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  • 1
    Monograph available for loan
    Monograph available for loan
    Stuttgart [u.a.] : Thieme
    Call number: M 11.0304
    Type of Medium: Monograph available for loan
    Pages: XX, 678 S.
    Edition: 8., vollst. überarb. und erw. Aufl.
    ISBN: 9783134446081
    Location: Upper compact magazine
    Branch Library: GFZ Library
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  • 2
    Publication Date: 1954-06-01
    Print ISSN: 0003-9276
    Topics: Biology
    Published by Springer
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  • 3
  • 4
    Publication Date: 1966-07-01
    Print ISSN: 0003-2697
    Electronic ISSN: 1096-0309
    Topics: Biology , Chemistry and Pharmacology
    Published by Elsevier
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  • 5
    ISSN: 1572-8900
    Keywords: Poly(3-hydroxybutyrate) ; poly(3-hydroxyalkanoate) ; PHB depolymerase ; degradation ; Comamonas sp.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Bacteria capable of growing on poly(3-hydroxybutyrate), PHB, as the sole source of carbon and energy were isolated from various soils, lake water, activated sludge, and air. Although all bacteria utilized a wide variety of monomeric substrates for growth, most of the strains were restricted to degrade PHB and copolymers of 3-hydroxybutyrate and 3-hydroxyvalerate, P(3HB-co-3HV). Five strains were also able to decompose a homopolymer of 3-hydroxyvalerate, PHV. Poly(3-hydroxyoctanoate), PHO, was not degraded by any of the isolates. One strain, which was identified asComamonas sp., was selected, and the extracellular depolymerase of this strain was purified from the medium by ammonium sulfate precipitation and by chromatography on DEAE-Sephacel and Butyl-Sepharose 4B. The purified PHB depolymerase was not a glycoprotein. The relative molecular masses of the native enzyme and of the subunits were 45,000 or 44,000, respectively. The purified enzyme hydrolyzed PHB, P(3HB-co-3HV), and—at a very low rate—also PHV. Polyhydroxyalkanoates, PHA, with six or more carbon atoms per monomer or characteristic substrates for lipases were not hydrolyzed. In contrast to the PHB depolymerases ofPseudomonas lemoignei andAlcaligenes faecalis T1, which are sensitive toward phenylmethylsulfonyl fluoride (PMSF) and which hydrolyze PHB mainly to the dimeric and trimeric esters of 3-hydroxybutyrate, the depolymerase ofComamonas sp. was insensitive toward PMSF and hydrolyzed PHB to monomeric 3-hydroxybutyrate indicating a different mechanism of PHB hydrolysis. Furthermore, the pH optimum of the reaction catalyzed by the depolymerase ofComamonas sp. was in the alkaline range at 9.4.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1572-8773
    Keywords: DNA-DNA homologies ; Klebsiella oxytoca ; nickel resistance ; transconjugants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Klebsiella oxytoca strain CCUG 15788, isolated from a mineral oil emulsion tank in Göteborg, Sweden, was found to be nickel-resistant (tolerating 10 mm NiCl2 in non-complexing mineral-gluconate media; inducible resistance). The nickel resistance determinants were transferred by helper-assisted conjugation to various strains of Escherichia coli and Citrobacter freundii and expressed to between 5 and 10 mm NiCl2. A 4.3 kb HindIII fragment was cloned from the genomic DNA of K. oxytoca. Ligated into the vector pSUP202, the fragment caused constitutive nickel resistance (of up to 3 or 10 mm Ni2+) in various E. coli strains. After cloning into the broad host range vector pVDZ'2 the fragment even expressed low nickel resistance in the transconjugant of Alcaligenes eutrophus AE104. With the 4.3 kb HindIII fragment as a biotinylated DNA probe it was shown by DNA-DNA hybridization that the nickel resistance determinant resides on the chromosome of K. oxytoca and not on its circular plasmid pKO1 (160 kb) or linear plasmid pKO2 (50 kb). Nickel resistance strongly correlated with the presence of the 4.3 kb HindIII fragment in the transconjugants. No homologies were detected when the nickel resistance determinants of other well-known nickel-resistant bacteria, such as A. eutrophus CH34 or A. denitrificans 4a-2, were used as target DNA. Among the 60 strains examined, positive signals only appeared with the 3.1 kb DNA fragment from A. xylosoxydans 31A and the genomic DNA of two enterobacterial strains (5-1 and 5–5) isolated from nickel-rich soil in New Caledonia.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 11 (1981), S. 172-178 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Heat treatment (10 min at 65° C) of cells of Alcaligenes eutrophus, which resulted in the release of RNA degradadation products into the medium, was found to activate cellular ribonucleases. Two ribonucleases degrading yeast RNA were found, one localized in the periplasmic space and the other in the soluble fraction of the ribosomes. Compared to non-heated cells, in the heat-treated cells the former enzyme, the cell debris ribonuclease, was present at an eightfold increased specific activity, and the latter, the cytoplasmic ribonuclease, was present at a fourfold increased specific activity. This increase was due to the inactivation of a thermolabile inhibitor and to denaturation of part of the soluble protein during heat treatment. With respect to their properties the enzymes were similar; they had endonuclease activity and hydrolysed only RNA. They were heat-stable, resistent to trypsin, highly sensitive to a ribonuclease inhibitor isolated from the same bacterium and were partially inhibited by ATP and GTP. These properties provided a partial explanation for the mechanism of the release of RNA dagradation products from A. eutrophus cells after heat treatment.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 117 (1978), S. 123-129 
    ISSN: 1432-072X
    Keywords: Hydrogenase ; Regulation ; CO2-effect ; H2-effect ; Mixotrophy ; Reverse electron flow ; Alcaligenes eutrophus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Forty-four mutants of Alcaligenes eutrophus H 16 were isolated which grew poorly or not at all under autotrophic conditions. Four types were characterized with respect to their defects and their physiological properties. One mutant lacked both enzymes specific for autotrophic CO2 fixation, another one lacked both hydrogenases, and two mutants lacked either the membrane-bound or the soluble hydrogenase. Comparing the results of studies on these mutant types, the following conclusions were drawn: the lack of each hydrogenase enzyme could be partially compensated by the other one; the lack of membrane-bound hydrogenase did not affect autotrophic growth, whereas the lack of the soluble hydrogenase resulted in a decreased autotrophic growth rate. When pyruvate as well as hydrogen were supplied to the wild-type, the cell yield was higher than in the presence of pyruvate alone. Mutant experiments under these conditions indicated that either of both hydrogenases was able to add to the energy supply of the cell. Only the soluble hydrogenase was involved in the control of the rate of hydrogen oxidation by carbon dioxide; the mutant lacking this enzyme did not respond to the presence or absence of CO2. The suppression of growth on fructose by hydrogen could be mediated by either of both hydrogenases alone.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 18 (1952), S. 362-390 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 118 (1978), S. 35-43 
    ISSN: 1432-072X
    Keywords: Autotrophic growth ; Hydrogen ; Carbon monoxide ; Gram-negative hydrogen bacteria ; Pseudomonas carboxydovorans ; Facultative autotrophs ; CO oxidation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract From enrichment cultures four carbon monoxide utilizing bacteria were isolated; strain OM5 isolated from waste water was studied in detail. The cells are Gram-negative, slightly curved rods, motile by a single subpolarly inserted flagellum. The colonies are smooth, translucent and not slimy. The cells are able to grow autotrophically in mineral medium under an atmosphere of 40% CO, 5% O2 and 55% N2 at a doubling time of 20h (30°C) or of 85% H2, 5% O2 and 10% CO2 at a doubling time of 7h. Heterotrophic growth occurrd on organic acids such as acetate (t d =8h), pyruvate (t d =8h), lactate, crotonate, malate, succinate (t d =8h), formate (t d =35h) and glyoxylate as substrates. The enzyme system for carbon monoxide utilization is formed only during growth on CO; hydrogenase is present in cells grown on CO or on H2+CO2 as well as grown on pyruvate. The rate of oxygen reduction by intact CO-grown cells is 3.7-fold higher in the presence of hydrogen than in the presence of carbon monoxide. During growth the stoichiometry of gas uptake was 6.1 CO+2.8 O2+H2O → 〈CH2O〉+5.1 CO2. For the new isolate the name Pseudomonas carboxydovorans (Kistner) comb. nov. has been proposed.
    Type of Medium: Electronic Resource
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