Literature DB >> 10861415

Immobilization of alliinase on porous aluminum oxide.

P Milka1, I Krest, M Keusgen.   

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.

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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


  2 in total

1.  Functionalized anodic aluminum oxide membrane-electrode system for enzyme immobilization.

Authors:  Zhiqiang Chen; Jianjun Zhang; Shanteri Singh; Pauline Peltier-Pain; Jon S Thorson; Bruce J Hinds
Journal:  ACS Nano       Date:  2014-08-26       Impact factor: 15.881

2.  Purification and characterisation of alliinase produced by Cupriavidus necator and its application for generation of cytotoxic agent: Allicin.

Authors:  Sagar Chhabria; Krutika Desai
Journal:  Saudi J Biol Sci       Date:  2016-01-07       Impact factor: 4.219

  2 in total

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