Free-standing nanogold membranes as scaffolds for enzyme immobilization

We demonstrate herein the formation of a free-standing gold nanoparticle membrane and its use in the immobilization of the enzyme, pepsin. The nanogold membrane is synthesized by the spontaneous reduction of aqueous chloroaurate ions at the liquid-liquid interface by the bifunctional molecule bis(2-...

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Publié dans:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 20(2004), 9 vom: 27. Apr., Seite 3717-23
Auteur principal: Phadtare, Sumant (Auteur)
Autres auteurs: Vinod, V P, Wadgaonkar, Prakash P, Rao, Mala, Sastry, Murali
Format: Article
Langue:English
Publié: 2004
Accès à la collection:Langmuir : the ACS journal of surfaces and colloids
Sujets:Journal Article Research Support, Non-U.S. Gov't Caseins Enzymes, Immobilized Gold 7440-57-5 Pepsin A EC 3.4.23.1
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Résumé:We demonstrate herein the formation of a free-standing gold nanoparticle membrane and its use in the immobilization of the enzyme, pepsin. The nanogold membrane is synthesized by the spontaneous reduction of aqueous chloroaurate ions at the liquid-liquid interface by the bifunctional molecule bis(2-(4-aminophenoxy)ethyl) ether (DAEE) taken in chloroform. This process results in the formation of a robust, malleable free-standing nanogold membrane consisting of gold nanoparticles embedded in a polymeric background. Recognizing that gold nanoparticles are excellent candidates for immobilization of enzymes, we have immobilized pepsin on the nanogold membrane, leading to a new class of biocatalyst. A highlight of the new pepsin-nanogold biocatalyst is the ease with which separation from the reaction medium may be achieved. The catalytic activity of pepsin in the bioconjugate was comparable to that of the free enzyme in solution. The pepsin-nanogold membrane bioconjugate material exhibited excellent biocatalytic activity over 10 successive reuse cycles as well as enhanced pH, temperature, and temporal stability
Description:Date Completed 09.02.2006
Date Revised 26.10.2019
published: Print
Citation Status MEDLINE
ISSN:1520-5827