Journal
ELECTROANALYSIS
Volume 20, Issue 13, Pages 1421-1426Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/elan.200704203
Keywords
horseradish peroxidase; direct electrochemistry; vaterite; phospholipids
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Protein electrochemistry affords a direct method to study the biological electron transfer processes. However, supplying a biocompatible environment to maintain the native state of protein is all-important and challengeable. Here, we chose vaterite, one of the crystalline polymorphs of calcium carbonate, with highly porous nature and large specific surface area, which was doped with phospholipids, as the matrix to immobilize horseradish peroxidase (HRP). The integrity of HRP was kept during the simple immobilization procedure. By virtue of this organic/inorganic complex matrix, the direct electrochemistry of HRP was realized, and the activity of HRP for catalyzing reduction of O-2 and H2O2 was preserved.
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