公司動(dòng)態(tài)
測量應(yīng)用案例-2016-82
閱讀:202 發(fā)布時(shí)間:2016-12-13文獻(xiàn)名: Entrapping cross-linked glucose oxidase aggregates within a graphitized mesoporous carbon network for enzymatic biofuel cells
作者: Tsai Garcia-Pereza, Sung-Gil Hongb, Jungbae Kimb, , , Su Haa,
a School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA, USA
b Department of Chemical and Biological Engineering, Korea University, Seoul 02841, Republic of Korea
摘要:This paper reports a novel method for producing glucose oxidase-nanocomposites by entrapping cross-linked glucose oxidase (GOx) aggregates within a graphitized mesoporous carbon (GMC) network. Entrapment was achieved by utilizing the strong self-aggregation tendency of GMC in aqueous buffer solution to form carbon networks. Using confocal microscopy and TEM, GOx-GMC nanocomposites were visualized. The electrochemical properties of GOx-GMC nanocomposites were studied by means of cyclic voltammograms, chronoamperometric and potentiostatic tests. Results therefrom suggested that the GOx-GMC nanocomposites offer a high electrical conductivity with the maximum electron transfer rate constant estimated at 5.16 ± 0.61 s−1. Furthermore, thermally treating the GOx-GMC nanocomposite and GOx aggregates at 60 °C for four hours, both samples maintained 99% of their initial activity, while the free GOx were compley deactivated. These performances suggested that our nanocomposite structure offered both improved electrochemical performance and stability by combining the high electrical conductivity offered by the GMC network with the high enzyme loading and stability offered by the cross-linked GOx aggregates. The GOx-GMC nanocomposite’s electrochemical activity towards glucose oxidation was also investigated by using an enzymatic biofuel cell without artificial mediators, producing a power density of up to 22.4 μW cm−2 at 0.24 V.
關(guān)鍵詞:Glucose oxidase; Graphitized mesoporous carbons; Efficient electron transfer; Enzymatic biofuel cells; Cross-linked glucose oxidase aggregates