JPH0517831B2 - - Google Patents
Info
- Publication number
- JPH0517831B2 JPH0517831B2 JP1171752A JP17175289A JPH0517831B2 JP H0517831 B2 JPH0517831 B2 JP H0517831B2 JP 1171752 A JP1171752 A JP 1171752A JP 17175289 A JP17175289 A JP 17175289A JP H0517831 B2 JPH0517831 B2 JP H0517831B2
- Authority
- JP
- Japan
- Prior art keywords
- amylase
- streptomyces
- culture
- amylase inhibitor
- aiu
- 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 - Lifetime
Links
- 239000003392 amylase inhibitor Substances 0.000 claims description 51
- 229940122816 Amylase inhibitor Drugs 0.000 claims description 38
- 241000187180 Streptomyces sp. Species 0.000 claims description 19
- 229920001817 Agar Polymers 0.000 claims description 17
- 239000008272 agar Substances 0.000 claims description 17
- 229910052799 carbon Inorganic materials 0.000 claims description 7
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims description 6
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 6
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 3
- GXCLVBGFBYZDAG-UHFFFAOYSA-N N-[2-(1H-indol-3-yl)ethyl]-N-methylprop-2-en-1-amine Chemical compound CN(CCC1=CNC2=C1C=CC=C2)CC=C GXCLVBGFBYZDAG-UHFFFAOYSA-N 0.000 claims description 2
- 235000020262 oat milk Nutrition 0.000 claims 1
- 239000000243 solution Substances 0.000 description 37
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 27
- 102000013142 Amylases Human genes 0.000 description 20
- 108010065511 Amylases Proteins 0.000 description 20
- 235000019418 amylase Nutrition 0.000 description 20
- 238000000034 method Methods 0.000 description 20
- 239000012141 concentrate Substances 0.000 description 19
- 239000004382 Amylase Substances 0.000 description 18
- 239000002609 medium Substances 0.000 description 18
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 16
- 239000002244 precipitate Substances 0.000 description 16
- 230000001580 bacterial effect Effects 0.000 description 15
- 229920002472 Starch Polymers 0.000 description 14
- 244000005700 microbiome Species 0.000 description 14
- 235000019698 starch Nutrition 0.000 description 14
- 239000008107 starch Substances 0.000 description 14
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 14
- 230000000694 effects Effects 0.000 description 13
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 12
- 239000012153 distilled water Substances 0.000 description 12
- 239000003112 inhibitor Substances 0.000 description 11
- 230000002401 inhibitory effect Effects 0.000 description 11
- 239000000126 substance Substances 0.000 description 10
- 241000699670 Mus sp. Species 0.000 description 9
- 241000187747 Streptomyces Species 0.000 description 9
- 235000000346 sugar Nutrition 0.000 description 9
- 239000011780 sodium chloride Substances 0.000 description 8
- 239000012535 impurity Substances 0.000 description 7
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 6
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 6
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 6
- 239000002518 antifoaming agent Substances 0.000 description 6
- 238000005119 centrifugation Methods 0.000 description 6
- 239000000706 filtrate Substances 0.000 description 6
- 238000002523 gelfiltration Methods 0.000 description 6
- 238000012360 testing method Methods 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 5
- 239000008103 glucose Substances 0.000 description 5
- 239000001963 growth medium Substances 0.000 description 5
- 230000005764 inhibitory process Effects 0.000 description 5
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 4
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 4
- 230000037396 body weight Effects 0.000 description 4
- 229940041514 candida albicans extract Drugs 0.000 description 4
- 239000012531 culture fluid Substances 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- 238000001179 sorption measurement Methods 0.000 description 4
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 4
- 239000012138 yeast extract Substances 0.000 description 4
- WFIYPADYPQQLNN-UHFFFAOYSA-N 2-[2-(4-bromopyrazol-1-yl)ethyl]isoindole-1,3-dione Chemical compound C1=C(Br)C=NN1CCN1C(=O)C2=CC=CC=C2C1=O WFIYPADYPQQLNN-UHFFFAOYSA-N 0.000 description 3
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 3
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 3
- 108090000790 Enzymes Proteins 0.000 description 3
- XEKOWRVHYACXOJ-UHFFFAOYSA-N Ethyl acetate Chemical compound CCOC(C)=O XEKOWRVHYACXOJ-UHFFFAOYSA-N 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 239000001888 Peptone Substances 0.000 description 3
- 108010080698 Peptones Proteins 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 102000016679 alpha-Glucosidases Human genes 0.000 description 3
- 108010028144 alpha-Glucosidases Proteins 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 230000000052 comparative effect Effects 0.000 description 3
- 229940088598 enzyme Drugs 0.000 description 3
- 235000011389 fruit/vegetable juice Nutrition 0.000 description 3
- 229910017053 inorganic salt Inorganic materials 0.000 description 3
- 235000013372 meat Nutrition 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 230000000877 morphologic effect Effects 0.000 description 3
- 229910052757 nitrogen Inorganic materials 0.000 description 3
- 239000003960 organic solvent Substances 0.000 description 3
- 235000019319 peptone Nutrition 0.000 description 3
- 235000020183 skimmed milk Nutrition 0.000 description 3
- 230000001954 sterilising effect Effects 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
- LWFUFLREGJMOIZ-UHFFFAOYSA-N 3,5-dinitrosalicylic acid Chemical compound OC(=O)C1=CC([N+]([O-])=O)=CC([N+]([O-])=O)=C1O LWFUFLREGJMOIZ-UHFFFAOYSA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 229920002261 Corn starch Polymers 0.000 description 2
- 208000007882 Gastritis Diseases 0.000 description 2
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 2
- 208000031226 Hyperlipidaemia Diseases 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-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
- 208000008589 Obesity Diseases 0.000 description 2
- 208000007107 Stomach Ulcer Diseases 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 229940024606 amino acid Drugs 0.000 description 2
- 235000001014 amino acid Nutrition 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 229940025131 amylases Drugs 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000035425 carbon utilization Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000007796 conventional method Methods 0.000 description 2
- 239000008120 corn starch Substances 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- 208000000718 duodenal ulcer Diseases 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 239000004093 hydrolase inhibitor Substances 0.000 description 2
- 201000001421 hyperglycemia Diseases 0.000 description 2
- 239000003456 ion exchange resin Substances 0.000 description 2
- 229920003303 ion-exchange polymer Polymers 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 230000007935 neutral effect Effects 0.000 description 2
- 235000020824 obesity Nutrition 0.000 description 2
- 239000000049 pigment Substances 0.000 description 2
- 229920001282 polysaccharide Polymers 0.000 description 2
- 239000005017 polysaccharide Substances 0.000 description 2
- 229920001296 polysiloxane Polymers 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- YGSDEFSMJLZEOE-UHFFFAOYSA-N salicylic acid Chemical compound OC(=O)C1=CC=CC=C1O YGSDEFSMJLZEOE-UHFFFAOYSA-N 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 231100000820 toxicity test Toxicity 0.000 description 2
- 238000005303 weighing Methods 0.000 description 2
- 239000001052 yellow pigment Substances 0.000 description 2
- BBBFYZOJHSYQMW-LGDQNDJISA-N (2s)-2,4-diamino-4-oxobutanoic acid;(2r,3s,4r,5r)-2,3,4,5,6-pentahydroxyhexanal Chemical compound OC(=O)[C@@H](N)CC(N)=O.OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O BBBFYZOJHSYQMW-LGDQNDJISA-N 0.000 description 1
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
- OHVLMTFVQDZYHP-UHFFFAOYSA-N 1-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-2-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]ethanone Chemical compound N1N=NC=2CN(CCC=21)C(CN1CCN(CC1)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)=O OHVLMTFVQDZYHP-UHFFFAOYSA-N 0.000 description 1
- LDXJRKWFNNFDSA-UHFFFAOYSA-N 2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-1-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]ethanone Chemical compound C1CN(CC2=NNN=C21)CC(=O)N3CCN(CC3)C4=CN=C(N=C4)NCC5=CC(=CC=C5)OC(F)(F)F LDXJRKWFNNFDSA-UHFFFAOYSA-N 0.000 description 1
- JQMFQLVAJGZSQS-UHFFFAOYSA-N 2-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]piperazin-1-yl]-N-(2-oxo-3H-1,3-benzoxazol-6-yl)acetamide Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)N1CCN(CC1)CC(=O)NC1=CC2=C(NC(O2)=O)C=C1 JQMFQLVAJGZSQS-UHFFFAOYSA-N 0.000 description 1
- JVKRKMWZYMKVTQ-UHFFFAOYSA-N 2-[4-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]pyrazol-1-yl]-N-(2-oxo-3H-1,3-benzoxazol-6-yl)acetamide Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C=1C=NN(C=1)CC(=O)NC1=CC2=C(NC(O2)=O)C=C1 JVKRKMWZYMKVTQ-UHFFFAOYSA-N 0.000 description 1
- YLZOPXRUQYQQID-UHFFFAOYSA-N 3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-1-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]propan-1-one Chemical compound N1N=NC=2CN(CCC=21)CCC(=O)N1CCN(CC1)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F YLZOPXRUQYQQID-UHFFFAOYSA-N 0.000 description 1
- 241000186361 Actinobacteria <class> Species 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 208000031648 Body Weight Changes Diseases 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000233866 Fungi Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 239000004366 Glucose oxidase Substances 0.000 description 1
- 108010015776 Glucose oxidase Proteins 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- FTNIPWXXIGNQQF-UHFFFAOYSA-N Maltopentose Chemical compound OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(OC3C(OC(OC4C(OC(O)C(O)C4O)CO)C(O)C3O)CO)C(O)C2O)CO)C(O)C1O FTNIPWXXIGNQQF-UHFFFAOYSA-N 0.000 description 1
- 229910002651 NO3 Inorganic materials 0.000 description 1
- NHNBFGGVMKEFGY-UHFFFAOYSA-N Nitrate Chemical compound [O-][N+]([O-])=O NHNBFGGVMKEFGY-UHFFFAOYSA-N 0.000 description 1
- IOVCWXUNBOPUCH-UHFFFAOYSA-M Nitrite anion Chemical compound [O-]N=O IOVCWXUNBOPUCH-UHFFFAOYSA-M 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex⢠Substances 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000000862 absorption spectrum Methods 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000004480 active ingredient 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
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 238000010170 biological method Methods 0.000 description 1
- 230000004579 body weight change Effects 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 150000002016 disaccharides Chemical class 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000005187 foaming Methods 0.000 description 1
- 235000013373 food additive Nutrition 0.000 description 1
- 239000002778 food additive Substances 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 201000005917 gastric ulcer Diseases 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 229940116332 glucose oxidase Drugs 0.000 description 1
- 235000019420 glucose oxidase Nutrition 0.000 description 1
- 235000011187 glycerol Nutrition 0.000 description 1
- 235000013882 gravy Nutrition 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 238000002329 infrared spectrum Methods 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 230000035764 nutrition Effects 0.000 description 1
- 239000006877 oatmeal agar Substances 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- FJKROLUGYXJWQN-UHFFFAOYSA-N papa-hydroxy-benzoic acid Natural products OC(=O)C1=CC=C(O)C=C1 FJKROLUGYXJWQN-UHFFFAOYSA-N 0.000 description 1
- 230000035699 permeability Effects 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 230000000069 prophylactic effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 229960004889 salicylic acid Drugs 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 238000004809 thin layer chromatography Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 230000004580 weight loss Effects 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
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/20—Bacteria; Culture media therefor
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Biotechnology (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Virology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Coloring Foods And Improving Nutritive Qualities (AREA)
- Saccharide Compounds (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
Description
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(Technical Field) The present invention relates to a novel microorganism, Streptomyces sp. Y-125, and a method for producing an amylase inhibitor therefrom. (Background Art) In general, most of carbohydrates, which are one of the three major nutrients necessary for the human body, are ingested in the form of disaccharides or polysaccharides, and then immediately before being absorbed into the body, carbohydrates are processed by amylase or maltase. Or, it is decomposed by the action of glycoside hydrolase such as satucalase, and if an excessive amount of sugar is produced in the body at this time, it causes diabetes, obesity, hyperlipidemia, gastritis, gastric ulcer, duodenal ulcer, etc. Therefore, in order to prevent and treat these diseases, excessive amounts of sugar can be prevented by suppressing the action of various glycoside hydrolases existing in the body using glycoside hydrolase inhibitors. Methods are known to prevent the production of glycoside hydrolase (U.S. Pat. Nos. 4,307,194 and 4,451,455), and such glycoside hydrolase inhibitors are inhibited by actinomycetes, particularly Streptomyces. It is known as a substance that is often produced. It has been reported that conventional glycoside hydrolases have a superior inhibitory effect on amylase depending on their molecular weight, whereas those with a low molecular weight have an excellent inhibitory effect on maltase or satucarase. What is obtained by the method of the present invention is an amylase inhibitor that has a relatively low molecular weight but exhibits a specific inhibitory effect on amylase. Conventionally known methods for producing amylase inhibitors include non-biological methods, i.e. physical adsorption of low molecular weight substances such as salicylic acid or abiscine to non-specifically inhibit the enzyme. There are also methods of manufacturing using polymeric substances that inhibit, denature, or precipitate the enzyme. However, these conventional amylase inhibitors only affect salivary amylase;
It has little effect on pancreatic amylase (E. Kneen, RMStandtest, "Arch.
Biochem . It is reported that the degree of activity is relatively low because it becomes inactive by (US Pat. No. 4,282,318). Therefore, the present inventors discovered a new microorganism with high activity that produces an amylase inhibitor, and conducted extensive research on its isolation and utilization. As a result, the amylase inhibitor produced by the new microorganism was found to We have discovered that this substance has better activity and stability than inhibitors, leading to the present invention. An object of the present invention is to provide a novel strain that produces amylase inhibitors and a method for effectively producing amylase inhibitors in high yield using the same. (Disclosure of the Invention) The microorganism of the present invention, Streptomyces sp.
Y-125 is a new bacterial strain isolated and cultured from soil samples collected in Chuncheon, Gangwon-do, and Osan, Gyeonggi-do, Republic of Korea.
Entrusted to the Korea Advanced Institute of Science and Technology under accession number KCTC8387P on July 5, 1988, and designated as the American Type Culture Collection on March 31, 1989.
(ATCC) under accession number ATCC53890. Below, the new strain Streptomyces sp.Yâ125
We will explain the phylogenetic characteristics of The characteristics were measured using the International Streptomyces project.
The methods recommended by the Bergey's Manual of Determinative Bacteriology (ISP) and the Bergey's Manual of Determinative Bacteriology (ISP)
This was carried out in accordance with the method described in "Manual of Determinative Bacteriology" Volume 2 (1986). Below is data comparing characteristics with the following five known Streptomyces microorganisms: Microorganism 1: Streptomyces carpus (St.
(J. Antibiotics) 35: 1156-1159
(1982)) Microorganism 2: St. Corchorusii (Agricultural and Biological Chemistry (Agric.
Biol.chem.) 49(1), 107-110 (1985)) Microorganism 3: amylostatics, a subspecies of St. diastaticus (Agricultural and biological chemistry,
41(6), 919-924 (1977)) Microorganism 4: St. griscosporeus (Agricultural and Biological Chemistry,
45(11), 2599-2604 (1981)) Microorganism 5: St. spiritus (U.S. Patent No. 4254256) The following properties were measured: (1) ISP No. 2 = yeast/malt agar medium (2) ISP No. 3 = oatmil agar medium (3) ISP No. 4 = starch/inorganic salt agar medium (4) ISP No. 5 = Glycerin/Asparagine Agar (5) ISP No. 6 = Peptide/Yeast/Iron Agar (6) ISP No. 7 = Tyrosine Agar (7) SM = Skim Milk Agar (8) NT = Nutrition Agar medium (9) GA = glucose-asparagine agar medium (Note) ISP = International Streptomyces project (International
Streptomuces Project) medium The new strain of Streptomuces of the present invention
Since sp. , starch/inorganic salt agar medium (ISP No.4), tyrosine agar medium (ISP
No. 7), and the growth state and color can be clearly observed especially on oatmeal agar medium (ISP No. 3). The hue of the back side is tan, and this hue is not affected by pH. A yellow pigment was produced on the tyrosine agar medium, a pale yellow pigment was produced on the skim milk agar medium, and no soluble pigment was produced on the other media. Table 2 shows comparative data between Streptomyces sp. Y-125 and the above-mentioned five known microorganisms of the genus Streptomyces.
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(2) Morphological characteristics Observation of the morphological characteristics of Streptomyces sp. Ta. In addition, sporophytes are produced at the edges of aerial hyphae, and the aerial hyphae are wavy in shape, and the spores are spherical or rod-shaped. The surface of the spore is soft and smooth, and its size is 0.7~1.2Ã
It was 1.2 to 1.8 ÎŒm. At this time, the morphological characteristics were investigated using an optical microscope, and the surface and size of the spores were observed using a scanning electron microscope. Table 3 shows comparative data between Streptomyces sp. Y-125 and the above-mentioned five known microorganisms of the genus Streptomyces.
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14æ¥åŸã«æž¬å®ãè¡ã€ãã[Table] (3) Physiological characteristics The following Table 4 shows comparative data between Streptomyces sp. Y-125 and the above-mentioned five known microorganisms of the genus Streptomyces. The degree of carbon utilization, that is, the assimilability of the carbon source shown in Table 4 is the result of measuring the degree of carbon utilization using a Pridham-Godlieb agar medium to which a sterilized carbon source was added to give a final concentration of 1.0%. The culture temperature was 30â.
Measurements were taken 14 days later.
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ãæ¶æ³¡å€ã䜿çšããã[Table] (Note) â: Not used; +: Used;
±: Unclear; Ã: No data As shown in Table 4, Streptomyces sp.
Y-125 hydrolyzed starch but did not liquefy (i.e. hydrolyze) gelatin, coagulate and peptonize skimmed milk, reduce nitrate to nitrite, or degrade cellulose. Furthermore, these strains grew at 20 to 80°C, particularly actively multiplied at 25 to 30°C, were aerobic, and produced melanin-like pigments on tyrosine agar (ISP No. 7). As mentioned above, the Streptomyces of the present invention
Since sp. 2, pp. 1383-1418 (1986)). The new strain of the present invention, Streptomyces sp.
The amylase inhibitor produced by Y-125 is a substance composed of polysaccharides and amino acids, and its activity is
It was extremely high at over 12,000 AIU/mg, and showed excellent inhibitory activity even when heated at 100°C for 120 minutes. One unit of amylase inhibitor (1 AIU) is defined as the amount of inhibitor when a unit of amylase is inhibited by 50%, and one unit of amylase is converted from starch per minute.
Defined as the enzyme amount when 1 ÎŒM of glucose is produced, the glucose produced was measured for reducing sugar using 3,5-dinitrosalicylic acid, and a standard curve was obtained using maltose.The activity of the amylase inhibitor according to the present invention was It was measured using the following method. That is, 100mM Tris-HCl buffer containing 5mM calcium chloride (PH
7.0) in 2 x 10 -2 % amylase solution (10~
Dissolve 0.5 ml of 20 AIU/ml), add 0.5 ml of inhibitor solution (0-300 Όg) or culture medium, mix and incubate at 37°C for 10 minutes, then
Add 2 ml of 1.5% soluble starch solution in 100 mM Tris-HCl buffer and incubate for 10 minutes. Next, 2 ml of 3,5-dinitrosalicylic acid was added, heated for 5 minutes, cooled thoroughly, and diluted with distilled water for 10 minutes.
After dilution, the absorbance was measured at 546 nm. The control test was carried out in the same manner as above except that 0.5 ml of distilled water was added instead of the inhibitor solution, and the blank test was carried out using 10 ml of distilled water instead of the amylase solution.
It was carried out in the same manner as described above, except that 0.5 ml of mM Tris-HCl buffer (PH 7.0) was added and 0.5 ml of distilled water was added instead of the inhibitor solution. Inhibition rate (%) was determined from the measured value of absorbance based on the following formula: Inhibition rate (%) = (B-T)-C/B-CÃ100 In the above formula, T, C, and B each represent an inhibitory substance. The absorbance obtained in the test, control test, and blank test is shown. The amylase inhibitor according to the present invention has extremely high stability against pH, being stable in the pH range of 2.0 to 12.0, and therefore its activity does not decrease during the decomposition process. The amylase inhibitor according to the present invention has a molecular weight of 700 to 1500 as measured by Sephadex G-25 (trade name), and is sufficient for amylase, maltase, and satucalase despite its relatively low molecular weight. It was found that the inhibitory effect on pancreatic amylase was particularly superior to that on salivary amylase. Streptomyces sp.Y-125 of the present invention
(KCTC8387P, ATCC53890) The amylase inhibitor produced by the bacterial species can be used as an active ingredient and by containing it in a pharmaceutically acceptable carrier or diluent, it can be used to treat obesity, diabetes, gastritis, hyperlipidemia, and gastric ulcers. , can be used as a prophylactic and therapeutic agent for duodenal ulcer, and Streptomyces sp. Y-125 (KCTC8387P, ATCC53890) of the present invention
Amylase inhibitors produced by the bacterial species are useful as food additives. Below, a method for culturing Streptomyces sp. Y-125, a new strain of the present invention, and a method for separating amylase inhibitors from the culture will be described in detail. (1) Cultivation of the strain A dilute aqueous hydrochloric acid solution is added to a medium containing yeast extract, defatted soybeans, a nitrogen source such as peptone, soluble starch, a carbon source such as glucose, and an inorganic salt such as sodium chloride. PH
After adjusting the temperature to 6.0 to 7.0 and sterilizing at 121â for 15 minutes, the bacteria were inoculated and incubated at 25 to 30â under aerobic conditions.
Culture was carried out for ~4 days. Table 5 below shows the activity of the inhibitors against various carbon sources (1% concentration). Table 6 shows the activity of inhibitors against nitrogen sources. As can be seen from Tables 5 and 6, the carbon source is soluble starch, and the nitrogen source is yeast extract and polypeptone.
The activity was highest when it was a mixture of Antifoaming agents may also be used at this time, and antifoaming agents are generally useful in preventing excessive foaming. A commonly used antifoam agent such as a silicone antifoam agent was used.
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è¡ã€ãã[Table] (2) Isolation of amylase inhibitors The process of separating the culture fluid from the bacterial cells from the bacterial strain culture can be carried out using centrifugation or a filtration method using a filter aid such as Celite (trade name). This can be done using conventional methods such as The step of separating the amylase inhibitor from the culture solution thus separated can be carried out using conventional methods, such as freeze-drying the culture solution, salting out, or precipitation with an organic solvent.
This can be done using methods such as adsorption, as well as adsorption with ion exchange resins, gel filtration. These methods will be explained in more detail below. (b) Centrifuge the bacterial strain culture medium (30,000 ~
40,000 rpm) to separate the bacterial cells and the culture solution, and then the culture solution was heated under reduced pressure (10 to 70°C) at 50 to 70°C.
50mmHg) and concentrate to 1/5 to 1/10. The precipitate is then filtered off. The obtained concentrate is freeze-dried as required. (b) A hydrophilic solvent such as methanol or acetone is added as an organic solvent to the centrifuged culture solution or concentrate to precipitate inhibitory substances. Impurities precipitate at low concentrations, with concentrations of 60-70%
It is easy to remove impurities if the (c) Separating the precipitate using salts such as ammonium sulfate or sodium chloride. The precipitate is centrifuged or directly washed with an organic solvent, dialyzed, and dried. (d) Adsorption by ion exchange resin: This method is the most suitable method for separating amylase inhibitors when they have polarity, and is based on changes in ionic strength or pH. The amylase inhibitor is separated by elution and gel filtration using its molecular weight. In addition to the above-mentioned separation methods, it is also possible to use methods such as precipitation of impurities due to thermal denaturation, permeability of molecular membranes based on molecular weight, and ultrafiltration. (Example) Next, the present invention will be described with reference to an example. Example 1 0.1% soluble starch in 2 thin flasks,
PH7.0 containing 1% glucose, 0.5% gravy, 0.5% peptone, and 0.3% sodium chloride
After adding 400 ml of culture medium and sterilizing it at 121°C for 15 minutes, Streptomyces sp.
20 ml of Y-125 bacterial solution was inoculated and cultured at 28°C for 4 days. After culturing, this culture fluid was separated into bacterial cells and culture fluid by centrifugation, and 270 ml of the resulting culture fluid with a concentration of 15 AIU/ml was heated at 40 to 60°C under reduced pressure (10 to 50 mm
Hg) to obtain 30 ml of concentrated solution. Add 90% ethanol to this concentrate, centrifuge the generated precipitate, then dissolve this concentrate in distilled water,
After that, freeze-dry for 36 hours to obtain 2Ã10 4 AIU/g.
0.07g of amylase inhibitor was obtained. Example 2 2 Five flasks were each filled with a pH 7.0 medium containing 1% soluble starch, 0.5% peptone, 0.5% meat juice, and 0.3% sodium chloride.
Pour 400 ml of Streptomyces sp.
20 ml of each bacterial solution was inoculated and cultured at 28°C for 4 days. Next, this culture was separated into bacterial cells and a culture solution by centrifugation, and 1500% of the culture solution with a concentration of 85AIU/ml was obtained.
ml of this culture under reduced pressure at 50-60 °C.
Concentrate to 150ml, filter to remove impurity precipitate,
Thereafter, it was treated with 60% ethanol, the precipitate formed was removed by filtration, and the filtrate was concentrated. This concentrate was freeze-dried for 24 hours to give a concentration of 3Ã10 5 AIU/g.
6.4g of amylase inhibitor was obtained. Example 3 2 Using 10 flasks, Example 2
Culture was carried out in the same manner as above to obtain 3000 ml of culture solution.
This culture solution was concentrated to 1/10 under reduced pressure at 60-70°C, then treated with 90% ethanol, the formed precipitate was filtered off, the filtrate was concentrated again, and the formed concentrate was mixed with distilled water. and then lyophilized for 24 hours to obtain 10.2 g of amylase inhibitor with 4.7Ã10 5 AIU/g. Example 4 2% soluble starch, 0.5% polypeptone, 0.5% meat juice, and 0.3% soluble starch in 5 thin flasks.
Pour 400 ml of a medium with a pH of 7.0 containing % sodium chloride into each plate, sterilize it at 121°C for 15 minutes, and then inoculate 20 ml of Streptomyces sp. The cells were cultured at 28° C. for 3 days, and then the culture was separated into bacterial cells and a culture medium by centrifugation. 218 AIU/ml culture solution obtained in this way 1550
ml was concentrated to 1/10 under reduced pressure at 60-70°C,
The impurity precipitate was removed by filtration, and then the concentrate was treated with 90% methanol, the formed precipitate was filtered out again, and then the filtrate was concentrated to obtain a concentrate. This concentrate was dissolved in distilled water and freeze-dried for 36 hours, resulting in 8.2 g, which is 5.5 Ã 10 5 AIU/g.
amylase inhibitor was obtained. Example 5 2 In 5 flasks, 1% corn starch, 0.5% polypeptone, 0.5% meat juice,
Pour 400 ml of PH7.0 medium containing 0.3% sodium chloride into each plate, sterilize them at 121°C for 15 minutes, and inoculate each with 20 ml of Streptomyces sp. and 28â
The cells were cultured for 4 days. Next, this culture solution was separated into bacterial cells and culture solution by centrifugation, and 1600 of culture solution with 186 AIU/ml was obtained.
ml was obtained, the culture solution was concentrated to 1/10, and the precipitate was removed by filtration. The concentrated solution was then treated with 90% ethanol, the resulting precipitate was filtered off again, and then the filtrate was concentrated to obtain a concentrate. This concentrate was dissolved in distilled water and freeze-dried for 42 hours.
9.8 g of amylase inhibitor, which is 5Ã10 5 AIU/g, was obtained. Example 6 Culture was carried out under the same conditions as in Example 5 except that a medium containing 1% corn starch was used. The culture solution had a concentration of 220 AIU/ml, and in this way, 12.0 g of amylase inhibitor was obtained. (5.8Ã
10 5 AIU/g) was obtained. Example 7 Five 2 flasks containing 2.5% soluble starch, 0.5% polypeptone, 0.5% yeast extract, and 0.3% sodium chloride, pH 6.0
Add 400 ml of culture medium adjusted to the above and sterilize it at 121°C for 15 minutes, then inoculate 20 ml of Streptomyces sp. did. Next, this culture was separated into bacterial cells and a culture solution by centrifugation to obtain a culture solution with a concentration of 2750 AIU/ml.
Obtained 1550ml. This culture solution was concentrated under reduced pressure at 60 to 70°C to obtain 200 ml of a concentrated solution, which was filtered to remove impurity precipitates and then treated with 90% ethanol. was concentrated. The concentrate was freeze-dried for 24 hours, resulting in 70Ã
An inhibitor of 10 5 AIU/g was obtained. After this inhibitory substance was dissolved again in distilled water, gel filtration was performed using a Sephadex G-10 column (1.8 x 30 cm). At this time, distilled water was used for elution, and only the active part was collected and freeze-dried.
0.8 g of amylase inhibitor which is 2.1Ã10 3 AIU/mg
I got it. Example 8 2 Using 10 flasks, Example 7
Cultured in the same manner as above, the yield was 3000 AIU/ml.
3000 ml of culture solution was obtained. The culture solution was then concentrated to 300 ml, then treated with 90% ethanol, the precipitate formed was filtered off, and the filtrate was concentrated to obtain a concentrate. This concentrate was redissolved in distilled water and then lyophilized for 24 hours to yield 7.1 x 10 5 AIU/g of inhibitor.
15.5g was obtained. This was dissolved in distilled water again, gel-filtered through a Cephadex G-10 column (2.1 x 30 cm), and only the active portion was collected and freeze-dried. As a result, 1.02 g of amylase inhibitor with a concentration of 2700 AIU/mg was obtained. I got it. Example 9 Culture was carried out in the same manner as in Example 8 except that 0.1% silicone A (manufactured by Sigma, trade name) was added as an antifoaming agent. As a result, inhibition was 7.3 Ã 10 5 AIU/g. 16.4 g of material was obtained. Further, using a Sephadex G-10 column (2.1 x 30 cm), 1.2 g of an amylase inhibitor having a concentration of 3100 AIU/mg was obtained in the same manner as in Example 8. Example 10 2.5% soluble starch, 0.5% polypeptone, 0.5% yeast extract,
Add 400 ml each of a medium containing 0.3% sodium chloride and 0.05% antifoaming agent and adjusted to pH 6.0.
After sterilizing this at 121â for 15 minutes, 20ml of the previously cultured bacterial solution was inoculated and cultured at 28â for 3 days. The resulting culture was centrifuged to obtain 3000ml of a culture solution with a concentration of 5250AIU/ml. Ta. This culture solution was heated to 60 to 70°C under reduced pressure (10 to 50 mm).
Concentrate to 1/10 under Hg), filter to remove impurities, treat it with 90% ethanol, filter out the formed precipitate, and concentrate the filtrate until ethanol is completely removed. . The concentrate was then freeze-dried to 7.5Ã10 5 AIU/
We obtained amylase inhibitor g. As a result of gel filtration through a Sephadex G-10 column (1.8 x 40 cm), 1.70 g of an amylase inhibitor with a concentration of 3300 AIU/mg was obtained. Obtained inhibitor
Transfer 1.70 g to a Cephadex G-25 column (2.6 x 60
As a result of gel filtration through cm), 15200AIU/mg
350 mg of inhibitor was obtained. Characteristics of changes in blood sugar level Animal experiments were conducted using the amylase inhibitor obtained in Example 10. The animals used were mice weighing 17 to 20 g. Hyperglycemia was induced in groups of five mice, and changes in blood glucose levels of these mice were measured at intervals of 5, 15, and 30 minutes. To induce hyperglycemia, add 2.5 g of starch or 2.5 g of maltose/
Orally administered at a dose of Kg mice or 5.0
Sutucarose was orally administered to g/Kg mice. Blood sugar levels were measured using glucose oxidase.
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ïŒã瀺ãã[Table] Toxicity experiment A toxicity experiment was conducted using the amylase inhibitor obtained in Example 10. The animals used were mice weighing 17 to 20 g, and groups of 5 were treated with amylase inhibitors.
A dose of 3000-3000000 AIU/Kg mouse was used. As a result of observation, no dead mice were observed.
Also, no special symptoms were found. Test on body weight change After administering the amylase inhibitors obtained in Example 10 by mixing them into mouse feed at different concentrations, changes in the body weight of mice were measured. The weight of the mouse used was 17
~20g, and as a result of observing changes in body weight for about 60 days in groups of 5 animals, it was found that amylase inhibitors
In the case of 3000 AIU/g, a gradual decrease in body weight was observed after 42 days, and amylase inhibitor
In the case of 9000 AIU/g, a decrease in body weight was observed after 21 days. Table 7 below shows the weight loss (%) of the mice.
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以äžã®é¡èãªé»å®³å¹æã瀺ããã[Table] The amylase inhibitor obtained in Example 10 exhibited the following properties. (1) Molecular weight In order to measure the molecular weight of amylase inhibitors, amylase inhibitors are
As a result of gel filtration using a 25 column and development by thin layer chromatography, the molecular weight was
It turned out to be between 700 and 1500. At this time, a mixture of ethyl acetate:methanol:water=27:15:23 was used as a developing solvent. (2) PH stability An amylase inhibitor was added to a solution with a pH of 2 to 12, and after incubation at 37°C for 30 minutes, the activity against human salivary amylase was measured. As a result, it was stable in all acidic, neutral, and basic conditions (see Figure 1). (3) Thermostability 1% amylase inhibitor was added to a neutral solution with a pH of 7.0, heated at 100°C for 30 to 120 minutes, then cooled, and the activity against human salivary amylase was measured. As a result, it was completely stable when heated for 30 minutes, and showed 85% activity even when heated for 120 minutes (see Figure 2). (4) Inhibitory effect on other amylases In addition to human salivary amylase, we tested the inhibitory properties against amylase produced by microorganisms such as bacteria and fungi. showed less than 50% inhibition, but 90% inhibition against animal amylases such as porcine pancreatic amylase and human salivary amylase.
The above-mentioned remarkable inhibitory effects were demonstrated.
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ãŒã«çã«ã¯äžæº¶æ§ã§ããã[Table] (5) Chemical properties of the amylase inhibitor The chemical properties of the amylase inhibitor according to the present invention are as shown in Table 9 below. It was also similar to maltopentose in that its absorption spectrum was similar to the absorption wavelength characteristics of oligosaccharides (see Figure 3). It was also found that the measured reducing sugar values increased significantly after hydrolysis with hydrochloric acid. From the above results, it can be seen that the amylase inhibitor according to the present invention is composed of 3 to 6 sugar compounds and is not a pure sugar but a heterooligoaccharide. Furthermore, the amylase inhibitor according to the present invention is thought to be in the form of a sugar and an amino acid bonded together.
Moreover, it is soluble only in water and insoluble in methanol, ethanol, etc.
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FIG. 1 is a graph showing the stability of an example of an amylase inhibitor produced by the method of the present invention, FIG. 2 is a graph showing the thermostability of an example of an amylase inhibitor produced by the method of the present invention, and FIG. FIG. 2 is a diagram showing an infrared spectrum of an example of an amylase inhibitor produced by the method of the invention.
Claims (1)
è糞ãçæãããªãŒããã«å¯å€©å¹å°ã«ãããŠèå
ãæ æãã波圢圢æ ã®æ°çè糞ãçæããâã°
ã«ã³ãŒã¹ã«å¯ŸããŠççŽ æºã®ååæ§ã瀺ãããã¢ã
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ã¹ãã¬ãããã€ã»ã¹sp.Yâ125ïŒKCTC8387Pã
ATCC53890ïŒã ïŒ ã¹ãã¬ãããã€ã»ã¹sp.Yâ125
ïŒKCTC8387PãATCC53890ïŒã®èæ ªãå¹é€ãã
ãã®å¹é€ç©ããã¢ãã©ãŒãŒé»å®³ç©è³ªãåé¢ããã
ãšãç¹åŸŽãšããã¢ãã©ãŒãŒé»å®³ç©è³ªã®è£œé æ¹æ³ã[Scope of Claims] 1. Produces white aerial mycelium on a yeast malt agar medium, produces corrugated aerial mycelia carrying spores on an oatmilk agar medium, and assimilates carbon sources for D-glucose. Streptomyces sp. Y-125 (KCTC8387P,
ATCC53890). 2 Streptomyces sp.Yâ125
(KCTC8387P, ATCC53890) strains were cultured,
A method for producing an amylase inhibitor, which comprises separating the amylase inhibitor from the culture.
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
KR1019880010151A KR900007643B1 (en) | 1988-08-09 | 1988-08-09 | Novel microorganism streptomyces sp.y-125 |
KR88-10151 | 1988-08-09 |
Publications (2)
Publication Number | Publication Date |
---|---|
JPH02131571A JPH02131571A (en) | 1990-05-21 |
JPH0517831B2 true JPH0517831B2 (en) | 1993-03-10 |
Family
ID=19276821
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
JP1171752A Granted JPH02131571A (en) | 1988-08-09 | 1989-07-03 | Novel microbe streptomyces sp. y-125 and amirase inhibitor substance produced from it |
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Country | Link |
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JP (1) | JPH02131571A (en) |
KR (1) | KR900007643B1 (en) |
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---|---|---|---|---|
NL1026239C2 (en) * | 2004-05-19 | 2005-11-22 | Ten Cate Thiolon Bv | Method for manufacturing a plastic fiber for use in an artificial grass sports field as well as such a plastic fiber. |
CN114540213B (en) * | 2021-11-11 | 2024-03-19 | äžåœç垊åäžç§åŠé¢æµ·å£å®éªç« | Actinomycetes with antibacterial activity and application thereof |
-
1988
- 1988-08-09 KR KR1019880010151A patent/KR900007643B1/en not_active IP Right Cessation
-
1989
- 1989-07-03 JP JP1171752A patent/JPH02131571A/en active Granted
Also Published As
Publication number | Publication date |
---|---|
KR900003360A (en) | 1990-03-26 |
JPH02131571A (en) | 1990-05-21 |
KR900007643B1 (en) | 1990-10-17 |
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