This work compares the main enzymatic parameters of a cationic peroxidase (AaP-1-4), purified and characterized from Asparagus acutifolius L. seeds (Mol. Biotechnol., 2014, 56, 738–746) and its immobilised form (Eup-AaP-1-4), on Eupergit® CM with Horseradish peroxidase. The optimum in the pH-activity profile was pH 4.0 and pH 3.0 for AaP-1-4 and Eup-AaP-1-4, respectively. Ca2+ cation enhanced both enzymatic activities, however, when submitted to a temperature stress (120 min at 50 C) Eup-AaP-1-4 lost only 20% activity while AaP-1-4 70%. Furthermore, AaP-1-4 was proved to be able to remove (poly)phenols in olive mill waste water (OMW), with hydrogen peroxide electron donor. The Eup-AaP-1-4 kinetic proprieties were investigated and the operational stability evaluated in a continuous stirred membrane bioreactor. AaP-1-4 appears to be a novel non-expensive source of peroxidases suitable for biotechnological applications in the environmental field for the removal of aqueous (poly)phenols produced from several industrial processes.
Immobilised peroxidases from Asparagus acutifolius L. seeds for olive mill waste water treatment
CANTARELLA, Laura;
2014-01-01
Abstract
This work compares the main enzymatic parameters of a cationic peroxidase (AaP-1-4), purified and characterized from Asparagus acutifolius L. seeds (Mol. Biotechnol., 2014, 56, 738–746) and its immobilised form (Eup-AaP-1-4), on Eupergit® CM with Horseradish peroxidase. The optimum in the pH-activity profile was pH 4.0 and pH 3.0 for AaP-1-4 and Eup-AaP-1-4, respectively. Ca2+ cation enhanced both enzymatic activities, however, when submitted to a temperature stress (120 min at 50 C) Eup-AaP-1-4 lost only 20% activity while AaP-1-4 70%. Furthermore, AaP-1-4 was proved to be able to remove (poly)phenols in olive mill waste water (OMW), with hydrogen peroxide electron donor. The Eup-AaP-1-4 kinetic proprieties were investigated and the operational stability evaluated in a continuous stirred membrane bioreactor. AaP-1-4 appears to be a novel non-expensive source of peroxidases suitable for biotechnological applications in the environmental field for the removal of aqueous (poly)phenols produced from several industrial processes.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
