)と比較して、変異体による性能の向上を示す一方、1のPI(PI=1)は、特定の親と同じ性能で実行する変異体を同定し、1未満のPI(PI<1)は、特定の親よりも悪い性能で実行する変異体を同定する。
タンパク質濃度判定を、積分ピーク面積を測定する高速液体クロマトグラフィ(HPLC)法を用いて実行して、96ウェルマイクロタイタープレート(MTP)中で増殖させた培養液由来の上澄み中でのタンパク質の発現レベルを判定した。サンプルを、濾過した培養液の上澄みから得て、25mMトリス-HClバッファ、pH7.5中の4倍希釈液として調製した。逆相HPLCを、Poroshell 300SB-C8カラム(2.1×75mm)を備えたAgilent 1200 Series HPLC系で、0.1%TFAをそれぞれ補った水及びアセトニトリルの溶媒で構成した勾配溶離を用いて実行した。サンプルを、50℃にて2mL/分の流量で溶出した。タンパク質を、220nmでの吸光度を測定することによって検出して、ピークを、ChemStationソフトウェア(Agilent Technologies)を用いて積分した。サンプルのタンパク質濃度を、精製した親タンパク質(例えば、PspMan4(配列番号2)又はBspMan5(配列番号16))の標準曲線に基づいて判定した。
後に続く実施例において記載するマンナナーゼ変異体のマンナナーゼ活性を、溶液中ローカストビーンガム(LBG)ガラクトマンナン(Sigma G0753)(おおよそ0.3%(w/v)のLBG基質)の加水分解を測定することによって試験した。用いた試薬溶液は、50mMトリス-HClバッファ、pH7.5(基質希釈バッファ)、及び50mM MOPSバッファ、pH7.2、0.005%TWEEN(登録商標)-80含有(酵素希釈バッファ)であった。作用基質溶液を調製するために、LBG粉末(製品No.G0753,Sigma-Aldrich,St.Louis,MO)を、50mMトリスHClバッファ、pH7.5の加熱溶液中に撹拌下で溶解させた。室温に冷却して直ぐに、溶液を遠心分離して、澄明な上澄みを基質溶液として用いた。
後に続く実施例において記載するマンナナーゼ変異体の安定性を、50mM MOPSバッファ、pH7.2、0.005%TWEEN(登録商標)-80中の57℃でのストレス条件下で、高温での5分間のインキュベーション後にサンプルの残留活性を測定することによって試験した。初期の(ストレスのない)活性を測定するために、先の節「マンナナーゼ活性アッセイ」に記載したアッセイを用いて、酵素サンプルを、50mM MOPSバッファ、pH7.2、0.005%TWEEN(登録商標)-80中に希釈して、直ちに、LBGに対する活性についてアッセイした。ストレスを受けた活性を測定するために、先の節「マンナナーゼ活性アッセイ」に記載したように、50mM MOPSバッファ、pH7.2、0.005%TWEEN(登録商標)-80中に希釈した酵素サンプルを、シールしたPCRプレート内で、サーモサイクラー(Tetrad2 Peltier Thermal Cycler,Bio-Rad Laboratories,Hercules,CA)において57℃にて5分間インキュベートしてから、活性についてアッセイした。
先に記載したように、ストレスを受けた活性の値及びストレスのない活性の値を、LBG基質の加水分解によって一旦測定して、ストレスを受けた活性の、ストレスのない活性に対する比率をとって、100を乗じることによって、%残留活性を算出した。変異体の残留活性を親の残留活性で割ることによって、安定性PI値を得た。
変異体を、LBGミクロスワッチ(CFT C-S-73,Center for Testmaterials,Vlaardingen,The Netherlands)に対する洗浄性能について、親の性能と比較して試験した。
」に記載した、親の標準曲線について測定した値のLangmuirフィットから抽出したパラメータを用いて、関連タンパク質濃度での親の洗浄性能についての理論値を算出した。
PspMan4の部位評価ライブラリの作成
PspMan4タンパク質配列中に単一アミノ酸置換を導入するための標準的な分子生物学プロトコルを用いて、PspMan4についての部位評価ライブラリ(SEL)を作成した。PspMan4遺伝子(配列番号1)を含有する鋳型プラスミドを構築した。SELを、PspMan4(配列番号2)の成熟した領域における予め選択した位置にて生産した。SELにおける各アミノ酸部位についてのフォワードNNSオリゴマー及びリバースNNSオリゴマー、並びに外側のプライマー(発現カセットの始点又は終点にハイブリダイズする)を、Eurofins Genomics,Huntsville,AL,USAに注文した。
PspMan4突然変異の評価
コンビナブル突然変異を、コンビナトリアル変異体を作製するのに用いることができる、分子中の置換として説明することができる。コンビナブル突然変異は、分子の少なくとも1つの所望される特性を向上させる一方で、発現、活性、又は安定性をいずれも大きく低下させないものである。生産的位置を、特性の向上を示すコンビナトリアル変異体を作製するのに最も有用な、分子内の位置として説明し、当該位置はそれ自体、少なくとも1つのコンビナブル突然変異を許容する。
PspMan4変異体の結晶構造
2つのPspMan4変異体、PspMan118及びPspMan148の三次元構造を、X線結晶学的方法を用いて判定した。
BspMan5及びその変異体のクローニング及び異種発現
BspMan5(配列番号16)は、US6566114-002(残基32~340)(配列番号17)の変異体であり、BspMan5のアミノ酸配列は、突然変異:P85L、及びN末端に挿入されたアミノ酸AGKを有し、アミノ酸位置は、配列番号2のアミノ酸配列との対応によって番号を付けている。
BspMan5~15を、清澄化した枯草菌(B.subtilis)培養ブロスから精製した。イオン交換、疎水性相互作用、又はサイジング分画樹脂が挙げられるカラムクロマトグラフィの組合せを用いた。LBGに対する活性を、PAHBAH(p-ヒドロキシ安息香酸ヒドラジド)アッセイ(Lever,Anal Biochem,47:248,1972)を介して試験することによって、マンナナーゼを含有する画分を同定した。注目する画分をプールして、10K Amicon Ultra装置を用いて濃縮して、サンプルを40%グリセロールに調整して、長期間の保存用に-20℃にて保存した。
BspMan5及びその変異体の熱安定性
熱安定性を、T50値を判定することによって評価した。これは、アッセイの条件下で酵素が活性を50%保持する温度として定義される。各酵素を、サーモサイクラー内で、0.005%Tween-80を含有する50mMクエン酸ナトリウムバッファpH6.0中で、以下の温度にて2時間インキュベートした:40、41.7、44.7、49.4、55、59.7、63、65、67、及び70℃。LBGを基質として用いて(50mMクエン酸ナトリウムバッファpH6.0中、0.45%LBG溶液)、50℃にて10分のインキュベーション後に、酵素活性を測定した。放出された還元糖を、PAHBAH(p-ヒドロキシ安息香酸ヒドラジド)アッセイ(Lever,Anal.Biochem,47:273,1972)で定量化した。氷上で維持した各酵素サンプルのアリコートを試験して、100%の活性値を判定した。T50温度値を、2時間のインキュベーション後に測定して、残留活性を判定した。データをプロットして、各酵素サンプルについてT50値を判定して、表5に示す。
BspMan5及びその変異体の洗浄性能
人為的な汚れからのLBGの放出を測定するミクロスワッチアッセイで、BspMan5~15マンナナーゼの洗浄性能を評価した。放出された還元糖を、PAHBAH(p-ヒドロキシ安息香酸ヒドラジド)アッセイ(Lever,Anal.Biochem,47:273,1972)を用いて定量化した。2つのCS-73ミクロスワッチ(直径5.5cm)(CFT,Vlaardingen,Holland)を、平底ノンバインディング96ウェルアッセイプレートの各ウェルに入れた。酵素サンプルを、脱イオン水中に希釈した。表6に、用いた洗剤及び購入場所を一覧にする。表7に、以下が挙げられる、用いた洗剤条件を一覧にする:洗浄アッセイ用の用量、pH、バッファ系(用いる場合)、硬度(3:1 Ca:Mg;ppm)、温度(℃)、及び洗い時間(分)。2.5ppmの最終用量に希釈した酵素、及び洗剤溶液を各ウェルに加えて、総容量を100μlにした。プレートをシールして、洗剤のそれぞれの洗浄条件下でインキュベートした。洗浄評価時間を終えた後、10μlの各反応混合液を、ウェルあたり100μlのPAHBAH溶液を含有するPCRプレートに移した。プレートをシールして、PCR機器内で95℃にて5分間インキュベートした。後に、プレートを25℃に冷却して、80μlの上澄みを、フレッシュな平底MTPに移して、405nmでの吸光度を分光光度計で測定した。405nmでの吸光度の増加を、マンナンベースのCS-73ミクロスワッチに対する洗浄性能の尺度として用いた。結果を、PI値として表8に示す。これは、変異体の吸光度の、BspMan5親酵素について観察された値に対する比率をとることによって算出した。
Claims (19)
- N10Q、P19E、T38E/I/L/M/Q/R/V、S59D/G/K/N/Q/T、L60F/M/V、T62E/I/Q/V、K63L、L66C/T/V、N67A/D/E/G/P/Q/S、A68L/M/R/S/W、K70R/V、N71D/H、N74E/C/Q/V、V75I、Q78A/D/L/M、N79E/F/W、K80Q/T、N97E/L/P/Q、Y129M、T131P、S135A/Q、A136E、K143Q/R、F167L/S/W/Y、P168A/E/G/L/M/S/T、Q184D/L/M/P、N213E、K214C/Q、G225A/C/P/W、T228A/G/H/I/K/S/V/Y、Y235G/I/L/Q/S/V、Q242S/E、K244A/C/G/L/M/P/S、S258A/D/E/G/M/N/P/T、G259A/E/R/S/W、N261I/M/P/Q/R/S/T/V/W/Y、D283G/H/T、P19EおよびP85L、T38EおよびP85L、H67DおよびP85L、P85LおよびF129M、P85LおよびP168S、P85LおよびQ184L、P85LおよびH225P、P85LおよびR244L、P85LおよびP258D、及びP85LおよびE261Rから選択される、配列番号2に対するアミノ酸置換を含むとともに、配列番号2のアミノ酸配列に対するアミノ酸配列同一性が少なくとも95%であるアミノ酸配列を含む、マンナナーゼ変異体であって:
前記アミノ酸置換が、天然に存在しないことを条件とし;
前記変異体のアミノ酸位置は、配列番号2のアミノ酸配列との対応によって番号を付けられ、
前記マンナナーゼ変異体は、配列番号2のアミノ酸配列を有する基準ポリペプチドに対して熱的安定性、洗剤安定性、マンナン基質に対する特異的活性、及び洗浄性能から選択される1つ又は複数の特性が向上している、マンナナーゼ変異体。 - 前記変異体はさらに:
(i)位置31~40にてWXaKNDLXbXcAI(配列番号11)のモチーフ(式中、Xaは、F又はYであり、XbはN、T、またはSであり、XcはTまたはEである);(ii)位置263~274にてLDX1V/AT/AGPX2GX3LT(配列番号13)のモチーフ(式中、X1は、M又はLであり、X2は、N、A、又はSであり、X3は、S、T、又はNである);及び(iii)位置263~274にてLDM/LATGPN/AGS/TLT(配列番号14)のモチーフから選択される1つ又は複数のモチーフを含む、請求項1に記載のマンナナーゼ変異体。 - 前記マンナナーゼ変異体は、配列番号2のアミノ酸配列に対するアミノ酸配列同一性が少なくとも98%であるアミノ酸配列を含む、請求項1に記載のマンナナーゼ変異体。
- 前記マンナナーゼ変異体は、マンナナーゼ活性を有する、請求項1~3のいずれか一項に記載のマンナナーゼ変異体。
- マンナナーゼ活性は、界面活性剤及び/又はプロテアーゼの存在下で示される、請求項4に記載のマンナナーゼ変異体。
- 前記マンナナーゼ変異体は、基準ポリペプチドに対してマンナナーゼ活性、洗浄性能、及び安定性の全てについて、PI≧0.7;並びにマンナナーゼ活性、洗浄性能、及び安定性の少なくとも1つについて、PI>1.0である、請求項1~5のいずれか一項に記載のマンナナーゼ変異体。
- 請求項1~6のいずれか一項に記載のマンナナーゼ変異体を含む洗浄組成物。
- 少なくとも1つの界面活性剤;カルシウム及び亜鉛から選択される少なくとも1つのイオン;少なくとも1つの補助剤成分;少なくとも1つの安定化剤;0.001重量%~1.0重量%の、請求項1~6のいずれか一項に記載のマンナナーゼ変異体;少なくとも1つの漂白剤;並びに/あるいはアシルトランスフェラーゼ、アミラーゼ、アルファ-アミラーゼ、ベータ-アミラーゼ、アルファ-ガラクトシダーゼ、アラビナーゼ、アラビノシダーゼ、アリールエステラーゼ、ベータ-ガラクトシダーゼ、ベータ-グルカナーゼ、カラギナーゼ、カタラーゼ、セロビオヒドラーゼ、セルラーゼ、コンドロイチナーゼ、クチナーゼ、エンド-ベータ-1,4-グルカナーゼ、エンド-ベータ-マンナナーゼ、エキソ-ベータ-マンナナーゼ、エステラーゼ、エキソ-マンナナーゼ、ガラクタナーゼ、グルコアミラーゼ、ヘミセルラーゼ、ヒアルロニダーゼ、ケラチナーゼ、ラッカーゼ、ラクターゼ、リグニナーゼ、リパーゼ、脂肪分解酵素、リポキシゲナーゼ、マンナナーゼ、オキシダーゼ、ペクチン酸リアーゼ、ペクチンアセチルエステラーゼ、ペクチナーゼ、ペントサナーゼ、ペルヒドロラーゼ、ペルオキシダーゼ、フェノールオキシダーゼ、ホスファターゼ、ホスホリパーゼ、フィターゼ、ポリガラクツロナーゼ、プロテアーゼ、プルラナーゼ、リダクターゼ、ラムノガラクツロナーゼ、ベータ-グルカナーゼ、タンナーゼ、トランスグルタミナーゼ、キシランアセチルエステラーゼ、キシラナーゼ、キシログルカナーゼ、キシロシダーゼ、メタロプロテアーゼ、及びそれら組合せから選択される少なくとも1つの酵素又は酵素誘導体:をさらに含む、請求項7に記載の洗浄組成物。
- 前記洗浄組成物は、洗濯洗剤、布地柔軟仕上げ洗剤、食器洗い洗剤、及び硬質表面洗浄洗剤から選択される洗剤組成物である、請求項7又は8に記載の洗浄組成物。
- 前記洗浄組成物は、液体、粉末、顆粒状の固体、タブレット、シート、及び単位用量から選択される形態である、請求項7~9のいずれか一項に記載の洗浄組成物。
- 前記組成物は、ホスフェートを含有し、若しくはホスフェートを含有せず、且つ/又はホウ素を含有し、若しくはホウ素を含有しない、請求項7~10のいずれか一項に記載の洗浄組成物。
- マンナンを含む汚れ又は染みを含む表面又はアイテムを、(i)請求項1~6のいずれか一項に記載のマンナナーゼ変異体、あるいは(ii)請求項7~11のいずれか一項に記載の洗浄組成物と接触させることを含み、前記汚れ又は前記染みに含有される前記マンナンは加水分解される、洗浄方法。
- 前記アイテムは、皿類又は布地である、請求項12に記載の方法。
- 請求項1~6のいずれか一項に記載のマンナナーゼ変異体をコードする核酸配列を含むポリヌクレオチド。
- 請求項14に記載のポリヌクレオチドを含む発現ベクター。
- 請求項15に記載の発現ベクターを含む宿主細胞。
- 請求項1~6のいずれか一項に記載のマンナナーゼ変異体を生産する方法であって:
(a)請求項15に記載の発現ベクターで請求項16に記載の宿主細胞を安定して形質転換することと;
(b)形質転換された前記宿主細胞を、前記宿主細胞が前記マンナナーゼ変異体を産生するのに適した条件下で培養することと;
(c)前記マンナナーゼ変異体を回収することと
を含む方法。 - 請求項1~6のいずれか一項に記載のマンナナーゼ変異体を含む食品組成物若しくは飼料組成物及び/又は食品添加物。
- 請求項1~6のいずれか一項に記載のマンナナーゼ変異体の、食品組成物若しくは飼料組成物、並びに/又は食品添加物若しくは飼料添加物、並びに/又は食品若しくは飼料及び/若しくはペットフードの調製における使用。
Applications Claiming Priority (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US201562251516P | 2015-11-05 | 2015-11-05 | |
US62/251,516 | 2015-11-05 | ||
US201662278383P | 2016-01-13 | 2016-01-13 | |
US62/278,383 | 2016-01-13 | ||
PCT/US2016/060850 WO2017079756A1 (en) | 2015-11-05 | 2016-11-07 | Paenibacillus and bacillus spp. mannanases |
Publications (2)
Publication Number | Publication Date |
---|---|
JP2019504616A JP2019504616A (ja) | 2019-02-21 |
JP7364330B2 true JP7364330B2 (ja) | 2023-10-18 |
Family
ID=57349138
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP2018522947A Active JP7364330B2 (ja) | 2015-11-05 | 2016-11-07 | パエニバチルス(Paenibacillus)属種及びバチルス(Bacillus)属種のマンナナーゼ |
Country Status (6)
Country | Link |
---|---|
US (1) | US20180320158A1 (ja) |
EP (1) | EP3371307A1 (ja) |
JP (1) | JP7364330B2 (ja) |
CN (1) | CN108603183B (ja) |
BR (1) | BR112018009050A8 (ja) |
WO (1) | WO2017079756A1 (ja) |
Families Citing this family (13)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
EP3464599A1 (en) | 2016-05-31 | 2019-04-10 | Danisco US Inc. | Protease variants and uses thereof |
DK3409768T3 (da) * | 2017-05-30 | 2020-05-18 | Ab Enzymes Oy | Mannanase-varianter |
US10501730B2 (en) | 2017-05-30 | 2019-12-10 | Ab Enzymes Oy | Mannanase variants |
CN111417725A (zh) | 2017-10-02 | 2020-07-14 | 诺维信公司 | 具有甘露聚糖酶活性的多肽和编码它们的多核苷酸 |
EP3692148A1 (en) * | 2017-10-02 | 2020-08-12 | Novozymes A/S | Polypeptides having mannanase activity and polynucleotides encoding same |
WO2019081515A1 (en) * | 2017-10-24 | 2019-05-02 | Novozymes A/S | COMPOSITIONS COMPRISING POLYPEPTIDES HAVING MANNANASE ACTIVITY |
US11535837B2 (en) | 2018-03-29 | 2022-12-27 | Novozymes A/S | Mannanase variants and polynucleotides encoding same |
CN108559739B (zh) * | 2018-05-11 | 2021-03-26 | 中国农业科学院北京畜牧兽医研究所 | 耐热性提高的甘露聚糖酶PMan5A突变体及其基因和应用 |
US20200199493A1 (en) * | 2018-12-21 | 2020-06-25 | Henkel IP & Holding GmbH | Unit dose detergent with zinc ricinoleate |
MX2021012399A (es) | 2019-04-12 | 2021-12-10 | Ecolab Usa Inc | Limpiador antimicrobiano multiuso y métodos de fabricación y uso de este. |
EP4204553A1 (en) | 2020-08-27 | 2023-07-05 | Danisco US Inc. | Enzymes and enzyme compositions for cleaning |
WO2023168234A1 (en) | 2022-03-01 | 2023-09-07 | Danisco Us Inc. | Enzymes and enzyme compositions for cleaning |
CN116463320A (zh) * | 2022-07-13 | 2023-07-21 | 中南大学 | 一种矿山排水宏基因组来源的β-甘露聚糖酶及其基因、酶制剂和应用 |
Family Cites Families (211)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GB400898A (en) | 1932-07-13 | 1933-11-02 | Chem Fab Buckau | Process for the production of rubber chloride |
GB514276A (en) | 1938-04-29 | 1939-11-03 | Betterwear Products Ltd | Improvements in or relating to combined combs and brushes |
GB1296839A (ja) | 1969-05-29 | 1972-11-22 | ||
GB1372034A (en) | 1970-12-31 | 1974-10-30 | Unilever Ltd | Detergent compositions |
EP0011340B1 (en) | 1978-11-20 | 1982-11-24 | THE PROCTER & GAMBLE COMPANY | Detergent composition having textile softening properties |
GB2048606B (en) | 1979-02-28 | 1983-03-16 | Barr & Stroud Ltd | Optical scanning system |
EP0026528B2 (en) | 1979-09-29 | 1992-08-19 | THE PROCTER & GAMBLE COMPANY | Detergent compositions |
JPS582673B2 (ja) | 1979-11-09 | 1983-01-18 | 工業技術院長 | 好アルカリ性バチルス属菌によるペクチン酸リア−ゼの製造法 |
JPS56131376A (en) | 1980-03-17 | 1981-10-14 | Agency Of Ind Science & Technol | Method for reducing nonwoody cellulosic fiber to pulp |
DK187280A (da) | 1980-04-30 | 1981-10-31 | Novo Industri As | Ruhedsreducerende middel til et fuldvaskemiddel fuldvaskemiddel og fuldvaskemetode |
GR76237B (ja) | 1981-08-08 | 1984-08-04 | Procter & Gamble | |
JPS5966588A (ja) | 1982-10-08 | 1984-04-16 | 工業技術院長 | 分繊化したペクトセルロ−ス系繊維の製造方法 |
US4760025A (en) | 1984-05-29 | 1988-07-26 | Genencor, Inc. | Modified enzymes and methods for making same |
US5972682A (en) | 1984-05-29 | 1999-10-26 | Genencor International, Inc. | Enzymatically active modified subtilisins |
US5801038A (en) | 1984-05-29 | 1998-09-01 | Genencor International Inc. | Modified subtilisins having amino acid alterations |
DK154572C (da) | 1985-08-07 | 1989-04-24 | Novo Industri As | Enzymatisk detergentadditiv, detergent og fremgangsmaade til vask af tekstiler |
US4933287A (en) | 1985-08-09 | 1990-06-12 | Gist-Brocades N.V. | Novel lipolytic enzymes and their use in detergent compositions |
DK122686D0 (da) | 1986-03-17 | 1986-03-17 | Novo Industri As | Fremstilling af proteiner |
GB8609883D0 (en) | 1986-04-23 | 1986-05-29 | Procter & Gamble | Softening detergent compositions |
JPS6342988A (ja) | 1986-08-08 | 1988-02-24 | 工業技術院長 | じん皮繊維の改良酵素パルプ化法 |
DE3750450T2 (de) | 1986-08-29 | 1995-01-05 | Novo Industri As | Enzymhaltiger Reinigungsmittelzusatz. |
GB8629837D0 (en) | 1986-12-13 | 1987-01-21 | Interox Chemicals Ltd | Bleach activation |
US4972017A (en) | 1987-03-24 | 1990-11-20 | The Clorox Company | Rinse soluble polymer film composition for wash additives |
US4765916A (en) | 1987-03-24 | 1988-08-23 | The Clorox Company | Polymer film composition for rinse release of wash additives |
EP0322429B1 (en) | 1987-05-29 | 1994-10-19 | Genencor International, Inc. | Cutinase cleaning composition |
US5019292A (en) | 1987-06-30 | 1991-05-28 | The Procter & Gamble Company | Detergent compositions |
EP0299575B1 (en) | 1987-07-14 | 1994-01-12 | The Procter & Gamble Company | Detergent compositions |
EP0305216B1 (en) | 1987-08-28 | 1995-08-02 | Novo Nordisk A/S | Recombinant Humicola lipase and process for the production of recombinant humicola lipases |
JPS6474992A (en) | 1987-09-16 | 1989-03-20 | Fuji Oil Co Ltd | Dna sequence, plasmid and production of lipase |
DE3881329T3 (de) | 1987-10-19 | 2002-05-23 | Procter & Gamble | Reinigungsmittel. |
DE68924654T2 (de) | 1988-01-07 | 1996-04-04 | Novo Nordisk As | Spezifische Protease. |
JP3079276B2 (ja) | 1988-02-28 | 2000-08-21 | 天野製薬株式会社 | 組換え体dna、それを含むシュードモナス属菌及びそれを用いたリパーゼの製造法 |
US4977252A (en) | 1988-03-11 | 1990-12-11 | National Starch And Chemical Investment Holding Corporation | Modified starch emulsifier characterized by shelf stability |
US5137819A (en) | 1988-07-08 | 1992-08-11 | University Of British Columbia | Cellulose binding fusion proteins for immobilization and purification of polypeptides |
WO1990009446A1 (en) | 1989-02-17 | 1990-08-23 | Plant Genetic Systems N.V. | Cutinase |
DE69032360T2 (de) | 1989-06-29 | 1998-12-03 | Genencor Int | Mutierte mikrobielle alpha-Amylasen mit erhöhter thermischer, saurer und/oder alkylischer Stabilität |
JP3112937B2 (ja) | 1990-04-14 | 2000-11-27 | カリ―ヒエミー アクチエンゲゼルシヤフト | アルカリ性バチルスーリパーゼ、これをコード化するdna配列およびこのリパーゼを生産するバチルス |
US5354559A (en) | 1990-05-29 | 1994-10-11 | Grain Processing Corporation | Encapsulation with starch hydrolyzate acid esters |
EP0550695B1 (en) | 1990-09-28 | 1997-07-16 | The Procter & Gamble Company | Polyhydroxy fatty acid amide surfactants to enhance enzyme performance |
EP0495258A1 (en) | 1991-01-16 | 1992-07-22 | The Procter & Gamble Company | Detergent compositions with high activity cellulase and softening clays |
GB9108136D0 (en) | 1991-04-17 | 1991-06-05 | Unilever Plc | Concentrated detergent powder compositions |
US5340735A (en) | 1991-05-29 | 1994-08-23 | Cognis, Inc. | Bacillus lentus alkaline protease variants with increased stability |
WO1994002597A1 (en) | 1992-07-23 | 1994-02-03 | Novo Nordisk A/S | MUTANT α-AMYLASE, DETERGENT, DISH WASHING AGENT, AND LIQUEFACTION AGENT |
US5965510A (en) | 1992-12-01 | 1999-10-12 | Novo Nordisk A/S | Enhancement of enzyme reactions |
US5646101A (en) | 1993-01-18 | 1997-07-08 | The Procter & Gamble Company | Machine dishwashing detergents containing an oxygen bleach and an anti-tarnishing mixture of a paraffin oil and sequestrant |
DK0689589T4 (da) | 1993-02-11 | 2010-01-04 | Genencor Int | Oxidativ stabil alfa-amylase |
CZ286401B6 (en) | 1993-05-08 | 2000-04-12 | Henkel Kgaa | Use of inorganic redox-active substances |
WO1994026860A1 (de) | 1993-05-08 | 1994-11-24 | Henkel Kommanditgesellschaft Auf Aktien | Silberkorrosionsschutzmittel ii |
DK77393D0 (da) | 1993-06-29 | 1993-06-29 | Novo Nordisk As | Aktivering af enzymer |
US5698504A (en) | 1993-07-01 | 1997-12-16 | The Procter & Gamble Company | Machine dishwashing composition containing oxygen bleach and paraffin oil and benzotriazole compound silver tarnishing inhibitors |
US5486303A (en) | 1993-08-27 | 1996-01-23 | The Procter & Gamble Company | Process for making high density detergent agglomerates using an anhydrous powder additive |
JPH09503916A (ja) | 1993-10-08 | 1997-04-22 | ノボ ノルディスク アクティーゼルスカブ | アミラーゼ変異体 |
DE4342680A1 (de) | 1993-12-15 | 1995-06-22 | Pfeiffer Erich Gmbh & Co Kg | Austragvorrichtung für Medien |
US5861271A (en) | 1993-12-17 | 1999-01-19 | Fowler; Timothy | Cellulase enzymes and systems for their expressions |
EP1921148B1 (en) | 1994-02-24 | 2011-06-08 | Henkel AG & Co. KGaA | Improved enzymes and detergents containing them |
ES2364774T3 (es) | 1994-02-24 | 2011-09-14 | HENKEL AG & CO. KGAA | Enzimas mejoradas y detergentes que las contienen. |
US5691295A (en) | 1995-01-17 | 1997-11-25 | Cognis Gesellschaft Fuer Biotechnologie Mbh | Detergent compositions |
WO1995026397A1 (en) | 1994-03-29 | 1995-10-05 | Novo Nordisk A/S | Alkaline bacillus amylase |
US5686014A (en) | 1994-04-07 | 1997-11-11 | The Procter & Gamble Company | Bleach compositions comprising manganese-containing bleach catalysts |
ES2137277T3 (es) | 1994-04-07 | 1999-12-16 | Nestle Sa | Hidrolisis de cafe, con una beta-mananasa inmovilizada. |
DE69534369T2 (de) | 1994-06-17 | 2006-03-09 | Genencor International, Inc., Palo Alto | Von der alpha-amylase aus b. licheniformis abgeleitete amylolytische enzyme mit verbesserten eigenschaften |
AU704022B2 (en) | 1994-06-17 | 1999-04-15 | Genencor International, Inc. | Cleaning compositions containing plant cell wall degrading enzymes and their use in cleaning methods |
GB2294268A (en) | 1994-07-07 | 1996-04-24 | Procter & Gamble | Bleaching composition for dishwasher use |
KR970704872A (ko) | 1994-08-11 | 1997-09-06 | 혼 마가렛 에이 | 개선된 세척 조성물 |
US5879584A (en) | 1994-09-10 | 1999-03-09 | The Procter & Gamble Company | Process for manufacturing aqueous compositions comprising peracids |
US5691297A (en) | 1994-09-20 | 1997-11-25 | The Procter & Gamble Company | Process for making a high density detergent composition by controlling agglomeration within a dispersion index |
US5516448A (en) | 1994-09-20 | 1996-05-14 | The Procter & Gamble Company | Process for making a high density detergent composition which includes selected recycle streams for improved agglomerate |
US5489392A (en) | 1994-09-20 | 1996-02-06 | The Procter & Gamble Company | Process for making a high density detergent composition in a single mixer/densifier with selected recycle streams for improved agglomerate properties |
CA2206992C (en) | 1994-12-09 | 2001-04-10 | The Procter & Gamble Company | Automatic dishwashing composition containing particles of diacyl peroxides |
AR000862A1 (es) | 1995-02-03 | 1997-08-06 | Novozymes As | Variantes de una ó-amilasa madre, un metodo para producir la misma, una estructura de adn y un vector de expresion, una celula transformada por dichaestructura de adn y vector, un aditivo para detergente, composicion detergente, una composicion para lavado de ropa y una composicion para la eliminacion del |
US5534179A (en) | 1995-02-03 | 1996-07-09 | Procter & Gamble | Detergent compositions comprising multiperacid-forming bleach activators |
EP2199378B1 (en) | 1995-02-03 | 2012-08-15 | Novozymes A/S | A method of designing alpha-amylase mutants with predetermined properties |
US5574005A (en) | 1995-03-07 | 1996-11-12 | The Procter & Gamble Company | Process for producing detergent agglomerates from high active surfactant pastes having non-linear viscoelastic properties |
BR9607751A (pt) | 1995-03-24 | 1998-06-23 | Genencor Int | Uma composiçao detergente aperfeiçoada para lavandeira compreendendo amílase |
US5569645A (en) | 1995-04-24 | 1996-10-29 | The Procter & Gamble Company | Low dosage detergent composition containing optimum proportions of agglomerates and spray dried granules for improved flow properties |
US5597936A (en) | 1995-06-16 | 1997-01-28 | The Procter & Gamble Company | Method for manufacturing cobalt catalysts |
AU5862396A (en) | 1995-06-16 | 1997-01-15 | Procter & Gamble Company, The | Automatic dishwashing compositions comprising cobalt catalysts |
US5565422A (en) | 1995-06-23 | 1996-10-15 | The Procter & Gamble Company | Process for preparing a free-flowing particulate detergent composition having improved solubility |
US5576282A (en) | 1995-09-11 | 1996-11-19 | The Procter & Gamble Company | Color-safe bleach boosters, compositions and laundry methods employing same |
JPH11514219A (ja) | 1995-09-13 | 1999-12-07 | ジェネンコア インターナショナル インコーポレーテッド | 好アルカリ性で好熱姓の微生物およびそれから得られる酵素 |
DE69635936T2 (de) | 1995-09-18 | 2006-12-28 | The Procter & Gamble Company, Cincinnati | Riechstofffreisetzungssystem |
ES2432519T3 (es) | 1996-04-30 | 2013-12-04 | Novozymes A/S | Mutantes de alfa-amilasa |
US5763385A (en) | 1996-05-14 | 1998-06-09 | Genencor International, Inc. | Modified α-amylases having altered calcium binding properties |
US6211134B1 (en) | 1996-05-14 | 2001-04-03 | Genecor International, Inc. | Mutant α-amylase |
EP0939801A1 (en) | 1996-09-26 | 1999-09-08 | Novo Nordisk A/S | An enzyme with amylase activity |
AU1461497A (en) | 1996-12-09 | 1998-07-03 | Genencor International, Inc. | Proteins Having Increased Stability |
CA2282477C (en) | 1997-03-07 | 2004-11-30 | The Procter & Gamble Company | Improved methods of making cross-bridged macropolycycles |
US6008026A (en) | 1997-07-11 | 1999-12-28 | Genencor International, Inc. | Mutant α-amylase having introduced therein a disulfide bond |
GB2327947A (en) | 1997-08-02 | 1999-02-10 | Procter & Gamble | Detergent tablet |
US6376445B1 (en) | 1997-08-14 | 2002-04-23 | Procter & Gamble Company | Detergent compositions comprising a mannanase and a protease |
US6080568A (en) | 1997-08-19 | 2000-06-27 | Genencor International, Inc. | Mutant α-amylase comprising modification at residues corresponding to A210, H405 and/or T412 in Bacillus licheniformis |
GB9719636D0 (en) | 1997-09-15 | 1997-11-19 | Genencor Int Bv | Proteases from gram-positive organisms |
GB9719637D0 (en) | 1997-09-15 | 1997-11-19 | Genencor Int Bv | Proteases from gram-positive organisms |
EP1023439B1 (en) | 1997-10-13 | 2009-02-18 | Novozymes A/S | alpha-AMYLASE MUTANTS |
AR015977A1 (es) | 1997-10-23 | 2001-05-30 | Genencor Int | Variantes de proteasa multiplemente substituida con carga neta alterada para su empleo en detergentes |
CA2845178A1 (en) | 1997-10-30 | 1999-05-14 | Novozymes A/S | .alpha.-amylase mutants |
US5935826A (en) | 1997-10-31 | 1999-08-10 | National Starch And Chemical Investment Holding Corporation | Glucoamylase converted starch derivatives and their use as emulsifying and encapsulating agents |
EP1032655B1 (en) | 1997-11-21 | 2005-06-29 | Novozymes A/S | Protease variants and compositions |
JP2002500019A (ja) | 1997-12-24 | 2002-01-08 | ジェネンコア インターナショナル インコーポレーテッド | 好ましい酵素および/または好ましい洗剤組成物についての改良された分析方法 |
GB9727471D0 (en) | 1997-12-30 | 1998-02-25 | Genencor Int Bv | Proteases from gram positive organisms |
GB9727464D0 (en) | 1997-12-30 | 1998-02-25 | Genencor Int Bv | Proteases from gram positive organisms |
EP1054957A1 (en) | 1998-02-18 | 2000-11-29 | Novo Nordisk A/S | Alkaline bacillus amylase |
ATE490312T1 (de) | 1998-02-27 | 2010-12-15 | Novozymes As | Maltogene alpha-amylase varianten |
EP1066374B1 (en) | 1998-02-27 | 2006-05-31 | Novozymes A/S | Amylolytic enzyme variants |
WO1999046399A1 (en) | 1998-03-09 | 1999-09-16 | Novo Nordisk A/S | Enzymatic preparation of glucose syrup from starch |
CN100497614C (zh) | 1998-06-10 | 2009-06-10 | 诺沃奇梅兹有限公司 | 甘露聚糖酶 |
US6060299A (en) | 1998-06-10 | 2000-05-09 | Novo Nordisk A/S | Enzyme exhibiting mannase activity, cleaning compositions, and methods of use |
US6376450B1 (en) | 1998-10-23 | 2002-04-23 | Chanchal Kumar Ghosh | Cleaning compositions containing multiply-substituted protease variants |
US6197565B1 (en) | 1998-11-16 | 2001-03-06 | Novo-Nordisk A/S | α-Amylase variants |
CA2348893A1 (en) | 1998-11-30 | 2000-06-08 | The Procter & Gamble Company | Process for preparing cross-bridged tetraaza macrocycles |
ES2496568T3 (es) | 1999-03-30 | 2014-09-19 | Novozymes A/S | Variantes de alfa-amilasa |
CN100523181C (zh) | 1999-03-31 | 2009-08-05 | 诺维信公司 | 具有碱性α-淀粉酶活性的多肽及其编码核酸 |
JP4745503B2 (ja) | 1999-03-31 | 2011-08-10 | ノボザイムス アクティーゼルスカブ | アルカリα−アミラーゼ活性を有するポリペプチド及びそれらをコードする核酸 |
AU6686200A (en) | 1999-08-20 | 2001-03-19 | Novozymes A/S | Alkaline bacillus amylase |
CN1390252A (zh) | 1999-11-10 | 2003-01-08 | 诺维信公司 | Fungamyl样α-淀粉酶变体 |
EP1261698A1 (en) * | 2000-03-01 | 2002-12-04 | Novozymes A/S | Family 5 xyloglucanases |
AU3724801A (en) | 2000-03-03 | 2001-09-12 | Novozymes A/S | Polypeptides having alkaline alpha-amylase activity and nucleic acids encoding same |
EP2221365A1 (en) | 2000-03-08 | 2010-08-25 | Novozymes A/S | Variants with altered properties |
AU2001258229A1 (en) | 2000-05-12 | 2001-11-26 | Novozymes A/S | Alpha-amylase variants with altered 1,6-activity |
WO2001096537A2 (en) | 2000-06-14 | 2001-12-20 | Novozymes A/S | Pre-oxidized alpha-amylase |
JP4855632B2 (ja) | 2000-08-01 | 2012-01-18 | ノボザイムス アクティーゼルスカブ | 変更された性質を有するα−アミラーゼ突然変異体 |
EP1326965A2 (en) | 2000-10-13 | 2003-07-16 | Novozymes A/S | Alpha-amylase variant with altered properties |
EP2159279A3 (en) | 2001-05-15 | 2010-05-12 | Novozymes A/S | Alpha-amylase variant with altered properties |
GB0114847D0 (en) | 2001-06-18 | 2001-08-08 | Unilever Plc | Water soluble package and liquid contents thereof |
US7189552B2 (en) | 2002-12-17 | 2007-03-13 | Novozymes A/S | Thermostable alpha-amylases |
JP4757191B2 (ja) | 2003-04-30 | 2011-08-24 | 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mHKcelセルラーゼ |
EP1479755B1 (en) | 2003-05-23 | 2008-02-27 | The Procter & Gamble Company | Cleaning composition for use in a laundry or dishwashing machine |
CA2538349C (en) | 2003-06-25 | 2014-08-12 | Novozymes A/S | Polypeptides having alpha-amylase activity and polynucleotides encoding same |
DK1675941T3 (da) | 2003-06-25 | 2013-08-26 | Novozymes As | Polypeptider med alfa-amylaseaktivitet og polynukleotider, der koder for dem |
JP2007526748A (ja) | 2003-06-25 | 2007-09-20 | ノボザイムス アクティーゼルスカブ | 澱粉加工用酵素 |
US20070264700A1 (en) | 2003-08-22 | 2007-11-15 | Novozymes A/S | Fungal Alpha-Amylase Variants |
EP1657981A1 (en) | 2003-08-22 | 2006-05-24 | Novozymes A/S | Process for preparing a dough comprising a starch-degrading glucogenic exo-amylase of family 13 |
CN102766614A (zh) | 2003-12-03 | 2012-11-07 | 明治制果药业株式会社 | 内切葡聚糖酶stce和含有内切葡聚糖酶的纤维素酶配制品 |
EP2664670B1 (en) | 2003-12-03 | 2015-05-06 | Danisco US Inc. | Perhydrolase |
EP1702981B1 (en) | 2003-12-08 | 2011-08-31 | Meiji Seika Pharma Co., Ltd. | Surfactant-tolerant cellulase and method of converting the same |
DK1709167T3 (da) | 2004-01-08 | 2010-08-16 | Novozymes As | Amylase |
JP4955546B2 (ja) | 2004-07-05 | 2012-06-20 | ノボザイムス アクティーゼルスカブ | 変更された性質を有するα−アミラーゼ変異体 |
WO2006012899A1 (en) | 2004-08-02 | 2006-02-09 | Novozymes A/S | Maltogenic alpha-amylase variants |
AU2005269082A1 (en) | 2004-08-02 | 2006-02-09 | Novozymes A/S | Creation of diversity in polypeptides |
EP1791966B1 (en) | 2004-09-10 | 2014-06-04 | Novozymes North America, Inc. | Methods for preventing, removing, reducing, or disrupting biofilm |
US7659101B2 (en) | 2004-12-15 | 2010-02-09 | Novozymes A/S | Alkaline Bacillus amylase |
CA2592083C (en) | 2004-12-22 | 2017-02-21 | Novozymes A/S | Hybrid enzymes consisting of an endo-amylase first amino acid sequence and a carbohydrate-binding module as second amino acid sequence |
MX2007007494A (es) | 2004-12-23 | 2007-08-15 | Novozymes As | Variantes de alfa-amilasa. |
MX2007015471A (es) | 2005-06-24 | 2008-04-04 | Novozymes As | Amilasas para uso farmaceutico. |
DK1934340T3 (da) | 2005-10-12 | 2014-06-16 | Danisco Us Inc | Anvendelse og fremstilling af en opbevaringsstabil neutral metalloprotease |
US20080004201A1 (en) | 2006-06-05 | 2008-01-03 | Jean-Pol Boutique | Enzyme stabilizer |
EP2038410A1 (en) | 2006-06-30 | 2009-03-25 | Novozymes A/S | Bacterial alpha-amylase variants |
CN104232365A (zh) | 2006-07-18 | 2014-12-24 | 丹尼斯科美国公司 | 在宽温度范围内具有活性的蛋白酶变体 |
PL2052078T3 (pl) * | 2006-07-18 | 2013-09-30 | Basf Se | Mannanazy |
US8097444B2 (en) | 2006-12-21 | 2012-01-17 | Danisco Us Inc. | Compositions and uses for an alpha-amylase polypeptide of bacillus species 195 |
US20100112637A1 (en) | 2007-02-01 | 2010-05-06 | Novozymes A/S | Polypeptides Having Alpha-Amylase Activity and Polynucleotides Encoding Same |
US8021863B2 (en) | 2007-02-19 | 2011-09-20 | Novozymes A/S | Polypeptides with starch debranching activity |
CN101679987A (zh) | 2007-03-09 | 2010-03-24 | 丹尼斯科美国公司 | 嗜碱芽孢杆菌物种α-淀粉酶变体、包括α-淀粉酶变体的组合物以及使用方法 |
CA2703975C (en) | 2007-10-31 | 2018-01-09 | Danisco Us Inc. | Use and production of citrate-stable neutral metalloproteases |
WO2009058303A2 (en) | 2007-11-01 | 2009-05-07 | Danisco Us Inc., Genencor Division | Production of thermolysin and variants thereof and use in liquid detergents |
EP2215110A2 (en) | 2007-11-05 | 2010-08-11 | Danisco US, Inc., Genencor Division | Alpha-amylase variants with altered properties |
AU2008325250B2 (en) | 2007-11-05 | 2013-06-13 | Danisco Us Inc. | Variants of Bacillus sp. TS-23 alpha-amylase with altered properties |
CA2713582C (en) | 2008-02-04 | 2017-02-21 | Danisco Us Inc. | Ts23 alpha-amylase variants with altered properties |
US10676751B2 (en) | 2008-02-29 | 2020-06-09 | The Trustees Of The University Of Pennsylvania | Production and use of plant degrading materials |
EP2100947A1 (en) | 2008-03-14 | 2009-09-16 | The Procter and Gamble Company | Automatic dishwashing detergent composition |
WO2009140504A1 (en) | 2008-05-16 | 2009-11-19 | Novozymes A/S | Polypeptides having alpha-amylase activity and polynucleotides encoding same |
WO2009149200A2 (en) | 2008-06-06 | 2009-12-10 | Danisco Us Inc. | Compositions and methods comprising variant microbial proteases |
PL2297313T3 (pl) | 2008-06-06 | 2015-08-31 | Danisco Us Inc | Warianty alfa-amylazy z Bacillus subtilis i sposoby ich zastosowania |
RU2509776C2 (ru) | 2008-10-15 | 2014-03-20 | ДАНИСКО ЮЭс ИНК. | МОДИФИЦИРОВАННЫЕ ВАРИАНТЫ ИНГИБИТОРОВ ПРОТЕАЗ Bowman Birk |
WO2010056634A1 (en) | 2008-11-11 | 2010-05-20 | Danisco Us Inc. | Compositions and methods comprising a subtilisin variant |
KR20110091671A (ko) | 2008-11-11 | 2011-08-12 | 다니스코 유에스 인크. | 세린 프로테아제 변이체를 포함하는 조성물 및 방법 |
WO2010056656A2 (en) | 2008-11-11 | 2010-05-20 | Dr. Reddy's Laboratories Ltd. | Preparation of crystalline palonosetron hydrochloride |
BRPI0922083A2 (pt) | 2008-11-11 | 2017-05-30 | Danisco Us Inc | proteases compreendendo uma ou mais mutações combináveis |
WO2010059413A2 (en) | 2008-11-20 | 2010-05-27 | Novozymes, Inc. | Polypeptides having amylolytic enhancing activity and polynucleotides encoding same |
WO2010088447A1 (en) | 2009-01-30 | 2010-08-05 | Novozymes A/S | Polypeptides having alpha-amylase activity and polynucleotides encoding same |
WO2010091221A1 (en) | 2009-02-06 | 2010-08-12 | Novozymes A/S | Polypeptides having alpha-amylase activity and polynucleotides encoding same |
CN102341495A (zh) | 2009-03-10 | 2012-02-01 | 丹尼斯科美国公司 | 巨大芽孢杆菌菌株DSM90相关的α-淀粉酶及其使用方法 |
CN102378813B (zh) | 2009-04-01 | 2014-05-14 | 丹尼斯科美国公司 | 包含具有改变的性质的α-淀粉酶变体的组合物和方法 |
US8877479B2 (en) | 2009-04-08 | 2014-11-04 | Danisco Us Inc. | Halomonas strain WDG195-related alpha-amylases, and methods of use, thereof |
EP2279804A1 (en) | 2009-07-28 | 2011-02-02 | Koninklijke Philips Electronics N.V. | Washing and sterilizing unit |
CN102762222B (zh) | 2009-12-09 | 2015-11-25 | 丹尼斯科美国公司 | 包含蛋白酶变体的组合物和方法 |
WO2011076123A1 (en) | 2009-12-22 | 2011-06-30 | Novozymes A/S | Compositions comprising boosting polypeptide and starch degrading enzyme and uses thereof |
US20130071913A1 (en) | 2009-12-22 | 2013-03-21 | Novozymes A/S | Use of amylase variants at low temperature |
US20120258497A1 (en) | 2010-01-04 | 2012-10-11 | Novozymes North America, Inc. | Alpha-Amylases |
WO2011098531A1 (en) | 2010-02-10 | 2011-08-18 | Novozymes A/S | Variants and compositions comprising variants with high stability in presence of a chelating agent |
PL2566960T3 (pl) | 2010-05-06 | 2017-08-31 | The Procter And Gamble Company | Produkty konsumenckie z odmianami proteaz |
CN103502445A (zh) * | 2011-04-29 | 2014-01-08 | 丹尼斯科美国公司 | 包含芽孢杆菌甘露聚糖酶的洗涤剂组合物及其使用方法 |
CN103764823B (zh) | 2011-05-05 | 2018-05-11 | 丹尼斯科美国公司 | 包含丝氨酸蛋白酶变体的组合物和方法 |
EP2771458B1 (en) | 2011-10-28 | 2016-12-21 | Danisco US Inc. | Variant maltohexaose-forming alpha-amylase variants |
US20130284637A1 (en) | 2012-04-30 | 2013-10-31 | Danisco Us Inc. | Unit-dose format perhydrolase systems |
US20150141316A1 (en) | 2012-06-08 | 2015-05-21 | Danisco Us Inc. | Variant alpha amylases with enhanced activity on starch polymers |
WO2014059360A1 (en) | 2012-10-12 | 2014-04-17 | Danisco Us Inc. | Compositions and methods comprising a lipolytic enzyme variant |
BR112015010104A2 (pt) | 2012-11-05 | 2017-08-22 | Danisco Us Inc | Variante de enzima termolisina, composição e método de limpeza |
WO2014100018A1 (en) * | 2012-12-19 | 2014-06-26 | Danisco Us Inc. | Novel mannanase, compositions and methods of use thereof |
DK2935575T3 (en) | 2012-12-21 | 2018-07-23 | Danisco Us Inc | ALPHA-amylase variants |
CN105229147B (zh) | 2013-03-11 | 2020-08-11 | 丹尼斯科美国公司 | α-淀粉酶组合变体 |
EP3260538B1 (en) | 2013-05-29 | 2021-04-14 | Danisco US Inc. | Novel metalloproteases |
WO2014194117A2 (en) | 2013-05-29 | 2014-12-04 | Danisco Us Inc. | Novel metalloproteases |
WO2014194032A1 (en) | 2013-05-29 | 2014-12-04 | Danisco Us Inc. | Novel metalloproteases |
EP3110833B1 (en) | 2013-05-29 | 2020-01-08 | Danisco US Inc. | Novel metalloproteases |
US20160160197A1 (en) | 2013-07-19 | 2016-06-09 | Danisco Us Inc. | Compositions and Methods Comprising a Lipolytic Enzyme Variant |
AU2014307813B2 (en) | 2013-08-15 | 2017-12-21 | Novozymes A/S | Method for producing a coffee extract employing enzymes having beta-1,3-galactanase activity |
CN105593365B (zh) | 2013-09-12 | 2021-08-27 | 丹尼斯科美国公司 | 包含lg12-进化枝蛋白酶变体的组合物和方法 |
MX2016006489A (es) | 2013-11-20 | 2016-08-03 | Danisco Us Inc | Alfa-amilasas variantes que tienen susceptibilidad reducida a la escision por proteasas y metodos de uso. |
TR201906371T4 (tr) | 2013-12-13 | 2019-05-21 | Danisco Inc | Bacillus türlerinin serin proteazları. |
EP3910057A1 (en) | 2013-12-13 | 2021-11-17 | Danisco US Inc. | Serine proteases of the bacillus gibsonii-clade |
MX2016012044A (es) | 2014-03-21 | 2017-06-29 | Danisco Us Inc | Serina proteasas de especies de bacillus. |
EP3166419B1 (en) | 2014-07-11 | 2019-09-18 | Danisco US Inc. | Paenibacillus and bacillus spp. mannanases |
US20170233710A1 (en) | 2014-10-17 | 2017-08-17 | Danisco Us Inc. | Serine proteases of bacillus species |
EP3212783A1 (en) | 2014-10-27 | 2017-09-06 | Danisco US Inc. | Serine proteases |
EP3224357A1 (en) | 2014-10-27 | 2017-10-04 | Danisco US Inc. | Serine proteases of bacillus species |
WO2016069563A1 (en) | 2014-10-27 | 2016-05-06 | Danisco Us Inc. | Serine proteases |
EP3212662B1 (en) | 2014-10-27 | 2020-04-08 | Danisco US Inc. | Serine proteases |
DK3212781T3 (da) | 2014-10-27 | 2019-12-16 | Danisco Us Inc | Serinproteaser |
EP3957729A1 (en) | 2014-10-27 | 2022-02-23 | Danisco US Inc. | Serine proteases |
US20180216090A1 (en) | 2015-03-12 | 2018-08-02 | Danisco Us Inc. | Compositions and methods comprising lg12-clade protease variants |
-
2016
- 2016-11-07 BR BR112018009050A patent/BR112018009050A8/pt active Search and Examination
- 2016-11-07 JP JP2018522947A patent/JP7364330B2/ja active Active
- 2016-11-07 WO PCT/US2016/060850 patent/WO2017079756A1/en active Application Filing
- 2016-11-07 US US15/773,340 patent/US20180320158A1/en not_active Abandoned
- 2016-11-07 EP EP16798334.5A patent/EP3371307A1/en active Pending
- 2016-11-07 CN CN201680077805.3A patent/CN108603183B/zh active Active
Also Published As
Publication number | Publication date |
---|---|
JP2019504616A (ja) | 2019-02-21 |
WO2017079756A1 (en) | 2017-05-11 |
BR112018009050A2 (pt) | 2018-11-06 |
EP3371307A1 (en) | 2018-09-12 |
BR112018009050A8 (pt) | 2019-02-26 |
CN108603183B (zh) | 2023-11-03 |
CN108603183A (zh) | 2018-09-28 |
US20180320158A1 (en) | 2018-11-08 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
JP7269907B2 (ja) | パエニバチルス(Paenibacillus)及びバチルス(Bacillus)種のマンナナーゼ | |
JP7364330B2 (ja) | パエニバチルス(Paenibacillus)属種及びバチルス(Bacillus)属種のマンナナーゼ | |
JP7364331B2 (ja) | パエニバチルス(Paenibacillus)属種マンナナーゼ | |
US8986970B2 (en) | Detergent compositions containing Bacillus agaradhaerens mannanase and methods of use thereof | |
US20140135252A1 (en) | Detergent compositions containing geobacillus tepidamans mannanase and methods of use thereof | |
US11866748B2 (en) | Compositions comprising polypeptides having mannanase activity | |
US20140073548A1 (en) | Detergent compositions containing bacillus sp. mannanase and methods of use thereof | |
CN111373036A (zh) | 具有甘露聚糖酶活性的多肽和编码它们的多核苷酸 | |
CN111417725A (zh) | 具有甘露聚糖酶活性的多肽和编码它们的多核苷酸 | |
CN103608356A (zh) | 包含黏琼脂芽孢杆菌(Bacillus agaradhaerens)甘露聚糖酶的洗涤剂组合物及其使用方法 | |
CN103502445A (zh) | 包含芽孢杆菌甘露聚糖酶的洗涤剂组合物及其使用方法 | |
CN103534266A (zh) | 包含喜温地芽孢杆菌(geobacillus tepidamans)甘露聚糖酶的洗涤剂组合物及其使用方法 | |
CN113056476A (zh) | 具有α-甘露聚糖降解活性的多肽以及编码它们的多核苷酸 | |
WO2024050339A1 (en) | Mannanase variants and methods of use |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20191031 |
|
A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20201006 |
|
A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20201223 |
|
A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20210308 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20210310 |
|
A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20210803 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20211203 |
|
C60 | Trial request (containing other claim documents, opposition documents) |
Free format text: JAPANESE INTERMEDIATE CODE: C60 Effective date: 20211203 |
|
A911 | Transfer to examiner for re-examination before appeal (zenchi) |
Free format text: JAPANESE INTERMEDIATE CODE: A911 Effective date: 20211213 |
|
C21 | Notice of transfer of a case for reconsideration by examiners before appeal proceedings |
Free format text: JAPANESE INTERMEDIATE CODE: C21 Effective date: 20211214 |
|
A912 | Re-examination (zenchi) completed and case transferred to appeal board |
Free format text: JAPANESE INTERMEDIATE CODE: A912 Effective date: 20220107 |
|
C211 | Notice of termination of reconsideration by examiners before appeal proceedings |
Free format text: JAPANESE INTERMEDIATE CODE: C211 Effective date: 20220118 |
|
C22 | Notice of designation (change) of administrative judge |
Free format text: JAPANESE INTERMEDIATE CODE: C22 Effective date: 20221206 |
|
RD03 | Notification of appointment of power of attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7423 Effective date: 20230220 |
|
A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20230802 |
|
A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20231005 |
|
R150 | Certificate of patent or registration of utility model |
Ref document number: 7364330 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |