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  • 1
    Electronic Resource
    Electronic Resource
    Biochemical and phylogenetic characterization of two novel deep-sea Thermococcus isolates with potentially biotechnological applications (1997)
    Springer
    Archives of microbiology 167 (1997), S. 233-238 
    Details
    ISSN: 1432-072X
    Keywords: Key words Deep-sea hydrothermal vents ; Thermophilic archaea ; Thermococcus ; Biotechnological applications
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The partial 16S rDNA gene sequences of two thermophilic archaeal strains, TY and TYS, previously isolated from the Guaymas Basin hydrothermal vent site were determined. Lipid analyses and a comparative analysis performed with 16S rDNA sequences of similar thermophilic species showed that the strains isolated from deep-sea vents were not identical to the other species belonging to the genus Thermococcus. On the basis of the results of the phylogenetic analyses, lipid analyses, and previously reported physiological data, we believe that strains TY and TYS are significantly different from the previously described Thermococcus species. According to specific physiological and molecular features, we propose the use of these isolates as potential tools for the development of biotechnological applications in the field of starch processing and DNA technology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050438
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and properties of a hyperthermoactive α-amylase from the archaeobacterium Pyrococcus woesei (1991)
    Springer
    Archives of microbiology 155 (1991), S. 572-578 
    Details
    ISSN: 1432-072X
    Keywords: Hyperthermophilic bacteria ; Thermostability ; Alpha-amylase ; Pyrococcus woesei
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cultivation of the hyperthermophilic archaeobacterium Pyrococcus woesei on starch under continuous gassing (80% H2:20% CO2) caused the formation of 250 U/l of an extremely thermoactive and thermostable α-amylase. In a complex medium without elemental sulphur under 80% N2 and 20% CO2 atmosphere enzyme production could be elevated up to 1000 U/l. Pyrococcus woesei grew preferentially on poly-and oligosaccharides. The amylolytic enzyme formation was constitutive. Enzyme production was also observed in continuous culture at dilution rates from 0.1 to 0.4 h-1. A 20-fold enrichment of α-amylase was achieved after adsorption of the enzyme onto starch and its desorption by preparative gel electrophoresis. The α-amylase consisted of a single subunit with a molecular mass of 70 000 and was catalytically active at a temperature range between 40°C and 130°C. Enzymatic activity was detected even after autoclaving at a pressure of 2 bars at 120°C for 5 h. The purified enzyme hydrolyzed exclusively α-1,4-glycosidic linkages present in glucose polymers of various sizes. Unlike many α-amylases from anaerobes the enzyme from P. woesei was unable to attack short chain oligosaccharides with a chain length between 2 and 6 glucose units.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00245352
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of citrate lyase from Clostridium sporosphaeroides (1985)
    Springer
    Archives of microbiology 141 (1985), S. 85-90 
    Details
    ISSN: 1432-072X
    Keywords: C. sporosphaeroides ; Citrate lyase ; Regulation ; Purification ; Properties ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cells of Clostridium sporosphaeroides which were grown on citrate contained citrate lyase and citrate lyase acetylating enzyme, but no detectable citrate synthase and citrate lyase deacetylase activities. Citrate lyase from C. sporosphaeroides was purified to homogeneity as judged by polyacrylamide gel electrophoresis and high performance liquid chromatography. In contrast to the enzyme from Clostridium sphenoides, the addition of l-glutamate was not necessary for activity and stabilization of the enzyme. The purified enzyme had a specific activity of 34 U/mg protein and was comparable to other citrate lyases with respect to its molecular weight and subunit composition. Electron microscopic investigations showed that similar to the lyase from C. sphenoides and in contrast to all other citrate lyases examined so far, the majority of the enzyme molecules was present in “star” form.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00446745
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  • 4
    Electronic Resource
    Electronic Resource
    Phosphorylation and nucleotidylation of proteins in Rhodocyclus gelatinosus (1986)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 33 (1986), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Cells of Rhodocyclus gelatinosus were radioactively labeled by addition of [32P]orthophosphate, [14C]inosine or [14C]orotic acid during anaerobic growth on citrate in the light. Protein analysis by two-dimensional gel electrophoresis and autoradiography of the gels revealed the presence of several radioactively labeled protein species in this organism. The molecular mass and the isoelectric point of all these proteins were determined. Treatment of the 32P-labeled protein fractions with acid and alkaline phosphatase clearly showed that at least 8 protein species were modified by phosphorylation. The experiments conducted with the 14C-labeled precursors of purines and pyrimidines indicated the presence of 4 protein species which were modified by a compound containing a purine and phosphate, and a single protein simultaneously being labeled with pyrimidine and phosphate.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01291.x
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  • 5
    Electronic Resource
    Electronic Resource
    Citrate metabolism in anaerobic bacteria (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 46 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract The regulation of anaerobic citrate metabolism is very diverse among different groups of bacteria. In organisms like Streptococcus lactis and Clostridium sporosphaeroides which lack citrate synthase, the activity of its antagonistic enzyme, citrate lyase, need not be regulated. Many anaerobes like Rhodocyclus gelatinosus and Clostridium sphenoides are able to synthesize their own l-glutamate and contain citrate synthase. In these bacteria the activity of citrate metabolizing enzymes which are involved in a cascade system are under strict control. In Rc. gelatinosus activation/inactivation of citrate lyase is controlled by acetylation/deacetylation which is catalyzed by its corresponding regulatory enzymes, citrate lyase ligase and citrate lyase deacetylase. In C. sphenoides inactivation of citrate lyase is accomplished by deacetylation as well as by changing in the enzyme conformation. Activation of citrate lyase is catalyzed by citrate lyase ligase whose activity in addition is modulated by phosphorylation/dephosphorylation. Further, electron transport process also seems to play a role in the inactivation of citrate metabolizing enzymes in enteric bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02458.x
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  • 6
    Electronic Resource
    Electronic Resource
    Covalent modification of proteins in Escherichia coli growing anaerobically with nitrate as electron acceptor (1986)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 34 (1986), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Escherichia coli cells were labeled with [32P]orthophosphate under anaerobic conditions using nitrate as electron acceptor. By 2-dimensional gel electrophoresis, 20 protein species were found to be radioactively labeled; their isoelectric points and molecular masses were determined. Treating the labeled extract with alkaline phosphatase revealed evidence for the presence of 9 proteins modified by phosphorylation. Treatment with snake venom phosphodiesterase also indicated that 2 protein species in E. coli were modified by phosphate-containing compounds which were bound to the protein by a phosphodiester bond.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1986.tb01410.x
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  • 7
    Electronic Resource
    Electronic Resource
    Crystallization and preliminary X-ray crystallographic studies of the thermoactive pullulanase type I, hydrolyzing α-1,6 glycosidic linkages, from Fervidobacterium pennivorans Ven5 (2000)
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 56 (2000), S. 1470-1472 
    Details
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: Crystals of the thermoactive recombinant F. pennivorans type I pullulanase, purified from the supernatant of a Bacillus subtilis culture, have been obtained by the vapour-diffusion method in the presence of the inhibitor β-cyclodextrin (2 mM) by mixing protein (15 mg ml−1) with an equal volume of crystallization solution containing 0.1 M bis–tris propane pH 6.5, 50 mM MgCl2 and 15% polyethylene glycol 3350. Crystals diffracted to 3.0 Å using conventional Cu Kα radiation and belong to space group P212121, with unit-cell parameters a = 76.8, b = 96.2, c = 98.5 Å. The asymmetric unit contains one monomer. A preliminary 26% complete data set has been collected at 2.2 Å resolution using synchrotron radiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S090744490001074X
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  • 8
    Electronic Resource
    Electronic Resource
    Cloning, expression and biochemical characterisation of a unique thermostable pullulan-hydrolysing enzyme from the hyperthermophilic archaeon Thermococcus aggregans (2000)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 190 (2000), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The gene for a new type of pullulan hydrolase from the hyperthermophilic archaeon Thermococcus aggregans was cloned and expressed in Escherichia coli. The 2181-bp open reading frame encodes a protein of 727 amino acids. A hypothetical membrane linker region was found to be cleaved during processing in E. coli. The recombinant enzyme was purified 70-fold by heat treatment, affinity and anion exchange chromatography. Optimal activity was detected at 95°C at a broad pH range from 3.5 to 8.5 with an optimum at pH 6.5. More than 35% of enzymatic activity was detected even at 120°C. The enzyme was stable at 90°C for several hours and exhibited a half-life of 2.5 h at 100°C. Unlike all pullulan-hydrolysing enzymes described to date, the enzyme is able to attack α-1,6- as well as α-1,4-glycosidic linkages in pullulan leading to the formation of a mixture of maltotriose, panose, maltose and glucose. The enzyme is also able to degrade starch, amylose and amylopectin forming maltotriose and maltose as main products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2000.tb09290.x
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization of the xylanases from the new isolated thermophilic xylan-degrading Bacillus thermoleovorans strain K-3d and Bacillus flavothermus strain LB3A (1997)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 148 (1997), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Three strictly aerobic strains (K-1, K-3d and K-4) were isolated from a hot-spring in Kobe, Japan, and a facultative anaerobic strain LB3A was isolated from sediments collected from the alkaline Lake Bogoria, Kenya. All strains were thermophilic and capable of growth on xylan. On the basis of morphological, physiological and phylogenetic studies the new aerobic isolates resemble the thermophilic species Bacillus thermoleovorans while the facultative anaerobic isolate LB3A resembles the facultative anaerobic thermophilic species Bacillus flavothermus. When grown on xylan as sole carbon source, all isolates produce thermoactive xylanases. Xylanases from strains K-3d and LB3A are active at temperatures between 40 and 90°C and pH values between 5.0 and 9.0. Applying SDS-PAGE the crude xylanase complex of isolate K-3d was shown to be composed of two active bands, with molecular masses of 40 and 69 kDa. The crude xylanase complex of isolate LB3A, on the other hand, is composed of at least four activity bands with molecular masses ranging from 80 to 130 kDa. Due to the product pattern of xylan hydrolysis both enzymes are classified as endoxylanases. The xylanolytic enzyme system of isolate K-3d produces xylotriose, xylotetraose and larger xylooligosacharides, whereas the xylanases from isolate LB3A release xylotetraose as the major product of hydrolysis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1997.tb10290.x
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  • 10
    Electronic Resource
    Electronic Resource
    Heat-stable pullulanase from Bacillus acidopullulyticus: characterization and refolding after guanidinium chloride-induced unfolding (1999)
    Springer
    Extremophiles 3 (1999), S. 147-152 
    Details
    ISSN: 1433-4909
    Keywords: Key words Pullulanase ; Bacillus acidopullulyticus ; Denaturation ; Renaturation ; Thermostability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Heat-stable pullulanase from Bacillus acidopullulyticus was characterized with respect to its stability against thermal and chemical denaturation and its reactivation after complete chemical unfolding. The enzyme was quite thermostable and retained 55% of activity after heating at 60°C for 30 min at pH 5.5. At pH 6.0, only 9% residual activity was observed. The addition of sucrose, polyols, and Na2SO4 strongly stabilized the enzyme against thermal inactivation. The processes of chemical unfolding by guanidinium chloride (GdmCl) and refolding were studied by enzymological and spectroscopic criteria. B. acidopullulyticus pullulanase was very sensitive to GdmCl denaturation and had a transition midpoint at 1.2 M GdmCl. Reactivation after complete unfolding in 5 M GdmCl was initiated by dilution of the unfolding mixture; 67% reactivation was observed under standard conditions. The influence of some chemical and physical parameters (pH, chemical agents, temperature, and unfolding and refolding time) on refolding was investigated. Of the additives tested to assist reactivation, only bovine serum albumin (BSA) increased the yield of activity to 80%. The full regain of structure and activity was proven by comparing the enzymological, physicochemical, and spectroscopic properties of the native and refolded pullulanase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050110
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