JPH02222675A - 変異枯草菌 - Google Patents

変異枯草菌

Info

Publication number: JPH02222675A
Authority: JP; Japan
Prior art keywords: maltotetraose; dna; enzyme; bacillus subtilis; producing
Prior art date: 1989-02-27
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.): Granted

Application number

JP4331389A

Other languages

English (en)

Japanese (ja)

Other versions

JPH0533028B2 (fr

Inventor

Toshiya Takano

高野　敏弥

Shoichi Kobayashi

昭一小林

Kenka Shiyuu

建華周

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

National Food Research Institute

Original Assignee

National Food Research Institute

Priority date (The priority date 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 date listed.)

1989-02-27

Filing date

1989-02-27

Publication date

1990-09-05

1989-02-27 Application filed by National Food Research Institute filed Critical National Food Research Institute

1989-02-27 Priority to JP4331389A priority Critical patent/JPH02222675A/ja

1990-09-05 Publication of JPH02222675A publication Critical patent/JPH02222675A/ja

1993-05-18 Publication of JPH0533028B2 publication Critical patent/JPH0533028B2/ja

Status Granted legal-status Critical Current

Links

244000063299 Bacillus subtilis Species 0.000 title claims abstract description 16
235000014469 Bacillus subtilis Nutrition 0.000 title claims abstract description 16
108090000790 Enzymes Proteins 0.000 claims abstract description 39
LUEWUZLMQUOBSB-UHFFFAOYSA-N UNPD55895 Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(OC3C(OC(O)C(O)C3O)CO)C(O)C2O)CO)C(O)C1O LUEWUZLMQUOBSB-UHFFFAOYSA-N 0.000 claims abstract description 32
UYQJCPNSAVWAFU-UHFFFAOYSA-N malto-tetraose Natural products OC1C(O)C(OC(C(O)CO)C(O)C(O)C=O)OC(CO)C1OC1C(O)C(O)C(OC2C(C(O)C(O)C(CO)O2)O)C(CO)O1 UYQJCPNSAVWAFU-UHFFFAOYSA-N 0.000 claims abstract description 32
LUEWUZLMQUOBSB-OUBHKODOSA-N maltotetraose Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@H](CO)O[C@@H](O[C@@H]2[C@@H](O[C@@H](O[C@@H]3[C@@H](O[C@@H](O)[C@H](O)[C@H]3O)CO)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O LUEWUZLMQUOBSB-OUBHKODOSA-N 0.000 claims abstract description 32
102000004190 Enzymes Human genes 0.000 claims abstract description 31
108020004414 DNA Proteins 0.000 abstract description 20
244000005700 microbiome Species 0.000 abstract description 16
239000013598 vector Substances 0.000 abstract description 13
108091008146 restriction endonucleases Proteins 0.000 abstract description 10
230000000694 effects Effects 0.000 abstract description 9
241000894006 Bacteria Species 0.000 abstract description 8
108020004511 Recombinant DNA Proteins 0.000 abstract description 6
108090000623 proteins and genes Proteins 0.000 abstract description 4
239000000463 material Substances 0.000 abstract description 3
241000589779 Pelomonas saccharophila Species 0.000 abstract description 2
239000003153 chemical reaction reagent Substances 0.000 abstract description 2
235000013376 functional food Nutrition 0.000 abstract description 2
239000000203 mixture Substances 0.000 abstract description 2
210000005056 cell body Anatomy 0.000 abstract 2
230000015572 biosynthetic process Effects 0.000 abstract 1
230000009466 transformation Effects 0.000 abstract 1
229940088598 enzyme Drugs 0.000 description 26
239000013612 plasmid Substances 0.000 description 20
239000012634 fragment Substances 0.000 description 17
238000000034 method Methods 0.000 description 15
239000002609 medium Substances 0.000 description 11
210000004027 cell Anatomy 0.000 description 10
229920002472 Starch Polymers 0.000 description 7
239000004098 Tetracycline Substances 0.000 description 7
239000002245 particle Substances 0.000 description 7
239000008107 starch Substances 0.000 description 7
235000019698 starch Nutrition 0.000 description 7
229960002180 tetracycline Drugs 0.000 description 7
229930101283 tetracycline Natural products 0.000 description 7
235000019364 tetracycline Nutrition 0.000 description 7
150000003522 tetracyclines Chemical class 0.000 description 7
239000013611 chromosomal DNA Substances 0.000 description 5
210000000349 chromosome Anatomy 0.000 description 5
238000005516 engineering process Methods 0.000 description 5
238000000605 extraction Methods 0.000 description 5
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
241000701959 Escherichia virus Lambda Species 0.000 description 4
238000003776 cleavage reaction Methods 0.000 description 4
239000007788 liquid Substances 0.000 description 4
230000007017 scission Effects 0.000 description 4
238000004809 thin layer chromatography Methods 0.000 description 4
229920001817 Agar Polymers 0.000 description 3
241000588724 Escherichia coli Species 0.000 description 3
241000589516 Pseudomonas Species 0.000 description 3
239000008272 agar Substances 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
229930027917 kanamycin Natural products 0.000 description 3
229960000318 kanamycin Drugs 0.000 description 3
SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 3
229930182823 kanamycin A Natural products 0.000 description 3
238000000746 purification Methods 0.000 description 3
239000006152 selective media Substances 0.000 description 3
239000000725 suspension Substances 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 2
ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 2
102000002260 Alkaline Phosphatase Human genes 0.000 description 2
108020004774 Alkaline Phosphatase Proteins 0.000 description 2
102000012410 DNA Ligases Human genes 0.000 description 2
108010061982 DNA Ligases Proteins 0.000 description 2
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
102000003960 Ligases Human genes 0.000 description 2
108090000364 Ligases Proteins 0.000 description 2
LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 2
108091005804 Peptidases Proteins 0.000 description 2
239000004365 Protease Substances 0.000 description 2
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
102000006382 Ribonucleases Human genes 0.000 description 2
108010083644 Ribonucleases Proteins 0.000 description 2
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
229960000723 ampicillin Drugs 0.000 description 2
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 2
230000001580 bacterial effect Effects 0.000 description 2
229940041514 candida albicans extract Drugs 0.000 description 2
238000006243 chemical reaction Methods 0.000 description 2
230000002759 chromosomal effect Effects 0.000 description 2
238000012258 culturing Methods 0.000 description 2
238000002298 density-gradient ultracentrifugation Methods 0.000 description 2
238000000338 in vitro Methods 0.000 description 2
229910052740 iodine Inorganic materials 0.000 description 2
239000011630 iodine Substances 0.000 description 2
230000000813 microbial effect Effects 0.000 description 2
LWIHDJKSTIGBAC-UHFFFAOYSA-K potassium phosphate Substances [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
102000004196 processed proteins & peptides Human genes 0.000 description 2
108090000765 processed proteins & peptides Proteins 0.000 description 2
238000002525 ultrasonication Methods 0.000 description 2
238000005406 washing Methods 0.000 description 2
239000012138 yeast extract Substances 0.000 description 2
229920000936 Agarose Polymers 0.000 description 1
102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
101000925662 Enterobacteria phage PRD1 Endolysin Proteins 0.000 description 1
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
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 1
108010014251 Muramidase Proteins 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
-1 NaCj 25 g Substances 0.000 description 1
229930193140 Neomycin Natural products 0.000 description 1
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 1
102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
239000002202 Polyethylene glycol Substances 0.000 description 1
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 1
238000002105 Southern blotting Methods 0.000 description 1
229930006000 Sucrose Natural products 0.000 description 1
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 1
241001441723 Takifugu Species 0.000 description 1
239000002260 anti-inflammatory agent Substances 0.000 description 1
210000002421 cell wall Anatomy 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
238000010367 cloning Methods 0.000 description 1
238000007796 conventional method Methods 0.000 description 1
239000012531 culture fluid Substances 0.000 description 1
238000000432 density-gradient centrifugation Methods 0.000 description 1
ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
229910000396 dipotassium phosphate Inorganic materials 0.000 description 1
235000019797 dipotassium phosphate Nutrition 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
230000008014 freezing Effects 0.000 description 1
238000007710 freezing Methods 0.000 description 1
239000000499 gel Substances 0.000 description 1
108010064118 glucan 1,4-maltotetraohydrolase Proteins 0.000 description 1
239000008103 glucose Substances 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
238000004128 high performance liquid chromatography Methods 0.000 description 1
239000012535 impurity Substances 0.000 description 1
238000011534 incubation Methods 0.000 description 1
239000006166 lysate Substances 0.000 description 1
230000002934 lysing effect Effects 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
239000003550 marker Substances 0.000 description 1
229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
235000019796 monopotassium phosphate Nutrition 0.000 description 1
229960004927 neomycin Drugs 0.000 description 1
238000004806 packaging method and process Methods 0.000 description 1
229920001223 polyethylene glycol Polymers 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
102000004169 proteins and genes Human genes 0.000 description 1
210000001938 protoplast Anatomy 0.000 description 1
230000003248 secreting effect Effects 0.000 description 1
238000000926 separation method Methods 0.000 description 1
239000000377 silicon dioxide Substances 0.000 description 1
235000019333 sodium laurylsulphate Nutrition 0.000 description 1
239000002904 solvent Substances 0.000 description 1
238000005507 spraying Methods 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
239000004094 surface-active agent Substances 0.000 description 1
238000012360 testing method Methods 0.000 description 1
238000010257 thawing Methods 0.000 description 1
230000002463 transducing effect Effects 0.000 description 1
235000020138 yakult Nutrition 0.000 description 1

Landscapes

Enzymes And Modification Thereof (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)

JP4331389A 1989-02-27 1989-02-27 変異枯草菌 Granted JPH02222675A (ja)

Priority Applications (1)

Application Number	Priority Date	Filing Date	Title
JP4331389A JPH02222675A (ja)	1989-02-27	1989-02-27	変異枯草菌

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
JP4331389A JPH02222675A (ja)	1989-02-27	1989-02-27	変異枯草菌

Publications (2)

Publication Number	Publication Date
JPH02222675A true JPH02222675A (ja)	1990-09-05
JPH0533028B2 JPH0533028B2 (fr)	1993-05-18

Family

ID=12660314

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
JP4331389A Granted JPH02222675A (ja)	1989-02-27	1989-02-27	変異枯草菌

Country Status (1)

Country	Link
JP (1)	JPH02222675A (fr)

1989
- 1989-02-27 JP JP4331389A patent/JPH02222675A/ja active Granted

Also Published As

Publication number	Publication date
JPH0533028B2 (fr)	1993-05-18

Legal Events

Date	Code	Title	Description
2006-09-20	S111	Request for change of ownership or part of ownership	Free format text: JAPANESE INTERMEDIATE CODE: R313111
2006-09-28	R350	Written notification of registration of transfer	Free format text: JAPANESE INTERMEDIATE CODE: R350
2009-02-27	EXPY	Cancellation because of completion of term

Publication	Publication Date	Title
AU620026B2 (en)	1992-02-13	Molecular cloning and expression of genes encoding proteolytic enzymes
JPS6232888A (ja)	1987-02-12	アルカリ性プロテア−ゼ並びにハイブリツドベクタ−および形質転換微生物の調製
JP2530181B2 (ja)	1996-09-04	アルカリセルラ―ゼ遺伝子を含むｄｎａ断片並びに該ｄｎａ断片を組み込んだ組換えプラスミド及び組換え微生物
EP0057976B1 (fr)	1986-01-08	Procédé pour cloner le gène codant pour une alpha-amylase thermostable dans escherichia coli et bacillus subtilis
EP0941338B1 (fr)	2007-08-08	Procedes de preparation de nucleotide integrases
US4464471A (en)	1984-08-07	Biologically engineered plasmid coding for production of β-glucosidase, organisms modified by this plasmid and methods of use
EP0149241B1 (fr)	1991-03-27	Séquence de bases d'ADN contenant des régions impliquées dans la production et la sécrétion d'une protéine, ADN recombinant comprenant la totalité ou une partie de la séquence de base d'ADN et méthode pour la production de protéines utilisant cet ADN recombinant
JPH01108978A (ja)	1989-04-26	中性プロテアーゼ遺伝子の分子クローニングおよび発現
Park et al.	1986	Cloning and expression of a Bacillus cellulase gene in Escherichia coli
JPH02222675A (ja)	1990-09-05	変異枯草菌
JPH0363357B2 (fr)	1991-09-30
EP0073436A2 (fr)	1983-03-09	Plasmide hybride et sa préparation
CA1285233C (fr)	1991-06-25	Methode de production de protease neutre
JPH06233687A (ja)	1994-08-23	組換えｄｎａ
JPH0156756B2 (fr)	1989-12-01
JPH0354551B2 (fr)	1991-08-20
EP0115936A1 (fr)	1984-08-15	Plasmides chimériques
JPS61280282A (ja)	1986-12-10	組換えベクタ−及びその含有微生物
JPH02222686A (ja)	1990-09-05	マルトテトラオース生成酵素遺伝子
SU1532584A1 (ru)	1989-12-30	Штамм бактерий ВRеVIвастеRIUм IммотUм - продуцент эндонуклеазы рестрикции В @ 1
JPS59179081A (ja)	1984-10-11	プラスミドｐＴＰ１１０２
JPH09259A (ja)	1997-01-07	β−ガラクトシダーゼ産生プラスミド及びβ−ガラクトシダーゼの製造法
JP2688861B2 (ja)	1997-12-10	枝作り酵素遺伝子及び該遺伝子を保有する微生物並びに該微生物を用いる枝作り酵素の製造法
SU908793A1 (ru)	1982-02-28	Штамм еSснеRIснIа coLI в834 ( @ , @ ),несущий плазмиду RSF 2124,-тест субстрат дл рестрикционной эндонуклеазы ecoR11
JPH0113358B2 (fr)	1989-03-06