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Encapsulation hemoglobin in ordered mesoporous silicas: Influence factors for immobilization and bioelectrochemistry
Institution:1. Department of Chemistry, East China Normal University, Shanghai 200062, PR China;2. Center of Analysis and Research, East China University of Science and Technology, Shanghai 2000237, PR China;1. Departamento de Física, Universidad de La Laguna, 38206 La Laguna, Tenerife, Spain;2. Departamento de Química, Universidad de La Laguna, 38206 La Laguna, Tenerife, Spain;3. Izaña Atmospheric Research Center, Meteorological State Agency of Spain, Spain;4. CIC biomaGUNE, Paseo de Miramón 182, 20009 Donostia-San Sebastián, Spain;5. Departamento de Ingeniería Química y Tecnología Farmacéutica, Universidad de La Laguna, 38206 La Laguna, Tenerife, Spain;1. College of Materials and Textiles, Zhejiang Sci-Tech University, Hangzhou 310018, China;2. Keyi College, Zhejiang Sci-Tech University, Hangzhou 311121, China
Abstract: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/Au-SBA-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 μM, 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 (Km) of 2.87 mM, significantly lower than the 7.78 mM value for the Hb/SBA-15.
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