Entrapment of concanavalin A‐glycoenzyme complexes in calcium alginate gels

Glucose oxidase, invertase, and amyloglucosidase were entrapped in calcium alginate gels as concanavalin A complexes in order to prevent the leaching out of the enzymes from the porous matrix. The free as well as the gel‐entrapped concanavalin A‐glycoenzyme complexes exhibited a relatively high effectiveness factor, η, indicating good accessibility to the substrates. Concanavalin A‐invertase complex exhibited marked broadening of pH‐activity and temperature‐activity profiles and was highly resistant to temperature inactivation even after entrapment in the alginate beads. It was possible to entrap considerable quantities of invertase as concanavalin A complex in the beads without a marked decrease in η. A column containing crosslinked concanavalin A‐invertase complex entrapped in alginate beads retained the ability to completely hydrolyze 1 M sucrose even after continuous operation for over four months.