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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 15 (1976), S. 582-588 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Company
    Nature biotechnology 3 (1985), S. 358-358 
    ISSN: 1546-1696
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: [Auszug] Enzyme Technology. Edited by R. M. Lafferty. Pp. 314. ISBN 3-540-12479-9. $46.50. (Springer-Verlag, Berlin-Heidelberg: 1983). This book represents the proceedings of the Illrd Rotenburger Fermentation Symposium held in 1982 in Kassel. Enzyme technology was the main subject of the symposium ...
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  • 3
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 501 (1987), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 434 (1984), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 9 (1992), S. 103-107 
    ISSN: 1476-5535
    Keywords: Fatty acid bioconversion ; hydroxy octadecenoic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Previously, we reported the discovery of a new compound, 7,10-dihydroxy-8(E)-octadecenoic acid (DOD) which was produced from oleic acid by a new bacterial isolate PR3 [6,7]. The reaction is unique in that it involves a hydroxylation at two positions and a rearrangement of the double bond of the substrate molecule. Now, we have isolated another compound from the reaction mixture determined by GC/MS to be 10-hydroxy-8-octadecenoic acid (HOD). NMR and IR data indicate that the unsaturation is probablycis. The optimum pH and temperature for the production of HOD by strain PR3 were 6.5 and 30°C, about the same as those for DOD. However, the amount of HOD detected remained small throughout an 48-h reaction period during which the amount of DOD increased sharply. At 48 h of reaction, the ratio between HOD∶DOD was 1∶10. HOD may be an intermediate in the biosynthesis of DOD from oleic acid.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 7 (1991), S. 123-129 
    ISSN: 1476-5535
    Keywords: Fatty acid biotransformation ; Dihydroxy octadecenoic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Sixty-two cultures from the ARS Culture Collection and 10 cultures isolated from soil and water samples collected in Illinois were screened for their ability to convert agricultural oils to value-added industrial chemicals. A new compound, 7,10-dihydroxy-8-(E)-octadecenoic acid (DOD) was produced from oleic acid by a new strain,Pseudomonas sp. PR3 isolated from a water sample in Morton, IL. Strain PR3 is a motile, small rod-shaped, Gram-negative bacterium. It has multiple polar flagellae and is oxidase-positive. Strain PR3 grows aerobically and cannot grow anaerobically. The strain produces white, smooth colonies on agar plate and no water-soluble pigment. The yield of the product was greater than 60%. The optimum time, pH and temperature for the production of DOD were: 2 days, 7.0, and 30°C, respectively. Glycerol and dextrose support the growth of strain PR3, but the cells grown from the former failed to catalyse the conversion of oleic acid to DOD. The production of DOD is unique in that it involves a hydroxylation at two positions and a rearrangement of the double bond of the substrate molecule.
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Applied microbiology and biotechnology 19 (1984), S. 1-4 
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Methanotrophic bacteria have been shown to oxidize gaseous alkenes to the corresponding epoxides utilizing an NADH2-dependent methane monooxygenase. A cell paste of methane-grown methylotrophs was coated on porous glass beads. The production of propylene oxide from propylene was performed in a gas-solid bioreactor to ensure continuous production and removal of product epoxide from the microenvironment of the biocatalyst. The amount of propylene oxide produced before cofactor regeneration was between 120–145 μmoles/20 mg cells in about 10 h depending on the microbial strains used. The conversion rate for propylene was 2.7%. Regeneration of cofactor NADH2 was performed in the bioreactor with the vapor of a cosubstrate, methanol.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Archives of microbiology 73 (1970), S. 261-267 
    ISSN: 1432-072X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Viridicatin, C15H11O2N, has been shown to be a metabolic product of several fungi including P. palitans, P. olivino-viride, P. puberulum, P. martensii, P. crustosum, P. granulatum, and P. cyclopium. Although these strains also produce the tremorgenic mycotoxin, tremortin, no toxicity could be shown for viridicatin. Viridicatin does not appear to be a component of the tremortin molecule. A quantitative colorimetric assay has been developed for viridicatin.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 1 (1986), S. 31-37 
    ISSN: 1476-5535
    Keywords: Xanthan ; Xanthan degradation ; Biodegradation ; Salt-tolerant bacteria ; Bacillus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Three salt-tolerant bacteria which degraded xanthan were isolated from various water and soil samples collected from New Jersey, Illinois, and Louisiana. The mixed culture, HD1, contained aBacillus sp. which produced an inducible enzyme(s) having the highest extracellular xanthan-degrading activity found. Xanthan alone induced the observed xanthan-degrading activity. The optimum pH and temperature for cell growth were 5–7 and 30–35°C, respectively. The optimum temperature for activity of the xanthan-degrading enzyme(s) was 35–45°C, slightly higher than the optimum growth temperature. With a cell-free enzyme preparation, the optimum pH for the reduction of solution viscosity and for the release of reducing sugar groups were different (5 and 6, respectively), suggesting the involvement of more than one enzyme for these two reactions. Products of enzymatic xanthan degradation were identified as glucose, glucuronic acid, mannose, pyruvated mannose, acetylated mannose and unidentified oligo- and polysaccharides. The weight average molecular weight of xanthan samples shifted from 6.5·106 down to 6.0·104 during 18 h of incubation with the cell-free crude enzymes. The activity of the xanthan-degrading enzyme(s) was not influenced by the presence or absence of air or by the presence of Na2S2O4 and low levels of biocides such as formaldehyde (25 ppm) and 2,2-dibromo-3-nitrilopropionamide (10 ppm). Formaldehyde at 50 ppm effectively inhibited growth of the xanthan degraders.
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