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Entrapment of DyP‐type peroxidase from Pseudomonas fluorescens Pf‐5 into Ca‐alginate magnetic beads
Author(s) -
Wasak Agata,
Drozd Radosław,
Struk Łukasz,
Grygorcewicz Bartłomiej
Publication year - 2017
Publication title -
biotechnology and applied biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.468
H-Index - 70
eISSN - 1470-8744
pISSN - 0885-4513
DOI - 10.1002/bab.1562
Subject(s) - pseudomonas fluorescens , chemistry , peroxidase , entrapment , immobilized enzyme , chromatography , nuclear chemistry , calcium alginate , magnetite , enzyme , biochemistry , bacteria , organic chemistry , calcium , materials science , biology , medicine , genetics , surgery , metallurgy
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.