A layer-by-layer deposition of concanavalin A (Con A) and glycoproteins suc
h as glucose oxidase (GOx) and horseradish peroxidase (HRP) afforded multil
ayer thin films on the surfaces of a quartz slide and a platinum electrode,
through biospecific complexation of Con A and sugar residues in the glycoe
nzymes. Lactate oxidase (LOx), which contains intrinsically no sugar chain,
was also built into a multilayer assembly by being modified extrinsically
with mannose residues. The enzymes formed monomolecular or sub-monomolecula
r layers in each layer of the multilayer films. Electrochemical measurement
s using Con A-enzyme multilayer-modified electrodes revealed that the enzym
es are catalytically active in the multilayer films. The Con A-enzyme multi
layer films are relatively stable against low concentrations of mannose and
urea, although the films destructed gradually in high concentrations of ur
ea solutions (>3 M).