Meso-Cellular Silicate Foam-Modified Reduced Graphene Oxide with a Sandwich Structure for Enzymatic Immobilization and Bioelectrocatalysis
| Autor: | Shun Li, Hairan Zhang, Wang Huiting, Tingting Pei, Teng Fei, Qian Zhang, Ling Zhang, Lixin Xia |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Materials science
Immobilized enzyme Cholesterol oxidase Oxide Biosensing Techniques 02 engineering and technology 010402 general chemistry 01 natural sciences law.invention chemistry.chemical_compound law Electrochemistry General Materials Science Glucose oxidase Nanosheet Detection limit biology Graphene Silicates Enzymes Immobilized 021001 nanoscience & nanotechnology 0104 chemical sciences chemistry Chemical engineering Electrode biology.protein Graphite 0210 nano-technology |
| Zdroj: | ACS Applied Materials & Interfaces. 11:29522-29535 |
| ISSN: | 1944-8252 1944-8244 |
| DOI: | 10.1021/acsami.9b08569 |
| Popis: | An integrated composite of meso-cellular silicate foam (MCF)-modified reduced graphene oxide (MCF@rGO) was designed and synthesized based on polyethylene oxide-polypropylene oxide-polyethylene oxide (P123)-modified rGO (P123-rGO). As the polymeric template for the fabrication of mesoporous silicates, modified P123 greatly improved the affinity between the nanosheet and the in situ formed MCFs, resulting in the formation of thin layers of MCFs on both sides of rGO. Therefore, the MCFs@rGO formed exhibited a unique sandwich structure with an inner skeleton of rGO and two outer layers of MCFs. The outer modification by MCFs, with the presence of large mesopores, not only shifted the surface property of rGO from hydrophobic to hydrophilic but also offered immobilized enzymes a favorable microenvironment to maintain their bioactivity. Meanwhile, the inner skeleton of rGO compensated for the weak conductivity of MCFs, providing a pathway for the direct electron transfer (DET) of various redox enzymes or proteins, such as hemoglobin (Hb), horseradish peroxidase, glucose oxidase (GOD), and cholesterol oxidase. It was found that the DET signal obtained from Hb-MCFs@rGO/glassy carbon electrode (GCE) was much larger than the sum of the signals from two components-based modified electrodes of Hb-P123-rGO/GCE and Hb-MCFs/GCE. A similar improvement in DET signal was also observed using GOD-MCFs@rGO/GCE. The significant enhancement of DET signals for both protein electrodes can be ascribed to the synergistic effects generated from the integration of the two components, one of which enhances biocompatibility and the other enhances conductivity. The bioelectrocatalytic performance of Hb and GOD electrodes was further investigated. As for Hb-MCFs@rGO/GCE, the GOD electrode displayed excellent analytical performance for the detection of hydrogen peroxide (H2O2), including a good sensitivity of 0.25 μA μmol-1 L cm-2, a low detection limit of 63.6 nmol L-1 based on S/N = 3, and a low apparent Michaelis-Menten constant (KMapp) of 49.05 μmol L-1. GOD-MCFs@rGO/GCE also exhibited good analytical performance for the detection of glucose, with a wide linear range of 0.25-8.0 mmol L-1. In addition, blood glucose detection in samples of human serum was successfully achieved using GOD-MCFs@rGO/GCE with a low quantification limit. |
| Databáze: | OpenAIRE |
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