| Literature DB >> 10861415 |
Abstract
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. Copyright 2000 John Wiley & Sons, Inc.Entities:
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Year: 2000 PMID: 10861415 DOI: 10.1002/1097-0290(20000805)69:3<344::aid-bit13>3.0.co;2-d
Source DB: PubMed Journal: Biotechnol Bioeng ISSN: 0006-3592 Impact factor: 4.530