Concanavalin a Immobilized Monosize and Magnetic Poly(glycidyl Methacrylate) Beads for Use in Yeast Invertase Adsorption


AKKAYA B. , UZUN L., Altintas E. B. , CANDAN F. , DENİZLİ A.

JOURNAL OF MACROMOLECULAR SCIENCE PART A-PURE AND APPLIED CHEMISTRY, cilt.46, ss.232-239, 2009 (SCI İndekslerine Giren Dergi) identifier identifier

  • Cilt numarası: 46 Konu: 3
  • Basım Tarihi: 2009
  • Doi Numarası: 10.1080/10601320802637086
  • Dergi Adı: JOURNAL OF MACROMOLECULAR SCIENCE PART A-PURE AND APPLIED CHEMISTRY
  • Sayfa Sayıları: ss.232-239

Özet

Concanavalin A (Con A) immobilized monosize and magnetic poly(glycidyl methacrylate)[m-poly(GMA)] beads were investigated for specific adsorption of yeast invertase from aqueous solutions. m-Poly(GMA) beads (1.6 m in diameter) were prepared by dispersion polymerization in the presence of Fe3O4 nanopowder. The epoxy groups of m-poly(GMA) beads were opened by base catalyses. Then, Con A was immobilized by covalent binding onto the beads. Con A immobilization amount was 12.5 mg/g. The invertase adsorption capacity of the m-poly(GMA)/Con A beads was 111 mg/g. The maximum invertase adsorption on the m-poly(GMA)/Con A beads was observed at pH 5.5. The optimum activity for both free and adsorbed invertase was observed at 50C. Vmax values were determined as 330 U/mg and 292 U/mg enzyme, for free and adsorbed invertase, respectively. KM values were found to be the same for free and adsorbed invertase (20 mM). Adsorption of invertase via Con A improved the pH stability of invertase. Thermal stability also increased with adsorption. The adsorbed enzyme activity was found to be quite stable in repeated experiments.