Recombinant Expression and Functional Analysis of Mytilus coruscu s Foot Protein-3

Mussels Mytilus coruscus can adhere to various solid surfaces in the presence of moisture. Mussel foot protein-3 ( mfp-3 ) has been suggested as the main adhesive protein in the plaques closest to the adhesion interface and also has been suggested as potential environmentally friendly adhesives for use in aqueous conditions and in medicine. To obtain enough M. coruscus mfp-3 for the further study , using E. coli expression system , recombinant mfp3 with a 6 × His tag at C-termini was successfully expressed and purified by Ni-NTA affinity purification followed by reverse phase HPLC separation. The actual molecular mass of recombinant mfp3 was determined as 9. 18 kD by MALDI-TOF , which is almost identical to the calculated mass of 9. 15 kD and confirmed that recombinant mfp-3 had been successfully purified to a high level. Recombinant mfp3 was modified by tyrosinase and DOPA content assay was performed to detect the conversion efficiency of Tyr to DOPA. Adhesion ability tests such as coating assay and QCM revealed that recombinant mfp3 has significant adhesion ability especially after modified by tyrosinase. These assays revealed the correlation between DOPA content and adhesion ability , and that