The adhesive protein of the common blue mussel, Mytilus edulis(L) is a novel biopolymer in that it contains a catechol, L,3,4-dihydroxy-phenylalanine (L-Dopa) in its primary sequence. Adsorption of this protein onto S30403 stainless steel coupons imparts a significant resistance to corrosion when the test coupons are immersed in 3% NaCl and with an applied potential up to +350 mV (SCE). Comparison with other proteins and polymers such as serum albumin (BSA), a low molecular weight catechol (DHBA), and poly-L-lysine indicates that none are as effective as the mussel protein at inhibiting corrosion of the stainless steel alloy tested. This indicates that the adhesive protein may have an advantage over other organic polymers in use at the present time in corrosion control technology.

Subject
Pits, Metal surfaces, Repassivation potentials, Adsorption, Molecular weight, Polymers, Interfaces, Metals, Corrosion inhibitors, Corrosion coupons, Stainless steel, Corrosion potential, Electrode potential
Keywords:
Corrosion, protein, organic, stainless steel, inhibitor
© 1993 Association for Materials Protection and Performance (AMPP). All rights reserved. No part of this publication may be reproduced, stored in a retrieval system, or transmitted, in any form or by any means (electronic, mechanical, photocopying, recording, or otherwise) without the prior written permission of AMPP. Positions and opinions advanced in this work are those of the author(s) and not necessarily those of AMPP. Responsibility for the content of the work lies solely with the author(s).
1993
Association for Materials Protection and Performance (AMPP)
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