Marine mussels produce strong underwater adhesives called mussel adhesive proteins (MAPs) that can adhere to a variety of surfaces under physiological conditions. Thus, MAPs have been investigated as a potentially sustainable alternative to conventional petrochemical-based adhesives. Recombinant MAPs would be promising for large-scale production and commercialization; however, MAPs are intrinsically adhesive, aggregative, and insoluble in water. In this study, we have developed a solubilization method for the control of MAP adhesion by fusion protein technique. Foot protein 1 (Fp1), a kind of MAP, was fused with the highly water-soluble protein, which is the C-terminal domain of ice-nucleation protein K (InaKC), separated by a protease cleaving site. The fusion protein exhibited low adhesion but high solubility and stability. Notably, Fp1 recovered its adhesive property after removal from the InaKC moiety by protease cleaving, which was evaluated and confirmed by the agglomeration of magnetite particles in water. The ability to control adhesion and agglomeration makes MAPs favorable prospects for bio-based adhesives.