• Title of article

    Employment of immobilised lipase from Candida rugosa for the bioremediation of waters polluted by dimethylphthalate, as a model of endocrine disruptors

  • Author/Authors

    Mita، نويسنده , , Luigi and Sica، نويسنده , , Vincenzo and Guida، نويسنده , , Marco and Nicolucci، نويسنده , , Carla and Grimaldi، نويسنده , , Tiziana and Caputo، نويسنده , , Lucia and Bianco، نويسنده , , Mariangela and Rossi، نويسنده , , Sergio and Bencivenga، نويسنده , , Umberto and Eldin، نويسنده , , Mohamed S. Mohy and Tufano، نويسنده , , Maria Antonietta and Mita، نويسنده , , Damiano G. and Diano، نويسنده , , Nadia، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2010
  • Pages
    9
  • From page
    133
  • To page
    141
  • Abstract
    A planar bioreactor, equipped with a polypropylene membrane on which a lipase was immobilised, has been employed in a bioremediation process involving water polluted by dimethylphthalate (DMP), a model for a class of endocrine disruptors. The dependence of enzyme activity on pH, temperature and DMP concentration has been characterised under isothermal conditions, whereas the kinetics parameters have been studied under non-isothermal conditions. The following sequence was found for the values of lipase affinity, Km, towards the DMP: K m free < K m , non-isoth imm < K m , isoth imm . A comparison of the results obtained under isothermal and non-isothermal conditions indicated that there was an advantage in using non-isothermal bioreactors in the environmental field. These advantages in particular resulted in: (i) an increase in the enzyme activity proportional to the applied transmembrane temperature difference and (ii) a reduction in the bioremediation times and, consequently, the process costs. The advantages in using bioremediation processes in the place of classical membrane processes, such as ultrafiltration or reverse osmosis, are also discussed.
  • Keywords
    endocrine disruptors , Lipase , Phthalates , Bioremediation , Non-isothermal bioreactors
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Serial Year
    2010
  • Journal title
    Journal of Molecular Catalysis B Enzymatic
  • Record number

    1716844