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  • 1
    Electronic Resource
    Electronic Resource
    Biological denitration of propylene glycol dinitrate by Bacillus sp. ATCC 51912 (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 525-529 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  In previous studies, bacterial cultures were isolated that had the ability to degrade the nitrate ester glyceryl trinitrate (i.e. nitroglycerin). The goal of the present study was to examine the ability of resting cells and cell-free extracts of the isolate Bacillus sp. ATCC 51912 to degrade the more recalcitrant nitrate ester propylene glycol dinitrate (PGDN). It was observed that the PGDN-denitrating activity was expressed during growth even when cells were cultured in the absence of nitrate esters. This indicates that nitrate esters are not required for expression of denitration activity. Using cell-free extracts, PGDN was observed to be sequentially denitrated to propylene glycol mononitrate (PGMN) and propylene glycol with the second denitration step proceeding more slowly than the first. Also it was observed that dialysis of the cell-free extracts did not affect denitration activity indicating that regenerable cofactors [e.g. NAD(P)H or ATP] are not required for denitration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00578466
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Biological denitration of propylene glycol dinitrate byBacillus sp. ATCC 51912 (1996)
    Springer
    Applied microbiology and biotechnology 45 (1996), S. 525-529 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract In previous studies, bacterial cultures were isolated that had the ability to degrade the nitrate ester glyceryl trinitrate (i.e. nitroglycerin). The goal of the present study was to examine the ability of resting cells and cell-free extracts of the isolateBacillus sp. ATCC 51912 to degrade the more recalcitrant nitrate ester propylene glycol dinitrate (PGDN). It was observed that the PGDN-denitrating activity was expressed during growth even when cells were cultured in the absence of nitrate esters. This indicates that nitrate esters are not required for expression of denitration activity. Using cell-free extracts, PGDN was observed to be sequentially denitrated to propylene glycol mononitrate (PGMN) and propylene glycol with the second denitration step proceeding more slowly than the first. Also it was observed that dialysis of the cell-free extracts did not affect denitration activity indicating that regenerable cofactors [e.g. NAD(P)H or ATP] are not required for denitration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00578466
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Putrescine metabolism: Enzymatic formation and non-enzymatic isotope exchange of Δ′-pyrroline (1984)
    Chichester : Wiley-Blackwell
    Biological Mass Spectrometry 11 (1984), S. 118-120 
    Details
    ISSN: 0306-042X
    Keywords: Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The deamination of putrescine catalysed by diamine oxidase was carried out in deuterium oxide and deuterated buffers. Enamine and α,β-unsaturated intermediates were excluded, based on the observation that deuterium was not incorporated into Δ1-pyrroline during its enzymatic formation in deuterium oxide. When the reaction mixture was buffered with phosphate, isolated Δ1-pyrroline contained two deuterium atoms at C-3, indicating that a phosphate-promoted, non-enzymatic isotope exchange had occurred. Using 5,5-dimethyl-Δ1-pyrroline as a model compound, the nature of the non-enzymatic deuterium exchange was studied and a bifunctional catalysis mechanism proposed. The results suggest that the choice of buffer could alter the conclusions drawn from enzyme mechanism studies involving imine-enamine tautomerism.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bms.1200110305
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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