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pro vyhledávání: '"Thermococcus hydrothermalis"'
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Publikováno v:
Biologia. 65:408-415
The presented work is focused on the naturally thermostable α-amylase from the archaebacterium Thermococcus hydrothermalis. From the evolutionary point of view, the archaeal α-amylases are most closely related to plant α-amylases. In a wider sense
Publikováno v:
Enzyme and Microbial Technology. 39:1300-1305
A gene encoding the thermostable α-amylase from hyperthermophilic archaeon Thermococcus hydrothermalis was cloned in Escherichia coli . In an effort to achieve the improved expression, four DNA primers (three reverse and one forward) were designed t
Publikováno v:
European Journal of Biochemistry. 271:2863-2872
Fifty-nine amino acid sequences belonging to family 57 (GH-57) of the glycoside hydrolases were collected using the CAZy server, Pfam database and blast tools. Owing to the sequence heterogeneity of the GH-57 members, sequence alignments were perform
Publikováno v:
International Journal of Systematic and Evolutionary Microbiology
International Journal of Systematic and Evolutionary Microbiology, 2003, 53 (3), pp.847-851. ⟨10.1099/ijs.0.02503-0⟩
International Journal of Systematic and Evolutionary Microbiology, 2003, 53 (3), pp.847-851. ⟨10.1099/ijs.0.02503-0⟩
Enrichments for anaerobic organotrophic hyperthermophiles were performed with hydrothermal chimney samples collected at the Guaymas Basin (27 degrees 01' N, 111 degrees 24' W). Positive enrichments were submitted to gamma-irradiation at a dose of 30
Autor:
Michael J. O’Donohue, Florent Chang-Pi-Hin, Marta Erra-Pujada, Philippe Debeire, Francis Duchiron
Publikováno v:
Biotechnology Letters. 23:1273-1277
A pullulanase type II was produced in Escherichia coli using the relevant gene from Thermococcus hydrothermalis. This protein was purified and its pullulanolytic and amylolytic activities were characterised. The optimum temperature and Ca2+ concentra
Autor:
Hubert Gantelet, Francis Duchiron
Publikováno v:
Biotechnology Letters. 21:71-75
A crude preparation of thermostable pullulanase from Thermococcus hydrothermalis produced glucose and maltose syrups from starches. The use of pullulanase reduced the saccharification reaction time up to 37.5%. In the case of maltose syrup production
Autor:
H. Gantelet, F. Duchiron
Publikováno v:
Applied Microbiology and Biotechnology. 49:770-777
The extremely thermophilic archaeon Thermococcus hydrothermalis, isolated from a deep-sea hydrothermal vent in the East Pacific Rise at 21°N, produced an extracellular pullulanase. This enzyme was purified 97-fold to homogeneity from cell-free cultu
Publikováno v:
Starch - Stärke. 50:84-89
Hydrolysis of native starch at 90°C by the α-amylase from Bacillus licheniformis and the α-glucosidase of Thermococcus hydrothermalis, an archaeum, has been investigated. The archaeal enzyme is optimally active at 110°C and pH 5.5. At 96°C, the
Publikováno v:
Biotechnology Letters. 20:363-367
A cell extract of Thermococcus hydrothermalis, grown for 6 h, gave α-glucosidase activity at 14.9 U/l, degrading oligosaccharides and maltose. α-Amylase, α-glucosidase and pullulanase activities were detected at 289 U/l, 13.5 U/l and 30 U/l respec