LT3366B - Crosslinked crystals as a novel form of enzyme immobilization - Google Patents
Crosslinked crystals as a novel form of enzyme immobilization Download PDFInfo
- Publication number
- LT3366B LT3366B LTIP1077A LTIP1077A LT3366B LT 3366 B LT3366 B LT 3366B LT IP1077 A LTIP1077 A LT IP1077A LT IP1077 A LTIP1077 A LT IP1077A LT 3366 B LT3366 B LT 3366B
- Authority
- LT
- Lithuania
- Prior art keywords
- enzyme
- crystal
- cross
- clec
- hydrolase
- Prior art date
Links
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 258
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 258
- 239000013078 crystal Substances 0.000 title claims abstract description 160
- 238000000034 method Methods 0.000 claims abstract description 97
- 238000006243 chemical reaction Methods 0.000 claims abstract description 60
- 238000004132 cross linking Methods 0.000 claims abstract description 51
- 238000004519 manufacturing process Methods 0.000 claims abstract description 38
- 239000003153 chemical reaction reagent Substances 0.000 claims abstract description 13
- 229940088598 enzyme Drugs 0.000 claims description 254
- 108090001109 Thermolysin Proteins 0.000 claims description 111
- 230000000694 effects Effects 0.000 claims description 86
- 239000000758 substrate Substances 0.000 claims description 60
- 235000018102 proteins Nutrition 0.000 claims description 48
- 102000004169 proteins and genes Human genes 0.000 claims description 47
- 108090000623 proteins and genes Proteins 0.000 claims description 47
- 108090000371 Esterases Proteins 0.000 claims description 43
- 239000002904 solvent Substances 0.000 claims description 39
- 108090001060 Lipase Proteins 0.000 claims description 35
- 102000004882 Lipase Human genes 0.000 claims description 35
- 108010067372 Pancreatic elastase Proteins 0.000 claims description 35
- 102000016387 Pancreatic elastase Human genes 0.000 claims description 35
- 239000004367 Lipase Substances 0.000 claims description 33
- 235000019421 lipase Nutrition 0.000 claims description 33
- 108010024976 Asparaginase Proteins 0.000 claims description 32
- 102000015790 Asparaginase Human genes 0.000 claims description 32
- 102000016943 Muramidase Human genes 0.000 claims description 30
- 108010014251 Muramidase Proteins 0.000 claims description 30
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims description 30
- 229960003272 asparaginase Drugs 0.000 claims description 30
- DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 claims description 29
- 238000011534 incubation Methods 0.000 claims description 29
- 239000004325 lysozyme Substances 0.000 claims description 29
- 229960000274 lysozyme Drugs 0.000 claims description 29
- 235000010335 lysozyme Nutrition 0.000 claims description 29
- 229940040461 lipase Drugs 0.000 claims description 28
- 102000004157 Hydrolases Human genes 0.000 claims description 25
- 108090000604 Hydrolases Proteins 0.000 claims description 25
- 239000000126 substance Substances 0.000 claims description 20
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 19
- 239000012491 analyte Substances 0.000 claims description 17
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 16
- 230000003197 catalytic effect Effects 0.000 claims description 15
- 230000017854 proteolysis Effects 0.000 claims description 15
- 108060001084 Luciferase Proteins 0.000 claims description 14
- 239000005089 Luciferase Substances 0.000 claims description 13
- 229940024606 amino acid Drugs 0.000 claims description 12
- 235000001014 amino acid Nutrition 0.000 claims description 12
- 150000001413 amino acids Chemical class 0.000 claims description 11
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 10
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 9
- 239000000463 material Substances 0.000 claims description 9
- 235000019441 ethanol Nutrition 0.000 claims description 7
- 230000000977 initiatory effect Effects 0.000 claims description 7
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 claims description 6
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 claims description 6
- 229920000669 heparin Polymers 0.000 claims description 6
- 229960002897 heparin Drugs 0.000 claims description 6
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 5
- 108010059712 Pronase Proteins 0.000 claims description 5
- 229960001230 asparagine Drugs 0.000 claims description 5
- 239000004202 carbamide Substances 0.000 claims description 5
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims description 4
- BPYKTIZUTYGOLE-IFADSCNNSA-N Bilirubin Chemical compound N1C(=O)C(C)=C(C=C)\C1=C\C1=C(C)C(CCC(O)=O)=C(CC2=C(C(C)=C(\C=C/3C(=C(C=C)C(=O)N\3)C)N2)CCC(O)=O)N1 BPYKTIZUTYGOLE-IFADSCNNSA-N 0.000 claims description 4
- 235000009582 asparagine Nutrition 0.000 claims description 4
- 239000008103 glucose Substances 0.000 claims description 4
- 239000003791 organic solvent mixture Substances 0.000 claims description 4
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 claims description 3
- 229930006000 Sucrose Natural products 0.000 claims description 3
- 235000011054 acetic acid Nutrition 0.000 claims description 3
- 150000002823 nitrates Chemical class 0.000 claims description 3
- 150000002826 nitrites Chemical class 0.000 claims description 3
- 239000005720 sucrose Substances 0.000 claims description 3
- NBSCHQHZLSJFNQ-GASJEMHNSA-N D-Glucose 6-phosphate Chemical compound OC1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H](O)[C@H]1O NBSCHQHZLSJFNQ-GASJEMHNSA-N 0.000 claims description 2
- VFRROHXSMXFLSN-UHFFFAOYSA-N Glc6P Natural products OP(=O)(O)OCC(O)C(O)C(O)C(O)C=O VFRROHXSMXFLSN-UHFFFAOYSA-N 0.000 claims description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 claims description 2
- 229910019142 PO4 Inorganic materials 0.000 claims description 2
- 235000012000 cholesterol Nutrition 0.000 claims description 2
- 230000014759 maintenance of location Effects 0.000 claims description 2
- 150000003013 phosphoric acid derivatives Chemical class 0.000 claims description 2
- 150000003890 succinate salts Chemical class 0.000 claims description 2
- 150000003467 sulfuric acid derivatives Chemical class 0.000 claims description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 claims 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 claims 2
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 claims 2
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 claims 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 claims 2
- 229960000485 methotrexate Drugs 0.000 claims 2
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 claims 1
- 229930182555 Penicillin Natural products 0.000 claims 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 claims 1
- 239000013543 active substance Substances 0.000 claims 1
- 229910021529 ammonia Inorganic materials 0.000 claims 1
- 229960000510 ammonia Drugs 0.000 claims 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 claims 1
- 235000013877 carbamide Nutrition 0.000 claims 1
- 239000001569 carbon dioxide Substances 0.000 claims 1
- 229910002092 carbon dioxide Inorganic materials 0.000 claims 1
- 229940109239 creatinine Drugs 0.000 claims 1
- 235000019253 formic acid Nutrition 0.000 claims 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 claims 1
- 239000012092 media component Substances 0.000 claims 1
- 229940049954 penicillin Drugs 0.000 claims 1
- 235000021317 phosphate Nutrition 0.000 claims 1
- 229940045136 urea Drugs 0.000 claims 1
- 108010093096 Immobilized Enzymes Proteins 0.000 abstract description 25
- 238000004108 freeze drying Methods 0.000 abstract description 11
- 230000001588 bifunctional effect Effects 0.000 abstract description 4
- 230000003100 immobilizing effect Effects 0.000 abstract description 4
- 230000002255 enzymatic effect Effects 0.000 description 60
- 239000000047 product Substances 0.000 description 38
- 238000002425 crystallisation Methods 0.000 description 37
- 230000008025 crystallization Effects 0.000 description 37
- 239000003054 catalyst Substances 0.000 description 35
- 239000000243 solution Substances 0.000 description 32
- 230000015572 biosynthetic process Effects 0.000 description 24
- 239000003960 organic solvent Substances 0.000 description 23
- 238000011156 evaluation Methods 0.000 description 22
- 238000003786 synthesis reaction Methods 0.000 description 22
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 21
- 102000035195 Peptidases Human genes 0.000 description 20
- 108091005804 Peptidases Proteins 0.000 description 20
- 230000008569 process Effects 0.000 description 20
- 239000004365 Protease Substances 0.000 description 19
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 18
- 239000001639 calcium acetate Substances 0.000 description 18
- 235000011092 calcium acetate Nutrition 0.000 description 18
- 229960005147 calcium acetate Drugs 0.000 description 18
- 239000002253 acid Substances 0.000 description 17
- 238000009792 diffusion process Methods 0.000 description 16
- 238000003860 storage Methods 0.000 description 16
- JRGRHYPAYAJGAF-LBPRGKRZSA-N (2s)-2-[[2-[3-(furan-2-yl)prop-2-enoylamino]acetyl]amino]-4-methylpentanamide Chemical compound CC(C)C[C@@H](C(N)=O)NC(=O)CNC(=O)C=CC1=CC=CO1 JRGRHYPAYAJGAF-LBPRGKRZSA-N 0.000 description 15
- 239000007983 Tris buffer Substances 0.000 description 15
- 230000008901 benefit Effects 0.000 description 15
- 238000005119 centrifugation Methods 0.000 description 15
- 239000002245 particle Substances 0.000 description 15
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 15
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 14
- 239000000203 mixture Substances 0.000 description 14
- 235000019419 proteases Nutrition 0.000 description 14
- 108010011485 Aspartame Proteins 0.000 description 13
- 239000000605 aspartame Substances 0.000 description 13
- 229960003438 aspartame Drugs 0.000 description 13
- 235000010357 aspartame Nutrition 0.000 description 13
- 238000005516 engineering process Methods 0.000 description 13
- 230000001965 increasing effect Effects 0.000 description 13
- IAOZJIPTCAWIRG-QWRGUYRKSA-N aspartame Chemical compound OC(=O)C[C@H](N)C(=O)N[C@H](C(=O)OC)CC1=CC=CC=C1 IAOZJIPTCAWIRG-QWRGUYRKSA-N 0.000 description 12
- 238000002835 absorbance Methods 0.000 description 11
- 239000002609 medium Substances 0.000 description 11
- 239000000725 suspension Substances 0.000 description 11
- 239000004366 Glucose oxidase Substances 0.000 description 10
- 108010015776 Glucose oxidase Proteins 0.000 description 10
- 238000006555 catalytic reaction Methods 0.000 description 10
- 210000004027 cell Anatomy 0.000 description 10
- 229940116332 glucose oxidase Drugs 0.000 description 10
- 235000019420 glucose oxidase Nutrition 0.000 description 10
- 239000002243 precursor Substances 0.000 description 10
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 9
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 9
- -1 ethyl aspartame Chemical compound 0.000 description 9
- 210000004369 blood Anatomy 0.000 description 8
- 239000008280 blood Substances 0.000 description 8
- 238000005259 measurement Methods 0.000 description 8
- 239000011148 porous material Substances 0.000 description 8
- 239000011541 reaction mixture Substances 0.000 description 8
- 230000000707 stereoselective effect Effects 0.000 description 8
- 238000003756 stirring Methods 0.000 description 8
- 108010016626 Dipeptides Proteins 0.000 description 7
- 239000007864 aqueous solution Substances 0.000 description 7
- 230000015556 catabolic process Effects 0.000 description 7
- 238000006731 degradation reaction Methods 0.000 description 7
- 238000001514 detection method Methods 0.000 description 7
- 238000006911 enzymatic reaction Methods 0.000 description 7
- 230000007062 hydrolysis Effects 0.000 description 7
- 238000006460 hydrolysis reaction Methods 0.000 description 7
- 210000004185 liver Anatomy 0.000 description 7
- 239000012429 reaction media Substances 0.000 description 7
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 6
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 6
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 6
- 238000010521 absorption reaction Methods 0.000 description 6
- 150000007513 acids Chemical class 0.000 description 6
- 239000003125 aqueous solvent Substances 0.000 description 6
- 238000003776 cleavage reaction Methods 0.000 description 6
- 150000001875 compounds Chemical class 0.000 description 6
- 238000007796 conventional method Methods 0.000 description 6
- 230000036425 denaturation Effects 0.000 description 6
- 238000004925 denaturation Methods 0.000 description 6
- 239000012530 fluid Substances 0.000 description 6
- 238000004128 high performance liquid chromatography Methods 0.000 description 6
- 230000003993 interaction Effects 0.000 description 6
- 239000000543 intermediate Substances 0.000 description 6
- 230000000813 microbial effect Effects 0.000 description 6
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 6
- 230000007017 scission Effects 0.000 description 6
- 230000006641 stabilisation Effects 0.000 description 6
- 238000011105 stabilization Methods 0.000 description 6
- 241000511343 Chondrostoma nasus Species 0.000 description 5
- 241000588724 Escherichia coli Species 0.000 description 5
- 108010024026 Nitrile hydratase Proteins 0.000 description 5
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 5
- 239000012736 aqueous medium Substances 0.000 description 5
- 239000003431 cross linking reagent Substances 0.000 description 5
- 239000011549 crystallization solution Substances 0.000 description 5
- 238000001914 filtration Methods 0.000 description 5
- 238000002386 leaching Methods 0.000 description 5
- 239000013081 microcrystal Substances 0.000 description 5
- 238000002156 mixing Methods 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 230000009467 reduction Effects 0.000 description 5
- 230000000717 retained effect Effects 0.000 description 5
- 239000001632 sodium acetate Substances 0.000 description 5
- 235000017281 sodium acetate Nutrition 0.000 description 5
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 5
- 102000003992 Peroxidases Human genes 0.000 description 4
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 4
- 108010046334 Urease Proteins 0.000 description 4
- 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 4
- 239000000872 buffer Substances 0.000 description 4
- 239000012876 carrier material Substances 0.000 description 4
- 238000001311 chemical methods and process Methods 0.000 description 4
- 238000005112 continuous flow technique Methods 0.000 description 4
- 125000004122 cyclic group Chemical group 0.000 description 4
- 238000010908 decantation Methods 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 239000011521 glass Substances 0.000 description 4
- 210000001822 immobilized cell Anatomy 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 229910021645 metal ion Inorganic materials 0.000 description 4
- VSDUZFOSJDMAFZ-VIFPVBQESA-N methyl L-phenylalaninate Chemical compound COC(=O)[C@@H](N)CC1=CC=CC=C1 VSDUZFOSJDMAFZ-VIFPVBQESA-N 0.000 description 4
- 210000003205 muscle Anatomy 0.000 description 4
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 4
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 4
- 108040007629 peroxidase activity proteins Proteins 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 238000012552 review Methods 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- IHQKEDIOMGYHEB-UHFFFAOYSA-M sodium dimethylarsinate Chemical compound [Na+].C[As](C)([O-])=O IHQKEDIOMGYHEB-UHFFFAOYSA-M 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- 238000011282 treatment Methods 0.000 description 4
- YSCNREZXFSZAQO-ROUUACIJSA-N (3s)-4-[[(2s)-1-methoxy-1-oxo-3-phenylpropan-2-yl]amino]-4-oxo-3-(phenylmethoxycarbonylamino)butanoic acid Chemical compound C([C@@H](C(=O)OC)NC(=O)[C@H](CC(O)=O)NC(=O)OCC=1C=CC=CC=1)C1=CC=CC=C1 YSCNREZXFSZAQO-ROUUACIJSA-N 0.000 description 3
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 3
- 102000004092 Amidohydrolases Human genes 0.000 description 3
- 108090000531 Amidohydrolases Proteins 0.000 description 3
- 208000035404 Autolysis Diseases 0.000 description 3
- BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 description 3
- 206010057248 Cell death Diseases 0.000 description 3
- 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 3
- 102000002322 Egg Proteins Human genes 0.000 description 3
- 108010000912 Egg Proteins Proteins 0.000 description 3
- 241000196324 Embryophyta Species 0.000 description 3
- VZCYOOQTPOCHFL-OWOJBTEDSA-N Fumaric acid Chemical compound OC(=O)\C=C\C(O)=O VZCYOOQTPOCHFL-OWOJBTEDSA-N 0.000 description 3
- 244000168141 Geotrichum candidum Species 0.000 description 3
- 235000017388 Geotrichum candidum Nutrition 0.000 description 3
- 108010022901 Heparin Lyase Proteins 0.000 description 3
- 108010020056 Hydrogenase Proteins 0.000 description 3
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 3
- 102000004316 Oxidoreductases Human genes 0.000 description 3
- 108090000854 Oxidoreductases Proteins 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 239000011324 bead Substances 0.000 description 3
- 150000001720 carbohydrates Chemical class 0.000 description 3
- 235000014633 carbohydrates Nutrition 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 210000000991 chicken egg Anatomy 0.000 description 3
- 238000000502 dialysis Methods 0.000 description 3
- 210000003743 erythrocyte Anatomy 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 210000004907 gland Anatomy 0.000 description 3
- 230000001976 improved effect Effects 0.000 description 3
- 239000003317 industrial substance Substances 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 239000003456 ion exchange resin Substances 0.000 description 3
- 229920003303 ion-exchange polymer Polymers 0.000 description 3
- 239000003041 laboratory chemical Substances 0.000 description 3
- 210000004379 membrane Anatomy 0.000 description 3
- 230000003647 oxidation Effects 0.000 description 3
- 238000007254 oxidation reaction Methods 0.000 description 3
- 238000012856 packing Methods 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 102000004196 processed proteins & peptides Human genes 0.000 description 3
- 239000012460 protein solution Substances 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 230000035484 reaction time Effects 0.000 description 3
- 238000005057 refrigeration Methods 0.000 description 3
- 230000028043 self proteolysis Effects 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 3
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 2
- XYXYXSKSTZAEJW-VIFPVBQESA-N (2s)-2-(phenylmethoxycarbonylamino)butanedioic acid Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)OCC1=CC=CC=C1 XYXYXSKSTZAEJW-VIFPVBQESA-N 0.000 description 2
- YBADLXQNJCMBKR-UHFFFAOYSA-M (4-nitrophenyl)acetate Chemical compound [O-]C(=O)CC1=CC=C([N+]([O-])=O)C=C1 YBADLXQNJCMBKR-UHFFFAOYSA-M 0.000 description 2
- GVUGADOWXGKRAE-SRVKXCTJSA-N 4-[[(2s)-1-[[(2s)-1-[[(2s)-1-(4-nitroanilino)-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid Chemical compound OC(=O)CCC(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(=O)NC1=CC=C([N+]([O-])=O)C=C1 GVUGADOWXGKRAE-SRVKXCTJSA-N 0.000 description 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 2
- 108010025188 Alcohol oxidase Proteins 0.000 description 2
- 102000003677 Aldehyde-Lyases Human genes 0.000 description 2
- 108090000072 Aldehyde-Lyases Proteins 0.000 description 2
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 2
- 241000272517 Anseriformes Species 0.000 description 2
- 240000003291 Armoracia rusticana Species 0.000 description 2
- 235000011330 Armoracia rusticana Nutrition 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241000193830 Bacillus <bacterium> Species 0.000 description 2
- 244000063299 Bacillus subtilis Species 0.000 description 2
- 235000014469 Bacillus subtilis Nutrition 0.000 description 2
- 101000950981 Bacillus subtilis (strain 168) Catabolic NAD-specific glutamate dehydrogenase RocG Proteins 0.000 description 2
- 241000193389 Bacillus thermoproteolyticus Species 0.000 description 2
- 241000186146 Brevibacterium Species 0.000 description 2
- 102000016938 Catalase Human genes 0.000 description 2
- 108010053835 Catalase Proteins 0.000 description 2
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- 102000001390 Fructose-Bisphosphate Aldolase Human genes 0.000 description 2
- 108010068561 Fructose-Bisphosphate Aldolase Proteins 0.000 description 2
- 108010036781 Fumarate Hydratase Proteins 0.000 description 2
- 102100036160 Fumarate hydratase, mitochondrial Human genes 0.000 description 2
- 102000016901 Glutamate dehydrogenase Human genes 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-Phenylalanine Natural products OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- 102000004317 Lyases Human genes 0.000 description 2
- 108090000856 Lyases Proteins 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 108010085143 N-benzyloxycarbonyl-aspartylphenylalanine methyl ester Proteins 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 201000011252 Phenylketonuria Diseases 0.000 description 2
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 241001646398 Pseudomonas chlororaphis Species 0.000 description 2
- 241000589776 Pseudomonas putida Species 0.000 description 2
- 241000187747 Streptomyces Species 0.000 description 2
- 108090000787 Subtilisin Proteins 0.000 description 2
- 102000003425 Tyrosinase Human genes 0.000 description 2
- 108060008724 Tyrosinase Proteins 0.000 description 2
- 241000607598 Vibrio Species 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 230000010933 acylation Effects 0.000 description 2
- 238000005917 acylation reaction Methods 0.000 description 2
- 230000006978 adaptation Effects 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- 238000013019 agitation Methods 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 102000006635 beta-lactamase Human genes 0.000 description 2
- 244000309464 bull Species 0.000 description 2
- 229910001424 calcium ion Inorganic materials 0.000 description 2
- 201000011510 cancer Diseases 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000010382 chemical cross-linking Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000006482 condensation reaction Methods 0.000 description 2
- 238000011109 contamination Methods 0.000 description 2
- 238000001784 detoxification Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 201000010099 disease Diseases 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 238000004090 dissolution Methods 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 238000005538 encapsulation Methods 0.000 description 2
- 230000009088 enzymatic function Effects 0.000 description 2
- 230000005284 excitation Effects 0.000 description 2
- 230000007717 exclusion Effects 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 230000035876 healing Effects 0.000 description 2
- 239000004009 herbicide Substances 0.000 description 2
- WJRBRSLFGCUECM-UHFFFAOYSA-N hydantoin Chemical compound O=C1CNC(=O)N1 WJRBRSLFGCUECM-UHFFFAOYSA-N 0.000 description 2
- 229940091173 hydantoin Drugs 0.000 description 2
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 230000003907 kidney function Effects 0.000 description 2
- 238000009533 lab test Methods 0.000 description 2
- 238000011031 large-scale manufacturing process Methods 0.000 description 2
- 208000032839 leukemia Diseases 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 208000019423 liver disease Diseases 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 238000012423 maintenance Methods 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 150000002825 nitriles Chemical class 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 210000000496 pancreas Anatomy 0.000 description 2
- 229960005190 phenylalanine Drugs 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 102000040430 polynucleotide Human genes 0.000 description 2
- 108091033319 polynucleotide Proteins 0.000 description 2
- 239000002157 polynucleotide Substances 0.000 description 2
- 239000001103 potassium chloride Substances 0.000 description 2
- 235000011164 potassium chloride Nutrition 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 239000002994 raw material Substances 0.000 description 2
- 239000000376 reactant Substances 0.000 description 2
- 239000007974 sodium acetate buffer Substances 0.000 description 2
- 239000012064 sodium phosphate buffer Substances 0.000 description 2
- 230000004083 survival effect Effects 0.000 description 2
- 210000001519 tissue Anatomy 0.000 description 2
- VZCYOOQTPOCHFL-UHFFFAOYSA-N trans-butenedioic acid Natural products OC(=O)C=CC(O)=O VZCYOOQTPOCHFL-UHFFFAOYSA-N 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 238000000844 transformation Methods 0.000 description 2
- 210000002700 urine Anatomy 0.000 description 2
- NOOLISFMXDJSKH-KXUCPTDWSA-N (-)-Menthol Chemical compound CC(C)[C@@H]1CC[C@@H](C)C[C@H]1O NOOLISFMXDJSKH-KXUCPTDWSA-N 0.000 description 1
- BJEPYKJPYRNKOW-REOHCLBHSA-N (S)-malic acid Chemical compound OC(=O)[C@@H](O)CC(O)=O BJEPYKJPYRNKOW-REOHCLBHSA-N 0.000 description 1
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- KPGXRSRHYNQIFN-UHFFFAOYSA-L 2-oxoglutarate(2-) Chemical compound [O-]C(=O)CCC(=O)C([O-])=O KPGXRSRHYNQIFN-UHFFFAOYSA-L 0.000 description 1
- KPGXRSRHYNQIFN-UHFFFAOYSA-N 2-oxoglutaric acid Chemical compound OC(=O)CCC(=O)C(O)=O KPGXRSRHYNQIFN-UHFFFAOYSA-N 0.000 description 1
- GACDQMDRPRGCTN-KQYNXXCUSA-N 3'-phospho-5'-adenylyl sulfate Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OS(O)(=O)=O)[C@@H](OP(O)(O)=O)[C@H]1O GACDQMDRPRGCTN-KQYNXXCUSA-N 0.000 description 1
- HVYWMOMLDIMFJA-UHFFFAOYSA-N 3-cholesterol Natural products C1C=C2CC(O)CCC2(C)C2C1C1CCC(C(C)CCCC(C)C)C1(C)CC2 HVYWMOMLDIMFJA-UHFFFAOYSA-N 0.000 description 1
- 241000187843 Actinoplanes missouriensis Species 0.000 description 1
- 235000001674 Agaricus brunnescens Nutrition 0.000 description 1
- 108700023418 Amidases Proteins 0.000 description 1
- 102000004400 Aminopeptidases Human genes 0.000 description 1
- 108090000915 Aminopeptidases Proteins 0.000 description 1
- 241000611184 Amphora Species 0.000 description 1
- 102000004452 Arginase Human genes 0.000 description 1
- 108700024123 Arginases Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 208000034318 Argininemia Diseases 0.000 description 1
- 241000186063 Arthrobacter Species 0.000 description 1
- YZQCXOFQZKCETR-UWVGGRQHSA-N Asp-Phe Chemical compound OC(=O)C[C@H](N)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 YZQCXOFQZKCETR-UWVGGRQHSA-N 0.000 description 1
- 108700016171 Aspartate ammonia-lyases Proteins 0.000 description 1
- 241000228245 Aspergillus niger Species 0.000 description 1
- 201000001320 Atherosclerosis Diseases 0.000 description 1
- 241000193744 Bacillus amyloliquefaciens Species 0.000 description 1
- 241000193755 Bacillus cereus Species 0.000 description 1
- 108090000363 Bacterial Luciferases Proteins 0.000 description 1
- 102100026189 Beta-galactosidase Human genes 0.000 description 1
- 108020004256 Beta-lactamase Proteins 0.000 description 1
- 108010015428 Bilirubin oxidase Proteins 0.000 description 1
- 238000009010 Bradford assay Methods 0.000 description 1
- 206010006326 Breath odour Diseases 0.000 description 1
- TUFKXBSYCAKZAV-UHFFFAOYSA-N C.C.F Chemical compound C.C.F TUFKXBSYCAKZAV-UHFFFAOYSA-N 0.000 description 1
- UGTXMOXOBHBWNJ-VWMHFEHESA-N CC(C)[C@H](N)C(O)=O.C1=CC=C2NC=CC2=C1 Chemical compound CC(C)[C@H](N)C(O)=O.C1=CC=C2NC=CC2=C1 UGTXMOXOBHBWNJ-VWMHFEHESA-N 0.000 description 1
- 102000005701 Calcium-Binding Proteins Human genes 0.000 description 1
- 108010045403 Calcium-Binding Proteins Proteins 0.000 description 1
- 244000045232 Canavalia ensiformis Species 0.000 description 1
- 235000010520 Canavalia ensiformis Nutrition 0.000 description 1
- 241000222120 Candida <Saccharomycetales> Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 108090000209 Carbonic anhydrases Proteins 0.000 description 1
- 102000003846 Carbonic anhydrases Human genes 0.000 description 1
- 102000005367 Carboxypeptidases Human genes 0.000 description 1
- 108010006303 Carboxypeptidases Proteins 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
- 108010089254 Cholesterol oxidase Proteins 0.000 description 1
- 241000251730 Chondrichthyes Species 0.000 description 1
- 244000223760 Cinnamomum zeylanicum Species 0.000 description 1
- 206010010356 Congenital anomaly Diseases 0.000 description 1
- 102000004420 Creatine Kinase Human genes 0.000 description 1
- 108010042126 Creatine kinase Proteins 0.000 description 1
- 102000018832 Cytochromes Human genes 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- CKLJMWTZIZZHCS-UHFFFAOYSA-N D-OH-Asp Natural products OC(=O)C(N)CC(O)=O CKLJMWTZIZZHCS-UHFFFAOYSA-N 0.000 description 1
- KZSNJWFQEVHDMF-SCSAIBSYSA-N D-valine Chemical compound CC(C)[C@@H](N)C(O)=O KZSNJWFQEVHDMF-SCSAIBSYSA-N 0.000 description 1
- 229930182831 D-valine Natural products 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 208000005189 Embolism Diseases 0.000 description 1
- 241000588698 Erwinia Species 0.000 description 1
- 101710134988 Esterase-5 Proteins 0.000 description 1
- YTNIXZGTHTVJBW-SCRDCRAPSA-N FMNH2 Chemical compound OP(=O)(O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2NC2=C1NC(=O)NC2=O YTNIXZGTHTVJBW-SCRDCRAPSA-N 0.000 description 1
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 0.000 description 1
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 108010073324 Glutaminase Proteins 0.000 description 1
- 102000009127 Glutaminase Human genes 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Natural products NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 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
- 102000051366 Glycosyltransferases Human genes 0.000 description 1
- 108700023372 Glycosyltransferases Proteins 0.000 description 1
- 241001670157 Gymnura Species 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 description 1
- 241000257303 Hymenoptera Species 0.000 description 1
- 102000004195 Isomerases Human genes 0.000 description 1
- 108090000769 Isomerases Proteins 0.000 description 1
- 206010023138 Jaundice neonatal Diseases 0.000 description 1
- 229930194542 Keto Natural products 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- CKLJMWTZIZZHCS-UWTATZPHSA-N L-Aspartic acid Natural products OC(=O)[C@H](N)CC(O)=O CKLJMWTZIZZHCS-UWTATZPHSA-N 0.000 description 1
- 235000019766 L-Lysine Nutrition 0.000 description 1
- 229930195714 L-glutamate Natural products 0.000 description 1
- 102000003855 L-lactate dehydrogenase Human genes 0.000 description 1
- 108700023483 L-lactate dehydrogenases Proteins 0.000 description 1
- JVTAAEKCZFNVCJ-REOHCLBHSA-N L-lactic acid Chemical compound C[C@H](O)C(O)=O JVTAAEKCZFNVCJ-REOHCLBHSA-N 0.000 description 1
- 108010059881 Lactase Proteins 0.000 description 1
- 108010073450 Lactate 2-monooxygenase Proteins 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 241001599018 Melanogaster Species 0.000 description 1
- 235000006679 Mentha X verticillata Nutrition 0.000 description 1
- 235000002899 Mentha suaveolens Nutrition 0.000 description 1
- 235000001636 Mentha x rotundifolia Nutrition 0.000 description 1
- 102000016397 Methyltransferase Human genes 0.000 description 1
- 108060004795 Methyltransferase Proteins 0.000 description 1
- 241000235395 Mucor Species 0.000 description 1
- OVRNDRQMDRJTHS-CBQIKETKSA-N N-Acetyl-D-Galactosamine Chemical compound CC(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-CBQIKETKSA-N 0.000 description 1
- CJBIUUVHWWAIPX-VIVJKLKVSA-N N-[(3R,4R,5R,6R)-2,4,5-trihydroxy-6-(hydroxymethyl)-2-[(3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxan-3-yl]acetamide Chemical compound C1([C@H](O)[C@@H](O)[C@@H](O)[C@H](O1)CO)C1(O)[C@H](NC(C)=O)[C@@H](O)[C@@H](O)[C@H](O1)CO CJBIUUVHWWAIPX-VIVJKLKVSA-N 0.000 description 1
- MBLBDJOUHNCFQT-UHFFFAOYSA-N N-acetyl-D-galactosamine Natural products CC(=O)NC(C=O)C(O)C(O)C(O)CO MBLBDJOUHNCFQT-UHFFFAOYSA-N 0.000 description 1
- DMNDRHADQRHLGX-QZIVUABBSA-N N[C@@H](CCSC)C(=O)O.N[C@@H]([C@@H](C)CC)C(=O)O.N[C@@H](CS)C(=O)O Chemical compound N[C@@H](CCSC)C(=O)O.N[C@@H]([C@@H](C)CC)C(=O)O.N[C@@H](CS)C(=O)O DMNDRHADQRHLGX-QZIVUABBSA-N 0.000 description 1
- 201000006346 Neonatal Jaundice Diseases 0.000 description 1
- 108010033272 Nitrilase Proteins 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 235000019482 Palm oil Nutrition 0.000 description 1
- 108010087702 Penicillinase Proteins 0.000 description 1
- 241000228129 Penicillium janthinellum Species 0.000 description 1
- 108700023158 Phenylalanine ammonia-lyases Proteins 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108090001050 Phosphoric Diester Hydrolases Proteins 0.000 description 1
- 102000004861 Phosphoric Diester Hydrolases Human genes 0.000 description 1
- 241000588767 Proteus vulgaris Species 0.000 description 1
- 241000920685 Pseudomonas sp. 7A Species 0.000 description 1
- 235000004789 Rosa xanthina Nutrition 0.000 description 1
- 241000109329 Rosa xanthina Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 101150094640 Siae gene Proteins 0.000 description 1
- 244000300264 Spinacia oleracea Species 0.000 description 1
- 235000009337 Spinacia oleracea Nutrition 0.000 description 1
- 241000970854 Streptomyces violaceusniger Species 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 229910052776 Thorium Inorganic materials 0.000 description 1
- 102000003929 Transaminases Human genes 0.000 description 1
- 108090000340 Transaminases Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 206010053648 Vascular occlusion Diseases 0.000 description 1
- 244000195452 Wasabia japonica Species 0.000 description 1
- 235000000760 Wasabia japonica Nutrition 0.000 description 1
- 238000002441 X-ray diffraction Methods 0.000 description 1
- 101710204001 Zinc metalloprotease Proteins 0.000 description 1
- QUWBSOKSBWAQER-UHFFFAOYSA-N [C].O=C=O Chemical compound [C].O=C=O QUWBSOKSBWAQER-UHFFFAOYSA-N 0.000 description 1
- XPPVUWCDAAXHML-UHFFFAOYSA-N [Cl].CCC(O)=O Chemical class [Cl].CCC(O)=O XPPVUWCDAAXHML-UHFFFAOYSA-N 0.000 description 1
- 239000006096 absorbing agent Substances 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000001476 alcoholic effect Effects 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 239000003513 alkali Substances 0.000 description 1
- 102000005922 amidase Human genes 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 238000007098 aminolysis reaction Methods 0.000 description 1
- XKMRRTOUMJRJIA-UHFFFAOYSA-N ammonia nh3 Chemical compound N.N XKMRRTOUMJRJIA-UHFFFAOYSA-N 0.000 description 1
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 239000008122 artificial sweetener Substances 0.000 description 1
- 235000021311 artificial sweeteners Nutrition 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 229960005261 aspartic acid Drugs 0.000 description 1
- OGBUMNBNEWYMNJ-UHFFFAOYSA-N batilol Chemical class CCCCCCCCCCCCCCCCCCOCC(O)CO OGBUMNBNEWYMNJ-UHFFFAOYSA-N 0.000 description 1
- 125000001584 benzyloxycarbonyl group Chemical group C(=O)(OCC1=CC=CC=C1)* 0.000 description 1
- 239000002876 beta blocker Substances 0.000 description 1
- 229940097320 beta blocking agent Drugs 0.000 description 1
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 235000013361 beverage Nutrition 0.000 description 1
- 239000011942 biocatalyst Substances 0.000 description 1
- 230000000740 bleeding effect Effects 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 239000006172 buffering agent Substances 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 229920001429 chelating resin Polymers 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 230000003098 cholesteric effect Effects 0.000 description 1
- 208000020832 chronic kidney disease Diseases 0.000 description 1
- 208000022831 chronic renal failure syndrome Diseases 0.000 description 1
- 235000017803 cinnamon Nutrition 0.000 description 1
- 239000003240 coconut oil Substances 0.000 description 1
- 235000019864 coconut oil Nutrition 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 108010029444 creatinine deiminase Proteins 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 150000005690 diesters Chemical class 0.000 description 1
- 238000002050 diffraction method Methods 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 238000003912 environmental pollution Methods 0.000 description 1
- 238000002641 enzyme replacement therapy Methods 0.000 description 1
- 235000020774 essential nutrients Nutrition 0.000 description 1
- 230000032050 esterification Effects 0.000 description 1
- 238000005886 esterification reaction Methods 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 230000003090 exacerbative effect Effects 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000010408 film Substances 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- VZCYOOQTPOCHFL-OWOJBTEDSA-L fumarate(2-) Chemical class [O-]C(=O)\C=C\C([O-])=O VZCYOOQTPOCHFL-OWOJBTEDSA-L 0.000 description 1
- 239000001530 fumaric acid Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 229940045189 glucose-6-phosphate Drugs 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 108700014210 glycosyltransferase activity proteins Proteins 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000001631 haemodialysis Methods 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000000322 hemodialysis Effects 0.000 description 1
- 238000002615 hemofiltration Methods 0.000 description 1
- 230000002008 hemorrhagic effect Effects 0.000 description 1
- 230000002440 hepatic effect Effects 0.000 description 1
- 230000002363 herbicidal effect Effects 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 201000011286 hyperargininemia Diseases 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 238000003842 industrial chemical process Methods 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 239000002917 insecticide Substances 0.000 description 1
- 125000000468 ketone group Chemical group 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 229940116871 l-lactate Drugs 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 229940116108 lactase Drugs 0.000 description 1
- 238000007273 lactonization reaction Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 235000019626 lipase activity Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000000464 low-speed centrifugation Methods 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 235000018977 lysine Nutrition 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- SWVMLNPDTIFDDY-FVGYRXGTSA-N methyl (2s)-2-amino-3-phenylpropanoate;hydrochloride Chemical compound Cl.COC(=O)[C@@H](N)CC1=CC=CC=C1 SWVMLNPDTIFDDY-FVGYRXGTSA-N 0.000 description 1
- 239000013080 microcrystalline material Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004899 motility Effects 0.000 description 1
- VBEGHXKAFSLLGE-UHFFFAOYSA-N n-phenylnitramide Chemical compound [O-][N+](=O)NC1=CC=CC=C1 VBEGHXKAFSLLGE-UHFFFAOYSA-N 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 229920000620 organic polymer Polymers 0.000 description 1
- 239000012430 organic reaction media Substances 0.000 description 1
- 238000012261 overproduction Methods 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 230000020477 pH reduction Effects 0.000 description 1
- 239000002540 palm oil Substances 0.000 description 1
- 229950009506 penicillinase Drugs 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 210000004303 peritoneum Anatomy 0.000 description 1
- 150000002989 phenols Chemical class 0.000 description 1
- 125000000951 phenoxy group Chemical group [H]C1=C([H])C([H])=C(O*)C([H])=C1[H] 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
- UYWQUFXKFGHYNT-UHFFFAOYSA-N phenylmethyl ester of formic acid Natural products O=COCC1=CC=CC=C1 UYWQUFXKFGHYNT-UHFFFAOYSA-N 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 238000006068 polycondensation reaction Methods 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- ARQTVSWBVIWYSF-UHFFFAOYSA-N prop-2-enamide;prop-2-enenitrile Chemical compound C=CC#N.NC(=O)C=C ARQTVSWBVIWYSF-UHFFFAOYSA-N 0.000 description 1
- 235000019833 protease Nutrition 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 229940007042 proteus vulgaris Drugs 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000002728 pyrethroid Substances 0.000 description 1
- 150000004053 quinones Chemical class 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 230000001953 sensory effect Effects 0.000 description 1
- 230000021148 sequestering of metal ion Effects 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 238000007614 solvation Methods 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 150000003431 steroids Chemical class 0.000 description 1
- KDYFGRWQOYBRFD-UHFFFAOYSA-L succinate(2-) Chemical compound [O-]C(=O)CCC([O-])=O KDYFGRWQOYBRFD-UHFFFAOYSA-L 0.000 description 1
- 108010067016 succinyl-trialanine-4-nitroanilide Proteins 0.000 description 1
- 238000001149 thermolysis Methods 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 239000003440 toxic substance Substances 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
- 238000005809 transesterification reaction Methods 0.000 description 1
- 229960004799 tryptophan Drugs 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 208000021331 vascular occlusion disease Diseases 0.000 description 1
- 210000003462 vein Anatomy 0.000 description 1
- 239000000052 vinegar Substances 0.000 description 1
- 235000021419 vinegar Nutrition 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
- 150000003952 β-lactams Chemical class 0.000 description 1
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/531—Production of immunochemical test materials
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K5/00—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof
- C07K5/04—Peptides containing up to four amino acids in a fully defined sequence; Derivatives thereof containing only normal peptide links
- C07K5/06—Dipeptides
- C07K5/06104—Dipeptides with the first amino acid being acidic
- C07K5/06113—Asp- or Asn-amino acid
- C07K5/06121—Asp- or Asn-amino acid the second amino acid being aromatic or cycloaliphatic
- C07K5/0613—Aspartame
-
- 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
- C12N11/00—Carrier-bound or immobilised enzymes; Carrier-bound or immobilised microbial cells; Preparation thereof
-
- 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)
-
- 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)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
- C12N9/18—Carboxylic ester hydrolases (3.1.1)
- C12N9/20—Triglyceride splitting, e.g. by means of lipase
-
- 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)
- C12N9/2462—Lysozyme (3.2.1.17)
-
- 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)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/52—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea
- C12N9/54—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from bacteria or Archaea bacteria being Bacillus
-
- 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)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6448—Elastases, e.g. pancreatic elastase (3.4.21.36); leukocyte elastase (3.4.31.37)
-
- 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)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C12N9/80—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in linear amides (3.5.1)
-
- 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)
- C12N9/78—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5)
- C12N9/80—Hydrolases (3) acting on carbon to nitrogen bonds other than peptide bonds (3.5) acting on amide bonds in linear amides (3.5.1)
- C12N9/82—Asparaginase (3.5.1.1)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/001—Enzyme electrodes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/001—Enzyme electrodes
- C12Q1/002—Electrode membranes
- C12Q1/003—Functionalisation
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
- C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Biomedical Technology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
- Analytical Chemistry (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Cell Biology (AREA)
- Food Science & Technology (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Enzymes And Modification Thereof (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
- Crystals, And After-Treatments Of Crystals (AREA)
- Piezo-Electric Or Mechanical Vibrators, Or Delay Or Filter Circuits (AREA)
- Liquid Crystal Substances (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US56228090A | 1990-08-03 | 1990-08-03 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| LTIP1077A LTIP1077A (en) | 1995-04-25 |
| LT3366B true LT3366B (en) | 1995-07-25 |
Family
ID=24245600
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| LTIP1077A LT3366B (en) | 1990-08-03 | 1993-09-22 | Crosslinked crystals as a novel form of enzyme immobilization |
Country Status (25)
| Country | Link |
|---|---|
| EP (2) | EP0550450B1 (ro) |
| JP (2) | JPH05508549A (ro) |
| AT (2) | ATE240391T1 (ro) |
| AU (1) | AU662104B2 (ro) |
| BR (1) | BR9106732A (ro) |
| CA (1) | CA2087730C (ro) |
| CZ (1) | CZ12393A3 (ro) |
| DE (2) | DE69133258T2 (ro) |
| DK (2) | DK0861888T3 (ro) |
| ES (2) | ES2263187T3 (ro) |
| FI (1) | FI120099B (ro) |
| HU (2) | HUT65904A (ro) |
| IE (1) | IE912767A1 (ro) |
| IL (1) | IL99046A (ro) |
| LT (1) | LT3366B (ro) |
| LV (1) | LV10304B (ro) |
| MD (1) | MD1592B2 (ro) |
| NO (1) | NO930360L (ro) |
| PT (1) | PT98564B (ro) |
| RU (1) | RU2124052C1 (ro) |
| SG (1) | SG70966A1 (ro) |
| SK (1) | SK283185B6 (ro) |
| TJ (1) | TJ210R3 (ro) |
| UA (1) | UA27035C2 (ro) |
| WO (1) | WO1992002617A1 (ro) |
Families Citing this family (25)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5932212A (en) * | 1996-05-24 | 1999-08-03 | Altus Biologics, Inc. | Crosslinked protein crystal formulations and their use as catalysts in organic solvents |
| AU4738197A (en) * | 1996-09-24 | 1998-04-17 | Altus Biologics Inc. | Crosslinked protein crystals as universal separation media |
| US6140475A (en) * | 1997-04-11 | 2000-10-31 | Altus Biologics Inc. | Controlled dissolution crosslinked protein crystals |
| US6500933B1 (en) | 1997-09-05 | 2002-12-31 | Altus Biologics Inc. | Methods of preparing carbohydrate crosslinked glycoprotein crystals |
| DK1009759T3 (da) * | 1997-09-05 | 2008-08-04 | Altus Pharmaceuticals Inc | Carbohydrat-tværbundne glycoproteinkrystaller |
| US6979561B1 (en) | 1998-10-09 | 2005-12-27 | Gilead Sciences, Inc. | Non-homogeneous systems for the resolution of enantiomeric mixtures |
| GB9823334D0 (en) | 1998-10-23 | 1998-12-23 | Darwin Discovery Ltd | Enzyme coupling |
| JP2004523240A (ja) * | 2001-02-16 | 2004-08-05 | アイベックス テクノロジーズ | マトリックス安定化酵素結晶および使用方法 |
| US7241272B2 (en) | 2001-11-13 | 2007-07-10 | Baxter International Inc. | Method and composition for removing uremic toxins in dialysis processes |
| WO2005066341A1 (en) * | 2004-01-01 | 2005-07-21 | Council Of Scientific & Industrial Research | A method for the preparation of cross linked protein crystals |
| CA2560613C (en) | 2004-03-22 | 2015-11-24 | Solvay Pharmaceuticals Gmbh | Oral pharmaceutical compositions of lipase-containing products, in particular of pancreatin, containing surfactants |
| DK1809320T3 (da) | 2004-10-14 | 2010-11-15 | Cystic Fibrosis Foundation The | Præparater indeholdende lipase, protease og amylase til behandling af pankreatisk insufficiens |
| PL2278002T3 (pl) | 2005-07-29 | 2017-12-29 | Abbott Laboratories Gmbh | Pankreatyna o zmniejszonej zawartości wirusowej |
| US11266607B2 (en) | 2005-08-15 | 2022-03-08 | AbbVie Pharmaceuticals GmbH | Process for the manufacture and use of pancreatin micropellet cores |
| US9198871B2 (en) | 2005-08-15 | 2015-12-01 | Abbott Products Gmbh | Delayed release pancreatin compositions |
| US10072256B2 (en) | 2006-05-22 | 2018-09-11 | Abbott Products Gmbh | Process for separating and determining the viral load in a pancreatin sample |
| US8852904B2 (en) | 2009-05-22 | 2014-10-07 | Sanyo Foods Co., Ltd. | Protein complex having activity catalyzing asymmetric oxidation reaction and process for producing the same |
| DK2478005T3 (en) * | 2009-09-15 | 2015-02-16 | Ajinomoto Althea Inc | Protein a crystals and cross bound crystals and methods of use thereof |
| US9303255B2 (en) | 2010-08-26 | 2016-04-05 | Aisin Seiki Kabushiki Kaisha | Electrode having enzyme crystals immobilized thereon, method for producing electrode having enzyme crystals immobilized thereon, and biological fuel cell and biosensor provided with electrode having enzyme crystals immobilized thereon |
| CA2913476A1 (en) * | 2013-06-07 | 2014-12-11 | Allena Pharmaceuticals, Inc. | Compositions, methods, and devices for dialysis |
| US20180028454A1 (en) | 2015-02-04 | 2018-02-01 | Abbvie Inc. | Pharmaceutical compositions and methods of use thereof to treat pancreatic enzyme insufficiency |
| WO2018232273A1 (en) | 2017-06-15 | 2018-12-20 | The University Of Chicago | Methods and compositions for treating cancer |
| EP4199947A4 (en) | 2020-08-18 | 2024-10-16 | Onchilles Pharma, Inc. | Modified porcine pancreatic elastase proteins |
| WO2022085419A1 (ja) * | 2020-10-19 | 2022-04-28 | 不二製油グループ本社株式会社 | 酵素固定化用担体及びそれを用いた固定化酵素 |
| EP4504961A1 (en) * | 2022-04-07 | 2025-02-12 | Need4Health B.V. | Method for determining insulin dosage |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3664926A (en) | 1970-02-26 | 1972-05-23 | Merck & Co Inc | Crystallization of l-asparaginase |
| US4436925A (en) | 1977-01-27 | 1984-03-13 | Toyo Soda Manufacturing Co., Ltd. | Addition compound of dipeptide derivative and amino acid derivative |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4373023A (en) * | 1980-10-14 | 1983-02-08 | Massachusetts Institute Of Technology | Process for neutralizing heparin |
| DK182483A (da) * | 1982-04-23 | 1983-10-24 | Wako Pure Chem Ind Ltd | Fremgangsmaade til semi-syntese af humant insulin og alkalisk protease til anvendelse derved |
| US4411996A (en) * | 1982-06-30 | 1983-10-25 | Nabisco Brands, Inc. | Process for isomerizing glucose |
| EP0168487A1 (en) * | 1984-01-20 | 1986-01-22 | Eye Products Limited Partnership | Method for cleaning contact lenses |
| FR2566798B1 (fr) * | 1984-06-27 | 1986-12-12 | Centre Nat Rech Scient | Membrane porteuse de la luciferase pour le dosage de l'atp et son procede de production |
| US4650758A (en) * | 1984-09-21 | 1987-03-17 | Cetus Corporation | Stabilization of enzymes useful in the production of glucosone and other enzymatic processes |
| JPS6317691A (ja) * | 1986-07-09 | 1988-01-25 | Agency Of Ind Science & Technol | アスパルテ−ム製造用固定化酵素 |
| FI85285C (fi) * | 1988-05-13 | 1992-03-25 | Stabra Ag | Tvaerbundet, vattenoloesligt glukosisomeras och foerfarande foer framstaellning daerav. |
| US5010006A (en) * | 1988-08-11 | 1991-04-23 | Her Majesty The Queen In Right Of Canada As Represented By The National Research Council Of Canada | Lipase immdoilized by cross-linking with inert protein for glyceride synthesis |
-
1991
- 1991-07-30 AU AU83154/91A patent/AU662104B2/en not_active Expired
- 1991-07-30 ES ES98105856T patent/ES2263187T3/es not_active Expired - Lifetime
- 1991-07-30 EP EP91914256A patent/EP0550450B1/en not_active Expired - Lifetime
- 1991-07-30 DK DK98105856T patent/DK0861888T3/da active
- 1991-07-30 EP EP98105856A patent/EP0861888B1/en not_active Expired - Lifetime
- 1991-07-30 BR BR919106732A patent/BR9106732A/pt not_active Application Discontinuation
- 1991-07-30 CA CA002087730A patent/CA2087730C/en not_active Expired - Lifetime
- 1991-07-30 RU RU93005166A patent/RU2124052C1/ru active
- 1991-07-30 HU HU9300275A patent/HUT65904A/hu unknown
- 1991-07-30 JP JP91513405A patent/JPH05508549A/ja not_active Withdrawn
- 1991-07-30 AT AT91914256T patent/ATE240391T1/de not_active IP Right Cessation
- 1991-07-30 DE DE69133258T patent/DE69133258T2/de not_active Expired - Lifetime
- 1991-07-30 WO PCT/US1991/005415 patent/WO1992002617A1/en not_active Ceased
- 1991-07-30 SK SK59-93A patent/SK283185B6/sk not_active IP Right Cessation
- 1991-07-30 SG SG1996002857A patent/SG70966A1/en unknown
- 1991-07-30 ES ES91914256T patent/ES2199933T3/es not_active Expired - Lifetime
- 1991-07-30 AT AT98105856T patent/ATE323158T1/de not_active IP Right Cessation
- 1991-07-30 UA UA93002104A patent/UA27035C2/uk unknown
- 1991-07-30 DK DK91914256T patent/DK0550450T3/da active
- 1991-07-30 DE DE69133521T patent/DE69133521T2/de not_active Expired - Lifetime
- 1991-07-30 IE IE276791A patent/IE912767A1/en not_active IP Right Cessation
- 1991-08-01 IL IL9904691A patent/IL99046A/en not_active IP Right Cessation
- 1991-08-02 PT PT98564A patent/PT98564B/pt not_active IP Right Cessation
-
1993
- 1993-02-02 FI FI930454A patent/FI120099B/fi not_active IP Right Cessation
- 1993-02-02 NO NO93930360A patent/NO930360L/no not_active Application Discontinuation
- 1993-02-02 CZ CZ93123A patent/CZ12393A3/cs unknown
- 1993-06-30 LV LVP-93-807A patent/LV10304B/en unknown
- 1993-09-22 LT LTIP1077A patent/LT3366B/lt not_active IP Right Cessation
-
1994
- 1994-04-11 TJ TJ94000012A patent/TJ210R3/xx unknown
- 1994-07-14 MD MD94-0406A patent/MD1592B2/ro unknown
-
1995
- 1995-06-30 HU HU95P/P00666P patent/HU211521A9/hu unknown
-
2003
- 2003-05-26 JP JP2003148217A patent/JP2004000230A/ja not_active Withdrawn
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3664926A (en) | 1970-02-26 | 1972-05-23 | Merck & Co Inc | Crystallization of l-asparaginase |
| US4436925A (en) | 1977-01-27 | 1984-03-13 | Toyo Soda Manufacturing Co., Ltd. | Addition compound of dipeptide derivative and amino acid derivative |
Non-Patent Citations (29)
| Title |
|---|
| A. AKIYAMA ET AL.: "Enzymes in Organic Synthesis", CHEMTECH, 1988, pages 627 - 634 |
| A. M. KLIBANOV ET AL.: "Enzymatic Catalysis in Anhydrous Organic Solvent", TRENDS IN BIOCHEMICAL SCIENCES, 1989, pages 141 - 144, XP023568949, DOI: doi:10.1016/0968-0004(89)90146-1 |
| A. M. KLIBANOV: "Asymmetric transformations catalyzed by enzymes in organic solvents", ACC. CHEM. RES, 1990, pages 114 - 120, XP002073769, DOI: doi:10.1021/ar00172a004 |
| ALEKSEY ZAKS ET AL.: "Potentially commercial enzymatic processes for the fine and specialty chemical industries", TRENDS IN BIOTECHNOLOGY, 1988, pages 272 - 275 |
| C. C. F. BLAKE ET AL.: "Structure Of Lysozyme: A Fourier Map of the Electron Density at 6 A Resolution obtained by X-ray Diffraction", NATURE, 22 December 1962 (1962-12-22), pages 1173 |
| CH WONG: "Enzymatic catalysts in organic synthesis", SCIENCE, 1989, pages 1145 - 1152 |
| CW CARTER JR, CW CARTER: "Protein crystallization using incomplete factorial experiments", THE JOURNAL OF BIOLOGICAL CHEMISTRY, 1979, pages 12219 - 12223, XP055044544 |
| D. W. CELANDER, T. R. CECH: "Visualizing the higher order folding of a catalytic RNA molecule", SCIENCE, 1991, pages 401 - 407, XP001097281, DOI: doi:10.1126/science.1989074 |
| E. HALL: "Biosensors" |
| F. A. QUIOCHO, F. M. RICHARDS: "Enzyme behavior of carboxypeptidase-A in the solid state", BIOCHEMISTRY, 1967, pages 4062 - 4076 |
| FLORANTE A. QUIOCHO, FREDERIC M. RICHARDS: "INTERMOLECULAR CROSS LINKING OF A PROTEIN IN THE CRYSTALLINE STATE: CARBOXYPEPTIDASE-A", PROC. NATL. ACAD. SCI. USA, 1964, pages 833 - 839 |
| FRANCES C. BERNSTEIN ET AL.: "The protein data bank: A computer-based archival file for macromolecular structures", JOURNAL OF MOLECULAR BIOLOGY, 1977, pages 535 - 542 |
| G. LINDEBERG: "A Convenient Synthesis of Aspartame", J. CHEM. ED., 1987, pages 1062 - 1064 |
| GARY L. GILLILAND: "A biological macromolecule crystallization database: A basis for a crystallization strategy", JOURNAL OF CRYSTAL GROWTH, 1988, pages 51 - 59, XP028857647, DOI: doi:10.1016/0022-0248(88)90298-9 |
| J. B. JONES: "Enzymes in Organic Synthesis", TETRAHEDRON, 1986, pages 3351 - 3403, XP001319341 |
| J. TRAMPER: "Immobilizing biocatalysts for use in syntheses", TRENDS IN BIOTECHNOLOGY, 1985, pages 45 - 50, XP023595078, DOI: doi:10.1016/0167-7799(85)90058-7 |
| K. NAKANISHI ET AL.: "Continuous Synthesis of N-(Benzyloxycarbonyl)-L-Aspartyl-L-Phenylalanine Methyl Ester with Immobilized Thermolysin in an Organic Solvent", NATURE BIOTECHNOLOGY, 1985, pages 459 - 464, XP001319879 |
| K. OYAMA ET AL.: "Production of aspartame by immobilized thermolase", METHODS IN ENZYMOLOGY, 1987, pages 503 - 516 |
| L. SAWYER ET AL.: "The atomic structure of crystalline porcine pancreatic elastase at 2.5 A resolution: comparisons with the structure of alpha-chymotrypsin", J.MOL.BIOL., 1978, pages 137 - 208, XP024019619, DOI: doi:10.1016/0022-2836(78)90412-6 |
| M. KLEIN, R. LANGER: "Removal of asparagine", TRENDS IN BIOTECHNOLOGY, 1986, pages 179 - 185 |
| M.J. DANIELS: "Industrial operation of immobilized enzymes", METHODS IN ENZYMOLOGY, 1987, pages 371 - 379 |
| MCPHERSON A.: "Crystallization of macromolecules: general principles", METHODS IN ENZYMOLOGY, 1985, pages 112, XP009001314, DOI: doi:10.1016/0076-6879(85)14007-3 |
| R. A. LERNER, S. J. BENKOVIC, P. G. SCHULTZ: "At the crossroads of chemistry and immunology: catalytic antibodies", SCIENCE, 1991, pages 659 - 667, XP000220254, DOI: doi:10.1126/science.2024118 |
| R. HOLMES ET AL: "Structure of thermolysin refined at 1,6 A resolution", JOURNAL OF MOLECULAR BIOLOGY, 1982, pages 623 - 639, XP024013040, DOI: doi:10.1016/0022-2836(82)90319-9 |
| T. G. COOPER: "The Tools of Biochemistry", pages: 379 - 380 |
| T. H. MAUGH: "A Renewed Interest in Immobilized Enzymes", SCIENCE, 1984, pages 474 - 476, XP009011405, DOI: doi:10.1126/science.223.4635.474 |
| T. R. CECH: "RNA editing Worlds smallest introns", CELL, 1991, pages 667 - 669 |
| TORU NAGASAWA, HIDEAKI YAMADA: "Microbial transformations of nitriles", TRENDS IN BIOTECHNOLOGY, 1989, pages 153 - 158 |
| W. HARTMEIER: "Immobilized biocatalysts - From simple to complex systems", TRENDS IN BIOTECHNOLOGY, 1985, pages 149 - 153, XP023595341, DOI: doi:10.1016/0167-7799(85)90104-0 |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US5618710A (en) | Crosslinked enzyme crystals | |
| AU662104B2 (en) | Use of crosslinked crystals as a novel form of enzyme immobilization | |
| IE83874B1 (en) | Use of crosslinked crystals as a novel form of enzyme immobilization | |
| Chen et al. | A novel and efficient method for the immobilization of thermolysin using sodium chloride salting-in and consecutive microwave irradiation | |
| US5801022A (en) | Method of producing a product with crosslinked crystals of thermolysin | |
| IE85134B1 (en) | Use of Crosslinked Crystals as a Novel Form of Enzyme Immobilization | |
| Rai et al. | Production of D-amino acids using immobilized D-hydantoinase from lentil, Lens esculenta, seeds | |
| NZ264042A (en) | Crosslinked crystalline immobilized protein, biosensor containing the crosslinked protein crystal | |
| HK1012411B (en) | Use of crosslinked crystals as a novel form of enzyme immobilization | |
| HK1023362B (en) | Use of crosslinked crystals as a novel form of enzyme immobilization | |
| EP0367302A2 (en) | Process for semi-synthesis of human insulin, water-soluble cross-linked Achromobacter protease I for use therein and a process for preparing the same | |
| Inada et al. | Fibrin membrane endowed with biological function VI. Immobilization of multienzymes of urea cycle | |
| Hagiwara et al. | Fibrin membrane endowed with biological function VII. An approach to an artificial liver; Conversion of ammonia to urea invitro | |
| Vuolanto | Cross-linked protein crystal technology in bioseparation and biocatalytic applications | |
| Arya et al. | Pigeonpea (Cajanus cajan) urease immobilized on alginate beads, showing improved stability and operational parameters | |
| Al-Khafaji et al. | Immobilization of urease in gelatin beads for urea estimation | |
| LIU | ISOLATION, PURIFICATION, AND CHARACTERIZATION OF ESCHERICHIA COLI L-ASPARAGINASE | |
| LÁSZLÓ | SUPERVISOR: MÁRIA L. SIMON | |
| JPH055475B2 (ro) |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM9A | Lapsed patents |
Effective date: 20100922 |