Recognition of substrates by immobilized bienzyme membranes.

概要

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Glucose oxidase and/or ascorbate oxidase were immobilized (entrapped) in poly(L-leucine-co-<I>N</I><SUP>ε</SUP>-benzyloxycarbonyl-L-lysin) using a spin casting method. Current shifts and time lags for immobilized single-enzyme and bienzyme membranes were investigated as a function of the substrate concentration at 37°C. The current shifts of L-ascorbic acid in the bienzyme membrane were found to be 2–3.5 times higher than those of a single-enzyme membrane. Both the time lags of L-ascorbic acid and D-glucose were found to depend on the concentration of the substrates for both single-enzyme and bienzyme membranes. The method was presented in order to estimate the concentration of two substrates simultaneously. The concentration of D-glucose and L-ascorbic acid in a model solution was simultaneously estimated from an analysis of the current shifts and the time lags using a nonlinear least-squares method as an example.
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