Characterization of an Endo-.BETA.-1,4-glucanase of Thermotoga maritima Expressed in Escherichia coli.
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منابع مشابه
Purification and properties of an endo-1,4-beta-glucanase translated from a Clostridium josui gene in Escherichia coli.
An endoglucanase encoded by a gene of Clostridium josui was expressed in Escherichia coli and purified. The homogeneous enzyme, with a molecular weight of 39,000, revealed maximum endoglucanase activity at pH 7.2 to 7.5 and a temperature of 65 to 70 degrees C. The enzyme was stable at a temperature lower than 45 degrees C (the growth temperature of the bacterium) in the range of pH 4.5 to 9.0. ...
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The human granulocyte-macrophage colony stimulation factor (hGM-CSF) gene was cloned in the pET 23a( +) expression vector under the control of strong bacteriophage T7 transcription and translation signals. The hGM-CSF gene was transferred into E. coli strainBL21 (DE3)pLysS andIPTG was used for induction of GM-CSF gene. Production of the target protein was obtained as revealed by ELISA and ...
متن کاملAn essential GTPase, der, containing double GTP-binding domains from Escherichia coli and Thermotoga maritima.
A gene encoding a putative GTPase containing two tandemly repeated GTP-binding domains from a hyperthermophilic bacterium, Thermotoga maritima, was cloned and expressed in Escherichia coli. The gene (TM1446) termed der is highly conserved in Eubacteria including E. coli. The purified der product (Tm-Der) has GTPase activity but no ATPase activity. GTP, GDP, and dGTP but not GMP, ATP, CTP, and U...
متن کاملCloning of an endo-(1-->4)-beta-glucanase gene, celA, from the rumen bacterium Clostridium sp. ('C. longisporum') and characterization of its product, CelA, in Escherichia coli.
A genomic library of Clostridium sp. ('C. longisporum') ATCC 49440 in the host Escherichia coli was screened for endo-beta-glucanases, and plasmids pCM64 and pCM4 were isolated. The nucleotide sequence of a 3620 bp fragment was found to contain a 1548 bp open reading frame (ORF), termed celA, which encodes an endo-(1-->4)-beta-glucanase, CelA, assigned to family A4. N-terminal amino acid sequen...
متن کاملPurification and Characterization of an Endo-(1,3)-beta-d-Glucanase from Trichoderma longibrachiatum.
A laminarinase [endo-(1,3)-beta-d-glucanase] has been purified from Trichoderma longibrachiatum cultivated with d-glucose as the growth substrate. The enzyme was found to hydrolyze laminarin to oligosaccharides varying in size from glucose to pentaose and to lesser amounts of larger oligosaccharides. The enzyme was unable to cleave laminaribiose but hydrolyzed triose to laminaribiose and glucos...
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ژورنال
عنوان ژورنال: Journal of Applied Glycoscience
سال: 2002
ISSN: 1344-7882,1880-7291
DOI: 10.5458/jag.49.487