Mussel adhesive proteins (MAPs) have received increased attention as potential biomedical and environmentally friendly underwater adhesives due to their fascinating properties. Particularly, foot protein type 3 (fp-3), is located at the interface between the substratum and the adhesion plaque of mussels, and it is expected as one of the key components for surface adhesion with high concentration of 3, 4-dihydroxyphenyl-L-alanine (Dopa). Although our previous research reported the production of Mytilus galloprovincialis foot protein type 3 variant A (fp-3A) in Escherichia coli, its bulk adhesive strength has not been characterized due to availability in limited quantities. In the present work, fp-3A gene was codon-optimized based on the preference of E. coli codon usage and signal sequence was eliminated. A feasible production (~47 mg l-1) of recombinant fp-3 fused with a hexahistidine affinity ligand and its purification with affinity chromatography were achieved, and its bulk adhesive strength was measured for the first time; ~0.57 MPa for unmodified form and ~0.94 and ~2.28 MPa for Dopa-modified form having 9.6% yield without and with oxidant treatment, respectively. Further, the bulk adhesive strength values of several Dopa-modified recombinant MAPs were compared. The maximum adhesive strength of Dopa-modified fp-3 after oxidant treatment was stronger than that of type 5 (fp-5), which has 6.2% modification yields, and comparable to that of hybrid types fp-131 and fp-151, which have similar yields (~5%). In conclusion, the strong bulk adhesive property of recombinant fp-3 demonstrates its potential use as a promising bioadhesive.

Investigation on the bulk adhesive strength of the recombinant mussel adhesive protein fp-3

247th National Meeting (2014)

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