JPS6463377A - Thermostable cellulase and production thereof - Google Patents

Thermostable cellulase and production thereof

Info

Publication number
JPS6463377A
JPS6463377A JP62220792A JP22079287A JPS6463377A JP S6463377 A JPS6463377 A JP S6463377A JP 62220792 A JP62220792 A JP 62220792A JP 22079287 A JP22079287 A JP 22079287A JP S6463377 A JPS6463377 A JP S6463377A
Authority
JP
Japan
Prior art keywords
cellulase
thermostable
pnb6
thermostable cellulase
plasmid
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.)
Pending
Application number
JP62220792A
Other languages
Japanese (ja)
Inventor
Takeshi Kobayashi
Shinji Iijima
Hiroyuki Honda
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.)
Suntory Ltd
Original Assignee
Suntory Ltd
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.)
Filing date
Publication date
Application filed by Suntory Ltd filed Critical Suntory Ltd
Priority to JP62220792A priority Critical patent/JPS6463377A/en
Publication of JPS6463377A publication Critical patent/JPS6463377A/en
Pending legal-status Critical Current

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2405Glucanases
    • C12N9/2434Glucanases acting on beta-1,4-glucosidic bonds
    • C12N9/2437Cellulases (3.2.1.4; 3.2.1.74; 3.2.1.91; 3.2.1.150)

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Molecular Biology (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Enzymes And Modification Thereof (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Abstract

PURPOSE:To enable production of a cellulase having more excellent thermostability, by cultivating a bacterium containing a plasmid vector integrated with a gene to code thermostable cellulase protein. CONSTITUTION:Chromosome DNA derived from the genus Thermoanaerobacter is blended with restriction enzyme EcoR1 and a plasmid vector to form recobminant plasmid pNB6. Then recombinant plasmid pNB6 is inoculated into Escherichia coli C600 strain to give transformant SAM0772 having a thermostable cellulase gene. Then SAM0722 is to produce cellulase is inoculated into ampicillin-containing L medium and cultivated at about 37 deg.C for 18hr. Then a supernatant liquid of the destroyed cell is obtained as a thermostable cellulase enzyme solution. The optimum temperature of cellulase produced by pNB6 is 80 deg.C. Consequently, thermostable cellulase can be produced by a bacterium such as Escherichia coli to be readily cultivated and productivity of the thermostable cellulase having properties can be raised.
JP62220792A 1987-09-03 1987-09-03 Thermostable cellulase and production thereof Pending JPS6463377A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP62220792A JPS6463377A (en) 1987-09-03 1987-09-03 Thermostable cellulase and production thereof

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP62220792A JPS6463377A (en) 1987-09-03 1987-09-03 Thermostable cellulase and production thereof

Publications (1)

Publication Number Publication Date
JPS6463377A true JPS6463377A (en) 1989-03-09

Family

ID=16756637

Family Applications (1)

Application Number Title Priority Date Filing Date
JP62220792A Pending JPS6463377A (en) 1987-09-03 1987-09-03 Thermostable cellulase and production thereof

Country Status (1)

Country Link
JP (1) JPS6463377A (en)

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2015173602A (en) * 2014-03-13 2015-10-05 本田技研工業株式会社 Method for obtaining natural variant of enzyme, and super thermostable cellobiohydrolase
JP2016111953A (en) * 2014-12-12 2016-06-23 本田技研工業株式会社 Heat-resistant cellobiohydrolase
JP2016167985A (en) * 2015-03-11 2016-09-23 本田技研工業株式会社 Heat-resistant cellobiohydrolase

Cited By (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JP2015173602A (en) * 2014-03-13 2015-10-05 本田技研工業株式会社 Method for obtaining natural variant of enzyme, and super thermostable cellobiohydrolase
US9944914B2 (en) 2014-03-13 2018-04-17 Honda Motor Co., Ltd. Method for obtaining natural variant of enzyme and super thermostable cellobiohydrolase
JP2016111953A (en) * 2014-12-12 2016-06-23 本田技研工業株式会社 Heat-resistant cellobiohydrolase
JP2016167985A (en) * 2015-03-11 2016-09-23 本田技研工業株式会社 Heat-resistant cellobiohydrolase
US10131892B2 (en) 2015-03-11 2018-11-20 Honda Motor Co., Ltd. Thermostable cellobiohydrolase

Similar Documents

Publication Publication Date Title
Tabita et al. Expression and assembly of active cyanobacterial ribulose-1, 5-bisphosphate carboxylase/oxygenase in Escherichia coli containing stoichiometric amounts of large and small subunits.
JPS6474992A (en) Dna sequence, plasmid and production of lipase
WO1991000920A3 (en) Process for preparing a protein by a fungus transformed by multicopy integration of an expression vector
US5439822A (en) Gene expression regulatory DNA
ATE93867T1 (en) RECOMBINANT DNA VECTORS CAPABLE OF EXPRESSING APOAEQUORIN, APOAEQUORINPEPTIDES AND THEIR PRODUCTION AND MICROORGANISMS CONTAINING THESE VECTORS.
Sanbongi et al. Cloning, nucleotide sequence and expression of the cytochrome c‐552 gene from Hydrogenobacter thermophilus
Ishida et al. Production of D-tagatose 3-epimerase of Pseudomonas cichorii ST-24 using recombinant Escherichia coli
AU531972B2 (en) Genetically engineered microorganism producing galactosidase
Passoth et al. Production of a heterologous endo-1, 4-β-xylanase in the yeast Pichia stipitis with an O2-regulated promoter
JPS6463377A (en) Thermostable cellulase and production thereof
ATE30741T1 (en) RECOMBINANT PLASMID AND MICROORGANISM CONTAINING SAME.
Dai et al. Expression of penicillin G acylase from the cloned pac gene of Escherichia coli ATCC11105: Effects of pacR and temperature
Suzuki et al. Gene cloning, overproduction, and characterization of thermolabile alkaline phosphatase from a psychrotrophic bacterium
Neubauer et al. Introduction of the tac‐promoter by lactose under fermentation conditions
JPS6439990A (en) Fused gene by bonding aequorin gene to functional gene
HENNINGSEN et al. Cloning, sequencing and expression of the sialidase gene from Actinomyces viscosus DSM 43798
Brand et al. Molecular cloning of the gene encoding the valyl-tRNA synthetase from Bacillus stearothermophilus
Chan Expression and purification of recombinant lysostaphin in Escherichia coli
Shinomiya et al. Genetic and Enzymatic Studies on Thermostable α-Amylase of Bacillus subtilis Carrying the Amylase Gene from a Thermophilic Bacterium
Kim et al. Changes in Optimum pH and Thermostability of $\alpha $-amylase from Bacillus licheniformis by Site-directed Mutagenesis of His 235 and Asp 328
KR880011334A (en) Method for producing L-phenylalanine by genetically engineered microorganism
Lee et al. Optimization of fermentation conditions for production of recombinant human interleukin-2 in Escherichia coli
EP0263716A3 (en) A process for the preparation of 5'-guanylic acid and expression vectors for use therein
Nikaidou et al. Production, purification, and properties of a pectin lyase from Pseudomonas marginalis N6301
Beppu RECOMBINANT DNA TECHNOLOGY FOR PRODUCTION OF USEFUL SUBSTANCES BY MICROORGANISMS