Results 171 to 180 of about 4,623 (199)

Transformation of Clostridium Thermocellum by Electroporation

2012
In this work, we provide detailed instructions for transformation of Clostridium thermocellum by electroporation. In addition, we describe two schemes for genetic modification: allelic replacement-where the gene of interest is replaced by an antibiotic marker and markerless gene deletion-where the gene of interest is removed and the selective markers ...
Daniel G, Olson, Lee R, Lynd
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Cellulolytic and physiological properties of Clostridium thermocellum

Archives of Microbiology, 1977
Three strains of Clostridium thermocellum obtained from various sources were found to have nearly identical deoxyribonucleic acid guanosine plus cytosine contents that ranged from 38.1–39.5 mole-%. All strain examined fermented only cellulose and cellulose derivatives, but not glucose, or xylose or other sugars.
T K, Ng, T K, Weimer, J G, Zeikus
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Nucleotide sequence of the Clostridium thermocellum laminarinase gene

Biochemical and Biophysical Research Communications, 1991
The sequence presented (1022 bp) shows the Clostridium thermocellum laminarinase gene (lam1) and its flanking regions. The gene lam1 comprises an open reading frame of 726 nt, encoding a 242-aa protein with predicted Mr 27661. The ORF startswith the translation initiation codon ATG.
V V, Zverlov, D A, Laptev, V I, Tishkov, G A, Velikodvorskaja   +3 more
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The Cellulosome of Clostridium thermocellum

1988
Publisher Summary The accelerated interest in microbial cellulases stems from their potential industrial application. This area is an excellent example in which basic and applied science are closely interlinked: the better understood the mechanism of cellulase action; the better can be the applicative value as a biotechnological process. This chapter
Raphael Lamed, Edward A. Bayer
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Thermostable, ammonium-activated malic enzyme of Clostridium thermocellum

Biochimica et Biophysica Acta (BBA) - Enzymology, 1981
"Malic" enzyme (L-malate:NADP+ oxidoreductase (oxaloacetate-decarboxylating, EC 1.1.1.40) was purified from Clostridium thermocellum by DEAE-cellulose, agarose-NADP and Sephadex G-200 column chromatography. The 117-fold purified "malic" enzyme displayed a maximum activity of 135 units/mg at 40 degrees C and represented 0.8% of the total cell protein ...
R, Lamed, J G, Zeikus
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Studies on cellulase production by Clostridium thermocellum

European Journal of Applied Microbiology and Biotechnology, 1980
Clostridium thermocellum ATCC 27405 (and its improved cellulase-producing mutant, AS-39) is an anaerobic thermophile that produces endo-β-glucanase and exo-β-glucanase when grown on cellobiose or cellulose as major carbon source (Shinmyo et al. 1979). The site of cellulase accumulation was at least 95% extracellular.
D. V. Garcia-Martinez, A. Shinmyo, A. Madia, A. L. Demain   +3 more
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Transcriptome data for Clostridium thermocellum

Transcriptome data for rare earth-treated Clostridium thermocellum and untreated.
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The cellulosome of Clostridium thermocellum

Biochemical Society Transactions, 1998
P, Béguin, P M, Alzari
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Xylan-breakdown apparatus of Clostridium thermocellum

Cellulose, 2022
Pedro R. V. Hamann, Eliane F. Noronha
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Clostridium thermocellum

2015
Steven D. Brown, Kyle B. Sander, Chia-Wei Wu, Adam M. Guss   +3 more
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