Abstract
Mussel adhesive proteins (MAPs) have been suggested as promising bioadhesives for diverse application fields, including medical uses. Previously, we successfully constructed and produced a new type of functional recombinant MAP, fp‐151, in a prokaryotic Escherichia coli expression system. Even though the E. coli‐derived MAP showed several excellent features, such as high production yield and efficient purification, in vitro enzymatic modification is required to convert tyrosine residues to l‐3,4‐dihydroxyphenyl alanine (dopa) molecules for its adhesive ability, due to the intrinsic inability of E. coli to undergo post‐translational modification. In this work, we produced a soluble recombinant MAP in insect __Sf__9 cells, which are widely used as an effective and convenient eukaryotic expression system for eukaryotic foreign proteins. Importantly, we found that insect‐derived MAP contained converted dopa residues by in vivo post‐translational modification. In addition, insect‐derived MAP also had other post‐translational modifications including phosphorylation of serine and hydroxylation of proline that originally occurred in some natural MAPs. To our knowledge, this is the first report on in vivo post‐translational modifications of MAP containing dopa and other modified amino acid residues. © 2011 American Institute of Chemical Engineers Biotechnol. Prog., 2011