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  • Articles  (6)
  • Articles: DFG German National Licenses  (6)
  • 1
    Electronic Resource
    Electronic Resource
    Nucleotide sequence of arfB of Clostridium stercorarium, and prediction of catalytic residues of α-l-arabinofuranosidases based on local similarity with several families of glycosyl hydrolases (1998)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 164 (1998), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The nucleotide sequence of the α-l-arabinofuranosidase gene arfB from Clostridium stercorarium was determined. The deduced protein has a molecular mass of 56.2 kDa with an amino terminus identical to the N-terminal sequence of the purified mature enzyme from C. stercorarium. Its sequence is homologous to arabinofuranosidases of glycosyl hydrolase family 51. Sequence alignment and cluster analysis reveal three new members of glycosyl hydrolase family 51, allowing for the definition of highly conserved regions. Two of these regions are remarkably similar to the most conserved regions within several other families of glycosyl hydrolases, which have in common a (β/α)8-barrel as the core super-secondary structure, and allow to predict the acid/base catalyst and the nucleophile of the active site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1998.tb13107.x
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  • 2
    Electronic Resource
    Electronic Resource
    The thermostable α-l-rhamnosidase RamA of Clostridium stercorarium: biochemical characterization and primary structure of a bacterial α-l-rhamnoside hydrolase, a new type of inverting glycoside hydrolase (2000)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 35 (2000), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: An α-l-rhamnosidase clone was isolated from a genomic library of the thermophilic anaerobic bacterium Clostridium stercorarium and its primary structure was determined. The recombinant gene product, RamA, was expressed in Escherichia coli, purified to homogeneity and characterized. It is a dimer of two identical subunits with a monomeric molecular mass of 95 kDa in SDS polyacrylamide gel electrophoresis. At pH 7.5 it is optimally active at 60°C and insensitive to moderate concentrations of Triton X100, ethanol and EDTA. It hydrolysed p-nitrophenyl-α-l-rhamnopyranoside, naringin and hesperidin with a specific activity of 82, 1.5 and 0.46 U mg−1 respectively. Hydrolysis occurs by inversion of the anomeric configuration as detected using 1H-NMR, indicating a single displacement mechanism. Naringin was hydrolysed to rhamnose and prunin, which could further be degraded by incubation with a thermostable β-glucosidase. The secondary structure of RamA consists of 27% α-helices and 50% β-sheets, as detected by circular dichroism. The primary structure of the ramA gene has no similarity to other glycoside hydrolase sequences and possibly is the first member of a new enzyme family.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.01691.x
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  • 3
    Electronic Resource
    Electronic Resource
    A major new component in the cellulosome of Clostridium thermocellum is a processive endo-β-1,4-glucanase producing cellotetraose (2005)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 249 (2005), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Cel9R, a major component in the cellulosome of Clostridium thermocellum, is one of the most prevalent β-glucanases in the complex after Cel48S and Cel8A. The recombinant product of gene celR is optimally active at 78.5°C on amorphous cellulose, carboxymethyl-cellulose, and barley β-1,3–1,4-glucan. From amorphous cellulose it produces initially cellotetraose which is slowly degraded to glucose, cellobiose and cellotriose. This product pattern indicates a processive endoglucanase-mode which was corroborated by the initial and simultaneous production of new reducing ends in the soluble as well as in the insoluble fraction of amorphous cellulose. p NP-Cellopentaoside is degraded to cellotetraose and p NP-glucoside, suggesting cellotetraose release from the non-reducing end. The newly discovered Cel9R thus is a novel type of cellulase in the cellulosome of C. thermocellum: a processive endo-β-1,4-glucanase producing cellotetraose as the primary hydrolysis product. The presence in the cellulosome and the hydrolytic mode of this cellotetraohydrolase has implications for our understanding of the in vivo conversion of cellulose by bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/j.femsle.2005.06.037
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  • 4
    Electronic Resource
    Electronic Resource
    High-level expression of Clostridium thermocellum cellulase genes in Escherichia coli (1987)
    Springer
    Applied microbiology and biotechnology 27 (1987), S. 50-56 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The Clostridium thermocellum cellulase genes celA and celC encoding endoglucanase A and C were subcloned in a temperature-regulated Escherichia coli expression vector containing the leftward promoterpl of bacteriophage lambda. The level of gene expression was controlled by thermal inactivation of the heat-sensitive lambda cI857 repressor. Under optimal conditions the recombinant endoglucanases A and C were expressed to a level of 10–15% of total cellular protein. Endoglucanase A was partially exported into the periplasmic space, whereas endoglucanase C was found sequestered within the cytoplasm. Overexpression of the celA gene resulted in decreased cell viability concomitant with the accumulation of endoglucanase A in the membrane fraction. In contrast, high-level synthesis of the celC gene product was well tolerated by the host cell. Overproduced endoglucanase C accumulated as a soluble enzyme without detectable formation of inactive inclusion bodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00257253
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  • 5
    Electronic Resource
    Electronic Resource
    Degradation of barley β-glucan by endoglucanase C of Clostridium thermocellum (1988)
    Springer
    Applied microbiology and biotechnology 29 (1988), S. 25-31 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Endoglucanase C encoded by the celC gene of Clostridium thermocellum has been purified to homogeneity from a recombinant Escherichia coli strain. It was found that this enzyme is highly efficient in degrading glucans with alternating β-1,4- and β-1,3-linkages but lacks activity on unmodified cellulosic substrates. The properties of endoglucanase C were compared to those of Bacillus subtilis β-glucanase, an enzyme used in the brewing industry for β-glucan degradation. Both enzyme cause a rapid decrease of the viscosity of barley β-glucan as a result of internal chain cleavage. Endoglucanase C hydrolyses non-specifically β-1,3- and β-1,4-bonds adjacent to unsubstituted or 4-O′-substituted cellobiose units. Due to its lower pH optimum and increased thermostability endoglucanase C compares favourably with B. subtilis β-glucanase and seems suitable for use in the mashing process of beer brewing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00258346
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  • 6
    Electronic Resource
    Electronic Resource
    Sequence analysis of the Clostridium stercorarium celZ gene encoding a thermoactive cellulase (Avicelase I): Identification of catalytic and cellulose-binding domains (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 258-267 
    Details
    ISSN: 1617-4623
    Keywords: DNA sequence ; Cellulase ; Endoglucanase ; Clostridium stercorarium ; Avocado
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of the celZ gene coding for a thermostable endo-β-1,4-glucanase (Avicelase I) of Clostridium stercorarium was determined. The structural gene consists of an open reading frame of 2958 by which encodes a preprotein of 986 amino acids with an Mr of 109000. The signal peptide cleavage site was identified by comparison with the N-terminal amino acid sequence of Avicelase I purified from C. stercorarium culture supernatants. The recombinant protein expressed in Escherichia coli is proteolytically cleaved into catalytic and cellulose-binding fragments of about 50 kDa each. Sequence comparison revealed that the N-terminal half of Avicelase I is closely related to avocado (Persea americana) cellulase. Homology is also observed with Clostridium thermocellum endoglucanase D and Pseudomonas fuorescens cellulase. The cellulose-binding region was located in the C-terminal half of Avicelase I. It consists of a reiterated domain of 88 amino acids flanked by a repeated sequence about 140 amino acids in length. The C-terminal flanking sequence is highly homologous to the non-catalytic domain of Bacillus subtilis endoglucanase and Caldocellum saccharolyticum endoglucanase B. It is proposed that the enhanced cellulolytic activity of Avicelase I is due to the presence of multiple cellulose-binding sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00265062
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