Production of fusion mussel adhesive fp-353 in Escherichia coli.

Mussel adhesive proteins (MAPs) have a potential as environmentally friendly adhesives for use under aqueous conditions. MAPs maybe of particular value in medical applications. We previously reported the functional expression of recombinant foot protein type 5 (fp-5) and foot protein type 3A (fp-3A), both of which have significant adhesion abilities, in Escherichia coli.

Practical recombinant hybrid mussel bioadhesive fp-151.

Mussel adhesive proteins (MAPs) have received increased attention as potential environmentally friendly adhesives under aqueous conditions and in medicine. However, attempts to produce functional recombinant MAPs (mainly foot protein type 1, fp-1) by several expression systems have failed. Even though we previously reported a functional expression of recombinant foot protein type 5 (fp-5) with significant adhesive ability in Escherichia coli, its practical use was limited by several problems such as low production yield, low purification yield, and high levels of post-purification insolubility.

Recombinant mussel adhesive protein Mgfp-5 as cell adhesion biomaterial.

Mytilus galloprovincialis foot protein type-5 (Mgfp-5) is one of the mussel adhesive proteins that participate in adhesion with the substratum. We previously reported the production of recombinant Mgfp-5 in Escherichia coli and showed that the recombinant protein had superior adhesion abilities versus those of Cell-Tak, a commercially available mussel adhesive protein mixture. In the present work, we investigated the feasibility of using recombinant Mgfp-5 as a cell adhesion agent.

Expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli.

Mussel adhesive proteins, including the 20-plus variants of foot protein type 3 (fp-3), have been suggested as potential environmentally friendly adhesives for use in aqueous conditions and in medicine. Here we report the novel production of a recombinant Mytilus galloprovincialis foot protein type 3 variant A (Mgfp-3A) fused with a hexahistidine affinity ligand in Escherichia coli and its approximately 99% purification with affinity chromatography. Recombinant Mgfp-3A showed a superior purification yield and better apparent solubility in 5% acetic acid (prerequisites for large-scale production and practical use) compared to those of the previously reported recombinant M.