Ionic binding of biologically active proteins on cross‐linked acrylic macromolecular supports

Abstract

The immobilization process of some biologically active proteins on acrylic ion exchange supports was studied. The cross-linking and swelling coefficient, as well as the molecular weight of the enzyme, were proved to influence the immobilization process. The kinetic data indicate mainly a binding process controlled by diffusion. The uptake coefficient values of different proteins ranged between 35.0 and 98.0%. The laboratory experiments per formed with some of the obtained enzymic preparation certify the preservation of the catalytic activity following the immobilization process.

Superparamagnetic Composites Based on Ionic Resin Beads/CaCO3/Magnetite

“…Sodium choloroacetate was obtained by the neutralization of monochloroacetic acid (Merck) with sodium hydroxide in aqueous solution. The ammonium salt of styrene/maleic anhydride copolymer was obtained in the laboratory, according to reference .…”

Glucoamylase absorption and desorption process

“…The flow rate was maintained constant at 1 ml min-I Recovery of the biologically active protein (D (%)) was defined as the percentage ratio between the instantaneously retained protein and the initial cp [34]. Table 1 lists the experimental conditions of the glucoamylase immobilization process and the recorded values of the total immobilized protein content observed as increasing with the initial enzyme solution concentration.…”