PL92400B1 - - Google Patents
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- Publication number
- PL92400B1 PL92400B1 PL1973160962A PL16096273A PL92400B1 PL 92400 B1 PL92400 B1 PL 92400B1 PL 1973160962 A PL1973160962 A PL 1973160962A PL 16096273 A PL16096273 A PL 16096273A PL 92400 B1 PL92400 B1 PL 92400B1
- Authority
- PL
- Poland
- Prior art keywords
- inhibitor
- amylase
- inhibitors
- sucrose
- activity
- Prior art date
Links
- 239000003112 inhibitor Substances 0.000 claims description 20
- 239000003392 amylase inhibitor Substances 0.000 claims description 6
- 102000004190 Enzymes Human genes 0.000 claims description 5
- 108090000790 Enzymes Proteins 0.000 claims description 5
- 101710184309 Probable sucrose-6-phosphate hydrolase Proteins 0.000 claims description 5
- 102400000472 Sucrase Human genes 0.000 claims description 5
- 101710112652 Sucrose-6-phosphate hydrolase Proteins 0.000 claims description 5
- 235000011073 invertase Nutrition 0.000 claims description 5
- 238000000034 method Methods 0.000 claims description 5
- 229940122816 Amylase inhibitor Drugs 0.000 claims description 3
- 239000002253 acid Substances 0.000 claims description 3
- 150000007513 acids Chemical class 0.000 claims description 3
- 150000004676 glycans Chemical class 0.000 claims description 3
- 229920001282 polysaccharide Polymers 0.000 claims description 3
- 239000005017 polysaccharide Substances 0.000 claims description 3
- 241000203809 Actinomycetales Species 0.000 claims description 2
- 244000005700 microbiome Species 0.000 claims description 2
- 150000002482 oligosaccharides Polymers 0.000 claims description 2
- 230000003301 hydrolyzing effect Effects 0.000 claims 1
- 239000004382 Amylase Substances 0.000 description 8
- 102000013142 Amylases Human genes 0.000 description 8
- 108010065511 Amylases Proteins 0.000 description 8
- 235000019418 amylase Nutrition 0.000 description 8
- 230000000694 effects Effects 0.000 description 7
- 229930006000 Sucrose Natural products 0.000 description 6
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 239000005720 sucrose Substances 0.000 description 6
- 229940088598 enzyme Drugs 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 239000004366 Glucose oxidase Substances 0.000 description 3
- 108010015776 Glucose oxidase Proteins 0.000 description 3
- 229920002472 Starch Polymers 0.000 description 3
- MSJMDZAOKORVFC-UAIGNFCESA-L disodium maleate Chemical compound [Na+].[Na+].[O-]C(=O)\C=C/C([O-])=O MSJMDZAOKORVFC-UAIGNFCESA-L 0.000 description 3
- 229940116332 glucose oxidase Drugs 0.000 description 3
- 235000019420 glucose oxidase Nutrition 0.000 description 3
- 235000019698 starch Nutrition 0.000 description 3
- 239000008107 starch Substances 0.000 description 3
- 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 2
- WDMUXYQIMRDWRC-UHFFFAOYSA-N 2-hydroxy-3,4-dinitrobenzoic acid Chemical compound OC(=O)C1=CC=C([N+]([O-])=O)C([N+]([O-])=O)=C1O WDMUXYQIMRDWRC-UHFFFAOYSA-N 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
- 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 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 239000012085 test solution Substances 0.000 description 2
- 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 1
- 229930091371 Fructose Natural products 0.000 description 1
- 239000005715 Fructose Substances 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
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 102000003992 Peroxidases Human genes 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
- 238000009835 boiling Methods 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 210000000813 small intestine Anatomy 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 125000000185 sucrose group Chemical group 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
Classifications
-
- 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
- C12P19/04—Polysaccharides, i.e. compounds containing more than five saccharide radicals attached to each other by glycosidic bonds
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K35/00—Medicinal preparations containing materials or reaction products thereof with undetermined constitution
- A61K35/66—Microorganisms or materials therefrom
- A61K35/74—Bacteria
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
-
- 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
- C12P19/22—Preparation of compounds containing saccharide radicals produced by the action of a beta-amylase, e.g. maltose
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/822—Microorganisms using bacteria or actinomycetales
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Health & Medical Sciences (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biochemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biotechnology (AREA)
- Genetics & Genomics (AREA)
- Epidemiology (AREA)
- Animal Behavior & Ethology (AREA)
- Medicinal Chemistry (AREA)
- Pharmacology & Pharmacy (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Mycology (AREA)
- Gastroenterology & Hepatology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Plant Substances (AREA)
- Enzymes And Modification Thereof (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Medicinal Preparation (AREA)
Description
Przedmiotem wynalazku jest sposób otrzymywa¬ nia inhibitora sacharazy.Opis patentowy RFN DOS nr 2064092 opiera sie na stwierdzeniu, ze szereg Actinomyceteis przede wszystkim Actinopilanaceae tworza inhibitory gli- kozydohydrolaz, korzystnie enizymów przewodu pokarmowego, rozszczepiajacych weglowodany.Grupa tych inhibitorów jest wzglednie odporna na wysokie temperatury i w temperaturze poko¬ jowej odporna, na kwasy i alkalia.Inhibitory te naleza pod wzgledem chemicznym do klasy oligo- lub polisacharydów lub ich po¬ chodnych. Wiekszosc inhibitorów z tej grupy jest wysokoaktywnymi inhibitorami amylazy, lecz tylko srednimi lub slabymi inhibitorami sacha¬ razy.Przedmiotem wynalazku jest sposób przeksztal¬ cenia wymienionych inhibitorów amylazy w silne inhibitory sacharazy.Sposób wedlug wynalazku polega na tym, ze inhibitory amylazy, nalezace do klasy oligo- lub polisacharydów, które sa wytwarzane przez mi¬ kroorganizmy rzedu Actinomycetales, hydrolizuje sie kwasami lub hydrolizuflacymii enzymami, gliko- zydohydrolazami i otrzymany inhibitor sacharazy wyodrebnia sie znana metoda i ewentualnie oczysz¬ cza.Test amylazy. Jednostka inhibitora amylazy (1 AIE) jest ilosc inhibitora, która hamuje aktyw¬ nosc dwóch jednostek amylazy o 50%. Jednostka amylazy (AE) jest ilosc enzymu, która w ciagu 1 minuty w podanych warunkach doswiadczenia rozszczepia 1 ^równowaznik wiazan glikozydowych w skrobi, przy czym l^wal rozszczepionych wiazan oznacza sie kolorymetrycznie kwasem dwunitro- salicylowym jako ^y/al redukujacych cukrów i za pomoca krzywej wzorcowej maltozy podaje sde jako |jwal maltozy. Dla przeprowadzenia testu 0,1 ml roztworu amylazy (20—22 AE/ml) traktuje sie 0—10 jxg inhibitora lub 0—20 ni testowanego roztworu w 0,4 ml 0,02 m buforu: gliceroifosforan sodu (0,001 m CaCl2 o wartosci pH=6,9) i utrzy¬ muje sie na lazni wodnej w temperaturze 35°C przez okolo 10—20 minut. Nastepnie przez 5 minut 1(5 utrzymuje sie z 0,5 ml 1% roztworu skrobi, ogrza¬ nego' wstepnie do temperatury 35°C (skrobia, roz¬ puszczalna, Firmy Merck, Darmstadt Nr 1252) i nastepnie traktuje sie 1 ml reagenitu dwunitro- salicylowego (P. Bernfeld w Colowick-Kaplain, Meth. Enzymol, tom 1, strona 149).Dla wywolania zabarwienia wsad ogrzewa sie przez 5 minut na wrzacej lazni wodnej, nasttejpnie chlodzi sie i traktuje 10 ml wody destylowanej.Ekstynkcje przy 540 mm mierzy sie w stosunku do odpowiednio zalozonej wartosci slepej bez amylazy.Przy obliczaniu odczytuje sie z uprzednio' spo¬ rzadzonej krzywej wzorcowej' amylazy jeszcze istniejaca aktywnosc amylazy po dodaniu inhibi¬ tora i z tego oblicza sie hamowanie procentowe «. aktywnosci wprowadzonej amylazy. Procentowo 92 4003 -*¦: , 02 400 4 hamowanie aktywnosci nanosi sie jako funkcje ilorazu: jxg inhibitora * AE** w którym* oznacza sie w stosunku do substancji suchej i ** we wsadzie tej samej serii bez inhibi¬ tora, odczytuje sie z krzywej punkt, w którym nastepuje hamowanie aktywnosci w 50% i prze¬ licza sie na zawartosc inhibitora w AIE/mg.Test sacharazy. Jednostka inhibitora sacharazy (SIE) jeist ilosc inhibitora, która hamuje o* 50% aktywnosc, dwóch jednostek sacharazy. Jednostka saciiar^zy^SE) jest ilosc enizymu, która w jednej mifritóe w podlanych warunkach testowych roz¬ szczepia^J»^JBiPi^^cJxaTOzy na glikoze i fruktoze, przl ^frWJS J^oJl Stworzonej sacharozy oznacza sie Ilosciowo za pomoda ok&ydazy glikozy w wa¬ runkach, w których aie nastepuje dalsze roz- szcA^i4!fi^^^2^^jrt trzy przeprowadzaniu testu Q,Qgii^lLo^l^u^S^l^razy *) o zawartosci 0,12 SE traktuje sie 0—20 ^g i/nhibitora lub - 0—20 jj.1 testowanego roztworu i dopelnia sie do 0,1 ml 0,1 m maleinianu sodu jako buforu o wartosci pH=6,0. Utrzymuje sie przez 10 minut w tempera¬ turze 35°C i nastepnie traktuje sie 0,1 ml ogrza¬ nego wstepnie do temperatury 35°C 0,05 m roz¬ tworu sacharozy w 0,1 m maleinianie sodowym jako buforze o wartosci pH = 6,0.Utrzymuje sie przez 20 minut w temperaturze °C, po czym zatrzymuje sie reakcje sacharozy przez dodanie 1 ml preparatu oksydazy glikozy2) i utrzymuje sie jeszcze przez 30 minut w tempe¬ raturze 35°C. Nastepnie dodaje sie 1 ml 50% H2SO4 i mierzy sie przy 545 mm w stosunku do odpo¬ wiedniej wartosci slepej. Przy obliczaniu oblicza sie procentowe hamowanie aktywnosci wprowa¬ dzanej sacharazy i z punktu 50% hamowania przelicza sie na SIE/g wzglednie SIE/litr za po- n*oca krzywej wzorcowej glikozy. 1. Solufedllizowana saeharaza z miukozy cienkiego jelita swin wg: B. Borgsfcrom, A. Dahlauist, Acta Chem.-Scand. 12, 1958 (strona 1997), rozcienczona do odpowiedniej zawartosci SE 0,1 m maleinianem sodu jako buforem o wartosci pH=6. 2. Preparat oksydazy glikozy otrzymuje sie przez rozpuszczenie 2 mg oksydazy glikozy (Fe. Boehrin- ger Nr 15423 ESAB) w 100 ml 0,565 m buforem Tris-HCl o pH=7 i nastepnie dodanie roztworu detergentu (2 g Tritonru 100 + 8 g 95% etanolu p.a), 1 ml roztworu dianizydyny (260 mg o-dianizy- dyny, 2 HC1 w 20 ml H2O i 0,5 ml 0,1% wodnego roztworu peroksydazy (Fe. Boehrkiger Nr 15302 EPAP). fri#feztalfcen,ie inhibitorów amylazy w inhibi¬ tory ssrtiharazy zachodzi na drodze odszczepdenia inall&^taijaeego elementu czasteczki (prcewaznie ifcómoy twu- lut* tr&jfettd-har^iu) z czasteczek inhi- t$fora. ' PL
Claims (1)
1. Zastrzezenie patentowe Sposób otrzymywania inhibitora sacharazy z in¬ hibitora amylazy, nalezacego do klasy oligo- lub polisacharydów, który jest wytwarzany przez mikroorganizmy rzedu Actinomycetales^ znamien¬ ny tym, ze (inhibitor aimylazy hyidrolizuje sie kwasami lub hydirolizujacymi enzymami, glikoizy^ dohydrolazarni i otrzymany inhibitor sacharazy wyodrebnia sie znana metoda i ewentualnie oczyszcza. 200 i 160 *xl*H 3 30 l \ / / S 20 10 l M I » 20 40 eo eo 100 FIG. 192 400 50} na 292 400 80 70 eof 50l 40l 301 »l ¦104 60 120 180 240 FIC, 3 -czyteTni* PL PL
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE2209832A DE2209832C3 (de) | 1972-03-01 | 1972-03-01 | Herstellung von Saccharaseinhibitoren |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| PL92400B1 true PL92400B1 (pl) | 1977-04-30 |
Family
ID=5837575
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PL1973160962A PL92400B1 (pl) | 1972-03-01 | 1973-02-28 |
Country Status (29)
| Country | Link |
|---|---|
| US (1) | US3879546A (pl) |
| JP (1) | JPS4898088A (pl) |
| KR (1) | KR780000001B1 (pl) |
| AR (1) | AR196913A1 (pl) |
| AT (1) | AT319171B (pl) |
| AU (1) | AU467011B2 (pl) |
| BE (1) | BE795994A (pl) |
| BG (1) | BG25655A3 (pl) |
| CA (1) | CA992018A (pl) |
| CH (1) | CH578020A5 (pl) |
| CS (1) | CS189590B2 (pl) |
| DD (1) | DD105243A5 (pl) |
| DE (1) | DE2209832C3 (pl) |
| DK (1) | DK129530B (pl) |
| ES (1) | ES412097A1 (pl) |
| FI (1) | FI49840C (pl) |
| FR (1) | FR2174238B1 (pl) |
| GB (1) | GB1376574A (pl) |
| HU (1) | HU171216B (pl) |
| IE (1) | IE37351B1 (pl) |
| IL (1) | IL41611A (pl) |
| LU (1) | LU67107A1 (pl) |
| NL (1) | NL7302651A (pl) |
| NO (1) | NO136844C (pl) |
| PL (1) | PL92400B1 (pl) |
| RO (1) | RO77618A (pl) |
| SE (1) | SE418454B (pl) |
| SU (1) | SU576050A3 (pl) |
| ZA (1) | ZA731397B (pl) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2209834C3 (de) * | 1972-03-01 | 1978-04-20 | Bayer Ag, 5090 Leverkusen | Herstellung von Saccharase-Inhibitoren |
| US4010258A (en) * | 1974-03-15 | 1977-03-01 | Ajinomoto Co., Inc. | Microbial amylase inhibitor and preparation thereof with the use of streptomyces diasticus var. amylostaticus |
| KR100383435B1 (ko) | 1999-10-28 | 2003-05-12 | 주식회사종근당 | 고순도 아카보스 제조방법 |
| HRP20010792A2 (en) | 2001-10-26 | 2003-04-30 | Pliva D D | Acarbose purification process |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE2064092C2 (de) * | 1970-12-28 | 1983-06-01 | Bayer Ag, 5090 Leverkusen | Inhibitoren für Glykosidhydrolasen aus Actinomyceten |
| JPS5111197B1 (pl) * | 1971-05-31 | 1976-04-09 |
-
1972
- 1972-03-01 DE DE2209832A patent/DE2209832C3/de not_active Expired
-
1973
- 1973-02-06 RO RO7385990A patent/RO77618A/ro unknown
- 1973-02-23 SU SU7301885529A patent/SU576050A3/ru active
- 1973-02-24 BG BG022817A patent/BG25655A3/xx unknown
- 1973-02-26 IL IL41611A patent/IL41611A/xx unknown
- 1973-02-26 NL NL7302651A patent/NL7302651A/xx not_active Application Discontinuation
- 1973-02-27 LU LU67107A patent/LU67107A1/xx unknown
- 1973-02-27 ES ES412097A patent/ES412097A1/es not_active Expired
- 1973-02-27 CA CA164,665A patent/CA992018A/en not_active Expired
- 1973-02-27 BE BE128125A patent/BE795994A/xx not_active IP Right Cessation
- 1973-02-27 AU AU52659/73A patent/AU467011B2/en not_active Expired
- 1973-02-27 DD DD169102A patent/DD105243A5/xx unknown
- 1973-02-27 FI FI730593A patent/FI49840C/fi active
- 1973-02-27 CH CH284373A patent/CH578020A5/xx not_active IP Right Cessation
- 1973-02-27 AT AT172873A patent/AT319171B/de not_active IP Right Cessation
- 1973-02-27 CS CS731417A patent/CS189590B2/cs unknown
- 1973-02-28 DK DK109473AA patent/DK129530B/da not_active IP Right Cessation
- 1973-02-28 US US336720A patent/US3879546A/en not_active Expired - Lifetime
- 1973-02-28 KR KR7300331A patent/KR780000001B1/ko not_active Expired
- 1973-02-28 SE SE7302815A patent/SE418454B/xx unknown
- 1973-02-28 IE IE315/73A patent/IE37351B1/xx unknown
- 1973-02-28 PL PL1973160962A patent/PL92400B1/pl unknown
- 1973-02-28 ZA ZA731397A patent/ZA731397B/xx unknown
- 1973-02-28 NO NO822/73A patent/NO136844C/no unknown
- 1973-02-28 GB GB972973A patent/GB1376574A/en not_active Expired
- 1973-03-01 HU HU73BA00002882A patent/HU171216B/hu unknown
- 1973-03-01 FR FR7307331A patent/FR2174238B1/fr not_active Expired
- 1973-03-01 JP JP48024742A patent/JPS4898088A/ja active Pending
- 1973-03-01 AR AR246886A patent/AR196913A1/es active
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