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|Title:||Covalent immobilization of glucose oxidase on well-defined poly(glycidyl methacrylate)-Si(111) hybrids from surface-initiated atom-transfer radical polymerization||Authors:||Xu, F.J.
|Issue Date:||Mar-2005||Citation:||Xu, F.J., Cai, Q.J., Li, Y.L., Kang, E.T., Neoh, K.G. (2005-03). Covalent immobilization of glucose oxidase on well-defined poly(glycidyl methacrylate)-Si(111) hybrids from surface-initiated atom-transfer radical polymerization. Biomacromolecules 6 (2) : 1012-1020. ScholarBank@NUS Repository. https://doi.org/10.1021/bm0493178||Abstract:||A simple one-step procedure was employed for the covalent immobilization of an atom-transfer radical polymerization (ATRP) initiator, via the robust Si-C bond, on the hydrogen-terminated Si(111) surface (Si-H surface). Well-defined poly(glycidyl methacrylate) [P(GMA)] brushes, tethered directly on the (111)-oriented single-crystal silicon surface, were prepared via surface-initiated ATRP. Kinetics study on the surface-initiated ATRP of glycidyl methacrylate revealed that the chain growth from the silicon surface was consistent with a "controlled" process. A relatively high concentration of glucose oxidase (GOD; above 0.2 mg/cm2) could be coupled directly to the well-defined P(GMA) brushes via the ring-opening reaction of the epoxide groups with the amine moieties of the enzyme. The resultant GOD-functionalized P(GMA) brushes, with the accompanying hydroxyl groups from the ring-opening reaction of the epoxide groups, serves as an effective spacer to provide the GOD with a higher degree of conformational freedom and a more hydrophilic environment. An equivalent enzyme activity above 1.6 units/cm2 [μmoles Of β-D-(+)-glucose oxidized to D-gluconolactone per minute per square centimeter] and a corresponding relative activity of about 60% could be readily achieved. The immobilized GOD also exhibited an improved stability during storage over that of the free enzyme. The GOD-functionalized silicon substrates are potentially useful to the development of silicon-based glucose biosensors. © 2005 American Chemical Society.||Source Title:||Biomacromolecules||URI:||http://scholarbank.nus.edu.sg/handle/10635/88712||ISSN:||15257797||DOI:||10.1021/bm0493178|
|Appears in Collections:||Staff Publications|
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