Abstract: A simple enzyme immobilization technique using an adhesive protein isolated from Mytilus edulis blue mussels was optimized for constructing a glucose oxidase (GOD) based electrode. Owing to the presence of 10^-15% of 3,4-dihydroxyphenylalanine residues, the mussel adhesive protein (MAP) was easily oxidized to form a stable protein film on Pt, Au, and glassy C electrodes. Covalent attachment of glucose oxidase to adhesive protein modified electrodes was attained since the oxidized form of the L-Dopa moieties was very reactive towards various compounds containing amino, alcohol, and thiol groups. Glucose detection was performed using MAP/GOD modified electrodes at +0.8 V in 0.1 M phosphate buffer, pH 5. Pt modified electrodes (Pt/MAP/GOD) exhibited a considerably higher sensitivity (1.28 µA/mM) in comparison to its Au (Au/ MAP/GOD, 2.92 nA/mM) or glassy carbon (GC/MAP/GOD, 2.62 nA/mM) counterparts. Tetrachloro-1,4-benzoquinone (TCBQ), an oxidation product of pentachlorophenol, was detected using MAP/GOD modified electrodes at +0.45 V, in a deaerated 0.1 M tartaric acid buffer, pH 3.5 containing 40 mM glucose. In steady state, the current response of the Au/MAP/GOD electrode was higher (6.62 nA nM-1 cm-2, t95≈83 s, 5 nM) than the GC/MAP/GOD electrode (3.78 nA nM-1 cm-2, 8 nM). In flow injection analysis, GC/MAP/GOD electrodes exhibited a linear response for TCBQ ranging from 10 nM to 1 µM (3.96 nA nM-1) with a detection limit of 10 nM. The modified glassy C enzyme based electrode retained 90% and 87% of its activity after 150 and 250 repeated injections.