Cross-linking of horseradish peroxidase adsorbed on polycationic films: utilization for direct dye degradation

BAYRAMOĞLU G., Altintas B., Arica M. Y.

BIOPROCESS AND BIOSYSTEMS ENGINEERING, vol.35, no.8, pp.1355-1365, 2012 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 35 Issue: 8
  • Publication Date: 2012
  • Doi Number: 10.1007/s00449-012-0724-2
  • Journal Name: BIOPROCESS AND BIOSYSTEMS ENGINEERING
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1355-1365
  • Keywords: Polyaniline, Polyacrylonitrile, Graft copolymerization, Immobilization, Horseradish peroxidase, Dye decolorization, REVERSIBLE IMMOBILIZATION, POLYPHENOL OXIDASE, TEXTILE DYES, REMOVAL, LACCASE, BENZIDINE, PHENOL, BEADS, DECOLORIZATION, ADSORPTION
  • Gazi University Affiliated: Yes

Abstract

Horseradish peroxidase (HRP) was immobilized on the polyaniline (PANI) grafted polyacrylonitrile (PAN) films. The maximum HRP immobilization capacity of the PAN-g-PANI-3 film was 221 mu g/cm(2). The HRP-immobilized PAN-g-PANI-3 film retained 79 % of the activity of the same quantity free enzyme. The HRP-immobilized PAN-g-PANI-3 film was operated for the decolorization of two different benzidine-based dyes in the presence of hydrogen peroxide. The maximum decolorization grade was obtained at pH 6.0 for both dyes. The HRP-immobilized PAN-g-PANI-3 film was very effective for removal of Direct Blue-53 compared to Direct Black-38 from aqueous solutions. The immobilized HRP exhibited high resistance to proteolysis by trypsin compared to the free counterpart. Immobilized HRP preserved 83 % of its original activity even after 8 weeks of storage at 4 A degrees C, while the free enzyme lost its initial activity after 3 weeks of storage period.