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Direct Electrochemistry and Electrocatalysis Behaviors of Glucose Oxidase Based on Hyaluronic Acid‐Carbon Nanotubes‐Ionic Liquid Composite Film
Author(s) -
Shangguan Xiaodong,
Zheng Jianbin,
Zhang Hongfang,
Tang Hongsheng
Publication year - 2010
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201090315
Subject(s) - glucose oxidase , chemistry , ionic liquid , electrochemistry , redox , carbon nanotube , electrode , electrocatalyst , nuclear chemistry , detection limit , ferrocene , chemical engineering , analytical chemistry (journal) , inorganic chemistry , organic chemistry , catalysis , chromatography , engineering
Multi‐walled carbon nanotubes (MWNTs) were dispersed in the ionic liquid [BMIM][BF 4 ] to form a uniform black suspension. Based on it, a novel glucose oxidase (GOx)‐hyaluronic (HA)‐[BMIM][BF 4 ]‐MWNTs/GCE modified electrode was fabricated. UV‐vis spectroscopy confirmed that GOx immobilized in the composite film retained its native structure. The experimental results of EIS indicated MWNTs, [BMIM][BF 4 ] and HA were successfully immobilized on the surface of GCE and [BMIM][BF 4 ]‐MWNTs could obviously improve the diffusion of ferricyanide toward the electrode surface. The experimental results of CV showed that a pair of well‐defined and quasi‐reversible peaks of GOx at the modified electrode was exhibited, and the redox reaction of GOx at the modified electrode was surface‐confined and quasi‐reversible electrochemical process. The average surface coverage of GOx and the apparent Michaelis‐Menten constant were 8.5×10 −9 mol/cm 2 and 9.8 mmol/L, respectively. The cathodic peak current of GOx and the glucose concentration showed linear relationship in the range from 0.1 to 2.0 mmol/L with a detection limit of 0.03 mmol/L ( S / N =3). As a result, the method presented here could be easily extended to immobilize and obtain the direct electrochemistry of other redox enzymes or proteins.