concanavalin-a and alliin

Membrane filters prepared from porous aluminum oxide (Anopore) were investigated for their potential use as a durable support for enzymes. Alliinase (EC 4.4.1.4) was chosen as a model enzyme for immobilization experiments. To allow for smooth fixation, the enzyme was immobilized indirectly by sugar-lectin binding. Monomolecular layers of the lectin concanavalin A and alliinase were applied by self-assembling processes. As an anchor for these layers, the sugar, mannan, was covalently coupled to the membrane surface. This procedure exhibits several advantages: (i) enzyme immobilization can be carried out under smooth conditions; (ii) immobilization needs little time; and (iii) protein layers may be renewed.

Topics: Absorption; Aluminum Oxide; Carbon-Sulfur Lyases; Concanavalin A; Cysteine; Enzyme Stability; Enzymes, Immobilized; Garlic; Mannans; Micropore Filters; Microscopy, Electron, Scanning; Plant Lectins; Plants, Medicinal; Propylamines; Protein Binding; Silanes; Time Factors