Immobilization of laccase onto poly(glycidylmethacrylate) brush grafted poly(hydroxyethylmethacrylate) films: Enzymatic oxidation of phenolic compounds

Bayramoglu G., Arica M. Y.

MATERIALS SCIENCE & ENGINEERING C-MATERIALS FOR BIOLOGICAL APPLICATIONS, cilt.29, sa.6, ss.1990-1997, 2009 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 29 Sayı: 6
  • Basım Tarihi: 2009
  • Doi Numarası: 10.1016/j.msec.2009.03.011
  • Dergi Adı: MATERIALS SCIENCE & ENGINEERING C-MATERIALS FOR BIOLOGICAL APPLICATIONS
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1990-1997
  • Anahtar Kelimeler: ATRP, Polymer brushes, Immobilized enzyme, Adsorption, Laccase, Phenolic compounds, GLUCOSE-OXIDASE, REVERSIBLE IMMOBILIZATION, POLYPHENOL OXIDASE, POLYMER BRUSHES, CANDIDA-RUGOSA, HIGH-CAPACITY, MEMBRANES, TYROSINASE, STABILITY, REMOVAL
  • Gazi Üniversitesi Adresli: Evet

Özet

Poly(hydroxyethylmethacrylate), p(HEMA) films were prepared via UV-initiated photo-polymerization. After activation of the hydroxyl groups of p(HEMA) by bromination, surface-initiated atom transfer radical polymerization (ATRP) of glycidylmethacrylate was conducted in dioxane/bipyridine mixture with CuBr as catalyst at 65 degrees C. The epoxy groups of the poly(glycidylmethacrylate) brushes were converted into amino groups with the reaction of ammonia. The modified p(HEMA-g-GMA)-NH2 films were used as an ion-exchange support for the immobilization of laccase. The influence of pH and initial laccase concentration on the immobilization capacity of the p(HEMA-g-GMA)-NH2 films has been investigated. The amount of immobilized laccase on the p(HEMA-g-GMA)-NH2 films was determined as 139 mu g/cm(2) films. The recovered activity of the immobilized laccase on the fibrous polymer grafted films was about 71% compared to free enzyme. The maximum activity (V-max) and Michealis constant (K-m) of laccase immobilized on the films, were found to be 15.4 U/mg and 23 mM, respectively. Finally, the immobilized laccase was operated in a batch system for enzymatic oxidation of phenol, p-chlorophenol and aniline. (C) 2009 Elsevier B.V. All rights reserved.