CA1200518A - Process for preparing semisynthetic enzymes - Google Patents
Process for preparing semisynthetic enzymesInfo
- Publication number
- CA1200518A CA1200518A CA000432216A CA432216A CA1200518A CA 1200518 A CA1200518 A CA 1200518A CA 000432216 A CA000432216 A CA 000432216A CA 432216 A CA432216 A CA 432216A CA 1200518 A CA1200518 A CA 1200518A
- Authority
- CA
- Canada
- Prior art keywords
- protein
- inhibitor
- column
- milliliters
- native
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired
Links
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 70
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 70
- 238000004519 manufacturing process Methods 0.000 title description 3
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 231
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 231
- 239000003112 inhibitor Substances 0.000 claims abstract description 113
- 238000000034 method Methods 0.000 claims abstract description 88
- 230000008569 process Effects 0.000 claims abstract description 57
- 239000003431 cross linking reagent Substances 0.000 claims abstract description 28
- 229940125532 enzyme inhibitor Drugs 0.000 claims abstract description 23
- 239000002532 enzyme inhibitor Substances 0.000 claims abstract description 23
- 239000007787 solid Substances 0.000 claims abstract description 19
- 239000000243 solution Substances 0.000 claims description 140
- 230000000694 effects Effects 0.000 claims description 60
- 239000000758 substrate Substances 0.000 claims description 58
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 52
- 238000004132 cross linking Methods 0.000 claims description 21
- 239000003795 chemical substances by application Substances 0.000 claims description 19
- 239000007864 aqueous solution Substances 0.000 claims description 12
- 239000011543 agarose gel Substances 0.000 claims description 9
- 150000001720 carbohydrates Chemical class 0.000 claims description 8
- 238000002791 soaking Methods 0.000 claims description 6
- 230000003100 immobilizing effect Effects 0.000 claims description 5
- 150000007522 mineralic acids Chemical group 0.000 claims description 5
- 229910017053 inorganic salt Inorganic materials 0.000 claims description 3
- 239000003960 organic solvent Substances 0.000 claims description 3
- 239000012736 aqueous medium Substances 0.000 claims 4
- 125000000837 carbohydrate group Chemical group 0.000 claims 2
- 230000002255 enzymatic effect Effects 0.000 abstract description 22
- 230000004071 biological effect Effects 0.000 abstract description 3
- 235000018102 proteins Nutrition 0.000 description 176
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 66
- 102000035118 modified proteins Human genes 0.000 description 66
- 108091005573 modified proteins Proteins 0.000 description 66
- 229940088598 enzyme Drugs 0.000 description 65
- 229940098773 bovine serum albumin Drugs 0.000 description 62
- 238000002835 absorbance Methods 0.000 description 49
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 46
- 238000003556 assay Methods 0.000 description 40
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 34
- 239000007983 Tris buffer Substances 0.000 description 29
- 239000000872 buffer Substances 0.000 description 27
- YQDHCCVUYCIGSW-LBPRGKRZSA-N ethyl (2s)-2-benzamido-5-(diaminomethylideneamino)pentanoate Chemical compound NC(=N)NCCC[C@@H](C(=O)OCC)NC(=O)C1=CC=CC=C1 YQDHCCVUYCIGSW-LBPRGKRZSA-N 0.000 description 27
- 108090000371 Esterases Proteins 0.000 description 26
- 102100022624 Glucoamylase Human genes 0.000 description 25
- 239000011780 sodium chloride Substances 0.000 description 23
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 23
- CDBYLPFSWZWCQE-UHFFFAOYSA-L Sodium Carbonate Chemical compound [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 22
- 238000006243 chemical reaction Methods 0.000 description 22
- 239000007973 glycine-HCl buffer Substances 0.000 description 22
- 239000008367 deionised water Substances 0.000 description 21
- 229910021641 deionized water Inorganic materials 0.000 description 21
- 230000036425 denaturation Effects 0.000 description 20
- 238000004925 denaturation Methods 0.000 description 20
- 230000036961 partial effect Effects 0.000 description 20
- RSYYQCDERUOEFI-JTQLQIEISA-N N-benzoyl-L-arginine Chemical compound NC(=N)NCCC[C@@H](C(O)=O)NC(=O)C1=CC=CC=C1 RSYYQCDERUOEFI-JTQLQIEISA-N 0.000 description 17
- 230000008859 change Effects 0.000 description 17
- 239000011521 glass Substances 0.000 description 17
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 17
- 102000047352 Esterase-like Human genes 0.000 description 15
- 108700037229 Esterase-like Proteins 0.000 description 15
- 230000003134 recirculating effect Effects 0.000 description 15
- 102000016938 Catalase Human genes 0.000 description 13
- 108010053835 Catalase Proteins 0.000 description 13
- 239000000499 gel Substances 0.000 description 13
- 239000000126 substance Substances 0.000 description 13
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 12
- 239000008351 acetate buffer Substances 0.000 description 12
- -1 amino acid esters Chemical class 0.000 description 12
- 238000002360 preparation method Methods 0.000 description 12
- 239000012064 sodium phosphate buffer Substances 0.000 description 12
- 230000003197 catalytic effect Effects 0.000 description 11
- 238000004128 high performance liquid chromatography Methods 0.000 description 11
- 229910000029 sodium carbonate Inorganic materials 0.000 description 11
- 239000012153 distilled water Substances 0.000 description 10
- KCUNTYMNJVXYKZ-JTQLQIEISA-N methyl (2s)-2-amino-3-(1h-indol-3-yl)propanoate Chemical compound C1=CC=C2C(C[C@H](N)C(=O)OC)=CNC2=C1 KCUNTYMNJVXYKZ-JTQLQIEISA-N 0.000 description 10
- 239000011148 porous material Substances 0.000 description 10
- 239000007974 sodium acetate buffer Substances 0.000 description 10
- 238000004587 chromatography analysis Methods 0.000 description 9
- 238000002156 mixing Methods 0.000 description 9
- 108090000765 processed proteins & peptides Proteins 0.000 description 9
- IVLXQGJVBGMLRR-UHFFFAOYSA-N 2-aminoacetic acid;hydron;chloride Chemical compound Cl.NCC(O)=O IVLXQGJVBGMLRR-UHFFFAOYSA-N 0.000 description 8
- 108010047754 beta-Glucosidase Proteins 0.000 description 8
- 102000006995 beta-Glucosidase Human genes 0.000 description 8
- 230000015572 biosynthetic process Effects 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 239000011541 reaction mixture Substances 0.000 description 8
- 101000867659 Bos taurus Catalase Proteins 0.000 description 7
- 239000000356 contaminant Substances 0.000 description 7
- 230000000977 initiatory effect Effects 0.000 description 7
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 6
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 6
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 6
- GUBGYTABKSRVRQ-CUHNMECISA-N D-Cellobiose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-CUHNMECISA-N 0.000 description 6
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 6
- 239000004202 carbamide Substances 0.000 description 6
- 235000014633 carbohydrates Nutrition 0.000 description 6
- 150000002500 ions Chemical class 0.000 description 6
- 239000002245 particle Substances 0.000 description 6
- 239000000843 powder Substances 0.000 description 6
- 102000009027 Albumins Human genes 0.000 description 5
- 108010088751 Albumins Proteins 0.000 description 5
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- 235000014113 dietary fatty acids Nutrition 0.000 description 5
- ILKCDNKCNSNFMP-UHFFFAOYSA-N dimethyl octanediimidate;hydron;dichloride Chemical compound Cl.Cl.COC(=N)CCCCCCC(=N)OC ILKCDNKCNSNFMP-UHFFFAOYSA-N 0.000 description 5
- 229930195729 fatty acid Natural products 0.000 description 5
- 239000000194 fatty acid Substances 0.000 description 5
- 150000004665 fatty acids Chemical class 0.000 description 5
- 239000012634 fragment Substances 0.000 description 5
- 239000006225 natural substrate Substances 0.000 description 5
- 230000009897 systematic effect Effects 0.000 description 5
- WQZGKKKJIJFFOK-SVZMEOIVSA-N (+)-Galactose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-SVZMEOIVSA-N 0.000 description 4
- 101000760915 Delphinium grandiflorum Cyanidin 3-O-glucoside 7-O-glucosyltransferase (acyl-glucose) Proteins 0.000 description 4
- 101000760916 Dianthus caryophyllus Cyanidin 3-O-glucoside 5-O-glucosyltransferase (acyl-glucose) Proteins 0.000 description 4
- 108010015776 Glucose oxidase Proteins 0.000 description 4
- 239000004366 Glucose oxidase Substances 0.000 description 4
- 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 4
- 125000000539 amino acid group Chemical group 0.000 description 4
- 238000000502 dialysis Methods 0.000 description 4
- 229940031098 ethanolamine Drugs 0.000 description 4
- 229940116332 glucose oxidase Drugs 0.000 description 4
- 235000019420 glucose oxidase Nutrition 0.000 description 4
- 229930182478 glucoside Natural products 0.000 description 4
- 150000008131 glucosides Chemical class 0.000 description 4
- 150000004676 glycans Chemical class 0.000 description 4
- 229920001282 polysaccharide Polymers 0.000 description 4
- 239000005017 polysaccharide Substances 0.000 description 4
- BTJIUGUIPKRLHP-UHFFFAOYSA-N 4-nitrophenol Chemical compound OC1=CC=C([N+]([O-])=O)C=C1 BTJIUGUIPKRLHP-UHFFFAOYSA-N 0.000 description 3
- IFBHRQDFSNCLOZ-RMPHRYRLSA-N 4-nitrophenyl beta-D-glucoside Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1OC1=CC=C([N+]([O-])=O)C=C1 IFBHRQDFSNCLOZ-RMPHRYRLSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Natural products CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 102000004316 Oxidoreductases Human genes 0.000 description 3
- 108090000854 Oxidoreductases Proteins 0.000 description 3
- 108090000526 Papain Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 229920002684 Sepharose Polymers 0.000 description 3
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 235000001014 amino acid Nutrition 0.000 description 3
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 3
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 3
- 235000011130 ammonium sulphate Nutrition 0.000 description 3
- 230000015556 catabolic process Effects 0.000 description 3
- 239000000919 ceramic Substances 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
- 238000006731 degradation reaction Methods 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 239000012847 fine chemical Substances 0.000 description 3
- 238000012417 linear regression Methods 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- VIKNJXKGJWUCNN-XGXHKTLJSA-N norethisterone Chemical compound O=C1CC[C@@H]2[C@H]3CC[C@](C)([C@](CC4)(O)C#C)[C@@H]4[C@@H]3CCC2=C1 VIKNJXKGJWUCNN-XGXHKTLJSA-N 0.000 description 3
- 125000000636 p-nitrophenyl group Chemical group [H]C1=C([H])C(=C([H])C([H])=C1*)[N+]([O-])=O 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 229960004799 tryptophan Drugs 0.000 description 3
- WZYRMLAWNVOIEX-MOJAZDJTSA-N (2s)-2-[(2r,3r,4s)-3,4-dihydroxyoxolan-2-yl]-2-hydroxyacetaldehyde Chemical compound O=C[C@@H](O)[C@@H]1OC[C@H](O)[C@H]1O WZYRMLAWNVOIEX-MOJAZDJTSA-N 0.000 description 2
- DCQFFOLNJVGHLW-UHFFFAOYSA-N 4'-Me ether-Punctatin+ Natural products O1C(O)C(O)C2OCC1C2O DCQFFOLNJVGHLW-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 2
- 229920001503 Glucan Polymers 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 102000004366 Glucosidases Human genes 0.000 description 2
- 108010056771 Glucosidases Proteins 0.000 description 2
- CPLXHLVBOLITMK-UHFFFAOYSA-N Magnesium oxide Chemical compound [Mg]=O CPLXHLVBOLITMK-UHFFFAOYSA-N 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 102000035195 Peptidases Human genes 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- DKGAVHZHDRPRBM-UHFFFAOYSA-N Tert-Butanol Chemical compound CC(C)(C)O DKGAVHZHDRPRBM-UHFFFAOYSA-N 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 108010046334 Urease Proteins 0.000 description 2
- MCMNRKCIXSYSNV-UHFFFAOYSA-N Zirconium dioxide Chemical compound O=[Zr]=O MCMNRKCIXSYSNV-UHFFFAOYSA-N 0.000 description 2
- 108010028144 alpha-Glucosidases Proteins 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 230000008033 biological extinction Effects 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 2
- 238000006555 catalytic reaction Methods 0.000 description 2
- WZYRMLAWNVOIEX-UHFFFAOYSA-N cinnamtannin B-2 Natural products O=CC(O)C1OCC(O)C1O WZYRMLAWNVOIEX-UHFFFAOYSA-N 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- XBDQKXXYIPTUBI-UHFFFAOYSA-N dimethylselenoniopropionate Natural products CCC(O)=O XBDQKXXYIPTUBI-UHFFFAOYSA-N 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 2
- 125000000524 functional group Chemical group 0.000 description 2
- YVECGMZCTULTIS-PBXRRBTRSA-N glucal Chemical compound OC[C@H]1OC=C[C@@H](O)[C@@H]1O YVECGMZCTULTIS-PBXRRBTRSA-N 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 230000003301 hydrolyzing effect Effects 0.000 description 2
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical compound [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 108010043052 lysine monooxygenase Proteins 0.000 description 2
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
- 150000007524 organic acids Chemical class 0.000 description 2
- 229940055729 papain Drugs 0.000 description 2
- 235000019834 papain Nutrition 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- IOLCXVTUBQKXJR-UHFFFAOYSA-M potassium bromide Chemical compound [K+].[Br-] IOLCXVTUBQKXJR-UHFFFAOYSA-M 0.000 description 2
- FGIUAXJPYTZDNR-UHFFFAOYSA-N potassium nitrate Chemical compound [K+].[O-][N+]([O-])=O FGIUAXJPYTZDNR-UHFFFAOYSA-N 0.000 description 2
- 229940070376 protein Drugs 0.000 description 2
- 238000006722 reduction reaction Methods 0.000 description 2
- 239000011214 refractory ceramic Substances 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- FGDZQCVHDSGLHJ-UHFFFAOYSA-M rubidium chloride Chemical compound [Cl-].[Rb+] FGDZQCVHDSGLHJ-UHFFFAOYSA-M 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- JHJLBTNAGRQEKS-UHFFFAOYSA-M sodium bromide Chemical compound [Na+].[Br-] JHJLBTNAGRQEKS-UHFFFAOYSA-M 0.000 description 2
- VWDWKYIASSYTQR-UHFFFAOYSA-N sodium nitrate Chemical compound [Na+].[O-][N+]([O-])=O VWDWKYIASSYTQR-UHFFFAOYSA-N 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 230000002459 sustained effect Effects 0.000 description 2
- 125000003396 thiol group Chemical group [H]S* 0.000 description 2
- 239000012588 trypsin Substances 0.000 description 2
- 229960001322 trypsin Drugs 0.000 description 2
- RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 1
- SHKUUQIDMUMQQK-UHFFFAOYSA-N 2-[4-(oxiran-2-ylmethoxy)butoxymethyl]oxirane Chemical compound C1OC1COCCCCOCC1CO1 SHKUUQIDMUMQQK-UHFFFAOYSA-N 0.000 description 1
- MCLXKFUCPVGZEN-UHFFFAOYSA-N 4,6-dichloro-1,3,5-triazin-2-amine Chemical compound NC1=NC(Cl)=NC(Cl)=N1 MCLXKFUCPVGZEN-UHFFFAOYSA-N 0.000 description 1
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
- 102100036475 Alanine aminotransferase 1 Human genes 0.000 description 1
- 108010082126 Alanine transaminase Proteins 0.000 description 1
- 108090000531 Amidohydrolases Proteins 0.000 description 1
- 102000004092 Amidohydrolases Human genes 0.000 description 1
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- AKGWUHIOEVNNPC-LURJTMIESA-N Arg-OEt Chemical compound CCOC(=O)[C@@H](N)CCCNC(N)=N AKGWUHIOEVNNPC-LURJTMIESA-N 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
- 108010024976 Asparaginase Proteins 0.000 description 1
- 102000015790 Asparaginase Human genes 0.000 description 1
- 241000182988 Assa Species 0.000 description 1
- 108010004032 Bromelains Proteins 0.000 description 1
- 108010059892 Cellulase Proteins 0.000 description 1
- 102000003914 Cholinesterases Human genes 0.000 description 1
- 108090000322 Cholinesterases Proteins 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 102000018832 Cytochromes Human genes 0.000 description 1
- 108010052832 Cytochromes Proteins 0.000 description 1
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- BRLQWZUYTZBJKN-UHFFFAOYSA-N Epichlorohydrin Chemical compound ClCC1CO1 BRLQWZUYTZBJKN-UHFFFAOYSA-N 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 108090000270 Ficain Proteins 0.000 description 1
- 108010073324 Glutaminase Proteins 0.000 description 1
- 102000009127 Glutaminase Human genes 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 102000030789 Histidine Ammonia-Lyase Human genes 0.000 description 1
- 108700006308 Histidine ammonia-lyases Proteins 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 102000003820 Lipoxygenases Human genes 0.000 description 1
- 108090000128 Lipoxygenases Proteins 0.000 description 1
- 102100024295 Maltase-glucoamylase Human genes 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 108010059820 Polygalacturonase Proteins 0.000 description 1
- 101710151715 Protein 7 Proteins 0.000 description 1
- AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 1
- 108010083644 Ribonucleases Proteins 0.000 description 1
- 102000006382 Ribonucleases Human genes 0.000 description 1
- 108091006629 SLC13A2 Proteins 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 102100033220 Xanthine oxidase Human genes 0.000 description 1
- 108010093894 Xanthine oxidase Proteins 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000003929 acidic solution Substances 0.000 description 1
- 102000016679 alpha-Glucosidases Human genes 0.000 description 1
- PNEYBMLMFCGWSK-UHFFFAOYSA-N aluminium oxide Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 1
- 150000001412 amines Chemical class 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 238000004873 anchoring Methods 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000009697 arginine Nutrition 0.000 description 1
- 229960003272 asparaginase Drugs 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-M asparaginate Chemical compound [O-]C(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-M 0.000 description 1
- 239000012298 atmosphere Substances 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 108010049595 benzoylarginine ethyl esterase Proteins 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 230000003592 biomimetic effect Effects 0.000 description 1
- 230000002051 biphasic effect Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 108010089934 carbohydrase Proteins 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000003054 catalyst Substances 0.000 description 1
- 229940106157 cellulase Drugs 0.000 description 1
- 239000013043 chemical agent Substances 0.000 description 1
- 229940048961 cholinesterase Drugs 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 235000015165 citric acid Nutrition 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000006114 decarboxylation reaction Methods 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 230000009144 enzymatic modification Effects 0.000 description 1
- 238000001952 enzyme assay Methods 0.000 description 1
- 150000002148 esters Chemical class 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 108010093305 exopolygalacturonase Proteins 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 235000019985 fermented beverage Nutrition 0.000 description 1
- POTUGHMKJGOKRI-UHFFFAOYSA-N ficin Chemical compound FI=CI=N POTUGHMKJGOKRI-UHFFFAOYSA-N 0.000 description 1
- 235000019836 ficin Nutrition 0.000 description 1
- 239000012467 final product Substances 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 235000012041 food component Nutrition 0.000 description 1
- 239000005428 food component Substances 0.000 description 1
- 235000019253 formic acid Nutrition 0.000 description 1
- 229960002163 hydrogen peroxide Drugs 0.000 description 1
- MHAJPDPJQMAIIY-UHFFFAOYSA-N hydrogen peroxide Substances OO MHAJPDPJQMAIIY-UHFFFAOYSA-N 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 230000002427 irreversible effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 108010059345 keratinase Proteins 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 239000000395 magnesium oxide Substances 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 238000007833 oxidative deamination reaction Methods 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 235000010333 potassium nitrate Nutrition 0.000 description 1
- ZNNZYHKDIALBAK-UHFFFAOYSA-M potassium thiocyanate Chemical compound [K+].[S-]C#N ZNNZYHKDIALBAK-UHFFFAOYSA-M 0.000 description 1
- 239000002244 precipitate Substances 0.000 description 1
- 238000004321 preservation Methods 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 235000019260 propionic acid Nutrition 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000005086 pumping Methods 0.000 description 1
- IUVKMZGDUIUOCP-BTNSXGMBSA-N quinbolone Chemical compound O([C@H]1CC[C@H]2[C@H]3[C@@H]([C@]4(C=CC(=O)C=C4CC3)C)CC[C@@]21C)C1=CCCC1 IUVKMZGDUIUOCP-BTNSXGMBSA-N 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000005057 refrigeration Methods 0.000 description 1
- IOVGROKTTNBUGK-SJCJKPOMSA-N ritodrine Chemical compound N([C@@H](C)[C@H](O)C=1C=CC(O)=CC=1)CCC1=CC=C(O)C=C1 IOVGROKTTNBUGK-SJCJKPOMSA-N 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- ACECBHHKGNTVPB-UHFFFAOYSA-N silylformic acid Chemical group OC([SiH3])=O ACECBHHKGNTVPB-UHFFFAOYSA-N 0.000 description 1
- 238000005245 sintering Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 229910000033 sodium borohydride Inorganic materials 0.000 description 1
- 239000012279 sodium borohydride Substances 0.000 description 1
- 235000010344 sodium nitrate Nutrition 0.000 description 1
- VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000010183 spectrum analysis Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 229920001059 synthetic polymer Polymers 0.000 description 1
- 238000010998 test method Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- ZCUFMDLYAMJYST-UHFFFAOYSA-N thorium dioxide Chemical compound O=[Th]=O ZCUFMDLYAMJYST-UHFFFAOYSA-N 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 239000013638 trimer Substances 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2408—Glucanases acting on alpha -1,4-glucosidic bonds
- C12N9/2411—Amylases
- C12N9/2428—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
-
- 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
-
- 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)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2405—Glucanases
- C12N9/2434—Glucanases acting on beta-1,4-glucosidic bonds
- C12N9/2445—Beta-glucosidase (3.2.1.21)
-
- 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)
- C12Y302/01003—Glucan 1,4-alpha-glucosidase (3.2.1.3), i.e. glucoamylase
-
- 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)
- C12Y302/01021—Beta-glucosidase (3.2.1.21)
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Medicinal Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Enzymes And Modification Thereof (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US41888482A | 1982-09-16 | 1982-09-16 | |
| US418,884 | 1982-09-16 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA1200518A true CA1200518A (en) | 1986-02-11 |
Family
ID=23659947
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA000432216A Expired CA1200518A (en) | 1982-09-16 | 1983-07-11 | Process for preparing semisynthetic enzymes |
Country Status (8)
| Country | Link |
|---|---|
| JP (1) | JPS5966884A (enrdf_load_stackoverflow) |
| AU (1) | AU539729B2 (enrdf_load_stackoverflow) |
| CA (1) | CA1200518A (enrdf_load_stackoverflow) |
| DE (1) | DE3329659A1 (enrdf_load_stackoverflow) |
| FR (1) | FR2533217B1 (enrdf_load_stackoverflow) |
| GB (1) | GB2127025B (enrdf_load_stackoverflow) |
| IT (1) | IT1171852B (enrdf_load_stackoverflow) |
| MX (1) | MX7645E (enrdf_load_stackoverflow) |
Family Cites Families (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5325030B2 (enrdf_load_stackoverflow) * | 1972-12-19 | 1978-07-24 | ||
| US4001085A (en) * | 1973-09-10 | 1977-01-04 | Owens-Illinois, Inc. | Immobilization of enzymes on an inorganic matrix |
| US4716116A (en) * | 1980-12-04 | 1987-12-29 | Owens-Illinois Glass Container Inc. | Protein modification to provide enzyme activity |
-
1983
- 1983-05-12 AU AU14507/83A patent/AU539729B2/en not_active Ceased
- 1983-05-27 GB GB08314852A patent/GB2127025B/en not_active Expired
- 1983-07-11 CA CA000432216A patent/CA1200518A/en not_active Expired
- 1983-07-20 IT IT48717/83A patent/IT1171852B/it active
- 1983-08-17 DE DE19833329659 patent/DE3329659A1/de active Granted
- 1983-08-30 JP JP58157263A patent/JPS5966884A/ja active Granted
- 1983-09-15 MX MX83948U patent/MX7645E/es unknown
- 1983-09-15 FR FR8314696A patent/FR2533217B1/fr not_active Expired
Also Published As
| Publication number | Publication date |
|---|---|
| MX7645E (es) | 1990-05-30 |
| DE3329659C2 (enrdf_load_stackoverflow) | 1987-08-13 |
| DE3329659A1 (de) | 1984-03-22 |
| GB2127025B (en) | 1986-01-15 |
| AU1450783A (en) | 1984-05-17 |
| JPS5966884A (ja) | 1984-04-16 |
| GB8314852D0 (en) | 1983-07-06 |
| FR2533217B1 (fr) | 1987-01-30 |
| IT8348717A0 (it) | 1983-07-20 |
| GB2127025A (en) | 1984-04-04 |
| AU539729B2 (en) | 1984-10-11 |
| JPS613478B2 (enrdf_load_stackoverflow) | 1986-02-01 |
| FR2533217A1 (fr) | 1984-03-23 |
| IT1171852B (it) | 1987-06-10 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US3519538A (en) | Chemically coupled enzymes | |
| CA1040561A (en) | Cyanogen halide activation of carbohydrates and protein binding thereto | |
| US3802997A (en) | Method of stabilizing enzymes | |
| Wingard Jr | Enzyme engineering | |
| Ke et al. | On enzymatic activity in organic solvents as a function of enzyme history | |
| Anderson et al. | Bovine enterokinase. Purification, specificity, and some molecular properties | |
| Sinha et al. | Refolding of reduced, denatured trypsinogen and trypsin immobilized on Agarose beads. | |
| Tulsiani et al. | Rat liver microsomal and lysosomal beta-glucuronidases differ in both carbohydrate and amino acid compositions. | |
| Janolino et al. | Catalytic effect of sulfhydryl oxidase on the formation of three-dimensional structure in chymotrypsinogen A | |
| Turner et al. | Effect of hydration on thermostability | |
| Orth et al. | Carrier‐Bound Biologically Active Substances and Their Applications | |
| Araujo et al. | Polyvinyl alcohol-glutaraldehyde network as a support for protein immobilisation | |
| Bowers et al. | Characterization of immobilized β-glucuronidase in aqueous and mixed solvent systems | |
| US4716116A (en) | Protein modification to provide enzyme activity | |
| Turkova | Affinity chromatography | |
| US4609625A (en) | Process for the production of modified proteins and product thereof | |
| Sulkowski et al. | Venom exonuclease (phosphodiesterase) immobilized on concanavalin-A-sepharose | |
| US4714677A (en) | Protein modification to provide enzyme activity | |
| CA1200518A (en) | Process for preparing semisynthetic enzymes | |
| US4714676A (en) | Protein modification to provide enzyme activity | |
| EP0128975B1 (en) | Biologically active conjugates and their preparation and use | |
| Shepherd et al. | α-d-Mannosidase. Preparation and properties of free and insolubilized enzyme | |
| US4713335A (en) | Protein modification to provide enzyme activity | |
| GB2127024A (en) | Modified proteins and process for the production thereof | |
| Dixon et al. | Immobilized lactate dehydrogenases |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MKEX | Expiry |