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  • 1
    Electronic Resource
    Electronic Resource
    Different detection systems for the HPLC analysis of oxylipins, by-products of the enzymatic generation of 2E-hexenal (1998)
    Springer
    Fresenius' journal of analytical chemistry 360 (1998), S. 830-832 
    Details
    ISSN: 1432-1130
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The incubation of 13-hydroperoxy-9Z,11E,15Z-octadecatrienoic acid (13-HPOT) with a hydroperoxide lyase containing extract of mung bean seedlings (Phaseolus radiatus L.) led not only to the formation of 2E-hexenal, but also to the generation of several non-volatile by-products (oxylipins). These oxylipins, generated by the catalysis of other 13-HPOT metabolizing enzymes, were analyzed by high performance liquid chromatography (HPLC) without time-comsuming derivatization procedures, which would be necessary for their volatilization and stabilization during gaschromatography (GC). Different detection systems such as an evaporative light-scattering detector (ELSD), diode-array detector (DAD), and particle beam-mass spectrometry (PB-MS) were applied. The utilization of an ELSD represented an improvement of sensitivity compared to a DAD, especially in the case of substances with low UV-activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002160050820
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  • 2
    Electronic Resource
    Electronic Resource
    Covalent immobilization of a hydroperoxide lyase from mung beans (Phaseolus radiatus L.) (1998)
    Springer
    Biotechnology techniques 12 (1998), S. 539-544 
    Details
    ISSN: 1573-6784
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A fatty acid hydroperoxide lyase of mung beans has been covalently immobilized on different commercially available gels which represents the first immobilization of this type of enzyme from a higher plant. UltraLink Iodoacetyl possessed optimum coupling properties and yielded a maximum activity of 1.3 U ml−1 gel and a yield of 84%. The effect of various protective reagents (e.g. thiols, antioxidants) and of the substrate concentration on the re-usability of the immobilized enzyme was investigated. Compared to a control, the relative activity during re-use was enhanced 1.8- to 2.3-fold in the presence of dithiothreitol. As the hydroperoxide lyase was irreversibly inhibited by the substrate, its re-usability depended strongly on the hydroperoxide concentration. The lowest inactivation was with 55 μM hydroperoxide which resulted in a relative activity of 73% after the third cycle. The storage stability of the hydroperoxide lyase was significantly improved by immobilization and resulted in a relative activity of 86% after 18 days, whereas the soluble enzyme lost 68% of its initial activity. © Rapid Science Ltd. 1998
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008855531469
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    Paper (German National Licenses)
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