用于辣根过氧化物酶生物电化学的介孔二氧化硅空心球（MSHS）
Mesoporous silica hollow sphere (MSHS) for the bioelectrochemistry of horseradish peroxidase.
作者信息
Cao Zhaoxia, Zhang Jian, Zeng Julan, Sun Lixian, Xu Fen, Cao Zhong, Zhang Ling, Yang Daowu
机构信息
Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Materials & Thermochemistry Laboratory, Dalian 116023, Liaoning Province, China.
出版信息
Talanta. 2009 Jan 15;77(3):943-7. doi: 10.1016/j.talanta.2008.06.043. Epub 2008 Jul 5.
In this work, novel mesoporous silica hollow spheres (MSHS) were chosen as an immobilization matrix, to construct a mediator-free third-generation HRP biosensor. UV-vis spectroscopy revealed that horseradish peroxidase (HRP) entrapped in MSHS could retain its native structure. FTIR spectroscopy and nitrogen adsorption-desorption isotherms indicated that HRP are intercalated into the mesopores. The direct electron transfer of HRP entrapped in MSHS was observed. A pair of stable and well-defined redox peaks of HRP with a formal potential of about -0.150 V (vs. Ag/AgCl) in 0.1M pH 7.0 phosphate-buffered solution (PBS) were obtained. The biosensor exhibited a fast amperometric response to H(2)O(2) with a linear range of 3.9 x 10(-6) to 1.4 x 10(-4)M (R=0.997, N=20). The detection limit was 1.2 x 10(-6)M based S/N=3.
在本工作中，选用新型介孔二氧化硅空心球（MSHS）作为固定化基质，构建无媒介体的第三代辣根过氧化物酶（HRP）生物传感器。紫外可见光谱表明，包裹于MSHS中的辣根过氧化物酶（HRP）能够保持其天然结构。傅里叶变换红外光谱和氮吸附-脱附等温线表明，HRP嵌入到介孔中。观察到包裹于MSHS中的HRP的直接电子转移。在0.1M pH 7.0磷酸盐缓冲溶液（PBS）中获得了一对稳定且明确的HRP氧化还原峰，其形式电位约为-0.150 V（相对于Ag/AgCl）。该生物传感器对H₂O₂呈现快速安培响应，线性范围为3.9×10⁻⁶至1.4×10⁻⁴M（R = 0.997，N = 20）。基于信噪比S/N = 3，检测限为1.2×10⁻⁶M。
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