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Direct Electrochemistry of Horseradish Peroxidase Immobilized in Calcium Carbonate Microsphere Doped with Phospholipids
Author(s) -
Li Gaiping,
Liu Xiaohua,
Du Liangwei,
Wang Erkang
Publication year - 2008
Publication title -
electroanalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.574
H-Index - 128
eISSN - 1521-4109
pISSN - 1040-0397
DOI - 10.1002/elan.200704203
Subject(s) - horseradish peroxidase , vaterite , chemistry , electrochemistry , calcium carbonate , chemical engineering , nuclear chemistry , inorganic chemistry , organic chemistry , enzyme , electrode , engineering , aragonite
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 H 2 O 2 was preserved.