Distribution of an enzyme in porous polymer beads

Abstract

Trypsin has been immobilized by adsorption onto Amberlite XAD-7 beads. The Michaelis constant (K_m) of the enzyme was increased about sevenfold following the immobilization. Its rate of penetration into the porous beads was determined by staining the beads, which had been split, with naphthol blue black. The extent of diffusional rate limitation of immobilized trypsin was related to the penetration depth of the enzyme into the beads. This can be controlled by manipulating the conditions during the preparation of the immobilized enzyme.