Influence of ionic liquids on the direct electrochemistry of glucose oxidase entrapped in nanogold-N,N-dimethylformamide-ionic liquid composite film

16. Peace & justice 01 natural sciences 0104 chemical sciences
DOI: 10.1016/j.electacta.2007.04.014 Publication Date: 2007-04-07T11:16:30Z
ABSTRACT
Abstract Glucose oxidase (GOD) immobilized in nanogold particles (NAs)- N , N -dimethylformamide (DMF) composite film on glassy carbon (GC) electrode exhibits a pair of quasi-reversible and unstable peaks due to the redox of flavin adenine dinucleotide (FAD) of GOD. When ionic liquids (ILs) 1-butyl-3-methylimidazolium tetrafluoroborate (BMIMBF 4 ) or trihexyltetradecylphosphorium bis (trifluoromethylsulfony) (P 666,14 NTf 2 ) is introduced in the film, the peaks become small. But ILs 1-butyl-3-methylimidazolium hexafluorophosphate (BMIMPF 6 ) and 1-octyl-3-methylimidazolium hexafluorophate (OMIMPF 6 ) make the peaks large and stable. In different composite films the formal potential ( E 0 ′) of GOD is different. UV–vis spectra show that the GOD dispersed in these films almost retains its native structure and there are weak interactions between ILs and GOD. Electrochemical impedance spectra display that NAs can promote the electron transfer between FAD and GC electrode; and ILs can affect the electron transfer through interacting with GOD. The thermal stability of GOD entrapped in NAs-DMF-ILs composite films is also influenced by ILs, and it follows such order as: in NAs-DMF-OMIMPF 6  > in NAs-DMF-BMIMPF 6  ≈ in NAs-DMF-BMIMBF 4  > in NAs-DMF. In addition, GOD immobilized in NAs-DMF-OMIMPF 6 and NAs-DMF-BMIMPF 6 films shows good catalytic activity to the oxidation of glucose. The I max of H 2 O 2 and the apparent K m (Michaelis–Menten constant) for the enzymatic reaction are calculated.
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