文献类型：期刊文献

英文题名：Encapsulation hemoglobin in ordered mesoporous silicas: Influence factors for immobilization and bio electrochemistry

作者：Xian, Yuezhong[1]; Xian, Yang[1]; Zhou, Lihui[2]; Wu, Fanghua[1]; Ling, Yun[1]; Jin, Litong[1]

机构：[1]E China Normal Univ, Dept Chem, Shanghai 200062, Peoples R China;[2]E China Univ Sci & Technol, Ctr Anal & Res, Shanghai 2000237, Peoples R China

年份：2007

卷号：9

期号：1

起止页码：142

外文期刊名：ELECTROCHEMISTRY COMMUNICATIONS

收录：;EI(收录号：20065010301917);WOS:【SCI-EXPANDED(收录号:WOS:000243847600026)】；

语种：英文

外文关键词：SBA-15; Au-SBA-15; hemoglobin; direct chemistry; hydrogen peroxide

摘要：The encapsulation of hemoglobin (Hb) on the mesoporous silicas SBA-15 and Au-doped SBA-15 (Au-SBA-15) has been studied as a model protein adsorption system. The influences of solution pH, structure of mesoporous silicas and gold nanoparticles incorporation on Hb immobilization are investigated in detail. The spectral characteristics of Hb/SBA-15 and Hb/Au-SBA-15 nanoconjugate show an absorption curve quite similar to that of native Hb, indicating that Hb retains its higher-order structure in the mesopores of SBA-15. Direct electrochemistry of Hb is obtained when Hb is adsorpted by mesoporous silicas SBA-15 or Au-SBA-15. Moreover, Hb/AuSBA-15 exerts enhancing electron transfer ability because of the Au incorporation. Additionally, the Hb/Au-SBA-15 displays good electrocatalytic reduction of hydrogen peroxide with a detection limit of 1.0 mu M, about 3 times as low as that for the Hb/SBA-15. The Hb/Au-SBA-15 exhibits higher peroxidase-like activity with the apparent Michaelis-Menton constant (K-m) of 2.87 mM, significantly lower than the 7.78 mM value for the Hb/SBA-15. (c) 2006 Elsevier B.V. All rights reserved.