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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
    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.
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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 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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  • 5
    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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  • 6
    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.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 11 (1993), S. 73-81 
    ISSN: 1476-5535
    Keywords: Esterase ; Ethylhexyl butyrate ; Hydrolytic stereospecificity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary A pH indicator agar plate method was used to screen for esterase activities for hydrolysis of 2-ethylhexyl butyrate. Seven hundred and fifty-seven selected microbial cultures, including 325 bacteria, and 432 yeasts and actinomycetes from the ARS Culture, Collection, were screened. Among them, 62 cultures hydrolyzed 2-ethylhexyl butyrate. Of these strains only 17 showed lipase activity on a rhodamine B lipase screen. The reaction products, 2-ethyl-1-hexanol andn-butyric acid were confirmed by gas-liquid chromatography (GC) and GC/MS analyses. The yield of 2-ethyl-1-hexanol varied depending on the strains of the microorganisms, with the highest yield at 79.1% by a strain ofPseudomonas myxogenes Product analyses with a cyclodextrin GC chiral column showed that two strains ofPseudomonas produced, greater than 80% enantiomeric excess of S(+)-2-ethyl-1-hexanol.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Journal of industrial microbiology and biotechnology 14 (1995), S. 31-34 
    ISSN: 1476-5535
    Keywords: Microbial conversion ; Enzymic hydration ; Hydratase ; Hydroxy unsaturated fatty acids ; α- and γ-Linolenic acids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Previously, we reported the isolation of a new microbial strain,Flavobacterium sp. DS5 (NRRL B-14859) which converted oleic and linoleic acids to their corresponding 10-keto- and 10--ydroxy-fatty acids. The hydration enzyme seemed to be specific to the C-10 position. Now we have identified, by GC/MS, NMR, and FTIR, the bioconversion products from α-linolenic acid as 10-hydroxy-12(Z), 15(Z)-octadecadienoic acid and from γ-linolenic acid as 10-hydroxy-6(Z), 12(Z)-octadecadienoic acid. Products from 9(E)-unsaturated fatty acids were also identified as their corresponding 10-hydroxy or 10-keto fatty acids. From these results, it is concluded that strain DS5 hydratase is indeed a C-10 positional-specific enzyme and prefers an 18-carbon mono-unsaturated fatty acid. Among the C18 unsaturated fatty acids, an additional double bond on either side of the C-9 position lowers the enzyme hydration activity.
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  • 9
    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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  • 10
    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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