Neutral red protonation behavior in the course of enzymatic glucose oxidation in aqueous and liposome media
Keywords:
glucose oxidation, kinetic analysis, neutral red, apparent ionization constant, absorbance-based optical biosensorAbstract
Kinetic analysis of glucose oxidation by glucose oxidase has been performed with a view to gain new information on the catalytic properties of the enzyme adsorbed onto a surface of lipid vesicles. The course of enzymatic reaction has been monitored spectrophotometrically with the pH-indicator neutral red. Neutral, positively, and negatively charged lipid vesicles have been prepared from egg phosphatidylcholine (PC), or its mixtures with cetyltrimethylammonium bromide (CTAB) (5 mol %) or cardiolipin (CL) (5 mol %). The apparent dissociation constant of neutral red in these systems in the presence of glucose oxidase has been found. The kinetic parameters of the glucose oxidase interaction with glucose and dioxygen have been found to remain unchanged on enzyme association with liposomes.
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