Abstract
The adsorbents for proteins are prepared by the modification of phenolic resins with gelatin. The modification is carried out under three different reaction conditions, using HCl catalyst in water and in 1-butanol, or NaOH catalyst in water. Adsorption of α-chymotrypsin on these modified resins and the activity of immobilized chymotrypsin are investigatad. Among three kinds of the modified resins, the resin prepared in HCl-butanol system shows the highest enzyme-adsorption ability and enzyme activity. In addition, the thermal and storage stabilities of enzyme are extremely improved by immobilization on this modified resin. Based on the adsorption behaviors of pepsin, BSA and lysozyme, it is concluded that the adsorption is due to the electrostatic interaction between the gelatin moiety in modified phenolic resins and the adsorbed proteins.
