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. However, these proteins were produced at low levels because of post-induction cell growth inhibition, and the proteins showed poor post-purification solubility. Here, we design and produce a new, type of recombinant MAP, fp-353, that is a fusion protein with fp-3A at each terminus of fp-5. Because fp-353 formed inclusion bodies, host cell growth inhibition did not occur. In addition, the solubility of MAP fp-353 after purification was significantly enhanced, permitting the preparation of a viscous concentrated glue solution for large-scale adhesion strength measurements. Together with large-scale cowhide adhesion measurements and cell-adhesion analyses, we successfully demonstrated that fusion mussel protein fp-353 has potential as a practical alternative bioadhesive.