Functionality of dielectrophoretically immobilized enzyme molecules. Issue 4 (20th December 2013)

• Record Type: Journal Article
• Authors: Laux, Eva‐Maria; Kaletta, Udo C.; Bier, Frank F.; Wenger, Christian; Hölzel, Ralph
• Is Part Of: Electrophoresis. Volume 35:Issue 4(2014:Feb.)
• Page Start: 459
• Page End: 466
• Publication Date: 2013-12-20
• Subjects: Electrophoresis -- Periodicals; Electrophoresis -- Periodicals; 541.372
• DOI: 10.1002/elps.201300447
• Languages: English
• ISSNs: 0173-0835

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The enzyme horseradish peroxidase has been immobilized on nanoelectrode arrays by alternating current dielectrophoresis (DEP). Preservation of its enzymatic function after field application was demonstrated by oxidizing dihydrorhodamine 123 with hydrogen peroxide as co‐oxidant to create its fluorescent form, rhodamine 123 (Rh123). Localization of the fluorescently labeled enzyme and its product was conducted by fluorescence microscopy. Nanoelectrodes were prepared as tungsten pins arranged in square arrays. Experimental parameters for dielectrophoretic immobilization were optimized for even enzyme distribution and for enzymatic efficiency. Enzyme activity was quantified by determination of fluorescence intensities of immobilized enzyme molecules and of Rh123 produced. These results demonstrate that DEP can be applied to immobilize enzyme molecules while retaining their activity and rendering any chemical modifications unnecessary. This introduces a novel way for the preparation of bioactive surfaces for processes such as biosensing.</p> </abstract>