| Adsorption and corrosion measurements of the adhesive protein isolated from the blue mussel, Mytilus edulis L adsorbed onto type 304L stainless steel were performed. The adhesive protein is a high molecular weight biopolymer (100 kD) that is unique in containing a catechol, L-3,4 dihydroxyphenylalanine (L-Dopa) in its primary sequence. From these measurements, adsorption isotherms were determined and the maximum number of binding sites/m;Corrosion measurements using cyclic potentiodynamic polarization of the mussel protein adsorbed onto type 304L stainless steel coupons indicate that the protein confers significant corrosion inhibition on the metal compared to the other adsorbates tested. This inhibition is concentration dependent, with a maximum effect measured at 1.0 mg/ml solution concentration. This results in a reduction in weight loss of more than 50% in both polarization measurements and acidic ferric chloride solution measurements for 72 hours. Measurements made with a synthetic analogue of the mussel protein show no inhibitory effect on the corrosion of the stainless steel samples. The conformation of the synthetic analogue is different from that of the natural protein, which indicates that the conformation of the natural protein plays an important role in its corrosion inhibition.;The combination of the mussel protein's affinity for the stainless steel metal, the formation of a protein-metal complex at the surface of the metal and the reduction in weight loss over time demonstrates that the protein is an effective corrosion inhibitor for type 304L stainless steel. |
