Decoration of virus-like particles (VLPs) expands the repertory of functions these particles can display. In the last years, VLPs have successfully been used as scaffolds to present different molecules, frequently through the specific reaction of chemical groups on the surface of the particles, or by protein engineering when the presentation of peptides or proteins is the primary goal. VLPs of parvovirus B19 (B19V), have been previously produced in vitro and its stability and ability to assemble into hybrid particles composed of wild-type and chimeric proteins evidenced their potential as research tools. Herein, we report the presentation of functional proteins on the surface of B19V VLPs, through the fusion of the gene coding for the heterologous protein within the gene coding for the structural protein VP2. Two model proteins were used for the construction of chimeras, a lipase from Bacillus pumilus (BplA) and the enhanced green fluorescent protein (EGFP). Both chimeras were folded and successfully assembled in vitro into VLPs. While the BplA chimera exhibited esterase activity, the chimera of EGFP showed no fluorescence. We replaced the EGFP by its fast-folding derivative "super folder GFP" (sfGFP) flanked by larger linkers to increase its movement freedom, which resulted in fluorescent protein able to assemble fluorescent VLPs. These results expand the toolbox for VLP decoration as well as for the construction of new nanobiomaterials.