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
Link To Document :
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