Immobilization of alliinase on porous aluminum oxide.
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.
Milka
P
P
Institute for Pharmaceutical Biology, University of Bonn, Germany.
Krest
I
I
Keusgen
M
M
D000042:Absorption; D000537:Aluminum Oxide / Q000378:metabolism*; D013437:Carbon-Sulfur Lyases / Q000378:metabolism*; D003208:Concanavalin A / Q000378:metabolism; D003545:Cysteine / Q000031:analogs & derivatives / Q000378:metabolism; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005737:Garlic / Q000201:enzymology; D008351:Mannans / Q000378:metabolism; D008851:Micropore Filters; D008855:Microscopy, Electron, Scanning; D037121:Plant Lectins; D010946:Plants, Medicinal; D011437:Propylamines; D011485:Protein Binding; D012821:Silanes / Q000378:metabolism; D013997:Time Factors
D004800:Enzymes, Immobilized; D008351:Mannans; D037121:Plant Lectins; D011437:Propylamines; D012821:Silanes; D003208:Concanavalin A; C006453:alliin; D013437:Carbon-Sulfur Lyases; C019243:alliin lyase; D003545:Cysteine; C477625:amino-propyl-triethoxysilane; D000537:Aluminum Oxide