Entrapment of DyP‐type peroxidase from Pseudomonas fluorescens Pf‐5 into Ca‐alginate magnetic beads

The aim of this study was to investigate the optimal conditions for the immobilization and stabilization of DyP1B dye decolorizing peroxidases type B (DyP1B) from Pseudomonas fluorescens Pf‐5 immobilized in Ca‐alginate ferromagnetic beads. The immobilized DyP1B was used in the degradation of the Reactive Blue 5 (RB5) synthetic dye. The enzyme was successfully entrapped in a Ca‐alginate matrix and showed an encapsulation efficiency of 94%. The concentration of DyP1B (0.8 mg mL −1 ), 2% of alginate and magnetite (10.0 mg mL −1 ) was optimal for immobilization. The immobilized DyP1B showed optimum activity at pH 7.0 and 40 °C compared with pH 5.5 and 30 °C for free peroxidase. Reusability studies showed that after five cycles, the immobilized DyP1B system retained more than 58% of its initial activity. The immobilized DyP1B was able to decolorize RB5 at concentrations of 0.1, 0.05, and 0.01% (w v −1 ) with efficiency rates of about 20, 29, and 45%, respectively. The immobilization of DyP1B in alginate beads with the addition of Fe 3 O 4 increased its catalytic and applicative potential.