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

Abstract

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 µm in diameter) were prepared by dispersion polymerization in the presence of Fe 3 O 4 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 50 • C. V max values were determined as 330 U/mg and 292 U/mg enzyme, for free and adsorbed invertase, respectively. K M 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.

Concanavalin A immobilized poly(ethylene glycol dimethacrylate) based affinity cryogel matrix and usability of invertase immobilization

“…For example, Akkaya et al [10] prepared magnetic poly(glycidyl methacrylate) beads for invertase adsorption from yeast and the adsorption capacity was found to be 111 mg/g polymer. In other study, Osman and co workers [34] prepared vinyl imidazole carrying poly(ethylene glycol dimethacrylate-n-vinyl imidazol) [poly(EGDMA-VIM)] beads for adsorption of invertase.…”

“…3.2.1.26), a glycoenzyme, catalyzes the hydrolysis of the sucrose to glucose and fructose [10]. The hydrolyzed sugar mixture obtained by invertase has the advantage of being colorless in contrast to the colored products obtained by acid hydrolysis [11,12].…”

Investigation of Yeast Invertase Immobilization onto Cupric Ion-Chelated, Porous, and Biocompatible Poly(Hydroxyethyl Methacrylate-n-Vinyl Imidazole) Microspheres

“…Enzymes have a long amino acid chain consist of several recognition sides for the substrates molecules. During the adsorption process, some conformational changes on invertase can be occurred [16]. Thus, the substrate specificity of the adsorbed enzyme was slightly changed.…”

“…Immobilization of invertase on corn grits, gelatin, and various agarose polymers has already been achieved, while its immobilization onto hydrogel polymer has been limited. The latter have good chemical properties and mechanical stability and are not susceptible to microbial attack [14][15][16].…”

Properties of an extracellular lipase from a traditional yoghurt yeast

“…Lipase activity was measured in 10 degree intervals at from 5 to 85 o C in 50 mM phosphate buffer (pH 7.0) and recorded as a percentage the highest value at each temperature [26].…”