Entrapment of concanavalin A‐glycoenzyme complexes in calcium alginate gels

Abstract

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, eta, 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 eta. A column containing crosslinked concanavalin A-invertase complex entrapped in alginate beads retained the ability to completely hydrolyze 1M sucrose even after continuous operation for over four months.

Entrapment of porous and stable concanavalin A–peroxidase complex into hybrid calcium alginate–pectin gel

“…Several earlier reports indicated that crosslinked enzymes or pre-immobilized enzymes could remain inside the polymeric matrices for longer periods of time than soluble enzymes. 20,24,25,27 Figure 1 demonstrates the precipitation of glycosylated turnip proteins by increasing concentration of jack bean meal extract. The maximum precipitation of peroxidase activity was 70%.…”

Chromium (VI) uptake by grape stalks wastes encapsulated in calcium alginate beads: equilibrium and kinetics studies

“…Entrapment in beads of calcium alginate gel is one of the most widely used techniques for immobilising bacteria (Scott et al, 1989), enzymes (Hussain et al, 1985), yeast (Bustard and McHale, 1997;Serp et al, 2000), algae (Crist et al,1994), animal cells (Lu et al, 2000). On the other hand, calcium alginate has been one of the most extensively investigated biopolymers for binding divalent heavy metals thus, it has been used for the removal of heavy metals from dilute aqueous solutions (Apel and Torma 1993;Araújo and Teixeira, 1997;Chen et al, 1997;Chen et al 1992;Ibañez and Umetsu, 2002;Jang et al, 1999;Lázaro et al, 2003;Veglio et al, 2002).…”

Immobilization of invertase on sepharose-linked enzyme glycosyl recognizing polyclonal antibodies

“…These observations suggest that the binding of invertase to the antibody support does not result in alteration of the microenvironment of the enzyme significantly while facilitating the retention of activity, presumably by restricting the unfolding of the enzyme especially at extremes of the investigated pH. Glucoseoxidase (Iqbal and Saleemuddin, 1983a) and invertase (Husain et al, 1985) immobilized on lectin supports also exhibit broader pH-activity curves than the respective soluble enzymes.…”

“…5). Immobilized invertase preparations obtained by attaching the enzyme via its glycosyls by affinity (Husain et al, 1985) or covalently (Woodward and Wiseman, 1978;Husain et al, 1996) for support also exhibit impressive improvement in their resistance to heat induced inactivation.…”