Lysine, poly-lysine and lysozyme were successfully intercalated in the MnPS3 layered phases. Intercalates were characterised by elemental and thermogravimetric analysis, and X-ray powder diffraction. Biomolecules conformation between the layers appears to result from the optimisation of the host-guest interactions. Moreover, infrared spectroscopy and differential scanning calorimetry measurements suggest that lysozyme is not denatured by the intercalation process.