Immobilization of glucoamylase onto polyaniline-grafted magnetic hydrogel via adsorption and adsorption/cross-linking

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

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, cilt.97, sa.3, ss.1149-1159, 2013 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 97 Sayı: 3
  • Basım Tarihi: 2013
  • Doi Numarası: 10.1007/s00253-012-3999-y
  • Dergi Adı: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.1149-1159
  • Anahtar Kelimeler: Ferrogel, Film, Enzyme immobilization, Adsorption, Glucoamylase, Starch hydrolysis, COVALENT IMMOBILIZATION, REVERSIBLE IMMOBILIZATION, POLY(GMA-MMA) BEADS, ASPERGILLUS-NIGER, BED REACTOR, NANOPARTICLES, HYDROLYSIS, POLYMER, LIPASE, MEMBRANES
  • Gazi Üniversitesi Adresli: Evet

Özet

Glucoamylase (GA) was immobilized onto polyaniline (PANI)-grafted magnetic poly(2-hydroxyethylmethacrylate-co-glycidylmethacrylate) hydrogel (m-p(HEMA-GMA)-PANI) with two different methods (i.e., adsorption and adsorption/cross-linking). The immobilized enzyme preparations were used for the hydrolysis of "starch" dextrin. The amount of enzyme loading on the ferrogel was affected by the medium pH and the initial concentration of enzyme. The maximum loading capacity of the enzyme on the ferrogel was found to be 36.7 mg/g from 2.0 mg/mL enzyme solution at pH 4.0. The adsorbed GA demonstrated higher activity (59%) compared to adsorbed/cross-linked GA (43%). Finally, the immobilized GA preparations exhibited greater stability against heat at 55 A degrees C and pH 4.5 compared to free enzyme (50 A degrees C and pH 5.5), suggesting that the ferrogel was suitable support for immobilization of glucoamylase.