Immobilization of laccase on the fibrous polymer-grafted film and study of textile dye degradation by MALDI-ToF-MS


Arica M. Y., SALİH B., ÇELİKBIÇAK Ö., BAYRAMOĞLU G.

CHEMICAL ENGINEERING RESEARCH & DESIGN, cilt.128, ss.107-119, 2017 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 128
  • Basım Tarihi: 2017
  • Doi Numarası: 10.1016/j.cherd.2017.09.023
  • Dergi Adı: CHEMICAL ENGINEERING RESEARCH & DESIGN
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.107-119
  • Anahtar Kelimeler: Polypropylene film, Grafting, Lactase, Dyes, MALDI-ToF-MS, Degradation, HORSERADISH-PEROXIDASE, MANGANESE PEROXIDASE, PHENOLIC-COMPOUNDS, ENZYMATIC REMOVAL, BISPHENOL-A, MEMBRANES, DECOLORIZATION, NANOPARTICLES, PERFORMANCE, STABILITY
  • Gazi Üniversitesi Adresli: Evet

Özet

This study assessed the immobilization of laccase on fibrous polymer-grafted polypropylene chloride film and the removal of three different dyes (i.e., Procion Green H4G, Brilliant Blue G, and Crystal Violet) using immobilized laccase. The polypropylene chloride (PP) film and poly(glycidylmethacrylate)-grafted (PP-g-pGMA) film were characterized by scanning electron microscopy (SEM), Fourier transform infrared spectroscopy (FTIR), and contact angle studies. The PP-g-pGMA film was used for the direct immobilization of laccase. The amount of immobilized enzyme and the enzyme activity on the film were found to be 1.185 mu g/m(2) and 1.71 x 10(-2) U/cm(2) film, respectively. The retained activity of the immobilized laccase was 72.3%. The optimal conditions for the free and immobilized enzymes and the kinetic parameters were determined. Additionally, the thermal, storage, and operational stabilities of the immobilized laccase were increased compared with those of the free form. Kinetic parameters Vmax and Km values were determined as 23.4U/mg protein and 0.38 mmol/L for free enzyme and 17.5 U/mg protein and 0.53 mmol/L for the immobilized laccase, respectively. The removal of the tested dyes with the immobilized laccases was evaluated in batch system and enzyme reactor. The maximum enzymatic removal of tested dyes was achieved at a pH of 5.5 and a temperature of 30 degrees C. The complete degradation time of the tested dyes was determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-ToF-MS). These results indicate that the immobilized laccase system can be effectively used for the removal of dyes, and it has a great potential for various biotechnological applications. (C) 2017 Institution of Chemical Engineers. Published by Elsevier B.V. All rights reserved.