GLORIA

GEOMAR Library Ocean Research Information Access

feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Keywords: Forschungsbericht ; Isomerasen ; Enzymkatalyse ; Thermoproteus ; Monosaccharide ; Kristallstrukturanalyse
    Type of Medium: Online Resource
    Pages: 1 Online-Ressource (31 Seiten, 6,06 MB) , Diagramme
    Language: German
    Note: Förderkennzeichen BMBF 031B0271 , Verbundnummer 01178234 , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 2
    Keywords: Forschungsbericht ; Transferasen ; Biokatalysator
    Type of Medium: Online Resource
    Pages: 1 Online-Ressource (13 Seiten, 512 KB)
    Language: German
    Note: Förderkennzeichen BMBF 031A222 , Unterschiede zwischen dem gedruckten Dokument und der elektronischen Ressource können nicht ausgeschlossen werden
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 3
    In: Biológia 〈Bratislava〉, Berlin : De Gruyter, 1953, 63(2008), 6, 0006-3088
    In: volume:63
    In: year:2008
    In: number:6
    Description / Table of Contents: Six glycoside hydrolase (GH) family 13 members, classified under the polyspecific neopullulanase subfamily GH13_20 (also termed cyclomaltodextrinase) were analysed. They originate from thermophilic bacterial strains (Anoxybacillus flavithermus, Laceyella sacchari, and Geobacillus thermoleovorans) or from environmental DNA, collected after in situ enrichments in Icelandic hot springs. The genes were isolated following the CODEHOP consensus primer strategy, utilizing the first two of the four conserved sequence regions in GH13. The typical domain structure of GH13_20, including an N-terminal domain (classified as CBM34), the catalytic module composed of the A-and B-domains, and a C-terminal domain, was found in five of the encoded enzymes (abbreviated Amy1, 89, 92, 98 and 132). These five enzymes degraded cyclomaltodextrins (CDs) and starch, while only three, Amy92 (L. sacchari), Amy98 (A. flavithermus) and Amy132 (environmental DNA), also harboured neopullulanase activity. The L. sacchari enzyme was monomeric, but with CD as the preferred substrate, which is an unusual combination. The sixth enzyme (Amy29 from environmental DNA), was composed of the ABC-domains only. Preferred substrate for Amy29 was pullulan, which was degraded to panose, and the enzyme had no detectable activity on CDs. In addition to its different activity profile and domain composition, Amy29 also displayed a different conservation (LPKF) in the fifth conserved region (MPKL) proposed to identify the subfamily. All enzymes had apparent temperature optima in the range 50-65°C, while thermostability varied, and was highest for Amy29 with a half-life of 480 min at 80ʿC. Calcium dependent activity or stability was monitored in four enzymes, but could not be detected for Amy29 or 98. Tightly bound calcium can, however, not be ruled out, and putative calcium ligands were conserved in Amy98.
    Type of Medium: Online Resource
    ISSN: 0006-3088
    Language: English
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 4
    Keywords: Hochschulschrift
    Type of Medium: Online Resource
    Pages: Online-Ressource (PDF-Datei: 119 Bl., 0.75 MB) , Ill., graph. Darst.
    Edition: 2008 [Online-Ausg.]
    DDC: 570
    Language: German
    Note: Kiel, Univ., Diss., 2005 , Online-Ausg.: , [Online-Ausg.]
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 5
    In: Applied and environmental microbiology, Washington, DC [u.a.] : Soc., 1976, 74(2008), 6, Seite 1914-1921, 1098-5336
    In: volume:74
    In: year:2008
    In: number:6
    In: pages:1914-1921
    Description / Table of Contents: Starch and pullulan-modifying enzymes of the α-amylase family (glycoside hydrolase family 13) have several industrial applications. To date, most of these enzymes have been derived from isolated organisms. To increase the number of members of this enzyme family, in particular of the thermophilic representatives, we have applied a consensus primer-based approach using DNA from enrichments from geothermal habitats. With this approach, we succeeded in isolating three new enzymes: a neopullulanase and two cyclodextrinases. Both cyclodextrinases displayed significant maltogenic amylase side activity, while one showed significant neopullulanase side activity. Specific motifs and domains that correlated with enzymatic activities were identified; e.g., the presence of the N domain was correlated with cyclodextrinase activity. The enzymes exhibited stability under thermophilic conditions and showed features appropriate for biotechnological applications.
    Type of Medium: Electronic Resource
    ISSN: 1098-5336
    Language: English
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 123 (1979), S. 105-107 
    ISSN: 1432-072X
    Keywords: Nickel ; Cobalt ; Molybdenum ; Iron ; Methanobacterium thermoautotrophicum ; Trace elements
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Growth of Methanobacterium thermoautotrophicum on H2 and CO2 as sole energy and carbon sources was found to be dependent on Ni, Co, and Mo. At low concentrations of Ni (〈100 nM), Co (〈10 nM) and Mo (〈10 nM) the amount of cells formed was roughly proportional to the amount of transition metal added to the medium; for the formation of 1 g cells (dry weight) approximately 150 nmol NiCl2, 20 nmol CoCl2 and 20 nmol Na2MoO4 were required. A dependence of growth on Cu, Mn, Zn, Ca, Al, and B could not be demonstrated. Conditions are described under which the bacterium grew exponentially with a doubling time of 1.8 h up to a cell density of 2 g cells (dry weight)/1.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 7
    ISSN: 1432-072X
    Keywords: Methanobacterium thermoautotrophicum ; Potassium accumulation ; Membrane potential ; pH gradient ; Energy coupling ; Active transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cultures of Methanobacterium thermoautotrophicum (Marburg) growing on media low in potassium accumulated the cation up to a maximal concentration gradient ([K+]intracellular/[K+]extracellular) of approximately 50,000-fold. Under these conditions, the membrane potential was determined by measuring the equilibrium distribution of the lipophilic cation (14C) tetraphenylphosphonium (TPP+). This cation was accumulated by the cells 350-to 1,000-fold corresponding to a membrane potential (inside negative) of 170–200 mV. The pH gradient, as measured by equilibrium distribution of the weak acid, benzoic acid, was found to be lower than 0.1 pH units (extracellular pH=6.8). The addition of valinomycin (0.5–1 nmol/mg cells) to the culture reduced the maximal concentration gradient of potassium from 50,000-to approximately 500-fold, without changing the membrane potential. After dissipation of the membrane potential by the addition of 12C-TTP+ (2 μmol/mg cells) or tetrachlorosalicylanilide (3 nmol/mg cells), a rapid and complete efflux of potassium was observed. These data indicate that potassium accumulation in the absence of valinomycin is not in equilibrium with the membrane potential. It is concluded that at low extracellular K+ concentrations potassium is not accumulated by M. thermoautotrophicum via an electrogenic uniport mechanism.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 155 (1991), S. 366-377 
    ISSN: 1432-072X
    Keywords: Pyrococcus furiosus ; Hyperthermophilic archabacteria ; Pyruvate fermentation ; Growth yields ; Hydrogen inhibition ; Sulfur stimulation ; Pyruvate:ferredoxin oxidoreductase ; Acetyl-CoA synthetase (ADP forming) ; Adenylate kinase ; ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The hyperthermophilic anaerobe Pyrococcus furiosus was found to grow on pyruvate as energy and carbon source. Growth was dependent on yeast extract (0.1%). The organism grew with doublings times of about 1 h up to cell densities of 1–2×108 cells/ml. During growth 0.6–0.8 mol acetate and 1.2–1.5 mol CO2 and 0.8 mol H2 were formed per mol of pyruvate consumed. The molar growth yield was 10–11 g cells(dry weight)/mol pyruvate. Cell suspensions catalyzed the conversion of 1 mol of pyruvate to 0.6–0.8 mol acetate, 1.2–1.5 mol CO2, 1.2 mol H2 and 0.03 mol acetoin. After fermentation of [3-14C]pyruvate the specific radioactivities of pyruvate, CO2 and acetate were equal to 1:0.01:1. Cellfree extracts contained the following enzymatic activities: pyruvate: ferredoxin (methyl viologen) oxidoreductase (0.2 U mg-1, T=60°C, with Clostridium pasteurianum ferredoxin as electron acceptor; 1.4 U mg-1 at 90°C, with methyl viologen as electron acceptor); acetyl-CoA synthetase (ADP forming) [acetyl-CoA+ADP+Pi⇆acetate+ATP+CoA] (0.34 U mg-1, T=90°C), and hydrogen: methyl viologen oxidoreductase (1.75 U mg-1). Phosphate acetyl-transferase activity, acetate kinase activity, and carbon monoxide:methyl viologen oxidoreductase activity could not be detected. These findings indicate that the archaebacterium P. furiosus ferments pyruvate to acetate, CO2 and H2 involving only three enzymes, a pyruvate:ferredoxin oxidoreductase, a hydrogenase and an acetyl-CoA synthetase (ADP forming).
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 9
    ISSN: 1432-072X
    Keywords: Pyrococcus furiosus ; Hyperthermophiles ; Sugar fermentation ; Non-phosphorylated Entner ; Doudoroff pathway ; 2-Keto-3-deoxy-gluconate aldolase ; Glyceraldehyde dehydrogenase ; 2-Phosphoglycerate-forming glycerate kinase ; ADP-depenent acetyl-CoA synthetase ; Substrate level phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The hyperthermophilic anaerobe Pyrococcus furiosus was grown on maltose as energy and carbon source. During growth 1 mol maltose was fermented to 3–4 mol acetate, 6–7 mol H2 and 3–4 mol CO2. The presence of the following enzyme activities in cell extracts of maltose-grown P. furiosus indicate that the sugar is degraded to pyruvate and H2 by a modified “non-phosphorylated” Entner-Doudoroff-pathway (the values given in brackets are specific enzyme activities at 100 °C): Glucose: methyl viologen oxidoreductase (0.03 U/mg); 2-keto-3-deoxy-gluconate aldolase (0.03 U/mg); glyceraldehyde: benzyl viologen oxidoreductase (2.6 U/mg), glycerate kinase (2-phosphoglycerate forming) (0.48 U/mg), enolase (10.4 U/mg), pyruvate kinase (1.4 U/mg). Hexokinase, glucose-6-phosphate dehydrogenase, 2-keto-3-deoxy-6-phosphogluconate aldolase and phosphofructokinase could not be detected. Further conversion of pyruvate to acetate, CO2 and H2 involves pyruvate: ferredoxin oxidoreductase (0.4 U/mg; T=60°C with Clostridium pasteurianum ferredoxin as electron acceptor), hydrogen: methyl viologen ixodoreductase (3.4 U/mg) and ADP-dependent acetyl-CoA synthetase (1.9 U/mg). Phosphate acetyl transferase and acetate kinase could not be detected. The ADP-dependent acetyl-CoA synthetase catalyzes ATP synthesis via the mechanism of substrate level phosphorylation and apparently constitutes the only ATP conserving site during maltose catabolism in P. furiosus. This novel pathway of maltose fermentation to acetate, CO2 and H2 in the anaerobic archaeon P. furiosus may represent a phylogenetically ancient pathway of sugar fermentation.
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
  • 10
    ISSN: 1432-072X
    Keywords: Thermotoga maritima ; Hyperthermophiles ; (Eu)Bacteria ; Glucose fermentation ; Acetate formation ; Embden-Meyerhof pathway ; Hexokinase ; Phosphofructokinase ; Acetake kinase ; Sulfur reduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The hyperthermophilic anaerobic eubacterium Thermotoga maritima was grown on glucose as carbon and energy source. During growth 1 mol glucose was fermented to 2 mol acetate, 2 mol CO2 and 4 mol H2. The molar growth yicld on glucose (Yglucose) was about 45 g cell dry mass/mol glucose. In the presence of elemental sulfur growing cultures of T. maritima converted 1 mol glucose to 2 mol acetate, 2 mol CO2 about 0.5 mol H2 and about 3.5 mol H2S. Yglucose was about 45 g/mol. Cell extracts contained all enzymes of the Embden-Meyerhof pathway: hexokinase (0.29 U/mg, 50°C), glucose-6-phosphate isomerase (0.56 U/mg, 50°C), phosphofructokinase (0.19 U/mg, 50° C), fructose-1,6-bisphosphate aldolase (0.033 U/mg, 50°C), triosephosphate isomerase (6.3 U/mg, 50°C), glyceraldehyde-3-phosphate dehydrogenase (NAD+ reducing: 0.63 U/mg, 50°C), phosphoglycerate kinase (3.7 U/mg, 50°C), phosphoglycerate mutase (0.4 U/mg, 50°C); enolase (4 U/mg, 80°C), pyruvate kinase (0.05 U/mg, 50°C). Furthermore, cell extracts contained pyruvate: ferredoxin oxidoreductasee (0.43 U/mg, 60°C); NADH: ferredoxin oxidoreductase (benzylviologen reduction: 0.46 U/mg, 80°C); hydrogenase (benzylviologen reduction: 15 U/mg, 80°C), phosphate acetyltransferase (0.13 U/mg, 80°C), acetate kinase (1.2 U/mg, 55°C), lactate dehydrogenase (0.16 U/mg, 80°C) and pyruvate carboxylase (0.02 U/mg, 50°C). The findings indicate that the hyperthermophilic eubacterium T. maritima ferments sugars (glucose) to acetate, CO2 and H2 involving the Embden-Meyerhof pathway, phosphate acetyltransferase and acetate kinase. Thus, the organism differs from the hyperthermophilic archaeon Pyrococcus furiosus which ferments sugars to acetate, CO2 and H2 involving a modified non-phosphorylated Entner-Doudoroff pathway and acetyl-CoA synthetase (ADP forming).
    Type of Medium: Electronic Resource
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...