JPS6225036B2 - - Google Patents
Info
- Publication number
- JPS6225036B2 JPS6225036B2 JP56088319A JP8831981A JPS6225036B2 JP S6225036 B2 JPS6225036 B2 JP S6225036B2 JP 56088319 A JP56088319 A JP 56088319A JP 8831981 A JP8831981 A JP 8831981A JP S6225036 B2 JPS6225036 B2 JP S6225036B2
- Authority
- JP
- Japan
- Prior art keywords
- bacillus
- debranching enzyme
- enzyme
- activity
- strain
- 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 claims abstract description 102
- 108090000790 Enzymes Proteins 0.000 claims abstract description 102
- 241001134780 Bacillus acidopullulyticus Species 0.000 claims abstract description 5
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 34
- 230000000694 effects Effects 0.000 claims description 29
- 108090000637 alpha-Amylases Proteins 0.000 claims description 26
- 238000000034 method Methods 0.000 claims description 24
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 21
- 238000004519 manufacturing process Methods 0.000 claims description 8
- 230000001580 bacterial effect Effects 0.000 claims description 7
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 claims description 6
- 238000011534 incubation Methods 0.000 claims description 6
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims description 5
- 239000008351 acetate buffer Substances 0.000 claims description 5
- 229910052799 carbon Inorganic materials 0.000 claims description 5
- 150000003839 salts Chemical class 0.000 claims description 4
- 229910052757 nitrogen Inorganic materials 0.000 claims description 3
- 235000015097 nutrients Nutrition 0.000 claims description 3
- HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 claims 1
- 238000001502 gel electrophoresis Methods 0.000 claims 1
- 229920000728 polyester Polymers 0.000 claims 1
- 239000000126 substance Substances 0.000 claims 1
- 108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 abstract description 29
- 102100022624 Glucoamylase Human genes 0.000 abstract description 28
- 229920002472 Starch Polymers 0.000 abstract description 26
- 235000019698 starch Nutrition 0.000 abstract description 26
- 239000008107 starch Substances 0.000 abstract description 25
- 230000007062 hydrolysis Effects 0.000 abstract description 12
- 238000006460 hydrolysis reaction Methods 0.000 abstract description 12
- 229940088598 enzyme Drugs 0.000 description 94
- 239000008121 dextrose Substances 0.000 description 22
- 239000000047 product Substances 0.000 description 19
- 239000000758 substrate Substances 0.000 description 19
- 239000000243 solution Substances 0.000 description 15
- 229920000945 Amylopectin Polymers 0.000 description 14
- 238000000855 fermentation Methods 0.000 description 14
- 230000004151 fermentation Effects 0.000 description 14
- 229920001218 Pullulan Polymers 0.000 description 10
- 239000004373 Pullulan Substances 0.000 description 10
- 235000019423 pullulan Nutrition 0.000 description 10
- 235000020357 syrup Nutrition 0.000 description 10
- 239000006188 syrup Substances 0.000 description 10
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 10
- 108010019077 beta-Amylase Proteins 0.000 description 9
- 238000006243 chemical reaction Methods 0.000 description 9
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 9
- 239000007787 solid Substances 0.000 description 9
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 8
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 8
- 239000008186 active pharmaceutical agent Substances 0.000 description 8
- 210000004027 cell Anatomy 0.000 description 8
- 235000008504 concentrate Nutrition 0.000 description 8
- 239000012141 concentrate Substances 0.000 description 8
- 239000008367 deionised water Substances 0.000 description 8
- 229910021641 deionized water Inorganic materials 0.000 description 8
- 239000002609 medium Substances 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 239000011541 reaction mixture Substances 0.000 description 8
- 108010028688 Isoamylase Proteins 0.000 description 7
- 229920002774 Maltodextrin Polymers 0.000 description 7
- 239000005913 Maltodextrin Substances 0.000 description 7
- 239000000872 buffer Substances 0.000 description 7
- 239000003795 chemical substances by application Substances 0.000 description 7
- 239000008103 glucose Substances 0.000 description 7
- 229940035034 maltodextrin Drugs 0.000 description 7
- 244000005700 microbiome Species 0.000 description 7
- 238000011160 research Methods 0.000 description 7
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 6
- 230000012010 growth Effects 0.000 description 6
- 102000004139 alpha-Amylases Human genes 0.000 description 5
- 229940024171 alpha-amylase Drugs 0.000 description 5
- 238000000760 immunoelectrophoresis Methods 0.000 description 5
- 239000007788 liquid Substances 0.000 description 5
- 229920001817 Agar Polymers 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 4
- 239000002253 acid Substances 0.000 description 4
- 239000008272 agar Substances 0.000 description 4
- 239000007640 basal medium Substances 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 230000000813 microbial effect Effects 0.000 description 4
- 235000018102 proteins Nutrition 0.000 description 4
- 102000004169 proteins and genes Human genes 0.000 description 4
- 108090000623 proteins and genes Proteins 0.000 description 4
- 239000004382 Amylase Substances 0.000 description 3
- 108010065511 Amylases Proteins 0.000 description 3
- 102000013142 Amylases Human genes 0.000 description 3
- 108060003951 Immunoglobulin Proteins 0.000 description 3
- 241000589516 Pseudomonas Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 235000019418 amylase Nutrition 0.000 description 3
- 229940041514 candida albicans extract Drugs 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 238000001962 electrophoresis Methods 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 102000018358 immunoglobulin Human genes 0.000 description 3
- 239000007981 phosphate-citrate buffer Substances 0.000 description 3
- NLKNQRATVPKPDG-UHFFFAOYSA-M potassium iodide Chemical compound [K+].[I-] NLKNQRATVPKPDG-UHFFFAOYSA-M 0.000 description 3
- 239000002002 slurry Substances 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- 239000007921 spray Substances 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- 239000012138 yeast extract Substances 0.000 description 3
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 241000194108 Bacillus licheniformis Species 0.000 description 2
- 229920002261 Corn starch Polymers 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
- 229920001353 Dextrin Polymers 0.000 description 2
- 239000004375 Dextrin Substances 0.000 description 2
- 241000588747 Klebsiella pneumoniae Species 0.000 description 2
- 241000533950 Leucojum Species 0.000 description 2
- IOVCWXUNBOPUCH-UHFFFAOYSA-M Nitrite anion Chemical compound [O-]N=O IOVCWXUNBOPUCH-UHFFFAOYSA-M 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- RVGRUAULSDPKGF-UHFFFAOYSA-N Poloxamer Chemical compound C1CO1.CC1CO1 RVGRUAULSDPKGF-UHFFFAOYSA-N 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 240000008042 Zea mays Species 0.000 description 2
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 2
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 2
- GZCGUPFRVQAUEE-SLPGGIOYSA-N aldehydo-D-glucose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O GZCGUPFRVQAUEE-SLPGGIOYSA-N 0.000 description 2
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 2
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 238000011109 contamination Methods 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 235000005822 corn Nutrition 0.000 description 2
- 239000008120 corn starch Substances 0.000 description 2
- 235000019425 dextrin Nutrition 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 238000006047 enzymatic hydrolysis reaction Methods 0.000 description 2
- 239000006167 equilibration buffer Substances 0.000 description 2
- 239000000835 fiber Substances 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 230000003301 hydrolyzing effect Effects 0.000 description 2
- 230000003053 immunization Effects 0.000 description 2
- 239000012133 immunoprecipitate Substances 0.000 description 2
- 229910052740 iodine Inorganic materials 0.000 description 2
- 239000011630 iodine Substances 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 230000000877 morphologic effect Effects 0.000 description 2
- 229920001542 oligosaccharide Polymers 0.000 description 2
- 150000002482 oligosaccharides Chemical class 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000012266 salt solution Substances 0.000 description 2
- 230000001954 sterilising effect Effects 0.000 description 2
- 238000004659 sterilization and disinfection Methods 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000008399 tap water Substances 0.000 description 2
- 235000020679 tap water Nutrition 0.000 description 2
- 108010075550 termamyl Proteins 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 239000012137 tryptone Substances 0.000 description 2
- GHCZTIFQWKKGSB-UHFFFAOYSA-N 2-hydroxypropane-1,2,3-tricarboxylic acid;phosphoric acid Chemical compound OP(O)(O)=O.OC(=O)CC(O)(C(O)=O)CC(O)=O GHCZTIFQWKKGSB-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 102000016938 Catalase Human genes 0.000 description 1
- 108010053835 Catalase Proteins 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 229920002271 DEAE-Sepharose Polymers 0.000 description 1
- 102000002322 Egg Proteins Human genes 0.000 description 1
- 108010000912 Egg Proteins Proteins 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- DKNPRRRKHAEUMW-UHFFFAOYSA-N Iodine aqueous Chemical compound [K+].I[I-]I DKNPRRRKHAEUMW-UHFFFAOYSA-N 0.000 description 1
- 239000005909 Kieselgur Substances 0.000 description 1
- 241000588915 Klebsiella aerogenes Species 0.000 description 1
- 240000003183 Manihot esculenta Species 0.000 description 1
- 235000016735 Manihot esculenta subsp esculenta Nutrition 0.000 description 1
- XBDQKXXYIPTUBI-UHFFFAOYSA-M Propionate Chemical compound CCC([O-])=O XBDQKXXYIPTUBI-UHFFFAOYSA-M 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 238000010793 Steam injection (oil industry) Methods 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 150000001242 acetic acid derivatives Chemical class 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 230000009603 aerobic growth Effects 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 230000009604 anaerobic growth Effects 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 230000000469 anti-sperm effect Effects 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- PYMYPHUHKUWMLA-WDCZJNDASA-N arabinose Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)C=O PYMYPHUHKUWMLA-WDCZJNDASA-N 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- WPYMKLBDIGXBTP-UHFFFAOYSA-N benzoic acid Chemical compound OC(=O)C1=CC=CC=C1 WPYMKLBDIGXBTP-UHFFFAOYSA-N 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
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
- 238000005842 biochemical reaction Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 239000005018 casein Substances 0.000 description 1
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 1
- 235000021240 caseins Nutrition 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 229920002301 cellulose acetate Polymers 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 239000012531 culture fluid Substances 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 1
- 229910000397 disodium phosphate Inorganic materials 0.000 description 1
- 235000019800 disodium phosphate Nutrition 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 235000013345 egg yolk Nutrition 0.000 description 1
- 210000002969 egg yolk Anatomy 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 230000007071 enzymatic hydrolysis Effects 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 230000008020 evaporation Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 235000013312 flour Nutrition 0.000 description 1
- 230000004907 flux Effects 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 230000000984 immunochemical effect Effects 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- FDZZZRQASAIRJF-UHFFFAOYSA-M malachite green Chemical compound [Cl-].C1=CC(N(C)C)=CC=C1C(C=1C=CC=CC=1)=C1C=CC(=[N+](C)C)C=C1 FDZZZRQASAIRJF-UHFFFAOYSA-M 0.000 description 1
- 229940107698 malachite green Drugs 0.000 description 1
- VZCYOOQTPOCHFL-UPHRSURJSA-N maleic acid Chemical compound OC(=O)\C=C/C(O)=O VZCYOOQTPOCHFL-UPHRSURJSA-N 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000006916 nutrient agar Substances 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000002135 phase contrast microscopy Methods 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 238000012805 post-processing Methods 0.000 description 1
- 229920001592 potato starch Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 238000011085 pressure filtration Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000012216 screening Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- VZCYOOQTPOCHFL-UHFFFAOYSA-N trans-butenedioic acid Natural products OC(=O)C=CC(O)=O VZCYOOQTPOCHFL-UHFFFAOYSA-N 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000002255 vaccination Methods 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
- C12N9/2451—Glucanases acting on alpha-1,6-glucosidic bonds
-
- 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
- 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
- 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
- C12N9/2451—Glucanases acting on alpha-1,6-glucosidic bonds
- C12N9/2457—Pullulanase (3.2.1.41)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/16—Preparation of compounds containing saccharide radicals produced by the action of an alpha-1, 6-glucosidase, e.g. amylose, debranched amylopectin
-
- 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)
- C12Y302/01041—Pullulanase (3.2.1.41)
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Biomedical Technology (AREA)
- Medicinal Chemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Fodder In General (AREA)
- Breeding Of Plants And Reproduction By Means Of Culturing (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Detergent Compositions (AREA)
- Immobilizing And Processing Of Enzymes And Microorganisms (AREA)
- Jellies, Jams, And Syrups (AREA)
- Saccharide Compounds (AREA)
- Compounds Of Unknown Constitution (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US25595281A | 1981-04-20 | 1981-04-20 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS57174089A JPS57174089A (en) | 1982-10-26 |
| JPS6225036B2 true JPS6225036B2 (OSRAM) | 1987-06-01 |
Family
ID=22970517
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP56088319A Granted JPS57174089A (en) | 1981-04-20 | 1981-06-10 | Chain dividing enzyme product |
| JP60174391A Pending JPS6143994A (ja) | 1981-04-20 | 1985-08-09 | 枝切り酵素製品 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP60174391A Pending JPS6143994A (ja) | 1981-04-20 | 1985-08-09 | 枝切り酵素製品 |
Country Status (18)
| Country | Link |
|---|---|
| EP (1) | EP0063909B2 (OSRAM) |
| JP (2) | JPS57174089A (OSRAM) |
| KR (1) | KR890002413B1 (OSRAM) |
| AT (1) | ATE28216T1 (OSRAM) |
| AU (1) | AU548122B2 (OSRAM) |
| BE (1) | BE892904A (OSRAM) |
| CA (1) | CA1199292A (OSRAM) |
| CH (1) | CH659825A5 (OSRAM) |
| DE (1) | DE3276707D1 (OSRAM) |
| DK (1) | DK153569C (OSRAM) |
| ES (2) | ES511504A0 (OSRAM) |
| FI (1) | FI79345C (OSRAM) |
| FR (1) | FR2504148A1 (OSRAM) |
| GB (1) | GB2097405B (OSRAM) |
| IE (1) | IE53031B1 (OSRAM) |
| IN (1) | IN155660B (OSRAM) |
| IT (1) | IT1190780B (OSRAM) |
| MX (1) | MX174149B (OSRAM) |
Families Citing this family (79)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS58183092A (ja) * | 1982-04-19 | 1983-10-26 | ノボ・インダストリ・アクテイ−ゼルスカブ | 枝切り酵素 |
| CA1211314A (en) * | 1983-05-20 | 1986-09-16 | William F. Line | Production of dextrose and maltose syrups using an enzyme derived from rice |
| EP0140410B2 (en) * | 1983-09-11 | 1996-12-04 | Gist-Brocades N.V. | Novel enzyme product and its use in the saccharification of starch |
| JPS60186283A (ja) * | 1984-03-07 | 1985-09-21 | Agency Of Ind Science & Technol | 微生物による新規な耐熱性プルラナ−ゼａの製造法 |
| US4673633A (en) * | 1984-06-28 | 1987-06-16 | Cooperbiomedical, Inc. | Method of determining cystic fibrosis ciliostatic factor |
| US4628028A (en) * | 1985-05-23 | 1986-12-09 | Cpc International Inc. | Novel thermostable pullulanase enzyme and method for its production |
| GB8609288D0 (en) * | 1986-04-16 | 1986-05-21 | Ici Plc | Debranching enzyme |
| US5234823A (en) * | 1986-06-30 | 1993-08-10 | Novo Industri A/S | Chimeric enzymes |
| US5055403A (en) * | 1989-06-26 | 1991-10-08 | Enzyme Bio-Systems, Ltd. | Thermoduric and aciduric pullulanase enzyme and method for its production |
| EP0405283A3 (en) * | 1989-06-26 | 1991-03-06 | Enzyme Bio-Systems Ltd. | Novel thermoduric and aciduric pullulanase enzyme and method for its production |
| DK47291D0 (da) * | 1991-03-15 | 1991-03-15 | Novo Nordisk As | Pullulanase |
| JPH05236959A (ja) * | 1992-02-28 | 1993-09-17 | Yoshiyuki Takasaki | プルラナーゼ、その製造法及び該酵素を用いる澱粉の 糖化法 |
| FR2688800B1 (fr) * | 1992-03-19 | 1995-06-16 | Roquette Freres | Procede de preparation de polysaccharides peu digestibles, eventuellement hydrogenes. |
| ATE183236T1 (de) * | 1992-12-28 | 1999-08-15 | Genencor Int | Pullulanase, mikroorganismen die sie produzieren, verfahren zur herstellung und ihre anwendung |
| BE1006483A3 (fr) * | 1992-12-28 | 1994-09-13 | Solvay | Pullulanase, microorganismes la produisant, procedes de preparation de cette pullulanase, utilisations et compositions comprenant celle-ci. |
| CA2186592C (en) | 1994-03-29 | 2008-02-19 | Helle Outtrup | Alkaline bacillus amylase |
| AR000862A1 (es) | 1995-02-03 | 1997-08-06 | Novozymes As | Variantes de una ó-amilasa madre, un metodo para producir la misma, una estructura de adn y un vector de expresion, una celula transformada por dichaestructura de adn y vector, un aditivo para detergente, composicion detergente, una composicion para lavado de ropa y una composicion para la eliminacion del |
| ES2432519T3 (es) | 1996-04-30 | 2013-12-04 | Novozymes A/S | Mutantes de alfa-amilasa |
| KR20010015754A (ko) | 1997-10-13 | 2001-02-26 | 한센 핀 베네드, 안네 제헤르, 웨이콥 마리안느 | α-아밀라제 변이체 |
| ES2515218T3 (es) | 1997-10-30 | 2014-10-29 | Novozymes A/S | Mutantes de alfa-amilasa |
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| EP1975229A3 (en) | 2000-10-13 | 2009-03-18 | Novozymes A/S | Alpha-amylase variant with altered properties |
| EP2264160A3 (en) | 2001-05-15 | 2011-08-31 | Novozymes A/S | Alpha-amylase variant with altered properties |
| AU2004252572B2 (en) | 2003-06-25 | 2011-09-08 | Novozymes A/S | Polypeptides having alpha-amylase activity and polypeptides encoding same |
| EP4269684A3 (en) | 2004-07-05 | 2024-02-21 | Novozymes A/S | Alpha-amylase variants with altered properties |
| WO2006012899A1 (en) | 2004-08-02 | 2006-02-09 | Novozymes A/S | Maltogenic alpha-amylase variants |
| US20080280328A1 (en) | 2005-11-18 | 2008-11-13 | Novozymes A/S | Glucoamylase Variants |
| US8206966B2 (en) | 2007-11-05 | 2012-06-26 | Danisco Us Inc. | Alpha-amylase variants with altered properties |
| CN101848985B (zh) | 2007-11-05 | 2014-12-03 | 丹尼斯科美国公司 | 具有改变性质的杆菌物种TS-23的α-淀粉酶变体 |
| BRPI0908768A2 (pt) | 2008-02-04 | 2015-07-28 | Danisco Us Inc | Variantes de olfa-amilase de ts23 com propriedades alteradas |
| PL2447361T3 (pl) | 2008-06-06 | 2015-03-31 | Danisco Us Inc | Warianty alfa-amylazy (AMYS) z Geobacillus stearothermophilus o poprawionych właściwościach |
| MX2011003178A (es) | 2008-09-25 | 2011-04-21 | Danisco Inc | Mezclas de alfa-amilasa y metodos para usar esas mezclas. |
| EP2414514B1 (en) | 2009-04-01 | 2015-05-27 | Danisco US Inc. | Compositions and methods comprising alpha-amylase variants with altered properties |
| US8545907B2 (en) | 2009-08-07 | 2013-10-01 | Danisco Us Inc. | Alpha-amylase blend for starch processing and method of use thereof |
| WO2011076123A1 (en) | 2009-12-22 | 2011-06-30 | Novozymes A/S | Compositions comprising boosting polypeptide and starch degrading enzyme and uses thereof |
| US20120270267A1 (en) | 2010-01-04 | 2012-10-25 | Novozymes A/S | Alpha-Amylases |
| EP2357220A1 (en) | 2010-02-10 | 2011-08-17 | The Procter & Gamble Company | Cleaning composition comprising amylase variants with high stability in the presence of a chelating agent |
| EP3404087A1 (en) | 2010-02-10 | 2018-11-21 | Novozymes A/S | Alpha-amylase variants with high stability in presence of a chelating agent |
| JP6204352B2 (ja) | 2011-06-30 | 2017-09-27 | ノボザイムス アクティーゼルスカブ | α−アミラーゼ変異体 |
| WO2013048700A1 (en) | 2011-09-29 | 2013-04-04 | Danisco Us Inc. | Liquefaction and saccharification of granular starch at high concentration |
| EP2748316B1 (en) | 2011-10-17 | 2018-12-19 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding same |
| CA2852601C (en) | 2011-10-17 | 2023-05-23 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding same |
| WO2013148152A1 (en) | 2012-03-28 | 2013-10-03 | Danisco Us Inc. | Method for making high maltose syrup |
| WO2014028434A2 (en) | 2012-08-16 | 2014-02-20 | Danisco Us Inc. | Method of using alpha-amylase from aspergillus clavatus and pullulanase for saccharification |
| WO2014092960A1 (en) | 2012-12-11 | 2014-06-19 | Danisco Us Inc. | Trichoderma reesei host cells expressing a glucoamylase from aspergillus fumigatus and methods of use thereof |
| CN104903461A (zh) | 2012-12-20 | 2015-09-09 | 丹尼斯科美国公司 | 将支链淀粉酶和来自土曲霉的α-淀粉酶用于糖化的方法 |
| CA2915336C (en) | 2013-07-17 | 2024-03-12 | Novozymes A/S | Pullulanase chimeras and polynucleotides encoding same |
| CN105960457B (zh) | 2014-01-22 | 2021-09-03 | 诺维信公司 | 普鲁兰酶变体以及编码它们的多核苷酸 |
| WO2015143144A1 (en) | 2014-03-19 | 2015-09-24 | Novozymes A/S | Method for enhancing activity of an x143 polypeptide |
| EP3550015B1 (en) | 2014-04-10 | 2021-11-10 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding same |
| WO2016062875A2 (en) | 2014-10-23 | 2016-04-28 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| WO2016087327A1 (en) | 2014-12-01 | 2016-06-09 | Novozymes A/S | Polypeptides having pullulanase activity comprising the x25, x45 and cbm41 domains |
| US10494685B2 (en) | 2015-10-14 | 2019-12-03 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| JP7626576B2 (ja) | 2015-12-30 | 2025-02-07 | ノボザイムス アクティーゼルスカブ | 酵素変異体およびこれをコードするポリヌクレオチド |
| WO2017191160A1 (en) | 2016-05-03 | 2017-11-09 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding the same |
| EP3455352A1 (en) | 2016-05-09 | 2019-03-20 | Novozymes A/S | Variant polypeptides with improved performance and use of the same |
| BR112018077458A2 (pt) | 2016-06-30 | 2019-04-02 | Danisco Us Inc. | proteases aspárticas |
| ES2884155T3 (es) | 2016-07-21 | 2021-12-10 | Novozymes As | Variantes de serina proteasa y polinucleótidos que codifican las mismas |
| DK3487996T5 (da) | 2016-07-21 | 2024-09-02 | Novozymes As | Serinproteasevarianter og polynukleotider, der koder for samme |
| EP3272767B1 (en) | 2016-07-21 | 2020-11-25 | Fornia BioSolutions, Inc. | G24 glucoamylase compositions and methods |
| WO2018017105A1 (en) | 2016-07-21 | 2018-01-25 | Fornia Biosolutions, Inc. | G24 glucoamylase compositions and methods |
| US9598680B1 (en) | 2016-08-05 | 2017-03-21 | Fornia Biosolutions, Inc. | G16 glucoamylase compositions and methods |
| WO2018102348A1 (en) | 2016-11-29 | 2018-06-07 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding same |
| EP3558026B1 (en) | 2016-12-21 | 2025-10-15 | International N&H Denmark ApS | Methods of using thermostable serine proteases |
| EP3596210A1 (en) | 2017-03-15 | 2020-01-22 | DuPont Nutrition Biosciences ApS | Trypsin-like serine proteases and uses thereof cross-reference to related application |
| DK3596211T3 (da) | 2017-03-15 | 2021-09-06 | Dupont Nutrition Biosci Aps | Fremgangsmåder til anvendelse af en archaea-serinprotease |
| EP3610027A1 (en) | 2017-04-11 | 2020-02-19 | Novozymes A/S | Glucoamylase variants and polynucleotides encoding same |
| BR112020003866A2 (pt) | 2017-08-30 | 2020-09-08 | Novozymes A/S | processo para produção de um produto de fermentação, e, composição. |
| ES2954431T3 (es) | 2017-12-08 | 2023-11-22 | Novozymes As | Variantes de alfa-amilasa y polinucleótidos que codifican las mismas |
| US11326153B2 (en) | 2017-12-08 | 2022-05-10 | Novozymes A/S | Alpha-amylase variants and polynucleotides encoding same |
| MX2020010526A (es) | 2018-04-09 | 2021-01-08 | Novozymes As | Polipéptidos que tienen actividad alfa-amilasa ypolinucleótidos que los codifican. |
| CN111757931B (zh) | 2018-12-21 | 2023-11-28 | 福尼亚生物处理股份有限公司 | 变体g6p g7p葡糖淀粉酶组合物及方法 |
| MX2021011287A (es) | 2019-03-21 | 2021-10-13 | Novozymes As | Variantes de alfa-amilasa y polinucleotidos que codifican las mismas. |
| MX2022009515A (es) | 2020-02-10 | 2022-09-02 | Novozymes As | Variantes de alfa-amilasa y polinucleotidos que las codifican. |
Family Cites Families (7)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3565765A (en) * | 1966-12-27 | 1971-02-23 | Cpc International Inc | Preparation of high maltose conversion products |
| US3827940A (en) * | 1968-04-01 | 1974-08-06 | Hayashibara Co | Preparation of alpha-1,6-glucosidase |
| JPS543937B1 (OSRAM) * | 1968-11-18 | 1979-02-28 | ||
| JPS543938B1 (OSRAM) * | 1968-11-26 | 1979-02-28 | ||
| JPS529739B1 (OSRAM) * | 1969-04-09 | 1977-03-18 | ||
| JPS536232B2 (OSRAM) * | 1974-01-11 | 1978-03-06 | ||
| US4011139A (en) * | 1974-11-26 | 1977-03-08 | Standard Brands Incorporated | Process for producing α-1,6 glucosidases using thermophilic microorganisms |
-
1981
- 1981-06-10 JP JP56088319A patent/JPS57174089A/ja active Granted
-
1982
- 1982-04-19 EP EP82302001A patent/EP0063909B2/en not_active Expired - Lifetime
- 1982-04-19 FI FI821355A patent/FI79345C/fi not_active IP Right Cessation
- 1982-04-19 CA CA000401249A patent/CA1199292A/en not_active Expired
- 1982-04-19 AT AT82302001T patent/ATE28216T1/de not_active IP Right Cessation
- 1982-04-19 ES ES511504A patent/ES511504A0/es active Granted
- 1982-04-19 DK DK172882A patent/DK153569C/da not_active IP Right Cessation
- 1982-04-19 KR KR8201726A patent/KR890002413B1/ko not_active Expired
- 1982-04-19 IE IE907/82A patent/IE53031B1/en not_active IP Right Cessation
- 1982-04-19 BE BE6/47645A patent/BE892904A/fr not_active IP Right Cessation
- 1982-04-19 IT IT20806/82A patent/IT1190780B/it active
- 1982-04-19 GB GB8211280A patent/GB2097405B/en not_active Expired
- 1982-04-19 AU AU82808/82A patent/AU548122B2/en not_active Ceased
- 1982-04-19 DE DE8282302001T patent/DE3276707D1/de not_active Expired
- 1982-04-20 FR FR8206786A patent/FR2504148A1/fr active Granted
- 1982-04-20 IN IN434/CAL/82A patent/IN155660B/en unknown
- 1982-04-20 CH CH2393/82A patent/CH659825A5/de not_active IP Right Cessation
- 1982-04-20 MX MX026679A patent/MX174149B/es unknown
-
1983
- 1983-03-14 ES ES520561A patent/ES520561A0/es active Granted
-
1985
- 1985-08-09 JP JP60174391A patent/JPS6143994A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| DK172882A (da) | 1982-12-29 |
| FI821355L (fi) | 1982-10-21 |
| IE820907L (en) | 1982-10-20 |
| FI79345C (fi) | 1989-12-11 |
| IT8220806A0 (it) | 1982-04-19 |
| DK153569B (da) | 1988-07-25 |
| EP0063909A1 (en) | 1982-11-03 |
| ES8500994A1 (es) | 1984-11-01 |
| AU8280882A (en) | 1982-10-28 |
| GB2097405B (en) | 1984-08-15 |
| IN155660B (OSRAM) | 1985-02-16 |
| EP0063909B2 (en) | 1990-09-12 |
| ES8307291A1 (es) | 1983-06-16 |
| FI79345B (fi) | 1989-08-31 |
| JPS6143994A (ja) | 1986-03-03 |
| CA1199292A (en) | 1986-01-14 |
| IT1190780B (it) | 1988-02-24 |
| KR830010192A (ko) | 1983-12-26 |
| EP0063909B1 (en) | 1987-07-08 |
| ES511504A0 (es) | 1983-06-16 |
| KR890002413B1 (ko) | 1989-07-03 |
| CH659825A5 (de) | 1987-02-27 |
| IE53031B1 (en) | 1988-05-11 |
| MX174149B (es) | 1994-04-25 |
| ATE28216T1 (de) | 1987-07-15 |
| AU548122B2 (en) | 1985-11-21 |
| DE3276707D1 (en) | 1987-08-13 |
| DK153569C (da) | 1988-12-05 |
| FI821355A0 (fi) | 1982-04-19 |
| FR2504148B1 (OSRAM) | 1984-05-18 |
| JPS57174089A (en) | 1982-10-26 |
| FR2504148A1 (fr) | 1982-10-22 |
| GB2097405A (en) | 1982-11-03 |
| ES520561A0 (es) | 1984-11-01 |
| BE892904A (fr) | 1982-10-19 |
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