Abstract
Methods for the preparation of shell-structured immobilized enzymes supported by a fluid impervious spherical core are outlined. The preparation of such trypsin resins by coreticulation of the enzyme with a copolymer of maleic anhydride and vinyl methylester in situ on the surface of glass beads is described and some properties of the product including its behavior in hydro-organic media are discussed. By using the same reactive polymer pellicular polyanionic conjugates of chymotrypsin, papain, ribonuclease, l-asparaginase and alkaline phosphatase were also obtained. Carbon, nylon, silica and alumina in pellicular form were employed for the preparation of immobilized enzymes by crosslinking with glutaraldehyde. Pellicular carbon was the most suitable carrier for wheat germ acid phosphatase, cathepsin C and chymotrypsin. The activity of the products compares favorably to that obtained with enzymes immobilized on porous glass. The results indicate that a variety of methods can be employed to obtain pellicular immobilized enzymes, which possess high mechanical stability for use in packed beds and offer an efficient utilization of the immobilized enzyme.
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