Kinetic behavior of gel entrapped enzymes

Abstract

A variety of enzymes have been successfully immobilized in our laboratory by entrapping them in hydrogels. The entrapment procedure consists of dissolving an enzyme in a polymerization reaction mixture which typically consists of about 50% water, a water-soluble polymer such as poly(vinylpyrrolidone), a monomer such as 2-hydroxyethylmeth-acrylate, a crosslinking monomer and a low-temperature, free radical initiating species. After immobilization, the enzymatic activity of the gel was measured against a suitable substrate, usually chosen for the ease of following its reaction. The gel itself is dried, crushed to a fine powder, sieved, and rehydrated before the enzymatic activity is measured. We have experimentally studied the activity of gels containing trypsin, glucose oxidase, β-galactosidase, and other enzymes. Details of this work and applications of these immobilized enzymes are discussed.